Articles - 1loz mentioned but not cited (3)
- A nanobody binding to non-amyloidogenic regions of the protein human lysozyme enhances partial unfolding but inhibits amyloid fibril formation. De Genst E, Chan PH, Pardon E, Hsu SD, Kumita JR, Christodoulou J, Menzer L, Chirgadze DY, Robinson CV, Muyldermans S, Matagne A, Wyns L, Dobson CM, Dumoulin M. J Phys Chem B 117 13245-13258 (2013)
- In silico prediction of novel residues involved in amyloid primary nucleation of human I56T and D67H lysozyme. Griffin JWD, Bradshaw PC. BMC Struct Biol 18 9 (2018)
- Lysozyme Mutants Accumulate in Cells while Associated at their N-terminal Alpha-domain with the Endoplasmic Reticulum Chaperone GRP78/BiP. Kamada Y, Nawata Y, Sugimoto Y. Int J Biol Sci 12 184-197 (2016)
Reviews citing this publication (102)
- Molecular mechanisms of amyloidosis. Merlini G, Bellotti V. N Engl J Med 349 583-596 (2003)
- Protein aggregation and aggregate toxicity: new insights into protein folding, misfolding diseases and biological evolution. Stefani M, Dobson CM. J Mol Med (Berl) 81 678-699 (2003)
- Folding proteins in fatal ways. Selkoe DJ. Nature 426 900-904 (2003)
- The alternative conformations of amyloidogenic proteins and their multi-step assembly pathways. Kelly JW. Curr Opin Struct Biol 8 101-106 (1998)
- Protein aggregation: folding aggregates, inclusion bodies and amyloid. Fink AL. Fold Des 3 R9-23 (1998)
- Conformational disease. Carrell RW, Lomas DA. Lancet 350 134-138 (1997)
- Protein-nanoparticle interactions: opportunities and challenges. Mahmoudi M, Lynch I, Ejtehadi MR, Monopoli MP, Bombelli FB, Laurent S. Chem Rev 111 5610-5637 (2011)
- Amyloid formation by globular proteins under native conditions. Chiti F, Dobson CM. Nat Chem Biol 5 15-22 (2009)
- Principles of protein folding, misfolding and aggregation. Dobson CM. Semin Cell Dev Biol 15 3-16 (2004)
- Protein aggregation and its inhibition in biopharmaceutics. Wang W. Int J Pharm 289 1-30 (2005)
- Evolution of amyloid: what normal protein folding may tell us about fibrillogenesis and disease. Lansbury PT. Proc Natl Acad Sci U S A 96 3342-3344 (1999)
- Hydrophobins: multipurpose proteins. Wösten HA. Annu Rev Microbiol 55 625-646 (2001)
- De novo design and structural characterization of proteins and metalloproteins. DeGrado WF, Summa CM, Pavone V, Nastri F, Lombardi A. Annu Rev Biochem 68 779-819 (1999)
- Islet amyloid and type 2 diabetes mellitus. Höppener JW, Ahrén B, Lips CJ. N Engl J Med 343 411-419 (2000)
- A new era for understanding amyloid structures and disease. Iadanza MG, Jackson MP, Hewitt EW, Ranson NA, Radford SE. Nat Rev Mol Cell Biol 19 755-773 (2018)
- Peptide fibrillization. Hamley IW. Angew Chem Int Ed Engl 46 8128-8147 (2007)
- Folding versus aggregation: polypeptide conformations on competing pathways. Jahn TR, Radford SE. Arch Biochem Biophys 469 100-117 (2008)
- Structural Studies of Amyloid Proteins at the Molecular Level. Eisenberg DS, Sawaya MR. Annu Rev Biochem 86 69-95 (2017)
- Deadly conformations--protein misfolding in prion disease. Horwich AL, Weissman JS. Cell 89 499-510 (1997)
- The activities of amyloids from a structural perspective. Riek R, Eisenberg DS. Nature 539 227-235 (2016)
- The transthyretin amyloidoses: from delineating the molecular mechanism of aggregation linked to pathology to a regulatory-agency-approved drug. Johnson SM, Connelly S, Fearns C, Powers ET, Kelly JW. J Mol Biol 421 185-203 (2012)
- A diversity of assembly mechanisms of a generic amyloid fold. Eichner T, Radford SE. Mol Cell 43 8-18 (2011)
- Protein-misfolding diseases and chaperone-based therapeutic approaches. Chaudhuri TK, Paul S. FEBS J 273 1331-1349 (2006)
- The Yin and Yang of protein folding. Jahn TR, Radford SE. FEBS J 272 5962-5970 (2005)
- Targeting protein aggregation for the treatment of degenerative diseases. Eisele YS, Monteiro C, Fearns C, Encalada SE, Wiseman RL, Powers ET, Kelly JW. Nat Rev Drug Discov 14 759-780 (2015)
- Protein misfolding and disease; protein refolding and therapy. Soto C. FEBS Lett 498 204-207 (2001)
- De novo design of helical bundles as models for understanding protein folding and function. Hill RB, Raleigh DP, Lombardi A, DeGrado WF. Acc Chem Res 33 745-754 (2000)
- Serpinopathies and the conformational dementias. Lomas DA, Carrell RW. Nat Rev Genet 3 759-768 (2002)
- Conformational changes and disease--serpins, prions and Alzheimer's. Carrell RW, Gooptu B. Curr Opin Struct Biol 8 799-809 (1998)
- Therapeutic strategies for human amyloid diseases. Sacchettini JC, Kelly JW. Nat Rev Drug Discov 1 267-275 (2002)
- Protein aggregation in disease: a role for folding intermediates forming specific multimeric interactions. Horwich A. J Clin Invest 110 1221-1232 (2002)
- Amyloid fibril formation and protein misassembly: a structural quest for insights into amyloid and prion diseases. Kelly JW. Structure 5 595-600 (1997)
- Optimization of protein purification and characterization using Thermofluor screens. Boivin S, Kozak S, Meijers R. Protein Expr Purif 91 192-206 (2013)
- Amyloidosis and the respiratory tract. Gillmore JD, Hawkins PN. Thorax 54 444-451 (1999)
- Protein unfolding--an important process in vivo? Matouschek A. Curr Opin Struct Biol 13 98-109 (2003)
- Amyloid accomplices and enforcers. Alexandrescu AT. Protein Sci 14 1-12 (2005)
- A molecular history of the amyloidoses. Buxbaum JN, Linke RP. J Mol Biol 421 142-159 (2012)
- [PSI+]: an epigenetic modulator of translation termination efficiency. Serio TR, Lindquist SL. Annu Rev Cell Dev Biol 15 661-703 (1999)
- Serum amyloid P component scintigraphy for diagnosis and monitoring amyloidosis. Hawkins PN. Curr Opin Nephrol Hypertens 11 649-655 (2002)
- The environmental dependency of protein folding best explains prion and amyloid diseases. Kelly JW. Proc Natl Acad Sci U S A 95 930-932 (1998)
- Role of islet amyloid in type 2 diabetes mellitus. Höppener JW, Lips CJ. Int J Biochem Cell Biol 38 726-736 (2006)
- Theory and practice of size exclusion chromatography for the analysis of protein aggregates. Fekete S, Beck A, Veuthey JL, Guillarme D. J Pharm Biomed Anal 101 161-173 (2014)
- Protein denaturation and aggregation: Cellular responses to denatured and aggregated proteins. Meredith SC. Ann N Y Acad Sci 1066 181-221 (2005)
- Amyloid assembly and disassembly. Chuang E, Hori AM, Hesketh CD, Shorter J. J Cell Sci 131 jcs189928 (2018)
- The role of cystatin C in cerebral amyloid angiopathy and stroke: cell biology and animal models. Levy E, Jaskolski M, Grubb A. Brain Pathol 16 60-70 (2006)
- UV resonance Raman investigations of peptide and protein structure and dynamics. Oladepo SA, Xiong K, Hong Z, Asher SA, Handen J, Lednev IK. Chem Rev 112 2604-2628 (2012)
- Amyloid-based nanosensors and nanodevices. Hauser CA, Maurer-Stroh S, Martins IC. Chem Soc Rev 43 5326-5345 (2014)
- Understanding the complex mechanisms of β2-microglobulin amyloid assembly. Eichner T, Radford SE. FEBS J 278 3868-3883 (2011)
- Amyloidogenicity and cytotoxicity of islet amyloid polypeptide. Kapurniotu A. Biopolymers 60 438-459 (2001)
- Bridging the gap: from protein misfolding to protein misfolding diseases. Luheshi LM, Dobson CM. FEBS Lett 583 2581-2586 (2009)
- Assays for α-synuclein aggregation. Giehm L, Lorenzen N, Otzen DE. Methods 53 295-305 (2011)
- Detecting cryptic epitopes created by nanoparticles. Lynch I, Dawson KA, Linse S. Sci STKE 2006 pe14 (2006)
- Conformational diseases: looking into the eyes. Surguchev A, Surguchov A. Brain Res Bull 81 12-24 (2010)
- A beta amyloidogenesis: unique, or variation on a systemic theme? Kisilevsky R, Fraser PE. Crit Rev Biochem Mol Biol 32 361-404 (1997)
- On the path to the heat shock response: destabilization and formation of partially folded protein intermediates, a consequence of protein thiol modification. Freeman ML, Borrelli MJ, Meredith MJ, Lepock JR. Free Radic Biol Med 26 737-745 (1999)
- Gelsolin amyloidosis: genetics, biochemistry, pathology and possible strategies for therapeutic intervention. Solomon JP, Page LJ, Balch WE, Kelly JW. Crit Rev Biochem Mol Biol 47 282-296 (2012)
- Engineering peptides and proteins that undergo alpha-to-beta transitions. Mihara H, Takahashi Y. Curr Opin Struct Biol 7 501-508 (1997)
- Systemic amyloidosis: lessons from β2-microglobulin. Stoppini M, Bellotti V. J Biol Chem 290 9951-9958 (2015)
- Hereditary cystatin C amyloid angiopathy. Olafsson I, Grubb A. Amyloid 7 70-79 (2000)
- Lysozyme: a paradigmatic molecule for the investigation of protein structure, function and misfolding. Merlini G, Bellotti V. Clin Chim Acta 357 168-172 (2005)
- The Amyloid Phenomenon and Its Links with Human Disease. Dobson CM. Cold Spring Harb Perspect Biol 9 a023648 (2017)
- Structural disorder in amyloid fibrils: its implication in dynamic interactions of proteins. Tompa P. FEBS J 276 5406-5415 (2009)
- Ostertag revisited: the inherited systemic amyloidoses without neuropathy. Benson MD. Amyloid 12 75-87 (2005)
- Structure and Aggregation Mechanisms in Amyloids. Almeida ZL, Brito RMM. Molecules 25 E1195 (2020)
- Protein folding and interactions revealed by mass spectrometry. Last AM, Robinson CV. Curr Opin Chem Biol 3 564-570 (1999)
- Copper-dependent functions for the prion protein. Brown DR, Sassoon J. Mol Biotechnol 22 165-178 (2002)
- Lysozyme amyloidosis: report of 4 cases and a review of the literature. Granel B, Valleix S, Serratrice J, Chérin P, Texeira A, Disdier P, Weiller PJ, Grateau G. Medicine (Baltimore) 85 66-73 (2006)
- Local environmental effects on the structure of the prion protein. DeMarco ML, Daggett V. C R Biol 328 847-862 (2005)
- beta(2)-microglobulin: from physiology to amyloidosis. Heegaard NH. Amyloid 16 151-173 (2009)
- Functionalized nanosystems for targeted mitochondrial delivery. Durazo SA, Kompella UB. Mitochondrion 12 190-201 (2012)
- Probing the origins, diagnosis and treatment of amyloid diseases using antibodies. Dumoulin M, Dobson CM. Biochimie 86 589-600 (2004)
- Microbial functional amyloids serve diverse purposes for structure, adhesion and defence. Shanmugam N, Baker MODG, Ball SR, Steain M, Pham CLL, Sunde M. Biophys Rev 11 287-302 (2019)
- Camelid single-domain antibody fragments: Uses and prospects to investigate protein misfolding and aggregation, and to treat diseases associated with these phenomena. Pain C, Dumont J, Dumoulin M. Biochimie 111 82-106 (2015)
- Design of peptides undergoing self-catalytic alpha-to-beta transition and amyloidogenesis. Mihara H, Takahashi Y, Ueno A. Biopolymers 47 83-92 (1998)
- Molecular chaperones and the heat shock response. Sponsored by Cold Spring Harbor Laboratory, 6-10 May 1998. Kaufman RJ. Biochim Biophys Acta 1423 R13-27 (1999)
- A biological cosmos of parallel universes: does protein structural plasticity facilitate evolution? Meier S, Ozbek S. Bioessays 29 1095-1104 (2007)
- Disulfide bonds in amyloidogenesis diseases related proteins. Li Y, Yan J, Zhang X, Huang K. Proteins 81 1862-1873 (2013)
- Amyloid arthropathy in chickens. Landman WJ. Vet Q 21 78-82 (1999)
- Antibodies as specific chaperones. Ermolenko DN, Zherdev AV, Dzantiev BB. Biochemistry (Mosc) 69 1233-1238 (2004)
- Antibody Aggregation: Insights from Sequence and Structure. Li W, Prabakaran P, Chen W, Zhu Z, Feng Y, Dimitrov DS. Antibodies (Basel) 5 E19 (2016)
- Drug Insight: emerging therapies for amyloidosis. Gillmore JD, Hawkins PN. Nat Clin Pract Nephrol 2 263-270 (2006)
- Equine lysozyme: the molecular basis of folding, self-assembly and innate amyloid toxicity. Morozova-Roche LA. FEBS Lett 581 2587-2592 (2007)
- Role of islet amyloid in type 2 diabetes mellitus: consequence or cause? Höppener JW, Nieuwenhuis MG, Vroom TM, Ahrén B, Lips CJ. Mol Cell Endocrinol 197 205-212 (2002)
- Molecular pathogenesis of human amyloidosis: Lessons from β2 -microglobulin-related amyloidosis. Naiki H, Okoshi T, Ozawa D, Yamaguchi I, Hasegawa K. Pathol Int 66 193-201 (2016)
- Analytical methods and formulation factors to enhance protein stability in solution. Jeong SH. Arch Pharm Res 35 1871-1886 (2012)
- Dynamic of beta(2)-microglobulin fibril formation and reabsorption: the role of proteolysis. Bellotti V, Gallieni M, Giorgetti S, Brancaccio D. Semin Dial 14 117-122 (2001)
- Molecular chaperones: clamps for the Clps? Feng HP, Gierasch LM. Curr Biol 8 R464-7 (1998)
- Functional Amyloids Are the Rule Rather Than the Exception in Cellular Biology. Balistreri A, Goetzler E, Chapman M. Microorganisms 8 E1951 (2020)
- Exploring critical determinants of protein amyloidogenesis: a review. Sarkar N, Dubey VK. J Pept Sci 19 529-536 (2013)
- Stability matters, too - the thermodynamics of amyloid fibril formation. Buell AK. Chem Sci 13 10177-10192 (2022)
- Understanding the Role of Protein Glycation in the Amyloid Aggregation Process. Sirangelo I, Iannuzzi C. Int J Mol Sci 22 6609 (2021)
- Clusterin, other extracellular chaperones, and eye disease. Wilson MR, Satapathy S, Jeong S, Fini ME. Prog Retin Eye Res 89 101032 (2022)
- Stabilization of partially folded states in protein folding/misfolding transitions by hydrostatic pressure. Ferreira ST, Chapeaurouge A, De Felice FG. Braz J Med Biol Res 38 1215-1222 (2005)
- The prion protein: Structural features and related toxic peptides. Ronga L, Tizzano B, Palladino P, Ragone R, Urso E, Maffia M, Ruvo M, Benedetti E, Rossi F. Chem Biol Drug Des 68 139-147 (2006)
- Lessons learned from protein aggregation: toward technological and biomedical applications. Avila CL, Chaves S, Socias SB, Vera-Pingitore E, González-Lizárraga F, Vera C, Ploper D, Chehín R. Biophys Rev 9 501-515 (2017)
- A role for B lymphocytes in anti-infective prion therapies? Tayebi M, Bate C, Hawke S, Williams A. Expert Rev Anti Infect Ther 5 631-638 (2007)
- Amyloid Formation by Globular Proteins: The Need to Narrow the Gap Between in Vitro and in Vivo Mechanisms. Faravelli G, Mondani V, Mangione PP, Raimondi S, Marchese L, Lavatelli F, Stoppini M, Corazza A, Canetti D, Verona G, Obici L, Taylor GW, Gillmore JD, Giorgetti S, Bellotti V. Front Mol Biosci 9 830006 (2022)
- Finding the right balance: a personal journey from individual proteins to membrane-embedded motors: based on a lecture delivered at the 36th FEBS Congress in Torino, Italy, June 2011. Robinson CV. FEBS J 279 663-677 (2012)
- Structural Lessons From the Mutant Proinsulin Syndrome. Dhayalan B, Chatterjee D, Chen YS, Weiss MA. Front Endocrinol (Lausanne) 12 754693 (2021)
- [Doxycycline or how to create new with the old?]. Shehwaro N, Langlois AL, Gueutin V, Gauthier M, Casenave M, Izzedine H. Therapie 69 129-141 (2014)
- Contact-Based Analysis of Aggregation of Intrinsically Disordered Proteins. Cieplak M, Mioduszewski Ł, Chwastyk M. Methods Mol Biol 2340 105-120 (2022)
- [BIG-H3 protein: mutation of codon 124 and corneal amyloidosis]. Schmitt-Bernard CF, Pouliquen Y, Argilès A. J Fr Ophtalmol 27 510-522 (2004)
Articles citing this publication (450)
- Letter Prediction of sequence-dependent and mutational effects on the aggregation of peptides and proteins. Fernandez-Escamilla AM, Rousseau F, Schymkowitz J, Serrano L. Nat Biotechnol 22 1302-1306 (2004)
- Common core structure of amyloid fibrils by synchrotron X-ray diffraction. Sunde M, Serpell LC, Bartlam M, Fraser PE, Pepys MB, Blake CC. J Mol Biol 273 729-739 (1997)
- Huntingtin-encoded polyglutamine expansions form amyloid-like protein aggregates in vitro and in vivo. Scherzinger E, Lurz R, Turmaine M, Mangiarini L, Hollenbach B, Hasenbank R, Bates GP, Davies SW, Lehrach H, Wanker EE. Cell 90 549-558 (1997)
- Designing conditions for in vitro formation of amyloid protofilaments and fibrils. Chiti F, Webster P, Taddei N, Clark A, Stefani M, Ramponi G, Dobson CM. Proc Natl Acad Sci U S A 96 3590-3594 (1999)
- Amyloid fibril formation by an SH3 domain. Guijarro JI, Sunde M, Jones JA, Campbell ID, Dobson CM. Proc Natl Acad Sci U S A 95 4224-4228 (1998)
- Identification and characterization of key kinetic intermediates in amyloid beta-protein fibrillogenesis. Kirkitadze MD, Condron MM, Teplow DB. J Mol Biol 312 1103-1119 (2001)
- Prediction of "aggregation-prone" and "aggregation-susceptible" regions in proteins associated with neurodegenerative diseases. Pawar AP, Dubay KF, Zurdo J, Chiti F, Vendruscolo M, Dobson CM. J Mol Biol 350 379-392 (2005)
- FTIR reveals structural differences between native beta-sheet proteins and amyloid fibrils. Zandomeneghi G, Krebs MR, McCammon MG, Fändrich M. Protein Sci 13 3314-3321 (2004)
- Cryo-electron microscopy structure of an SH3 amyloid fibril and model of the molecular packing. Jiménez JL, Guijarro JI, Orlova E, Zurdo J, Dobson CM, Sunde M, Saibil HR. EMBO J 18 815-821 (1999)
- Oligopeptide-repeat expansions modulate 'protein-only' inheritance in yeast. Liu JJ, Lindquist S. Nature 400 573-576 (1999)
- Polyglutamine aggregates alter protein folding homeostasis in Caenorhabditis elegans. Satyal SH, Schmidt E, Kitagawa K, Sondheimer N, Lindquist S, Kramer JM, Morimoto RI. Proc Natl Acad Sci U S A 97 5750-5755 (2000)
- Formation of insulin amyloid fibrils followed by FTIR simultaneously with CD and electron microscopy. Bouchard M, Zurdo J, Nettleton EJ, Dobson CM, Robinson CV. Protein Sci 9 1960-1967 (2000)
- Binding mode of Thioflavin T and other molecular probes in the context of amyloid fibrils-current status. Groenning M. J Chem Biol 3 1-18 (2010)
- An amyloid-forming peptide from the yeast prion Sup35 reveals a dehydrated beta-sheet structure for amyloid. Balbirnie M, Grothe R, Eisenberg DS. Proc Natl Acad Sci U S A 98 2375-2380 (2001)
- Amyloid formation under physiological conditions proceeds via a native-like folding intermediate. Jahn TR, Parker MJ, Homans SW, Radford SE. Nat Struct Mol Biol 13 195-201 (2006)
- Conformational transitions of islet amyloid polypeptide (IAPP) in amyloid formation in vitro. Kayed R, Bernhagen J, Greenfield N, Sweimeh K, Brunner H, Voelter W, Kapurniotu A. J Mol Biol 287 781-796 (1999)
- Formation and seeding of amyloid fibrils from wild-type hen lysozyme and a peptide fragment from the beta-domain. Krebs MR, Wilkins DK, Chung EW, Pitkeathly MC, Chamberlain AK, Zurdo J, Robinson CV, Dobson CM. J Mol Biol 300 541-549 (2000)
- Sequence-dependent denaturation energetics: A major determinant in amyloid disease diversity. Hammarström P, Jiang X, Hurshman AR, Powers ET, Kelly JW. Proc Natl Acad Sci U S A 99 Suppl 4 16427-16432 (2002)
- Conversion of alpha-lactalbumin to a protein inducing apoptosis. Svensson M, Håkansson A, Mossberg AK, Linse S, Svanborg C. Proc Natl Acad Sci U S A 97 4221-4226 (2000)
- Kinetic studies of amyloid beta-protein fibril assembly. Differential effects of alpha-helix stabilization. Fezoui Y, Teplow DB. J Biol Chem 277 36948-36954 (2002)
- Lipids revert inert Abeta amyloid fibrils to neurotoxic protofibrils that affect learning in mice. Martins IC, Kuperstein I, Wilkinson H, Maes E, Vanbrabant M, Jonckheere W, Van Gelder P, Hartmann D, D'Hooge R, De Strooper B, Schymkowitz J, Rousseau F. EMBO J 27 224-233 (2008)
- Prediction of the absolute aggregation rates of amyloidogenic polypeptide chains. DuBay KF, Pawar AP, Chiti F, Zurdo J, Dobson CM, Vendruscolo M. J Mol Biol 341 1317-1326 (2004)
- Human recombinant NACP/alpha-synuclein is aggregated and fibrillated in vitro: relevance for Lewy body disease. Hashimoto M, Hsu LJ, Sisk A, Xia Y, Takeda A, Sundsmo M, Masliah E. Brain Res 799 301-306 (1998)
- Removal of the N-terminal hexapeptide from human beta2-microglobulin facilitates protein aggregation and fibril formation. Esposito G, Michelutti R, Verdone G, Viglino P, Hernández H, Robinson CV, Amoresano A, Dal Piaz F, Monti M, Pucci P, Mangione P, Stoppini M, Merlini G, Ferri G, Bellotti V. Protein Sci 9 831-845 (2000)
- Cu/Zn superoxide dismutase mutants associated with amyotrophic lateral sclerosis show enhanced formation of aggregates in vitro. Stathopulos PB, Rumfeldt JA, Scholz GA, Irani RA, Frey HE, Hallewell RA, Lepock JR, Meiering EM. Proc Natl Acad Sci U S A 100 7021-7026 (2003)
- Amyloid deposition is delayed in mice with targeted deletion of the serum amyloid P component gene. Botto M, Hawkins PN, Bickerstaff MC, Herbert J, Bygrave AE, McBride A, Hutchinson WL, Tennent GA, Walport MJ, Pepys MB. Nat Med 3 855-859 (1997)
- Amyloid fibril formation and seeding by wild-type human lysozyme and its disease-related mutational variants. Morozova-Roche LA, Zurdo J, Spencer A, Noppe W, Receveur V, Archer DB, Joniau M, Dobson CM. J Struct Biol 130 339-351 (2000)
- A general model for amyloid fibril assembly based on morphological studies using atomic force microscopy. Khurana R, Ionescu-Zanetti C, Pope M, Li J, Nielson L, Ramírez-Alvarado M, Regan L, Fink AL, Carter SA. Biophys J 85 1135-1144 (2003)
- The protofilament substructure of amyloid fibrils. Serpell LC, Sunde M, Benson MD, Tennent GA, Pepys MB, Fraser PE. J Mol Biol 300 1033-1039 (2000)
- Amyloid-like fibrils of ribonuclease A with three-dimensional domain-swapped and native-like structure. Sambashivan S, Liu Y, Sawaya MR, Gingery M, Eisenberg D. Nature 437 266-269 (2005)
- Myoglobin forms amyloid fibrils by association of unfolded polypeptide segments. Fändrich M, Forge V, Buder K, Kittler M, Dobson CM, Diekmann S. Proc Natl Acad Sci U S A 100 15463-15468 (2003)
- Studies of the aggregation of mutant proteins in vitro provide insights into the genetics of amyloid diseases. Chiti F, Calamai M, Taddei N, Stefani M, Ramponi G, Dobson CM. Proc Natl Acad Sci U S A 99 Suppl 4 16419-16426 (2002)
- Functional amyloid in Pseudomonas. Dueholm MS, Petersen SV, Sønderkær M, Larsen P, Christiansen G, Hein KL, Enghild JJ, Nielsen JL, Nielsen KL, Nielsen PH, Otzen DE. Mol Microbiol 77 1009-1020 (2010)
- Characterization of the oligomeric states of insulin in self-assembly and amyloid fibril formation by mass spectrometry. Nettleton EJ, Tito P, Sunde M, Bouchard M, Dobson CM, Robinson CV. Biophys J 79 1053-1065 (2000)
- A scrapie-like unfolding intermediate of the prion protein domain PrP(121-231) induced by acidic pH. Hornemann S, Glockshuber R. Proc Natl Acad Sci U S A 95 6010-6014 (1998)
- Thermally induced fibrillar aggregation of hen egg white lysozyme. Arnaudov LN, de Vries R. Biophys J 88 515-526 (2005)
- A camelid antibody fragment inhibits the formation of amyloid fibrils by human lysozyme. Dumoulin M, Last AM, Desmyter A, Decanniere K, Canet D, Larsson G, Spencer A, Archer DB, Sasse J, Muyldermans S, Wyns L, Redfield C, Matagne A, Robinson CV, Dobson CM. Nature 424 783-788 (2003)
- The folding cooperativity of a protein is controlled by its chain topology. Shank EA, Cecconi C, Dill JW, Marqusee S, Bustamante C. Nature 465 637-640 (2010)
- ALS mutants of human superoxide dismutase form fibrous aggregates via framework destabilization. DiDonato M, Craig L, Huff ME, Thayer MM, Cardoso RM, Kassmann CJ, Lo TP, Bruns CK, Powers ET, Kelly JW, Getzoff ED, Tainer JA. J Mol Biol 332 601-615 (2003)
- Mutational analysis of the propensity for amyloid formation by a globular protein. Chiti F, Taddei N, Bucciantini M, White P, Ramponi G, Dobson CM. EMBO J 19 1441-1449 (2000)
- Polymorphic fibril formation by residues 10-40 of the Alzheimer's beta-amyloid peptide. Paravastu AK, Petkova AT, Tycko R. Biophys J 90 4618-4629 (2006)
- A highly amyloidogenic region of hen lysozyme. Frare E, Polverino De Laureto P, Zurdo J, Dobson CM, Fontana A. J Mol Biol 340 1153-1165 (2004)
- A systematic exploration of the influence of the protein stability on amyloid fibril formation in vitro. Ramirez-Alvarado M, Merkel JS, Regan L. Proc Natl Acad Sci U S A 97 8979-8984 (2000)
- Formation of amyloid-like fibrils by self-association of a partially unfolded fibronectin type III module. Litvinovich SV, Brew SA, Aota S, Akiyama SK, Haudenschild C, Ingham KC. J Mol Biol 280 245-258 (1998)
- Interactions of Alzheimer amyloid-beta peptides with glycosaminoglycans effects on fibril nucleation and growth. McLaurin J, Franklin T, Zhang X, Deng J, Fraser PE. Eur J Biochem 266 1101-1110 (1999)
- Improved 3D triple resonance experiments, HNN and HN(C)N, for HN and 15N sequential correlations in (13C, 15N) labeled proteins: application to unfolded proteins. Panchal SC, Bhavesh NS, Hosur RV. J Biomol NMR 20 135-147 (2001)
- Solution conformations and thermodynamics of structured peptides: molecular dynamics simulation with an implicit solvation model. Schaefer M, Bartels C, Karplus M. J Mol Biol 284 835-848 (1998)
- Dependence on solution conditions of aggregation and amyloid formation by an SH3 domain. Zurdo J, Guijarro JI, Jiménez JL, Saibil HR, Dobson CM. J Mol Biol 311 325-340 (2001)
- Crystal structure of monomeric human beta-2-microglobulin reveals clues to its amyloidogenic properties. Trinh CH, Smith DP, Kalverda AP, Phillips SE, Radford SE. Proc Natl Acad Sci U S A 99 9771-9776 (2002)
- Designed protein tetramer zipped together with a hydrophobic Alzheimer homology: a structural clue to amyloid assembly. Otzen DE, Kristensen O, Oliveberg M. Proc Natl Acad Sci U S A 97 9907-9912 (2000)
- In vitro polymerization of a functional Escherichia coli amyloid protein. Wang X, Smith DR, Jones JW, Chapman MR. J Biol Chem 282 3713-3719 (2007)
- Metabolite-initiated protein misfolding may trigger Alzheimer's disease. Zhang Q, Powers ET, Nieva J, Huff ME, Dendle MA, Bieschke J, Glabe CG, Eschenmoser A, Wentworth P, Lerner RA, Kelly JW. Proc Natl Acad Sci U S A 101 4752-4757 (2004)
- Protein aggregation and protein instability govern familial amyotrophic lateral sclerosis patient survival. Wang Q, Johnson JL, Agar NY, Agar JN. PLoS Biol 6 e170 (2008)
- Prediction of "hot spots" of aggregation in disease-linked polypeptides. Sánchez de Groot N, Pallarés I, Avilés FX, Vendrell J, Ventura S. BMC Struct Biol 5 18 (2005)
- Beta(2)-microglobulin and its deamidated variant, N17D form amyloid fibrils with a range of morphologies in vitro. Kad NM, Thomson NH, Smith DP, Smith DA, Radford SE. J Mol Biol 313 559-571 (2001)
- Conformational conversion during amyloid formation at atomic resolution. Eichner T, Kalverda AP, Thompson GS, Homans SW, Radford SE. Mol Cell 41 161-172 (2011)
- Inhibition of insulin amyloid formation by small stress molecules. Arora A, Ha C, Park CB. FEBS Lett 564 121-125 (2004)
- Ultrastructural organization of amyloid fibrils by atomic force microscopy. Chamberlain AK, MacPhee CE, Zurdo J, Morozova-Roche LA, Hill HA, Dobson CM, Davis JJ. Biophys J 79 3282-3293 (2000)
- Hereditary systemic amyloidosis due to Asp76Asn variant β2-microglobulin. Valleix S, Gillmore JD, Bridoux F, Mangione PP, Dogan A, Nedelec B, Boimard M, Touchard G, Goujon JM, Lacombe C, Lozeron P, Adams D, Lacroix C, Maisonobe T, Planté-Bordeneuve V, Vrana JA, Theis JD, Giorgetti S, Porcari R, Ricagno S, Bolognesi M, Stoppini M, Delpech M, Pepys MB, Hawkins PN, Bellotti V. N Engl J Med 366 2276-2283 (2012)
- Aggregation kinetics of bovine serum albumin studied by FTIR spectroscopy and light scattering. Militello V, Casarino C, Emanuele A, Giostra A, Pullara F, Leone M. Biophys Chem 107 175-187 (2004)
- Is polyproline II helix the killer conformation? A Raman optical activity study of the amyloidogenic prefibrillar intermediate of human lysozyme. Blanch EW, Morozova-Roche LA, Cochran DA, Doig AJ, Hecht L, Barron LD. J Mol Biol 301 553-563 (2000)
- Protein subunit interactions and structural integrity of amyloidogenic transthyretins: evidence from electrospray mass spectrometry. Nettleton EJ, Sunde M, Lai Z, Kelly JW, Dobson CM, Robinson CV. J Mol Biol 281 553-564 (1998)
- Protein quality control acts on folding intermediates to shape the effects of mutations on organismal fitness. Bershtein S, Mu W, Serohijos AW, Zhou J, Shakhnovich EI. Mol Cell 49 133-144 (2013)
- Exploring amyloid formation by a de novo design. Kammerer RA, Kostrewa D, Zurdo J, Detken A, García-Echeverría C, Green JD, Müller SA, Meier BH, Winkler FK, Dobson CM, Steinmetz MO. Proc Natl Acad Sci U S A 101 4435-4440 (2004)
- Dissecting the stability of a beta-hairpin peptide that folds in water: NMR and molecular dynamics analysis of the beta-turn and beta-strand contributions to folding. Griffiths-Jones SR, Maynard AJ, Searle MS. J Mol Biol 292 1051-1069 (1999)
- Exploring protein aggregation and self-propagation using lattice models: phase diagram and kinetics. Dima RI, Thirumalai D. Protein Sci 11 1036-1049 (2002)
- Parallel beta-sheets and polar zippers in amyloid fibrils formed by residues 10-39 of the yeast prion protein Ure2p. Chan JC, Oyler NA, Yau WM, Tycko R. Biochemistry 44 10669-10680 (2005)
- Physicochemical consequences of amino acid variations that contribute to fibril formation by immunoglobulin light chains. Raffen R, Dieckman LJ, Szpunar M, Wunschl C, Pokkuluri PR, Dave P, Wilkins Stevens P, Cai X, Schiffer M, Stevens FJ. Protein Sci 8 509-517 (1999)
- The V122I cardiomyopathy variant of transthyretin increases the velocity of rate-limiting tetramer dissociation, resulting in accelerated amyloidosis. Jiang X, Buxbaum JN, Kelly JW. Proc Natl Acad Sci U S A 98 14943-14948 (2001)
- A systematic investigation into the effect of protein destabilisation on beta 2-microglobulin amyloid formation. Smith DP, Jones S, Serpell LC, Sunde M, Radford SE. J Mol Biol 330 943-954 (2003)
- Amyloid fibril formation by a partially structured intermediate state of alpha-chymotrypsin. Pallarès I, Vendrell J, Avilés FX, Ventura S. J Mol Biol 342 321-331 (2004)
- Amyloid protofilament formation of hen egg lysozyme in highly concentrated ethanol solution. Goda S, Takano K, Yamagata Y, Nagata R, Akutsu H, Maki S, Namba K, Yutani K. Protein Sci 9 369-375 (2000)
- How ionic liquids can help to stabilize native proteins. Weingärtner H, Cabrele C, Herrmann C. Phys Chem Chem Phys 14 415-426 (2012)
- Amyloid fibril formation can proceed from different conformations of a partially unfolded protein. Calamai M, Chiti F, Dobson CM. Biophys J 89 4201-4210 (2005)
- Lysozyme amyloidogenesis is accelerated by specific nicking and fragmentation but decelerated by intact protein binding and conversion. Mishra R, Sörgjerd K, Nyström S, Nordigården A, Yu YC, Hammarström P. J Mol Biol 366 1029-1044 (2007)
- Protein structural perturbation and aggregation on homogeneous surfaces. Sethuraman A, Belfort G. Biophys J 88 1322-1333 (2005)
- Protective hinge in insulin opens to enable its receptor engagement. Menting JG, Yang Y, Chan SJ, Phillips NB, Smith BJ, Whittaker J, Wickramasinghe NP, Whittaker LJ, Pandyarajan V, Wan ZL, Yadav SP, Carroll JM, Strokes N, Roberts CT, Ismail-Beigi F, Milewski W, Steiner DF, Chauhan VS, Ward CW, Weiss MA, Lawrence MC. Proc Natl Acad Sci U S A 111 E3395-404 (2014)
- Solution structure and dynamics of bovine beta-lactoglobulin A. Kuwata K, Hoshino M, Forge V, Era S, Batt CA, Goto Y. Protein Sci 8 2541-2545 (1999)
- Comparative Fourier transform infrared spectroscopy study of cold-, pressure-, and heat-induced unfolding and aggregation of myoglobin. Meersman F, Smeller L, Heremans K. Biophys J 82 2635-2644 (2002)
- Foldon, the natural trimerization domain of T4 fibritin, dissociates into a monomeric A-state form containing a stable beta-hairpin: atomic details of trimer dissociation and local beta-hairpin stability from residual dipolar couplings. Meier S, Güthe S, Kiefhaber T, Grzesiek S. J Mol Biol 344 1051-1069 (2004)
- Lower kinetic limit to protein thermal stability: a proposal regarding protein stability in vivo and its relation with misfolding diseases. Plaza del Pino IM, Ibarra-Molero B, Sanchez-Ruiz JM. Proteins 40 58-70 (2000)
- Pauling and Corey's alpha-pleated sheet structure may define the prefibrillar amyloidogenic intermediate in amyloid disease. Armen RS, DeMarco ML, Alonso DO, Daggett V. Proc Natl Acad Sci U S A 101 11622-11627 (2004)
- Identification of the core structure of lysozyme amyloid fibrils by proteolysis. Frare E, Mossuto MF, Polverino de Laureto P, Dumoulin M, Dobson CM, Fontana A. J Mol Biol 361 551-561 (2006)
- Convergent chemical synthesis and high-resolution x-ray structure of human lysozyme. Durek T, Torbeev VY, Kent SB. Proc Natl Acad Sci U S A 104 4846-4851 (2007)
- From coiled coils to small globular proteins: design of a native-like three-helix bundle. Bryson JW, Desjarlais JR, Handel TM, DeGrado WF. Protein Sci 7 1404-1414 (1998)
- Transmission of mouse senile amyloidosis. Xing Y, Nakamura A, Chiba T, Kogishi K, Matsushita T, Li F, Guo Z, Hosokawa M, Mori M, Higuchi K. Lab Invest 81 493-499 (2001)
- Protein engineering as a strategy to avoid formation of amyloid fibrils. Villegas V, Zurdo J, Filimonov VV, Avilés FX, Dobson CM, Serrano L. Protein Sci 9 1700-1708 (2000)
- Modulation of S6 fibrillation by unfolding rates and gatekeeper residues. Pedersen JS, Christensen G, Otzen DE. J Mol Biol 341 575-588 (2004)
- Amyloid protofilaments from the calcium-binding protein equine lysozyme: formation of ring and linear structures depends on pH and metal ion concentration. Malisauskas M, Zamotin V, Jass J, Noppe W, Dobson CM, Morozova-Roche LA. J Mol Biol 330 879-890 (2003)
- Hereditary renal amyloidosis caused by a new variant lysozyme W64R in a French family. Valleix S, Drunat S, Philit JB, Adoue D, Piette JC, Droz D, MacGregor B, Canet D, Delpech M, Grateau G. Kidney Int 61 907-912 (2002)
- Lipids as cofactors in protein folding: stereo-specific lipid-protein interactions are required to form HAMLET (human alpha-lactalbumin made lethal to tumor cells). Svensson M, Mossberg AK, Pettersson J, Linse S, Svanborg C. Protein Sci 12 2805-2814 (2003)
- Amyloid fibril formation by pulmonary surfactant protein C. Gustafsson M, Thyberg J, Näslund J, Eliasson E, Johansson J. FEBS Lett 464 138-142 (1999)
- Evaluating the binding selectivity of transthyretin amyloid fibril inhibitors in blood plasma. Purkey HE, Dorrell MI, Kelly JW. Proc Natl Acad Sci U S A 98 5566-5571 (2001)
- Reduced global cooperativity is a common feature underlying the amyloidogenicity of pathogenic lysozyme mutations. Dumoulin M, Canet D, Last AM, Pardon E, Archer DB, Muyldermans S, Wyns L, Matagne A, Robinson CV, Redfield C, Dobson CM. J Mol Biol 346 773-788 (2005)
- A simple algorithm locates beta-strands in the amyloid fibril core of alpha-synuclein, Abeta, and tau using the amino acid sequence alone. Zibaee S, Makin OS, Goedert M, Serpell LC. Protein Sci 16 906-918 (2007)
- Interdomain side-chain interactions in human gammaD crystallin influencing folding and stability. Flaugh SL, Kosinski-Collins MS, King J. Protein Sci 14 2030-2043 (2005)
- DNA-induced partial unfolding of prion protein leads to its polymerisation to amyloid. Nandi PK, Leclerc E, Nicole JC, Takahashi M. J Mol Biol 322 153-161 (2002)
- Amyloid protofibrils of lysozyme nucleate and grow via oligomer fusion. Hill SE, Robinson J, Matthews G, Muschol M. Biophys J 96 3781-3790 (2009)
- Contributions of hydrophobic domain interface interactions to the folding and stability of human gammaD-crystallin. Flaugh SL, Kosinski-Collins MS, King J. Protein Sci 14 569-581 (2005)
- alpha-->beta transition of beta-lactoglobulin as evidenced by heteronuclear NMR. Kuwata K, Hoshino M, Era S, Batt CA, Goto Y. J Mol Biol 283 731-739 (1998)
- Characterization of bioactive recombinant human lysozyme expressed in milk of cloned transgenic cattle. Yang B, Wang J, Tang B, Liu Y, Guo C, Yang P, Yu T, Li R, Zhao J, Zhang L, Dai Y, Li N. PLoS One 6 e17593 (2011)
- Conformational characterization of oligomeric intermediates and aggregates in beta-lactoglobulin heat aggregation. Carrotta R, Bauer R, Waninge R, Rischel C. Protein Sci 10 1312-1318 (2001)
- Ectoine and hydroxyectoine inhibit aggregation and neurotoxicity of Alzheimer's beta-amyloid. Kanapathipillai M, Lentzen G, Sierks M, Park CB. FEBS Lett 579 4775-4780 (2005)
- Rapid acquisition of beta-sheet structure in the prion protein prior to multimer formation. Post K, Pitschke M, Schäfer O, Wille H, Appel TR, Kirsch D, Mehlhorn I, Serban H, Prusiner SB, Riesner D. Biol Chem 379 1307-1317 (1998)
- A novel lysozyme mutation Phe57Ile associated with hereditary renal amyloidosis. Yazaki M, Farrell SA, Benson MD. Kidney Int 63 1652-1657 (2003)
- Amyloid fibrils formation and amorphous aggregation in concanavalin A. Vetri V, Canale C, Relini A, Librizzi F, Militello V, Gliozzi A, Leone M. Biophys Chem 125 184-190 (2007)
- Hereditary amyloid cardiomyopathy caused by a variant apolipoprotein A1. Hamidi Asl L, Liepnieks JJ, Hamidi Asl K, Uemichi T, Moulin G, Desjoyaux E, Loire R, Delpech M, Grateau G, Benson MD. Am J Pathol 154 221-227 (1999)
- Structure, folding dynamics, and amyloidogenesis of D76N β2-microglobulin: roles of shear flow, hydrophobic surfaces, and α-crystallin. Mangione PP, Esposito G, Relini A, Raimondi S, Porcari R, Giorgetti S, Corazza A, Fogolari F, Penco A, Goto Y, Lee YH, Yagi H, Cecconi C, Naqvi MM, Gillmore JD, Hawkins PN, Chiti F, Rolandi R, Taylor GW, Pepys MB, Stoppini M, Bellotti V. J Biol Chem 288 30917-30930 (2013)
- Thermodynamics of model prions and its implications for the problem of prion protein folding. Harrison PM, Chan HS, Prusiner SB, Cohen FE. J Mol Biol 286 593-606 (1999)
- Cystatin forms a tetramer through structural rearrangement of domain-swapped dimers prior to amyloidogenesis. Sanders A, Jeremy Craven C, Higgins LD, Giannini S, Conroy MJ, Hounslow AM, Waltho JP, Staniforth RA. J Mol Biol 336 165-178 (2004)
- Guidelines on the diagnosis and investigation of AL amyloidosis. Gillmore JD, Wechalekar A, Bird J, Cavenagh J, Hawkins S, Kazmi M, Lachmann HJ, Hawkins PN, Pratt G, BCSH Committee. Br J Haematol 168 207-218 (2015)
- Monitoring the process of HypF fibrillization and liposome permeabilization by protofibrils. Relini A, Torrassa S, Rolandi R, Gliozzi A, Rosano C, Canale C, Bolognesi M, Plakoutsi G, Bucciantini M, Chiti F, Stefani M. J Mol Biol 338 943-957 (2004)
- Reversal of protein aggregation provides evidence for multiple aggregated States. Calamai M, Canale C, Relini A, Stefani M, Chiti F, Dobson CM. J Mol Biol 346 603-616 (2005)
- Structural diversity of ex vivo amyloid fibrils studied by cryo-electron microscopy. Jiménez JL, Tennent G, Pepys M, Saibil HR. J Mol Biol 311 241-247 (2001)
- Heat-induced conversion of beta(2)-microglobulin and hen egg-white lysozyme into amyloid fibrils. Sasahara K, Yagi H, Naiki H, Goto Y. J Mol Biol 372 981-991 (2007)
- Investigating the effects of mutations on protein aggregation in the cell. Calloni G, Zoffoli S, Stefani M, Dobson CM, Chiti F. J Biol Chem 280 10607-10613 (2005)
- Stimulation of insulin fibrillation by urea-induced intermediates. Ahmad A, Millett IS, Doniach S, Uversky VN, Fink AL. J Biol Chem 279 14999-15013 (2004)
- The controlling roles of Trp60 and Trp95 in beta2-microglobulin function, folding and amyloid aggregation properties. Esposito G, Ricagno S, Corazza A, Rennella E, Gümral D, Mimmi MC, Betto E, Pucillo CE, Fogolari F, Viglino P, Raimondi S, Giorgetti S, Bolognesi B, Merlini G, Stoppini M, Bolognesi M, Bellotti V. J Mol Biol 378 887-897 (2008)
- Contribution of individual residues to formation of the native-like tertiary topology in the alpha-lactalbumin molten globule. Song J, Bai P, Luo L, Peng ZY. J Mol Biol 280 167-174 (1998)
- Two-component dendritic gel: effect of stereochemistry on the supramolecular chiral assembly. Hirst AR, Smith DK, Feiters MC, Geurts HP. Chemistry 10 5901-5910 (2004)
- Soluble oligomers from a non-disease related protein mimic Abeta-induced tau hyperphosphorylation and neurodegeneration. Vieira MN, Forny-Germano L, Saraiva LM, Sebollela A, Martinez AM, Houzel JC, De Felice FG, Ferreira ST. J Neurochem 103 736-748 (2007)
- Amyloid-like aggregates of a plant protein: a case of a sweet-tasting protein, monellin. Konno T, Murata K, Nagayama K. FEBS Lett 454 122-126 (1999)
- News Cell biology. The importance of being unfolded. Plaxco KW, Gross M. Nature 386 657, 659 (1997)
- Formation of amyloid fibrils in vitro by human gammaD-crystallin and its isolated domains. Papanikolopoulou K, Mills-Henry I, Thol SL, Wang Y, Gross AA, Kirschner DA, Decatur SM, King J. Mol Vis 14 81-89 (2008)
- Is folding of beta-lactoglobulin non-hierarchic? Intermediate with native-like beta-sheet and non-native alpha-helix. Forge V, Hoshino M, Kuwata K, Arai M, Kuwajima K, Batt CA, Goto Y. J Mol Biol 296 1039-1051 (2000)
- The extracellular chaperone clusterin potently inhibits human lysozyme amyloid formation by interacting with prefibrillar species. Kumita JR, Poon S, Caddy GL, Hagan CL, Dumoulin M, Yerbury JJ, Stewart EM, Robinson CV, Wilson MR, Dobson CM. J Mol Biol 369 157-167 (2007)
- Conformational propagation with prion-like characteristics in a simple model of protein folding. Harrison PM, Chan HS, Prusiner SB, Cohen FE. Protein Sci 10 819-835 (2001)
- Elucidation of the molecular mechanism during the early events in immunoglobulin light chain amyloid fibrillation. Evidence for an off-pathway oligomer at acidic pH. Souillac PO, Uversky VN, Millett IS, Khurana R, Doniach S, Fink AL. J Biol Chem 277 12666-12679 (2002)
- Amylin deposition in the kidney of patients with diabetic nephropathy. Gong W, Liu ZH, Zeng CH, Peng A, Chen HP, Zhou H, Li LS. Kidney Int 72 213-218 (2007)
- Beta-hairpin conformation of fibrillogenic peptides: structure and alpha-beta transition mechanism revealed by molecular dynamics simulations. Daidone I, Simona F, Roccatano D, Broglia RA, Tiana G, Colombo G, Di Nola A. Proteins 57 198-204 (2004)
- Role of the single disulphide bond of beta(2)-microglobulin in amyloidosis in vitro. Smith DP, Radford SE. Protein Sci 10 1775-1784 (2001)
- The non-core regions of human lysozyme amyloid fibrils influence cytotoxicity. Mossuto MF, Dhulesia A, Devlin G, Frare E, Kumita JR, de Laureto PP, Dumoulin M, Fontana A, Dobson CM, Salvatella X. J Mol Biol 402 783-796 (2010)
- Amyloid formation from HypF-N under conditions in which the protein is initially in its native state. Marcon G, Plakoutsi G, Canale C, Relini A, Taddei N, Dobson CM, Ramponi G, Chiti F. J Mol Biol 347 323-335 (2005)
- Induction of peptide bond dipoles drives cooperative helix formation in the (AAQAA)3 peptide. Huang J, MacKerell AD. Biophys J 107 991-997 (2014)
- Spontaneous fibril formation by polyalanines; discontinuous molecular dynamics simulations. Nguyen HD, Hall CK. J Am Chem Soc 128 1890-1901 (2006)
- Protein unfolding at interfaces: slow dynamics of alpha-helix to beta-sheet transition. Sethuraman A, Vedantham G, Imoto T, Przybycien T, Belfort G. Proteins 56 669-678 (2004)
- Amyloid toxicity is independent of polypeptide sequence, length and chirality. Pastor MT, Kümmerer N, Schubert V, Esteras-Chopo A, Dotti CG, López de la Paz M, Serrano L. J Mol Biol 375 695-707 (2008)
- Deuterium-proton exchange on the native wild-type transthyretin tetramer identifies the stable core of the individual subunits and indicates mobility at the subunit interface. Liu K, Cho HS, Hoyt DW, Nguyen TN, Olds P, Kelly JW, Wemmer DE. J Mol Biol 303 555-565 (2000)
- Fibrillogenesis and cytotoxic activity of the amyloid-forming apomyoglobin mutant W7FW14F. Sirangelo I, Malmo C, Iannuzzi C, Mezzogiorno A, Bianco MR, Papa M, Irace G. J Biol Chem 279 13183-13189 (2004)
- Spatial extent of charge repulsion regulates assembly pathways for lysozyme amyloid fibrils. Hill SE, Miti T, Richmond T, Muschol M. PLoS One 6 e18171 (2011)
- Characterization of oligomeric species on the aggregation pathway of human lysozyme. Frare E, Mossuto MF, de Laureto PP, Tolin S, Menzer L, Dumoulin M, Dobson CM, Fontana A. J Mol Biol 387 17-27 (2009)
- Deep-UV Raman spectrometer tunable between 193 and 205 nm for structural characterization of proteins. Lednev IK, Ermolenkov VV, He W, Xu M. Anal Bioanal Chem 381 431-437 (2005)
- Early intermediate in human prion protein folding as evidenced by ultrarapid mixing experiments. Apetri AC, Maki K, Roder H, Surewicz WK. J Am Chem Soc 128 11673-11678 (2006)
- Chemical dissection and reassembly of amyloid fibrils formed by a peptide fragment of transthyretin. MacPhee CE, Dobson CM. J Mol Biol 297 1203-1215 (2000)
- Partial molar volume, surface area, and hydration changes for equilibrium unfolding and formation of aggregation transition state: high-pressure and cosolute studies on recombinant human IFN-gamma. Webb JN, Webb SD, Cleland JL, Carpenter JF, Randolph TW. Proc Natl Acad Sci U S A 98 7259-7264 (2001)
- Pressure-dissociable reversible assembly of intrinsically denatured lysozyme is a precursor for amyloid fibrils. Niraula TN, Konno T, Li H, Yamada H, Akasaka K, Tachibana H. Proc Natl Acad Sci U S A 101 4089-4093 (2004)
- Quantification of transthyretin kinetic stability in human plasma using subunit exchange. Rappley I, Monteiro C, Novais M, Baranczak A, Solis G, Wiseman RL, Helmke S, Maurer MS, Coelho T, Powers ET, Kelly JW. Biochemistry 53 1993-2006 (2014)
- Side-chain conformations in an unfolded protein: chi1 distributions in denatured hen lysozyme determined by heteronuclear 13C, 15N NMR spectroscopy. Hennig M, Bermel W, Spencer A, Dobson CM, Smith LJ, Schwalbe H. J Mol Biol 288 705-723 (1999)
- Avian amyloidosis. Landman WJ, Gruys E, Gielkens AL. Avian Pathol 27 437-449 (1998)
- Formation of amyloid fibrils by peptides derived from the bacterial cold shock protein CspB. Gross M, Wilkins DK, Pitkeathly MC, Chung EW, Higham C, Clark A, Dobson CM. Protein Sci 8 1350-1357 (1999)
- Glycine residues appear to be evolutionarily conserved for their ability to inhibit aggregation. Parrini C, Taddei N, Ramazzotti M, Degl'Innocenti D, Ramponi G, Dobson CM, Chiti F. Structure 13 1143-1151 (2005)
- Population of nonnative states of lysozyme variants drives amyloid fibril formation. Buell AK, Dhulesia A, Mossuto MF, Cremades N, Kumita JR, Dumoulin M, Welland ME, Knowles TPJ, Salvatella X, Dobson CM. J Am Chem Soc 133 7737-7743 (2011)
- Proteins with H-bond packing defects are highly interactive with lipid bilayers: Implications for amyloidogenesis. Fernández A, Berry RS. Proc Natl Acad Sci U S A 100 2391-2396 (2003)
- Kinetic analysis of amyloid formation in the presence of heparan sulfate: faster unfolding and change of pathway. Motamedi-Shad N, Monsellier E, Torrassa S, Relini A, Chiti F. J Biol Chem 284 29921-29934 (2009)
- Hydration structure of human lysozyme investigated by molecular dynamics simulation and cryogenic X-ray crystal structure analyses: on the correlation between crystal water sites, solvent density, and solvent dipole. Higo J, Nakasako M. J Comput Chem 23 1323-1336 (2002)
- Separating instability from aggregation propensity in γS-crystallin variants. Brubaker WD, Freites JA, Golchert KJ, Shapiro RA, Morikis V, Tobias DJ, Martin RW. Biophys J 100 498-506 (2011)
- Protein folding and misfolding: a paradigm of self-assembly and regulation in complex biological systems. Vendruscolo M, Zurdo J, MacPhee CE, Dobson CM. Philos Trans A Math Phys Eng Sci 361 1205-1222 (2003)
- Structural defects and the diagnosis of amyloidogenic propensity. Fernández A, Kardos J, Scott LR, Goto Y, Berry RS. Proc Natl Acad Sci U S A 100 6446-6451 (2003)
- An ultrastructural study of amyloid intermediates in A beta1-42 fibrillogenesis. Nybo M, Svehag SE, Holm Nielsen E. Scand J Immunol 49 219-223 (1999)
- The in vivo and in vitro aggregation properties of globular proteins correlate with their conformational stability: the SH3 case. Espargaró A, Castillo V, de Groot NS, Ventura S. J Mol Biol 378 1116-1131 (2008)
- An Insight into the pathway of the amyloid fibril formation of hen egg white lysozyme obtained from a small-angle X-ray and neutron scattering study. Yonezawa Y, Tanaka S, Kubota T, Wakabayashi K, Yutani K, Fujiwara S. J Mol Biol 323 237-251 (2002)
- Local cooperativity in an amyloidogenic state of human lysozyme observed at atomic resolution. Dhulesia A, Cremades N, Kumita JR, Hsu ST, Mossuto MF, Dumoulin M, Nietlispach D, Akke M, Salvatella X, Dobson CM. J Am Chem Soc 132 15580-15588 (2010)
- The component polypeptide chains of bovine insulin nucleate or inhibit aggregation of the parent protein in a conformation-dependent manner. Devlin GL, Knowles TP, Squires A, McCammon MG, Gras SL, Nilsson MR, Robinson CV, Dobson CM, MacPhee CE. J Mol Biol 360 497-509 (2006)
- A single disulfide bond differentiates aggregation pathways of beta2-microglobulin. Chen Y, Dokholyan NV. J Mol Biol 354 473-482 (2005)
- Amyloid aggregates of the prion peptide PrP106-126 are destabilised by oxidation and by the action of dendrimers. Heegaard PM, Pedersen HG, Flink J, Boas U. FEBS Lett 577 127-133 (2004)
- Does equilibrium polymerization describe the dynamic heterogeneity of glass-forming liquids? Douglas JF, Dudowicz J, Freed KF. J Chem Phys 125 144907 (2006)
- Trapping of palindromic ligands within native transthyretin prevents amyloid formation. Kolstoe SE, Mangione PP, Bellotti V, Taylor GW, Tennent GA, Deroo S, Morrison AJ, Cobb AJ, Coyne A, McCammon MG, Warner TD, Mitchell J, Gill R, Smith MD, Ley SV, Robinson CV, Wood SP, Pepys MB. Proc Natl Acad Sci U S A 107 20483-20488 (2010)
- Apolipoprotein A-I induced amyloidosis. Genschel J, Haas R, Pröpsting MJ, Schmidt HH. FEBS Lett 430 145-149 (1998)
- Unfolding a folding disease: folding, misfolding and aggregation of the marble brain syndrome-associated mutant H107Y of human carbonic anhydrase II. Almstedt K, Lundqvist M, Carlsson J, Karlsson M, Persson B, Jonsson BH, Carlsson U, Hammarström P. J Mol Biol 342 619-633 (2004)
- Disulfide bonds reduce the toxicity of the amyloid fibrils formed by an extracellular protein. Mossuto MF, Bolognesi B, Guixer B, Dhulesia A, Agostini F, Kumita JR, Tartaglia GG, Dumoulin M, Dobson CM, Salvatella X. Angew Chem Int Ed Engl 50 7048-7051 (2011)
- Early kinetics of amyloid fibril formation reveals conformational reorganisation of initial aggregates. Cerdà-Costa N, Esteras-Chopo A, Avilés FX, Serrano L, Villegas V. J Mol Biol 366 1351-1363 (2007)
- Equilibria and kinetics of folding of gelsolin domain 2 and mutants involved in familial amyloidosis-Finnish type. Isaacson RL, Weeds AG, Fersht AR. Proc Natl Acad Sci U S A 96 11247-11252 (1999)
- Flexibility of the murine prion protein and its Asp178Asn mutant investigated by molecular dynamics simulations. Gsponer J, Ferrara P, Caflisch A. J Mol Graph Model 20 169-182 (2001)
- Human phenotypically distinct TGFBI corneal dystrophies are linked to the stability of the fourth FAS1 domain of TGFBIp. Runager K, Basaiawmoit RV, Deva T, Andreasen M, Valnickova Z, Sørensen CS, Karring H, Thøgersen IB, Christiansen G, Underhaug J, Kristensen T, Nielsen NC, Klintworth GK, Otzen DE, Enghild JJ. J Biol Chem 286 4951-4958 (2011)
- Protonation favors aggregation of lysozyme with SDS. Khan JM, Chaturvedi SK, Rahman SK, Ishtikhar M, Qadeer A, Ahmad E, Khan RH. Soft Matter 10 2591-2599 (2014)
- Structure of amyloid beta fragments in aqueous environments. Takano K, Endo S, Mukaiyama A, Chon H, Matsumura H, Koga Y, Kanaya S. FEBS J 273 150-158 (2006)
- Assemblies of Alzheimer's peptides A beta 25-35 and A beta 31-35: reverse-turn conformation and side-chain interactions revealed by X-ray diffraction. Bond JP, Deverin SP, Inouye H, el-Agnaf OM, Teeter MM, Kirschner DA. J Struct Biol 141 156-170 (2003)
- Assembly and kinetic folding pathways of a tetrameric beta-sheet complex: molecular dynamics simulations on simplified off-lattice protein models. Jang H, Hall CK, Zhou Y. Biophys J 86 31-49 (2004)
- Cataract-causing defect of a mutant γ-crystallin proceeds through an aggregation pathway which bypasses recognition by the α-crystallin chaperone. Moreau KL, King JA. PLoS One 7 e37256 (2012)
- Chain-length dependence of alpha-helix to beta-sheet transition in polylysine: model of protein aggregation studied by temperature-tuned FTIR spectroscopy. Dzwolak W, Muraki T, Kato M, Taniguchi Y. Biopolymers 73 463-469 (2004)
- Engineering conformational destabilization into mouse apolipoprotein E. A model for a unique property of human apolipoprotein E4. Hatters DM, Peters-Libeu CA, Weisgraber KH. J Biol Chem 280 26477-26482 (2005)
- Kinetic properties of ASC protein aggregation in epithelial cells. Cheng J, Waite AL, Tkaczyk ER, Ke K, Richards N, Hunt AJ, Gumucio DL. J Cell Physiol 222 738-747 (2010)
- Molecular chaperone properties of serum amyloid P component. Coker AR, Purvis A, Baker D, Pepys MB, Wood SP. FEBS Lett 473 199-202 (2000)
- Amyloid fibrils derived from the apolipoprotein A1 Leu174Ser variant contain elements of ordered helical structure. Mangione P, Sunde M, Giorgetti S, Stoppini M, Esposito G, Gianelli L, Obici L, Asti L, Andreola A, Viglino P, Merlini G, Bellotti V. Protein Sci 10 187-199 (2001)
- Comment Amyloid fibrils. Mutations make enzyme polymerize. Perutz MF. Nature 385 773, 775 (1997)
- Response of native and denatured hen lysozyme to high pressure studied by (15)N/(1)H NMR spectroscopy. Kamatari YO, Yamada H, Akasaka K, Jones JA, Dobson CM, Smith LJ. Eur J Biochem 268 1782-1793 (2001)
- Structural changes in amelogenin upon self-assembly and mineral interactions. Beniash E, Simmer JP, Margolis HC. J Dent Res 91 967-972 (2012)
- Urea modulation of beta-amyloid fibril growth: experimental studies and kinetic models. Kim JR, Muresan A, Lee KY, Murphy RM. Protein Sci 13 2888-2898 (2004)
- Alpha-to-beta structural transformation of ovalbumin: heat and pH effects. Hu HY, Du HN. J Protein Chem 19 177-183 (2000)
- Impact of the native-state stability of human lysozyme variants on protein secretion by Pichia pastoris. Kumita JR, Johnson RJ, Alcocer MJ, Dumoulin M, Holmqvist F, McCammon MG, Robinson CV, Archer DB, Dobson CM. FEBS J 273 711-720 (2006)
- Inhibition of amyloid fiber assembly by both BiP and its target peptide. Davis PD, Raffen R, Dul LJ, Vogen MS, Williamson KE, Stevens JF, Argon Y. Immunity 13 433-442 (2000)
- A polar, solvent-exposed residue can be essential for native protein structure. Hill RB, DeGrado WF. Structure 8 471-479 (2000)
- An NMR investigation of solution aggregation reactions preceding the misassembly of acid-denatured cold shock protein A into fibrils. Alexandrescu AT, Rathgeb-Szabo K. J Mol Biol 291 1191-1206 (1999)
- Conformational flexibility and polymerization of vesicular stomatitis virus matrix protein. Gaudin Y, Sturgis J, Doumith M, Barge A, Robert B, Ruigrok RW. J Mol Biol 274 816-825 (1997)
- Decreased thermodynamic stability as a crucial factor for familial amyloidotic polyneuropathy. Niraula TN, Haraoka K, Ando Y, Li H, Yamada H, Akasaka K. J Mol Biol 320 333-342 (2002)
- Dissecting the hydrogen exchange properties of insulin under amyloid fibril forming conditions: a site-specific investigation by mass spectrometry. Tito P, Nettleton EJ, Robinson CV. J Mol Biol 303 267-278 (2000)
- Importance of metastable states in the free energy landscapes of polypeptide chains. Auer S, Miller MA, Krivov SV, Dobson CM, Karplus M, Vendruscolo M. Phys Rev Lett 99 178104 (2007)
- Conformational changes of lysozyme refolding intermediates and implications for aggregation and renaturation. Gu Z, Zhu X, Ni S, Su Z, Zhou HM. Int J Biochem Cell Biol 36 795-805 (2004)
- HDX-ESI-MS reveals enhanced conformational dynamics of the amyloidogenic protein beta(2)-microglobulin upon release from the MHC-1. Hodkinson JP, Jahn TR, Radford SE, Ashcroft AE. J Am Soc Mass Spectrom 20 278-286 (2009)
- In vitro amyloid fibril formation by synthetic peptides corresponding to the amino terminus of apoSAA isoforms from amyloid-susceptible and amyloid-resistant mice. Kirschner DA, Elliott-Bryant R, Szumowski KE, Gonnerman WA, Kindy MS, Sipe JD, Cathcart ES. J Struct Biol 124 88-98 (1998)
- Native state hydrogen exchange study of suppressor and pathogenic variants of transthyretin. Liu K, Kelly JW, Wemmer DE. J Mol Biol 320 821-832 (2002)
- Oxidation enhances human serum albumin thermal stability and changes the routes of amyloid fibril formation. Sancataldo G, Vetri V, Foderà V, Di Cara G, Militello V, Leone M. PLoS One 9 e84552 (2014)
- Rationalising lysozyme amyloidosis: insights from the structure and solution dynamics of T70N lysozyme. Johnson RJ, Christodoulou J, Dumoulin M, Caddy GL, Alcocer MJ, Murtagh GJ, Kumita JR, Larsson G, Robinson CV, Archer DB, Luisi B, Dobson CM. J Mol Biol 352 823-836 (2005)
- The natural osmolyte trimethylamine N-oxide (TMAO) restores the ability of mutant tau to promote microtubule assembly. Smith MJ, Crowther RA, Goedert M. FEBS Lett 484 265-270 (2000)
- The palmitoyl groups of lung surfactant protein C reduce unfolding into a fibrillogenic intermediate. Gustafsson M, Griffiths WJ, Furusjö E, Johansson J. J Mol Biol 310 937-950 (2001)
- The use of native cation-exchange chromatography to study aggregation and phase separation of monoclonal antibodies. Chen S, Lau H, Brodsky Y, Kleemann GR, Latypov RF. Protein Sci 19 1191-1204 (2010)
- Detection of altered protein conformations in living cells. Raquet X, Eckert JH, Müller S, Johnsson N. J Mol Biol 305 927-938 (2001)
- Distinct properties of wild-type and the amyloidogenic human cystatin C variant of hereditary cerebral hemorrhage with amyloidosis, Icelandic type. Calero M, Pawlik M, Soto C, Castaño EM, Sigurdsson EM, Kumar A, Gallo G, Frangione B, Levy E. J Neurochem 77 628-637 (2001)
- Effects of dithiothreitol on the amyloid fibrillogenesis of hen egg-white lysozyme. Wang SS, Liu KN, Wang BW. Eur Biophys J 39 1229-1242 (2010)
- Hen egg white lysozyme fibrillation: a deep-UV resonance Raman spectroscopic study. Xu M, Ermolenkov VV, Uversky VN, Lednev IK. J Biophotonics 1 215-229 (2008)
- Hydrogen/deuterium exchange mass spectrometry identifies two highly protected regions in recombinant full-length prion protein amyloid fibrils. Nazabal A, Hornemann S, Aguzzi A, Zenobi R. J Mass Spectrom 44 965-977 (2009)
- Surfactant-induced conformational transition of amyloid beta-peptide. Sureshbabu N, Kirubagaran R, Jayakumar R. Eur Biophys J 38 355-367 (2009)
- The effect of concentration, temperature and stirring on hen egg white lysozyme amyloid formation. Ow SY, Dunstan DE. Soft Matter 9 9692-9701 (2013)
- Acridine derivatives inhibit lysozyme aggregation. Gazova Z, Bellova A, Daxnerova Z, Imrich J, Kristian P, Tomascikova J, Bagelova J, Fedunova D, Antalik M. Eur Biophys J 37 1261-1270 (2008)
- De novo design of a two-stranded coiled-coil switch peptide. Kammerer RA, Steinmetz MO. J Struct Biol 155 146-153 (2006)
- Folding and stability of the three-stranded beta-sheet peptide Betanova: insights from molecular dynamics simulations. Colombo G, Roccatano D, Mark AE. Proteins 46 380-392 (2002)
- Laminin affects polymerization, depolymerization and neurotoxicity of Abeta peptide. Morgan C, Bugueño MP, Garrido J, Inestrosa NC. Peptides 23 1229-1240 (2002)
- Novel down-regulatory mechanism of the surface expression of the vasopressin V2 receptor by an alternative splice receptor variant. Sarmiento JM, Añazco CC, Campos DM, Prado GN, Navarro J, González CB. J Biol Chem 279 47017-47023 (2004)
- The mechanism of enhanced insulin amyloid fibril formation by NaCl is better explained by a conformational change model. Muzaffar M, Ahmad A. PLoS One 6 e27906 (2011)
- Tissue distribution, biochemical properties, and transmission of mouse type A AApoAII amyloid fibrils. Korenaga T, Fu X, Xing Y, Matsusita T, Kuramoto K, Syumiya S, Hasegawa K, Naiki H, Ueno M, Ishihara T, Hosokawa M, Mori M, Higuchi K. Am J Pathol 164 1597-1606 (2004)
- Bioactivity determination of native and variant forms of therapeutic interferons. Larocque L, Bliu A, Xu R, Diress A, Wang J, Lin R, He R, Girard M, Li X. J Biomed Biotechnol 2011 174615 (2011)
- Characterization of the structure and dynamics of amyloidogenic variants of human lysozyme by NMR spectroscopy. Chamberlain AK, Receveur V, Spencer A, Redfield C, Dobson CM. Protein Sci 10 2525-2530 (2001)
- Formation of amyloid fibers by monomeric light chain variable domains. Brumshtein B, Esswein SR, Landau M, Ryan CM, Whitelegge JP, Phillips ML, Cascio D, Sawaya MR, Eisenberg DS. J Biol Chem 289 27513-27525 (2014)
- Lysozyme fibrillation: deep UV Raman spectroscopic characterization of protein structural transformation. Xu M, Ermolenkov VV, He W, Uversky VN, Fredriksen L, Lednev IK. Biopolymers 79 58-61 (2005)
- Oleic acid inhibits amyloid formation of the intermediate of alpha-lactalbumin at moderately acidic pH. Yang F, Zhang M, Zhou BR, Chen J, Liang Y. J Mol Biol 362 821-834 (2006)
- On the role of aggregation prone regions in protein evolution, stability, and enzymatic catalysis: insights from diverse analyses. Buck PM, Kumar S, Singh SK. PLoS Comput Biol 9 e1003291 (2013)
- Simulations of human lysozyme: probing the conformations triggering amyloidosis. Moraitakis G, Goodfellow JM. Biophys J 84 2149-2158 (2003)
- A near-native state on the slow refolding pathway of hen lysozyme. Kulkarni SK, Ashcroft AE, Carey M, Masselos D, Robinson CV, Radford SE. Protein Sci 8 35-44 (1999)
- Evidence for water-tuned structural differences in proteins: an approach emphasizing variations in local hydrophilicity. Akdogan Y, Reichenwallner J, Hinderberger D. PLoS One 7 e45681 (2012)
- Folding of phage P22 coat protein monomers: kinetic and thermodynamic properties. Anderson E, Teschke CM. Virology 313 184-197 (2003)
- Mechanism of protein kinetic stabilization by engineered disulfide crosslinks. Sanchez-Romero I, Ariza A, Wilson KS, Skjøt M, Vind J, De Maria L, Skov LK, Sanchez-Ruiz JM. PLoS One 8 e70013 (2013)
- Unfolding of hen egg lysozyme by molecular dynamics simulations at 300K: insight into the role of the interdomain interface. Gilquin B, Guilbert C, Perahia D. Proteins 41 58-74 (2000)
- beta2-microglobulin H31Y variant 3D structure highlights the protein natural propensity towards intermolecular aggregation. Rosano C, Zuccotti S, Mangione P, Giorgetti S, Bellotti V, Pettirossi F, Corazza A, Viglino P, Esposito G, Bolognesi M. J Mol Biol 335 1051-1064 (2004)
- Amyloidosis in transgenic mice expressing murine amyloidogenic apolipoprotein A-II (Apoa2c). Ge F, Yao J, Fu X, Guo Z, Yan J, Zhang B, Zhang H, Tomozawa H, Miyazaki J, Sawashita J, Mori M, Higuchi K. Lab Invest 87 633-643 (2007)
- Changes in Lysozyme Flexibility upon Mutation Are Frequent, Large and Long-Ranged. Verma D, Jacobs DJ, Livesay DR. PLoS Comput Biol 8 e1002409 (2012)
- Cooperative alpha-helix formation of beta-lactoglobulin induced by sodium n-alkyl sulfates. Chamani J, Moosavi-Movahedi AA, Rajabi O, Gharanfoli M, Momen-Heravi M, Hakimelahi GH, Neamati-Baghsiah A, Varasteh AR. J Colloid Interface Sci 293 52-60 (2006)
- Echinacoside inhibits amyloid fibrillization of HEWL and protects against Aβ-induced neurotoxicity. Zhang D, Li H, Wang JB. Int J Biol Macromol 72 243-253 (2015)
- Fibers of tau fragments, but not full length tau, exhibit a cross beta-structure: implications for the formation of paired helical filaments. Giannetti AM, Lindwall G, Chau MF, Radeke MJ, Feinstein SC, Kohlstaedt LA. Protein Sci 9 2427-2435 (2000)
- Glutamate counteracts the denaturing effect of urea through its effect on the denatured state. Mandal AK, Samaddar S, Banerjee R, Lahiri S, Bhattacharyya A, Roy S. J Biol Chem 278 36077-36084 (2003)
- Mechanistic insight of photo-induced aggregation of chicken egg white lysozyme: the interplay between hydrophobic interactions and formation of intermolecular disulfide bonds. Xie J, Qin M, Cao Y, Wang W. Proteins 79 2505-2516 (2011)
- Optimization of hydrophobic domains in peptides that undergo transformation from alpha-helix to beta-fibril. Takahashi Y, Ueno A, Mihara H. Bioorg Med Chem 7 177-185 (1999)
- Pathway for unfolding of ubiquitin in sodium dodecyl sulfate, studied by capillary electrophoresis. Schneider GF, Shaw BF, Lee A, Carillho E, Whitesides GM. J Am Chem Soc 130 17384-17393 (2008)
- Structure of haze forming proteins in white wines: Vitis vinifera thaumatin-like proteins. Marangon M, Van Sluyter SC, Waters EJ, Menz RI. PLoS One 9 e113757 (2014)
- The glutamine-rich domain of the Drosophila GAGA factor is necessary for amyloid fibre formation in vitro, but not for chromatin remodelling. Agianian B, Leonard K, Bonte E, Van der Zandt H, Becker PB, Tucker PA. J Mol Biol 285 527-544 (1999)
- A Population Shift between Sparsely Populated Folding Intermediates Determines Amyloidogenicity. Karamanos TK, Pashley CL, Kalverda AP, Thompson GS, Mayzel M, Orekhov VY, Radford SE. J Am Chem Soc 138 6271-6280 (2016)
- Folding stability of amyloid-beta 40 monomer is an important determinant of the nucleation kinetics in fibrillization. Ni CL, Shi HP, Yu HM, Chang YC, Chen YR. FASEB J 25 1390-1401 (2011)
- Interplay between hydrophobic cluster and loop propensity in beta-hairpin formation: a mechanistic study. Colombo G, De Mori GM, Roccatano D. Protein Sci 12 538-550 (2003)
- Irreversible self-assembly of ovalbumin into fibrils and the resulting network rheology. Veerman C, de Schiffart G, Sagis LM, van der Linden E. Int J Biol Macromol 33 121-127 (2003)
- Partially Unfolded Forms of the Prion Protein Populated under Misfolding-promoting Conditions: CHARACTERIZATION BY HYDROGEN EXCHANGE MASS SPECTROMETRY AND NMR. Moulick R, Das R, Udgaonkar JB. J Biol Chem 290 25227-25240 (2015)
- Protein aggregation. Merlini G, Bellotti V, Andreola A, Palladini G, Obici L, Casarini S, Perfetti V. Clin Chem Lab Med 39 1065-1075 (2001)
- The stability and folding process of amyloidogenic mutant human lysozymes. Takano K, Funahashi J, Yutani K. Eur J Biochem 268 155-159 (2001)
- The structural impact of a polyglutamine tract is location-dependent. Robertson AL, Horne J, Ellisdon AM, Thomas B, Scanlon MJ, Bottomley SP. Biophys J 95 5922-5930 (2008)
- Thermo-reversible protein fibrillar hydrogels as cell scaffolds. Yan H, Nykanen A, Ruokolainen J, Farrar D, Gough JE, Saiani A, Saiani A, Miller AF. Faraday Discuss 139 71-84; discussion 105-28, 419-20 (2008)
- Transmissibility of mouse AApoAII amyloid fibrils: inactivation by physical and chemical methods. Zhang H, Sawashita J, Fu X, Korenaga T, Yan J, Mori M, Higuchi K. FASEB J 20 1012-1014 (2006)
- A metastable state in folding simulations of a protein model. Dinner AR, Karplus M. Nat Struct Biol 5 236-241 (1998)
- Co-fibrillogenesis of Wild-type and D76N β2-Microglobulin: THE CRUCIAL ROLE OF FIBRILLAR SEEDS. Natalello A, Mangione PP, Giorgetti S, Porcari R, Marchese L, Zorzoli I, Relini A, Ami D, Faravelli G, Valli M, Stoppini M, Doglia SM, Bellotti V, Raimondi S. J Biol Chem 291 9678-9689 (2016)
- Destabilization of Ca2+-free gelsolin may not be responsible for proteolysis in Familial Amyloidosis of Finnish Type. Ratnaswamy G, Huff ME, Su AI, Rion S, Kelly JW. Proc Natl Acad Sci U S A 98 2334-2339 (2001)
- Fibrillation of alpha-lactalbumin: effect of crocin and safranal, two natural small molecules from Crocus sativus. Ebrahim-Habibi MB, Amininasab M, Ebrahim-Habibi A, Sabbaghian M, Nemat-Gorgani M. Biopolymers 93 854-865 (2010)
- Heme binding inhibits the fibrillization of amyloidogenic apomyoglobin and determines lack of aggregate cytotoxicity. Iannuzzi C, Vilasi S, Portaccio M, Irace G, Sirangelo I. Protein Sci 16 507-516 (2007)
- Mutational analysis of designed peptides that undergo structural transition from alpha helix to beta sheet and amyloid fibril formation. Takahashi Y, Ueno A, Mihara H. Structure 8 915-925 (2000)
- Protein dissection enhances the amyloidogenic properties of alpha-lactalbumin. de Laureto PP, Frare E, Battaglia F, Mossuto MF, Uversky VN, Fontana A. FEBS J 272 2176-2188 (2005)
- Proteins can convert to beta-sheet in single crystals. Zheng R, Zheng X, Dong J, Carey PR. Protein Sci 13 1288-1294 (2004)
- Single molecular observation of the interaction of GroEL with substrate proteins. Yamasaki R, Hoshino M, Wazawa T, Ishii Y, Yanagida T, Kawata Y, Higurashi T, Sakai K, Nagai J, Goto Y. J Mol Biol 292 965-972 (1999)
- Structural fingerprints and their evolution during oligomeric vs. oligomer-free amyloid fibril growth. Foley J, Hill SE, Miti T, Mulaj M, Ciesla M, Robeel R, Persichilli C, Raynes R, Westerheide S, Muschol M. J Chem Phys 139 121901 (2013)
- Sub-micellar phospholipid accelerates amyloid formation by apolipoprotein C-II. Hatters DM, Lawrence LJ, Howlett GJ. FEBS Lett 494 220-224 (2001)
- Aggregate formation and the structure of the aggregates of disulfide-reduced proteins. Takase K, Higashi T, Omura T. J Protein Chem 21 427-433 (2002)
- Amyloid oligomers and protofibrils, but not filaments, self-replicate from native lysozyme. Mulaj M, Foley J, Muschol M. J Am Chem Soc 136 8947-8956 (2014)
- Betabellins 15D and 16D, de Novo designed beta-sandwich proteins that have amyloidogenic properties. Lim A, Makhov AM, Bond J, Inouye H, Connors LH, Griffith JD, Erickson BW, Kirschner DA, Costello CE. J Struct Biol 130 363-370 (2000)
- Comparison of the conformational stability of the non-native alpha-helical intermediate of thiol-modified beta-lactoglobulin upon interaction with sodium n-alkyl sulfates at two different pH. Chamani J. J Colloid Interface Sci 299 636-646 (2006)
- Contribution of disulfide bonds to stability, folding, and amyloid fibril formation: the PI3-SH3 domain case. Graña-Montes R, de Groot NS, Castillo V, Sancho J, Velazquez-Campoy A, Ventura S. Antioxid Redox Signal 16 1-15 (2012)
- Delicate balance between functionally required flexibility and aggregation risk in a β-rich protein. Ferrolino MC, Zhuravleva A, Budyak IL, Krishnan B, Gierasch LM. Biochemistry 52 8843-8854 (2013)
- Effect of sodium tetrathionate on amyloid fibril: Insight into the role of disulfide bond in amyloid progression. Sarkar N, Kumar M, Dubey VK. Biochimie 93 962-968 (2011)
- Exploring tryptophan dynamics in acid-induced molten globule state of bovine alpha-lactalbumin: a wavelength-selective fluorescence approach. Kelkar DA, Chaudhuri A, Haldar S, Chattopadhyay A. Eur Biophys J 39 1453-1463 (2010)
- Formation and dissolution of hen egg white lysozyme amyloid fibrils in protic ionic liquids. Byrne N, Angell CA. Chem Commun (Camb) 1046-1048 (2009)
- Induced Dipole-Dipole Interactions Influence the Unfolding Pathways of Wild-Type and Mutant Amyloid β-Peptides. Lemkul JA, Huang J, MacKerell AD. J Phys Chem B 119 15574-15582 (2015)
- Nucleolar Sequestration: Remodeling Nucleoli Into Amyloid Bodies. Wang M, Bokros M, Theodoridis PR, Lee S. Front Genet 10 1179 (2019)
- Use of anti-(beta2 microglobulin) mAb to study formation of amyloid fibrils. Stoppini M, Bellotti V, Mangione P, Merlini G, Ferri G. Eur J Biochem 249 21-26 (1997)
- A family with gastrointestinal amyloidosis associated with variant lysozyme. Granel B, Serratrice J, Valleix S, Grateau G, Droz D, Lafon J, Sault MC, Chaudier B, Disdier P, Laugier R, Delpech M, Weiller PJ. Gastroenterology 123 1346-1349 (2002)
- Deciphering the role of the thermodynamic and kinetic stabilities of SH3 domains on their aggregation inside bacteria. Castillo V, Espargaró A, Gordo V, Vendrell J, Ventura S. Proteomics 10 4172-4185 (2010)
- Disruption of an intermonomer salt bridge in the p53 tetramerization domain results in an increased propensity to form amyloid fibrils. Galea C, Bowman P, Kriwacki RW. Protein Sci 14 2993-3003 (2005)
- Mid-infrared free-electron laser tuned to the amide I band for converting insoluble amyloid-like protein fibrils into the soluble monomeric form. Kawasaki T, Fujioka J, Imai T, Torigoe K, Tsukiyama K. Lasers Med Sci 29 1701-1707 (2014)
- Molten globule and native state ensemble of Helicobacter pylori flavodoxin: can crowding, osmolytes or cofactors stabilize the native conformation relative to the molten globule? Cremades N, Sancho J. Biophys J 95 1913-1927 (2008)
- Picosecond dissociation of amyloid fibrils with infrared laser: A nonequilibrium simulation study. Hoang Viet M, Derreumaux P, Li MS, Roland C, Sagui C, Nguyen PH. J Chem Phys 143 155101 (2015)
- Raman optical activity characterization of native and molten globule states of equine lysozyme: comparison with hen lysozyme and bovine alpha-lactalbumin. Blanch EW, Morozova-Roche LA, Hecht L, Noppe W, Barron LD. Biopolymers 57 235-248 (2000)
- The elusive intermediate on the folding pathway of the prion protein. Jenkins DC, Sylvester ID, Pinheiro TJ. FEBS J 275 1323-1335 (2008)
- A pH-dependent conformational transition of Abeta peptide and physicochemical properties of the conformers in the glial cell. Matsunaga Y, Saito N, Fujii A, Yokotani J, Takakura T, Nishimura T, Esaki H, Yamada T. Biochem J 361 547-556 (2002)
- A single mutation in an SH3 domain increases amyloid aggregation by accelerating nucleation, but not by destabilizing thermodynamically the native state. Varela L, Morel B, Azuaga AI, Conejero-Lara F. FEBS Lett 583 801-806 (2009)
- Amyloid fibril formation by macrophage migration inhibitory factor. Lashuel HA, Aljabari B, Sigurdsson EM, Metz CN, Leng L, Callaway DJ, Bucala R. Biochem Biophys Res Commun 338 973-980 (2005)
- Analysis of the native structure, stability and aggregation of biotinylated human lysozyme. Ahn M, De Genst E, Kaminski Schierle GS, Erdelyi M, Kaminski CF, Dobson CM, Kumita JR. PLoS One 7 e50192 (2012)
- Characterization of membrane protein non-native states. 1. Extent of unfolding and aggregation of rhodopsin in the presence of chemical denaturants. Dutta A, Tirupula KC, Alexiev U, Klein-Seetharaman J. Biochemistry 49 6317-6328 (2010)
- Denatured-state energy landscapes of a protein structural database reveal the energetic determinants of a framework model for folding. Wang S, Gu J, Larson SA, Whitten ST, Hilser VJ. J Mol Biol 381 1184-1201 (2008)
- Differential effects of ionic and non-ionic surfactants on lysozyme fibrillation. Kumar EK, Prabhu NP. Phys Chem Chem Phys 16 24076-24088 (2014)
- Enhancement of thermal stability and inhibition of protein aggregation by osmolytic effect of hydroxyproline. Kar K, Kishore N. Biopolymers 87 339-351 (2007)
- Fibrinogen has chaperone-like activity. Tang H, Fu Y, Cui Y, He Y, Zeng X, Ploplis VA, Castellino FJ, Luo Y. Biochem Biophys Res Commun 378 662-667 (2009)
- Hydrogen sulfide inhibits amyloid formation. Rosario-Alomar MF, Quiñones-Ruiz T, Kurouski D, Sereda V, Ferreira EB, Jesús-Kim LD, Hernández-Rivera S, Zagorevski DV, López-Garriga J, Lednev IK. J Phys Chem B 119 1265-1274 (2015)
- Lysozyme encapsulated gold nanoclusters: effects of cluster synthesis on natural protein characteristics. Russell BA, Jachimska B, Komorek P, Mulheran PA, Chen Y. Phys Chem Chem Phys 19 7228-7235 (2017)
- Catalysis of protein folding by chaperones accelerates evolutionary dynamics in adapting cell populations. Cetinbaş M, Shakhnovich EI. PLoS Comput Biol 9 e1003269 (2013)
- Characterization of Protein Structural Changes in Living Cells Using Time-Lapsed FTIR Imaging. Gelfand P, Smith RJ, Stavitski E, Borchelt DR, Miller LM. Anal Chem 87 6025-6031 (2015)
- Copper ion / H2O2 oxidation of Cu/Zn-Superoxide dismutase: Implications for enzymatic activity and antioxidant action. Tiwari MK, Hägglund PM, Møller IM, Davies MJ, Bjerrum MJ. Redox Biol 26 101262 (2019)
- Disease-related amyloidogenic variants of human lysozyme trigger the unfolded protein response and disturb eye development in Drosophila melanogaster. Kumita JR, Helmfors L, Williams J, Luheshi LM, Menzer L, Dumoulin M, Lomas DA, Crowther DC, Dobson CM, Brorsson AC. FASEB J 26 192-202 (2012)
- Dynamic effects of mutations within two loops of cytochrome c551 from Pseudomonas aeruginosa. Ceruso MA, Grottesi A, Di Nola A. Proteins 50 222-229 (2003)
- Study of aggregation, denaturation and reduction of interferon alpha-2 products by size-exclusion high-performance liquid chromatography with fluorescence detection and biological assays. Diress A, Lorbetskie B, Larocque L, Li X, Alteen M, Isbrucker R, Girard M. J Chromatogr A 1217 3297-3306 (2010)
- Thermodynamics and stability of a beta-sheet complex: molecular dynamics simulations on simplified off-lattice protein models. Jang H, Hall CK, Zhou Y. Protein Sci 13 40-53 (2004)
- A non-natural variant of human lysozyme (I59T) mimics the in vitro behaviour of the I56T variant that is responsible for a form of familial amyloidosis. Hagan CL, Johnson RJ, Dhulesia A, Dumoulin M, Dumont J, De Genst E, Christodoulou J, Robinson CV, Dobson CM, Kumita JR. Protein Eng Des Sel 23 499-506 (2010)
- Amyloidogenic propensity of a natural variant of human apolipoprotein A-I: stability and interaction with ligands. Rosú SA, Rimoldi OJ, Prieto ED, Curto LM, Delfino JM, Ramella NA, Tricerri MA. PLoS One 10 e0124946 (2015)
- Characterization of the native and fibrillar conformation of the human Nalpha-acetyltransferase ARD1. Sánchez-Puig N, Fersht AR. Protein Sci 15 1968-1976 (2006)
- Competing intrachain interactions regulate the formation of beta-sheet fibrils in bovine PrP peptides. Tahiri-Alaoui A, Bouchard M, Zurdo J, James W. Protein Sci 12 600-608 (2003)
- Modulation of pathway of insulin fibrillation by a small molecule helix inducer 2,2,2-trifluoroethanol. Banerjee V, Das KP. Colloids Surf B Biointerfaces 92 142-150 (2012)
- Mutations in the B1 domain of protein G that delay the onset of amyloid fibril formation in vitro. Ramírez-Alvarado M, Cocco MJ, Regan L. Protein Sci 12 567-576 (2003)
- Rapid unfolding of a domain populates an aggregation-prone intermediate that can be recognized by GroEL. Doyle SM, Anderson E, Zhu D, Braswell EH, Teschke CM. J Mol Biol 332 937-951 (2003)
- Sulfonated molecules that bind a partially structured species of beta2-microglobulin also influence refolding and fibrillogenesis. Carazzone C, Colombo R, Quaglia M, Mangione P, Raimondi S, Giorgetti S, Caccialanza G, Bellotti V, De Lorenzi E. Electrophoresis 29 1502-1510 (2008)
- The formation of an intrachain disulfide bond in the leptin protein is necessary for efficient leptin secretion. Boute N, Zilberfarb V, Camoin L, Bonnafous S, Le Marchand-Brustel Y, Issad T. Biochimie 86 351-356 (2004)
- Understanding the relationship between the primary structure of proteins and their amyloidogenic propensity: clues from inclusion body formation. Idicula-Thomas S, Balaji PV. Protein Eng Des Sel 18 175-180 (2005)
- Aggregation of recombinant human botulinum protein antigen serotype C in varying solution conditions: implications of conformational stability for aggregation kinetics. Bai S, Manning MC, Randolph TW, Carpenter JF. J Pharm Sci 100 836-848 (2011)
- Amyloidogenic properties of the prion protein fragment PrP(185-208): comparison with Alzheimer's peptide Abeta(1-28), influence of heparin and cell toxicity. Cortijo-Arellano M, Ponce J, Durany N, Cladera J. Biochem Biophys Res Commun 368 238-242 (2008)
- Cellular processing of the amyloidogenic cystatin C variant of hereditary cerebral hemorrhage with amyloidosis, Icelandic type. Benedikz E, Merz GS, Schwenk V, Johansen TE, Wisniewski HM, Rushbrook JI. Amyloid 6 172-182 (1999)
- Dynamics of apomyoglobin in the alpha-to-beta transition and of partially unfolded aggregated protein. Fabiani E, Stadler AM, Madern D, Koza MM, Tehei M, Hirai M, Zaccai G. Eur Biophys J 38 237-244 (2009)
- Inhibition of TTR aggregation-induced cell death--a new role for serum amyloid P component. Andersson K, Pokrzywa M, Dacklin I, Lundgren E. PLoS One 8 e55766 (2013)
- Inhibitory effect of copper nanoparticles on rosin modified surfactant induced aggregation of lysozyme. Ishtikhar M, Usmani SS, Gull N, Badr G, Mahmoud MH, Mahmoud MH, Khan RH. Int J Biol Macromol 78 379-388 (2015)
- Monoclonal antibodies assisting refolding of firefly luciferase. Xu Q, Xie Z, Ding J, Lin SX, Xu G. Protein Sci 13 1851-1858 (2004)
- Most of the structural elements of the globular domain of murine prion protein form fibrils with predominant beta-sheet structure. Jamin N, Coïc YM, Landon C, Ovtracht L, Baleux F, Neumann JM, Sanson A. FEBS Lett 529 256-260 (2002)
- Nonequilibrium all-atom molecular dynamics simulation of the bubble cavitation and application to dissociate amyloid fibrils. Hoang Viet M, Derreumaux P, Nguyen PH. J Chem Phys 145 174113 (2016)
- Prevention of amyloid fibril formation of amyloidogenic chicken cystatin by site-specific glycosylation in yeast. He J, Song Y, Ueyama N, Saito A, Azakami H, Kato A. Protein Sci 15 213-222 (2006)
- Structural features of interferon-gamma aggregation revealed by hydrogen exchange. Tobler SA, Fernandez EJ. Protein Sci 11 1340-1352 (2002)
- Historical Article Exceptional matters. Peters K. Lancet 364 2142-2151 (2004)
- Growth-active peptides are produced from alpha-lactalbumin and lysozyme. Kanda Y, Hisayasu S, Abe Y, Katsura K, Mashimo K. Life Sci 81 449-457 (2007)
- Lysozyme stability and amyloid fibrillization dependence on Hofmeister anions in acidic pH. Poniková S, Antošová A, Demjén E, Sedláková D, Marek J, Varhač R, Gažová Z, Sedlák E. J Biol Inorg Chem 20 921-933 (2015)
- Multiple Aggregation Pathways in Human γS-Crystallin and Its Aggregation-Prone G18V Variant. Roskamp KW, Montelongo DM, Anorma CD, Bandak DN, Chua JA, Malecha KT, Martin RW. Invest Ophthalmol Vis Sci 58 2397-2405 (2017)
- Oil Palm Phenolics Inhibit the In Vitro Aggregation of β-Amyloid Peptide into Oligomeric Complexes. Weinberg RP, Koledova VV, Shin H, Park JH, Tan YA, Sinskey AJ, Sambanthamurthi R, Rha C. Int J Alzheimers Dis 2018 7608038 (2018)
- Probing supramolecular protein assembly using covalently attached fluorescent molecular rotors. Kubánková M, López-Duarte I, Bull JA, Vadukul DM, Serpell LC, de Saint Victor M, Stride E, Kuimova MK. Biomaterials 139 195-201 (2017)
- Protein fibrillation lag times during kinetic inhibition. Pagano RS, López Medus M, Gómez GE, Couto PM, Labanda MS, Landolfo L, D'Alessio C, Caramelo JJ. Biophys J 107 711-720 (2014)
- Structural basis of folding cooperativity in model proteins: insights from a microcanonical perspective. Bereau T, Deserno M, Bachmann M. Biophys J 100 2764-2772 (2011)
- Study of alpha-helix to beta-strand to beta-sheet transitions in amyloid: the role of segregated hydrophobic beta-strands. Jacchieri SG. Biophys Chem 74 23-34 (1998)
- Dynamics of the conformational transitions during the dimerization of an intrinsically disordered peptide: a case study on the human islet amyloid polypeptide fragment. Qiao Q, Qi R, Wei G, Huang X. Phys Chem Chem Phys 18 29892-29904 (2016)
- Equilibrium Ensembles for Insulin Folding from Bias-Exchange Metadynamics. Singh R, Bansal R, Rathore AS, Goel G. Biophys J 112 1571-1585 (2017)
- Hen lysozyme amyloid fibrils induce aggregation of erythrocytes and lipid vesicles. Chaudhary N, Nagaraj R. Mol Cell Biochem 328 209-215 (2009)
- How methyl cyanide induces aggregation in all-alpha proteins: a case study in four albumins. Sen P, Fatima S, Khan JM, Khan RH. Int J Biol Macromol 44 163-169 (2009)
- Residual structures in the acid-unfolded states of Vlambda6 proteins affect amyloid fibrillation. Mishima T, Ohkuri T, Monji A, Kanemaru T, Abe Y, Ueda T. J Mol Biol 392 1033-1043 (2009)
- Structural and kinetic mapping of side-chain exposure onto the protein energy landscape. Bernstein R, Schmidt KL, Harbury PB, Marqusee S. Proc Natl Acad Sci U S A 108 10532-10537 (2011)
- The Significance of the Location of Mutations for the Native-State Dynamics of Human Lysozyme. Ahn M, Hagan CL, Bernardo-Gancedo A, De Genst E, Newby FN, Christodoulou J, Dhulesia A, Dumoulin M, Robinson CV, Dobson CM, Kumita JR. Biophys J 111 2358-2367 (2016)
- Thermo- and pH-responsive fibrillization of squid suckerin A1H1 peptide. Sun Y, Ding F. Nanoscale 12 6307-6317 (2020)
- Amyloid misfolding, aggregation, and the early onset of protein deposition diseases: insights from AFM experiments and computational analyses. Lyubchenko YL. AIMS Mol Sci 2 190-210 (2015)
- Characterization of the nucleation process of lysozyme at physiological pH: primary but not sole process. Navarra G, Troia F, Militello V, Leone M. Biophys Chem 177-178 24-33 (2013)
- Comparative Study of Toluidine Blue O and Methylene Blue Binding to Lysozyme and Their Inhibitory Effects on Protein Aggregation. Saha B, Chowdhury S, Sanyal D, Chattopadhyay K, Suresh Kumar G. ACS Omega 3 2588-2601 (2018)
- Diagnosis and treatment of amyloidosis. Hawkins PN. Ann Rheum Dis 56 631-633 (1997)
- Diet, amyloid enhancing factor (AEF) and amyloidogenesis: an hypothesis. Cathcart ES, Elliott-Bryant R. Amyloid 6 107-113 (1999)
- In vivo glycosylation suppresses the aggregation of amyloidogenic hen egg white lysozymes expressed in yeast. Song Y, Azakami H, Hamasu M, Kato A. FEBS Lett 491 63-66 (2001)
- Insights into the determinants of beta-sheet stability: 1H and 13C NMR conformational investigation of three-stranded antiparallel beta-sheet-forming peptides. Santiveri CM, Rico M, Jiménez MA, Pastor MT, Pérez-Payá E. J Pept Res 61 177-188 (2003)
- Ion-specific effects on prion nucleation and strain formation. Rubin J, Khosravi H, Bruce KL, Lydon ME, Behrens SH, Chernoff YO, Bommarius AS. J Biol Chem 288 30300-30308 (2013)
- Simulation of pH-dependent edge strand rearrangement in human beta-2 microglobulin. Park S, Saven JG. Protein Sci 15 200-207 (2006)
- The Route from the Folded to the Amyloid State: Exploring the Potential Energy Surface of a Drug-Like Miniprotein. Taricska N, Horváth D, Menyhárd DK, Ákontz-Kiss H, Noji M, So M, Goto Y, Fujiwara T, Perczel A. Chemistry 26 1968-1978 (2020)
- A comparative study of fibrillation kinetics of two homologous proteins under identical solution condition. Chaudhary AP, Vispute NH, Shukla VK, Ahmad B. Biochimie 132 75-84 (2017)
- Amyloid fibril formation of hen lysozyme depends on the instability of the C-helix (88-99). Harada A, Azakami H, Kato A. Biosci Biotechnol Biochem 72 1523-1530 (2008)
- Density guided importance sampling: application to a reduced model of protein folding. Thomas GL, Sessions RB, Parker MJ. Bioinformatics 21 2839-2843 (2005)
- Different effects of calnexin deletion in Saccharomyces cerevisiae on the secretion of two glycosylated amyloidogenic lysozymes. Song Y, Azakami H, Shamima B, He J, Kato A. FEBS Lett 512 213-217 (2002)
- Kinetics of surfactant-induced aggregation of lysozyme studied by fluorescence spectroscopy. Jain N, Bhattacharya M, Mukhopadhyay S. J Fluoresc 21 615-625 (2011)
- Metal alloy solid-state nanopores for single nanoparticle detection. Coglitore D, Merenda A, Giamblanco N, Dumée LF, Janot JM, Balme S. Phys Chem Chem Phys 20 12799-12807 (2018)
- Oxidative refolding of amyloidogenic variants of human lysozyme. Wain R, Smith LJ, Dobson CM. J Mol Biol 351 662-671 (2005)
- Proteins in vacuo: a molecular dynamics study of the unfolding behavior of highly charged disulfide-bond-intact lysozyme subjected to a temperature pulse. Reimann CT, Velázquez I, Bittner M, Tapia O. Phys Rev E Stat Phys Plasmas Fluids Relat Interdiscip Topics 60 7277-7284 (1999)
- Purification and spectroscopic characterization of beta-amyloid precursor protein from porcine brains. de La Fournière-Bessueille L, Grange D, Buchet R. Eur J Biochem 250 705-711 (1997)
- Relationship between the stability of hen egg-white lysozymes mutated at sites designed to interact with alpha-helix dipoles and their secretion amounts in yeast. Harada A, Yagi H, Saito A, Azakami H, Kato A. Biosci Biotechnol Biochem 71 2952-2961 (2007)
- Structural analysis of human lysozyme using molecular dynamics simulations. Liu HL, Wu YC, Zhao JH, Fang HW, Ho Y. J Biomol Struct Dyn 24 229-238 (2006)
- Syntheses and structure-activity relationships of seven manganese-salen derivatives as anti-amyloidogenic and fibril-destabilizing agents against hen egg-white lysozyme aggregation. Bahramikia S, Yazdanparast R, Gheysarzadeh A. Chem Biol Drug Des 80 227-236 (2012)
- Tracking lysozyme unfolding during salt-induced precipitation with hydrogen exchange and mass spectrometry. Tobler SA, Sherman NE, Fernandez EJ. Biotechnol Bioeng 71 194-207 (2000)
- A non-native alpha-helix is formed in the beta-sheet region of the molten globule state of canine milk lysozyme. Watanabe M, Kobashigawa Y, Aizawa T, Demura M, Nitta K. Protein J 23 335-342 (2004)
- Attenuation of lysozyme amyloid cytotoxicity by SPION-mediated modulation of amyloid aggregation. Naik A, Kambli P, Borana M, Mohanpuria N, Ahmad B, Kelkar-Mane V, Ladiwala U. Int J Biol Macromol 74 439-446 (2015)
- Carbon Quantum Dots for Treatment of Amyloid Disorders. Damian Guerrero E, Lopez-Velazquez AM, Ahlawat J, Narayan M. ACS Appl Nano Mater 4 2423-2433 (2021)
- Characterization of heat induced spherulites of lysozyme reveals new insight on amyloid initiation. Sharma P, Verma N, Singh PK, Korpole S, Ashish. Sci Rep 6 22475 (2016)
- Computational study of aggregation mechanism in human lysozyme[D67H]. Patel D, Kuyucak S. PLoS One 12 e0176886 (2017)
- Domain interactions direct misfolding and amyloid formation of yeast phosphoglycerate kinase. Osváth S, Jäckel M, Agócs G, Závodszky P, Köhler G, Fidy J. Proteins 62 909-917 (2006)
- Effect of site-directed point mutations on protein misfolding: A simulation study. Kumar A, Biswas P. Proteins 87 760-773 (2019)
- Examining the inhibitory potency of food additive fast green FCF against amyloid fibrillogenesis under acidic conditions. How SC, Yang SM, Hsin A, Tseng CP, Hsueh SS, Lin MS, Chen RP, Chou WL, Wang SS. Food Funct 7 4898-4907 (2016)
- Formation of amyloid fibrils from β-amylase. Luo JC, Wang SC, Jian WB, Chen CH, Tang JL, Lee CI. FEBS Lett 586 680-685 (2012)
- Interplay between metal binding and cis/trans isomerization in legume lectins: structural and thermodynamic study of P. angolensis lectin. Garcia-Pino A, Buts L, Wyns L, Loris R. J Mol Biol 361 153-167 (2006)
- Investigating the effects of erythrosine B on amyloid fibril formation derived from lysozyme. Kuo CT, Chen YL, Hsu WT, How SC, Cheng YH, Hsueh SS, Liu HS, Lin TH, Wu JW, Wang SS. Int J Biol Macromol 98 159-168 (2017)
- Investigating the preventive effects of baicalin and gallocatechin against glyoxal-induced cystatin aggregation. Sohail A, Bhat WF, Bhat SA, Furkan M, Shah A, Bano B. J Biomol Struct Dyn 36 3791-3802 (2018)
- Microsecond sub-domain motions and the folding and misfolding of the mouse prion protein. Goluguri RR, Sen S, Udgaonkar J. Elife 8 e44766 (2019)
- Multiphase protein microgels. Shimanovich U, Song Y, Brujic J, Shum HC, Knowles TP. Macromol Biosci 15 501-508 (2015)
- Probing Conformational Diversity of Fc Domains in Aggregation-Prone Monoclonal Antibodies. Majumder S, Jones MT, Kimmel M, Alphonse Ignatius A. Pharm Res 35 220 (2018)
- Probing residue-level unfolding during lysozyme precipitation. Chang ST, Fernandez EJ. Biotechnol Bioeng 59 144-155 (1998)
- Structure and antibacterial activity relationships of native and amyloid fibril lysozyme loaded on layered double hydroxide. Bouaziz Z, Soussan L, Janot JM, Lepoitevin M, Bechelany M, Djebbi MA, Amara ABH, Balme S. Colloids Surf B Biointerfaces 157 10-17 (2017)
- Thermodynamic analysis of helix-engineered forms of the activation domain of human procarboxypeptidase A2. Fernández AM, Villegas V, Martínez JC, Van Nuland NA, Conejero-Lara F, Avilés FX, Serrano L, Filimonov VV, Mateo PL. Eur J Biochem 267 5891-5899 (2000)
- Trehalose Effect on the Aggregation of Model Proteins into Amyloid Fibrils. Mari E, Ricci C, Pieraccini S, Spinozzi F, Mariani P, Ortore MG. Life (Basel) 10 E60 (2020)
- Two distinct aggregation pathways in transthyretin misfolding and amyloid formation. Dasari AKR, Hung I, Gan Z, Lim KH. Biochim Biophys Acta Proteins Proteom 1867 344-349 (2019)
- A de novo designed 11 kDa polypeptide: model for amyloidogenic intrinsically disordered proteins. Topilina NI, Ermolenkov VV, Sikirzhytski V, Higashiya S, Lednev IK, Welch JT. Biopolymers 93 607-618 (2010)
- Amyloid fibrillogenesis of lysozyme is suppressed by a food additive brilliant blue FCF. Chen YH, Tseng CP, How SC, Lo CH, Chou WL, Wang SS. Colloids Surf B Biointerfaces 142 351-359 (2016)
- Amyloid fibrils formed by the programmed cell death regulator Bcl-xL. Chenal A, Vendrely C, Vitrac H, Karst JC, Gonneaud A, Blanchet CE, Pichard S, Garcia E, Salin B, Catty P, Gillet D, Hussy N, Marquette C, Almunia C, Forge V. J Mol Biol 415 584-599 (2012)
- Anti-Parkinsonian L-Dopa can also act as anti-systemic amyloidosis-A mechanistic exploration. Nusrat S, Zaidi N, Siddiqi MK, Zaman M, Siddique IA, Ajmal MR, Abdelhameed AS, Khan RH, Khan RH. Int J Biol Macromol 99 630-640 (2017)
- Benzothiazole-Based Neutral Ratiometric Fluorescence Sensor for Amyloid Fibrils. Mora AK, Murudkar S, Alamelu A, Singh PK, Chattopadhyay S, Nath S. Chemistry 22 16505-16512 (2016)
- Characteristics of human lysozyme and its disease-related mutants in their unfolded states. Sziegat F, Wirmer-Bartoschek J, Schwalbe H. Angew Chem Int Ed Engl 50 5514-5518 (2011)
- Characterization of the conformational space of a triple-stranded beta-sheet forming peptide with molecular dynamics simulations. Soto P, Colombo G. Proteins 57 734-746 (2004)
- Clinical characteristics and SAP scintigraphic findings in 10 patients with AGel amyloidosis. Rowczenio D, Tennent GA, Gilbertson J, Lachmann HJ, Hutt DF, Bybee A, Hawkins PN, Gillmore JD. Amyloid 21 276-281 (2014)
- Effect of pH on the aggregate formation of a non-amyloid component (1-13). Abe H, Nakanishi H. J Pept Sci 9 177-186 (2003)
- Equilibrium unfolding of A. niger RNase: pH dependence of chemical and thermal denaturation. Kumar GR, Sharma A, Kumari M, Jagannadham MV, Debnath M. Eur Biophys J 40 923-935 (2011)
- Interaction of nonionic detergents with the specific sites of lysozyme amyloidogenic region - inhibition of amyloid fibrillization. Siposova K, Kozar T, Musatov A. Colloids Surf B Biointerfaces 150 445-455 (2017)
- Molten globules. Redfield C. Curr Biol 9 R313 (1999)
- Primary biliary cirrhosis and systemic amyloidosis, a new association. Rodriguez-Luna H, Vargas HE, Williams J, De Petris G, Rakela J, Douglas DD. Dig Dis Sci 49 1196-1200 (2004)
- Structure and function of anhydride-modified forms of human insulin: In silico, in vitro and in vivo studies. Chinisaz M, Ebrahim-Habibi A, Dehpour AR, Yaghmaei P, Parivar K, Moosavi-Movahedi AA. Eur J Pharm Sci 96 342-350 (2017)
- Type I collagen prevents amyloid aggregation of hen egg white lysozyme. Dubey K, Kar K. Biochem Biophys Res Commun 448 480-484 (2014)
- Amyloid fibril formation by the CAD domain of caspase-activated DNase. Uegaki K, Nakamura T, Yamamoto H, Kobayashi A, Odahara T, Harata K, Hagihara Y, Ueyama N, Yamazaki T, Yumoto N. Biopolymers 79 39-47 (2005)
- Amyloid formation: an emulation of matrix protein assembly? Stevens FJ. Amyloid 11 232-244 (2004)
- Effect of silybin on the fibrillation of hen egg-white lysozyme. Zeng HJ, Miao M, Yang R, Qu LB. J Mol Recognit 30 (2017)
- Purine nucleoside phosphorylase activity decline is linked to the decay of the trimeric form of the enzyme. Wielgus-Kutrowska B, Modrak-Wójcik A, Dyzma A, Breer K, Zolkiewski M, Bzowska A. Arch Biochem Biophys 549 40-48 (2014)
- Recovery of functional enzyme from amyloid fibrils. Agócs G, Solymosi K, Varga A, Módos K, Kellermayer M, Závodszky P, Fidy J, Osváth S. FEBS Lett 584 1139-1142 (2010)
- Rituximab Therapy in Renal Amyloidosis Secondary to Rheumatoid Arthritis. Kilic L, Erden A, Sener YZ, Armagan B, Sari A, Kalyoncu U, Karadag O, Akdogan A, Dogan I, Apras Bilgen S, Kiraz S, Ertenli I. Biomolecules 8 E136 (2018)
- Solvent-amino acid interaction energies in three-dimensional-lattice Monte Carlo simulations of a model 27-mer protein: Folding thermodynamics and kinetics. Leonhard K, Prausnitz JM, Radke CJ. Protein Sci 13 358-369 (2004)
- Stable misfolded states of human serum albumin revealed by high-pressure infrared spectroscopic studies. Smeller L, Meersman F, Heremans K. Eur Biophys J 37 1127-1132 (2008)
- Synergistic Inhibition of Protein Fibrillation by Proline and Sorbitol: Biophysical Investigations. Choudhary S, Save SN, Kishore N, Hosur RV. PLoS One 11 e0166487 (2016)
- The development of transgenic mice for the expression of large amounts of human lysozyme in milk. Wu X, Lin Y, Xi Y, Shao Z, Zhou Y, Liu F, Chen H. Biotechnol Lett 36 1197-1202 (2014)
- The native state of prion protein (PrP) directly inhibits formation of PrP-amyloid fibrils in vitro. Honda RP, Kuwata K. Sci Rep 7 562 (2017)
- Unfolding Pathways of Hen Egg-White Lysozyme in Ethanol. Walker AR, Baddam N, Cisneros GA. J Phys Chem B 123 3267-3271 (2019)
- Apomyoglobin mutants with single point mutations at val10 can form amyloid structures at permissive temperature. Katina NS, Ilyina NB, Kashparov IA, Balobanov VA, Vasiliev VD, Bychkova VE. Biochemistry (Mosc) 76 555-563 (2011)
- Application of Lysine-specific Labeling to Detect Transient Interactions Present During Human Lysozyme Amyloid Fibril Formation. Ahn M, Waudby CA, Bernardo-Gancedo A, De Genst E, Dhulesia A, Salvatella X, Christodoulou J, Dobson CM, Kumita JR. Sci Rep 7 15018 (2017)
- Characterization of amyloidogenic intermediate states through a combined use of CD and NMR spectroscopy. Lim KH, Le YT, Collver HH, Putnam-Evans C, Kenney JM. Biophys Chem 151 155-159 (2010)
- Classical and alternative pathway complement activation are not required for reactive systemic AA amyloid deposition in mice. Hutchinson WL, Herbert J, Botto M, Pepys MB. Immunology 112 250-254 (2004)
- Crowded milieu prevents fibrillation of hen egg white lysozyme with retention of enzymatic activity. Ghosh S, Pandey NK, Dasgupta S. J Photochem Photobiol B 138 8-16 (2014)
- Elevated temperatures accelerate the formation of toxic amyloid fibrils of hen egg-white lysozyme. Feng Z, Li Y, Bai Y. Vet Med Sci 7 1938-1947 (2021)
- Guanidine-HCl dependent structural unfolding of M-crystallin: fluctuating native state like topologies and intermolecular association. Barnwal RP, Agarwal G, Chary KV. PLoS One 7 e42948 (2012)
- Hydrogen skeleton, mobility and protein architecture. Tompa K, Bokor M, Han KH, Tompa P. Intrinsically Disord Proteins 1 e25767 (2013)
- Insight into the aggregation of lipase from Pseudomonas sp. using mutagenesis: protection of aggregation prone region by adoption of α-helix structure. Rashno F, Khajeh K, Dabirmanesh B, Sajedi RH, Chiti F. Protein Eng Des Sel 31 419-426 (2018)
- Investigating the effects of plasma pretreatment on the formation of ordered aggregates of lysozyme. Chang CK, Chen WA, Sie CY, Lin SC, Lin LT, Lin TH, Hsu CC, Wang SS. Colloids Surf B Biointerfaces 126 154-161 (2015)
- Methylated BSA mimics amyloid-related proteins and triggers inflammation. Di Domizio J, Dorta-Estremera S, Cao W. PLoS One 8 e63214 (2013)
- Molten globule state of human placental cystatin (HPC) at low pH conditions and the effects of trifluoroethanol (TFE) and methanol. Rashid F, Sharma S, Baig MA, Bano B. Biochem Cell Biol 84 126-134 (2006)
- Origin, toxicity and characteristics of two amyloid oligomer polymorphs. Niyangoda C, Barton J, Bushra N, Karunarathne K, Strauss G, Fakhre F, Koria P, Muschol M. RSC Chem Biol 2 1631-1642 (2021)
- Proposing a minimal set of metrics and methods to predict probabilities of amyloidosis disease and onset age in individuals. Criddle RS, Lin HL, James I, Park JS, Hansen LD, Price JC. Aging (Albany NY) 12 22356-22369 (2020)
- Structural Water Stabilizes Protein Motifs in Liquid Protein Phase: The Folding Mechanism of Short β-Sheets Coupled to Phase Transition. Papp D, Szigyártó IC, Nordén B, Perczel A, Beke-Somfai T. Int J Mol Sci 22 8595 (2021)
- Evaluation of variability in high-resolution protein structures by global distance scoring. Anzai R, Asami Y, Inoue W, Ueno H, Yamada K, Okada T. Heliyon 4 e00510 (2018)
- Exploring the free energy landscape of a model β-hairpin peptide and its isoform. Narayanan C, Dias CL. Proteins 82 2394-2402 (2014)
- Fluorescence study of the membrane effects of aggregated lysozyme. Kutsenko OK, Trusova VM, Gorbenko GP, Lipovaya AS, Slobozhanina EI, Lukyanenko LM, Deligeorgiev T, Vasilev A. J Fluoresc 23 1229-1237 (2013)
- Folding superfunnel to describe cooperative folding of interacting proteins. Smeller L. Proteins 84 1009-1016 (2016)
- Interaction and inhibitory influence of the azo dye carmoisine on lysozyme amyloid fibrillogenesis. Basu A, Suresh Kumar G. Mol Biosyst 13 1552-1564 (2017)
- Methodological aspects of an off-line combination of preparative isotachophoresis and high-performance liquid chromatography with mass spectrometry in the analysis of biological matrices. Kondeková M, Staňová A, Marák J. Electrophoresis 35 1173-1180 (2014)
- Modulation Effects of Fe3+, Zn2+, and Cu2+ Ions on the Amyloid Fibrillation of α-Synuclein: Insights from a FTIR Investigation. Li Y, Yu Y, Ma G. Molecules 27 8383 (2022)
- Protein folding stabilizing time measurement: a direct folding process and three-dimensional random walk simulation. Chang CC, Lin PY, Yeh XC, Deng KH, Ho YP, Kan LS. Biochem Biophys Res Commun 328 845-850 (2005)
- Protein's native state stability in a chemically induced denaturation mechanism. Olivares-Quiroz L, Garcia-Colin LS. J Theor Biol 246 214-224 (2007)
- Resveratrol Interferes with an Early Step in the Fibrillization Pathway of Human Lysozyme and Modulates it towards Less-Toxic, Off-Pathway Aggregates. Kamal Zaidi F, Bhat R. Chembiochem 19 159-170 (2018)
- Analyses of Mutation Displacements from Homology Models. Carpentier M, Chomilier J. Methods Mol Biol 2627 195-210 (2023)
- Cataract-Causing S93R Mutant Destabilized Structural Conformation of βB1 Crystallin Linking With Aggregates Formation and Cellular Viability. Ren L, Hu L, Zhang Y, Liu J, Xu W, Wu W, Xu J, Chen X, Yao K, Yu Y. Front Mol Biosci 9 844719 (2022)
- Comparative Study of Protein Aggregation Arrest by Zwitterionic Polysulfobetaines: Using Contrasting Raft Agents. Sharma N, Rajan R, Makhaik S, Matsumura K. ACS Omega 4 12186-12193 (2019)
- Competition between inside-out unfolding and pathogenic aggregation in an amyloid-forming β-propeller. Saccuzzo EG, Mebrat MD, Scelsi HF, Kim M, Ma MT, Su X, Hill SE, Rheaume E, Li R, Torres MP, Gumbart JC, Van Horn WD, Lieberman RL. Nat Commun 15 155 (2024)
- Computer Simulations Aimed at Exploring Protein Aggregation and Dissociation. Nguyen PH, Derreumaux P. Methods Mol Biol 2340 175-196 (2022)
- Effect of pH on the Poly(acrylic acid)/Poly(vinyl alcohol)/Lysozyme Complexes Formation. Morariu S, Avadanei M, Nita LE. Molecules 29 208 (2023)
- Energy Landscapes and Heat Capacity Signatures for Monomers and Dimers of Amyloid-Forming Hexapeptides. Nicy, Wales DJ. Int J Mol Sci 24 10613 (2023)
- Environmental factors preceding aβ40 monomer to oligomers and the detection of oligomers in Alzheimer's disease patient serum. Matsunaga Y, Suenaga M. J Amino Acids 2012 206520 (2012)
- Expression of recombinant human lysozyme in transgenic chicken promotes the growth of Bifidobacterium in the intestine and improves postnatal growth of chicken. Wang H, Wu H, Wang K, Cao Z, Yu K, Lian L, Lian Z. AMB Express 6 110 (2016)
- Gold nanocolloid-protein interactions and their impact on β-sheet amyloid fibril formation. Barros HR, Kokkinopoulou M, Riegel-Vidotti IC, Landfester K, Thérien-Aubin H. RSC Adv 8 980-986 (2018)
- Host defense functions of the epididymal amyloid matrix. Myers C, Hastert MC, Cornwall GA. Mol Hum Reprod 28 gaac038 (2022)
- NMR characterization of hydrophobic collapses in amyloidogenic unfolded states and their implications for amyloid formation. Lim KH, Nagchowdhuri P, Rathinavelan T, Im W. Biochem Biophys Res Commun 396 800-805 (2010)
- The Ability of Some Polysaccharides to Disaggregate Lysozyme Amyloid Fibrils and Renature the Protein. Makshakova O, Bogdanova L, Faizullin D, Khaibrakhmanova D, Ziganshina S, Ermakova E, Zuev Y, Sedov I. Pharmaceutics 15 624 (2023)
- Unstable mutant lysozymes are degraded through the interaction with calnexin homolog Cne1p in Saccharomyces cerevisiae. Azakami H, Uehara M, Matsuo R, Tsurunaga Y, Yamashita Y, Usui M, Kato A. Biosci Biotechnol Biochem 78 1263-1269 (2014)