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PDBsum entry 1av1

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protein Protein-protein interface(s) links
Lipid transport PDB id
1av1
Jmol
Contents
Protein chains
201 a.a. *
* Residue conservation analysis
PDB id:
1av1
Name: Lipid transport
Title: Crystal structure of human apolipoprotein a-i
Structure: Apolipoprotein a-i. Chain: a, b, c, d. Fragment: lipid-binding domain. Synonym: apo a-i. Engineered: yes. Mutation: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Cell_line: bl21. Tissue: blood. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Biol. unit: Tetramer (from PQS)
Resolution:
4.00Å     R-factor:   0.382     R-free:   0.428
Authors: D.W.Borhani,D.P.Rogers,J.A.Engler,C.G.Brouillette
Key ref:
D.W.Borhani et al. (1997). Crystal structure of truncated human apolipoprotein A-I suggests a lipid-bound conformation. Proc Natl Acad Sci U S A, 94, 12291-12296. PubMed id: 9356442 DOI: 10.1073/pnas.94.23.12291
Date:
23-Sep-97     Release date:   04-Feb-98    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P02647  (APOA1_HUMAN) -  Apolipoprotein A-I
Seq:
Struc:
267 a.a.
201 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     extracellular region   1 term 
  Biological process     lipid transport   2 terms 
  Biochemical function     lipid binding     1 term  

 

 
DOI no: 10.1073/pnas.94.23.12291 Proc Natl Acad Sci U S A 94:12291-12296 (1997)
PubMed id: 9356442  
 
 
Crystal structure of truncated human apolipoprotein A-I suggests a lipid-bound conformation.
D.W.Borhani, D.P.Rogers, J.A.Engler, C.G.Brouillette.
 
  ABSTRACT  
 
The structure of truncated human apolipoprotein A-I (apo A-I), the major protein component of high density lipoprotein, has been determined at 4-A resolution. The crystals comprise residues 44-243 (exon 4) of apo A-I, a fragment that binds to lipid similarly to intact apo A-I and that retains the lipid-bound conformation even in the absence of lipid. The molecule consists almost entirely of a pseudo-continuous, amphipathic alpha-helix that is punctuated by kinks at regularly spaced proline residues; it adopts a shape similar to a horseshoe of dimensions 125 x 80 x 40 A. Four molecules in the asymmetric unit associate via their hydrophobic faces to form an antiparallel four-helix bundle with an elliptical ring shape. Based on this structure, we propose a model for the structure of apo A-I bound to high density lipoprotein.
 
  Selected figure(s)  
 
Figure 2.
Fig. 2. Stereoviews of the apo (1-43)A-I C^ trace. (a) The apo (1-43)A-I monomer, molecule A. The N- and C-termini are labeled, as are each of the secondary structural elements described in the^ text. These elements are also colored differently. (b and c) The^ apo (1-43)A-I A/B dimer, and the tetramer. The molecules are^ colored as in a to facilitate identification of the alignment of the extensive intermolecular interactions.
Figure 4.
Fig. 4. RIBBONS (34) representation illustrating the elliptical and curved shape of the apo (1-43)A-I tetramer. (a) The tetramer is shown with the three noncrystallographic (pseudo)dyads: molecule^ A is gold, molecule B is purple, molecule C is pink, and molecule^ D is green. (b) View down the A/C dyad. (c) As in b, rotated 90° around the horizontal axis i.e., viewed down the A/D pseudo-dyad. (d) As in c, rotated 70° around the vertical axis.
 
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
21499241 J.Frauenfeld, J.Gumbart, E.O.Sluis, S.Funes, M.Gartmann, B.Beatrix, T.Mielke, O.Berninghausen, T.Becker, K.Schulten, and R.Beckmann (2011).
Cryo-EM structure of the ribosome-SecYE complex in the membrane environment.
  Nat Struct Mol Biol, 18, 614-621.
PDB codes: 3j00 3j01
21399642 R.Huang, R.A.Silva, W.G.Jerome, A.Kontush, M.J.Chapman, L.K.Curtiss, T.J.Hodges, and W.S.Davidson (2011).
Apolipoprotein A-I structural organization in high-density lipoproteins isolated from human plasma.
  Nat Struct Mol Biol, 18, 416-422.  
20043647 B.Shao, M.N.Oda, J.F.Oram, and J.W.Heinecke (2010).
Myeloperoxidase: an oxidative pathway for generating dysfunctional high-density lipoprotein.
  Chem Res Toxicol, 23, 447-454.  
21060857 T.Vuorela, A.Catte, P.S.Niemelä, A.Hall, M.T.Hyvönen, S.J.Marrink, M.Karttunen, and I.Vattulainen (2010).
Role of lipids in spheroidal high density lipoproteins.
  PLoS Comput Biol, 6, e1000964.  
19770066 V.Narayanaswami, R.S.Kiss, and P.M.Weers (2010).
The helix bundle: a reversible lipid binding motif.
  Comp Biochem Physiol A Mol Integr Physiol, 155, 123-133.  
19546861 Y.Levin, L.Wang, E.Schwarz, D.Koethe, F.M.Leweke, and S.Bahn (2010).
Global proteomic profiling reveals altered proteomic signature in schizophrenia serum.
  Mol Psychiatry, 15, 1088-1100.  
19130896 A.C.Paula-Lima, M.A.Tricerri, J.Brito-Moreira, T.R.Bomfim, F.F.Oliveira, M.H.Magdesian, L.T.Grinberg, R.Panizzutti, and S.T.Ferreira (2009).
Human apolipoprotein A-I binds amyloid-beta and prevents Abeta-induced neurotoxicity.
  Int J Biochem Cell Biol, 41, 1361-1370.  
19318685 E.T.Alexander, M.Tanaka, M.Kono, H.Saito, D.J.Rader, and M.C.Phillips (2009).
Structural and functional consequences of the Milano mutation (R173C) in human apolipoprotein A-I.
  J Lipid Res, 50, 1409-1419.  
19453280 J.Borch, and T.Hamann (2009).
The nanodisc: a novel tool for membrane protein studies.
  Biol Chem, 390, 805-814.  
  20582235 M.G.Sorci-Thomas, S.Bhat, and M.J.Thomas (2009).
Activation of lecithin:cholesterol acyltransferase by HDL ApoA-I central helices.
  Clin Lipidol, 4, 113-124.  
19167289 M.K.Jones, A.Catte, J.C.Patterson, F.Gu, J.Chen, L.Li, and J.P.Segrest (2009).
Thermal stability of apolipoprotein A-I in high-density lipoproteins by molecular dynamics.
  Biophys J, 96, 354-371.  
19860440 M.K.Jones, A.Catte, L.Li, and J.P.Segrest (2009).
Dynamics of activation of lecithin:cholesterol acyltransferase by apolipoprotein A-I.
  Biochemistry, 48, 11196-11210.  
19812036 Z.Wu, V.Gogonea, X.Lee, M.A.Wagner, X.M.Li, Y.Huang, A.Undurti, R.P.May, M.Haertlein, M.Moulin, I.Gutsche, G.Zaccai, J.A.Didonato, and S.L.Hazen (2009).
Double superhelix model of high density lipoprotein.
  J Biol Chem, 284, 36605-36619.
PDB code: 3k2s
18065479 A.Catte, J.C.Patterson, D.Bashtovyy, M.K.Jones, F.Gu, L.Li, A.Rampioni, D.Sengupta, T.Vuorela, P.Niemelä, M.Karttunen, S.J.Marrink, I.Vattulainen, and J.P.Segrest (2008).
Structure of spheroidal HDL particles revealed by combined atomistic and coarse-grained simulations.
  Biophys J, 94, 2306-2319.  
18706282 C.R.White, G.Datta, Z.Zhang, H.Gupta, D.W.Garber, V.K.Mishra, M.N.Palgunachari, S.P.Handattu, M.Chaddha, and G.M.Anantharamaiah (2008).
HDL therapy for cardiovascular diseases: the road to HDL mimetics.
  Curr Atheroscler Rep, 10, 405-412.  
18783334 L.Cigliano, L.D.D'Andrea, B.Maresca, M.Serino, A.Carlucci, A.Salvatore, M.S.Spagnuolo, G.Scigliuolo, C.Pedone, and P.Abrescia (2008).
Relevance of the amino acid conversions L144R (Zaragoza) and L159P (Zavalla) in the apolipoprotein A-I binding site for haptoglobin.
  Biol Chem, 389, 1421-1426.  
18515783 M.J.Thomas, S.Bhat, and M.G.Sorci-Thomas (2008).
Three-dimensional models of HDL apoA-I: implications for its assembly and function.
  J Lipid Res, 49, 1875-1883.  
18719128 R.A.Silva, R.Huang, J.Morris, J.Fang, E.O.Gracheva, G.Ren, A.Kontush, W.G.Jerome, K.A.Rye, and W.S.Davidson (2008).
Structure of apolipoprotein A-I in spherical high density lipoproteins of different sizes.
  Proc Natl Acad Sci U S A, 105, 12176-12181.  
18385132 R.Carnemolla, X.Ren, T.K.Biswas, S.C.Meredith, C.A.Reardon, J.Wang, and G.S.Getz (2008).
The specific amino acid sequence between helices 7 and 8 influences the binding specificity of human apolipoprotein A-I for high density lipoprotein (HDL) subclasses: a potential for HDL preferential generation.
  J Biol Chem, 283, 15779-15788.  
17993480 V.M.Bolanos-Garcia, A.Renault, and S.Beaufils (2008).
Surface rheology and adsorption kinetics reveal the relative amphiphilicity, interfacial activity, and stability of human exchangeable apolipoproteins.
  Biophys J, 94, 1735-1745.  
17447731 A.Chroni, G.Koukos, A.Duka, and V.I.Zannis (2007).
The carboxy-terminal region of apoA-I is required for the ABCA1-dependent formation of alpha-HDL but not prebeta-HDL particles in vivo.
  Biochemistry, 46, 5697-5708.  
17154396 C.Beaufils, C.Alexopoulos, M.P.Petraki, A.D.Tselepis, N.Coudevylle, M.Sakarellos-Daitsiotis, C.Sakarellos, and M.T.Cung (2007).
Conformational study of new amphipathic alpha-helical peptide models of apoA-I as potential atheroprotective agents.
  Biopolymers, 88, 362-372.  
17239472 I.Kratzer, K.Wernig, U.Panzenboeck, E.Bernhart, H.Reicher, R.Wronski, M.Windisch, A.Hammer, E.Malle, A.Zimmer, and W.Sattler (2007).
Apolipoprotein A-I coating of protamine-oligonucleotide nanoparticles increases particle uptake and transcytosis in an in vitro model of the blood-brain barrier.
  J Control Release, 117, 301-311.  
17554795 M.D.Benson, and J.C.Kincaid (2007).
The molecular biology and clinical features of amyloid neuropathy.
  Muscle Nerve, 36, 411-423.  
17676661 R.Draisci, C.Montesissa, B.Santamaria, C.D'Ambrosio, G.Ferretti, R.Merlanti, C.Ferranti, M.De Liguoro, C.Cartoni, E.Pistarino, L.Ferrara, M.Tiso, A.Scaloni, and M.E.Cosulich (2007).
Integrated analytical approach in veal calves administered the anabolic androgenic steroids boldenone and boldione: urine and plasma kinetic profile and changes in plasma protein expression.
  Proteomics, 7, 3184-3193.  
17563120 S.Bhat, M.G.Sorci-Thomas, R.Tuladhar, M.P.Samuel, and M.J.Thomas (2007).
Conformational adaptation of apolipoprotein A-I to discretely sized phospholipid complexes.
  Biochemistry, 46, 7811-7821.  
17676061 Z.Wu, M.A.Wagner, L.Zheng, J.S.Parks, J.M.Shy, J.D.Smith, V.Gogonea, and S.L.Hazen (2007).
The refined structure of nascent HDL reveals a key functional domain for particle maturation and dysfunction.
  Nat Struct Mol Biol, 14, 861-868.  
16452169 A.A.Ajees, G.M.Anantharamaiah, V.K.Mishra, M.M.Hussain, and H.M.Murthy (2006).
Crystal structure of human apolipoprotein A-I: insights into its protective effect against cardiovascular diseases.
  Proc Natl Acad Sci U S A, 103, 2126-2131.
PDB code: 2a01
16581834 A.Catte, J.C.Patterson, M.K.Jones, W.G.Jerome, D.Bashtovyy, Z.Su, F.Gu, J.Chen, M.P.Aliste, S.C.Harvey, L.Li, G.Weinstein, and J.P.Segrest (2006).
Novel changes in discoidal high density lipoprotein morphology: a molecular dynamics study.
  Biophys J, 90, 4345-4360.  
16891368 A.G.Rocco, L.Mollica, E.Gianazza, L.Calabresi, G.Franceschini, C.R.Sirtori, and I.Eberini (2006).
A model structure for the heterodimer apoA-IMilano-apoA-II supports its peculiar susceptibility to proteolysis.
  Biophys J, 91, 3043-3049.  
16494423 A.Y.Shih, A.Arkhipov, P.L.Freddolino, and K.Schulten (2006).
Coarse grained protein-lipid model with application to lipoprotein particles.
  J Phys Chem B, 110, 3674-3684.  
16755201 B.Shao, M.N.Oda, J.F.Oram, and J.W.Heinecke (2006).
Myeloperoxidase: an inflammatory enzyme for generating dysfunctional high density lipoprotein.
  Curr Opin Cardiol, 21, 322-328.  
16820298 D.M.Hatters, C.A.Peters-Libeu, and K.H.Weisgraber (2006).
Apolipoprotein E structure: insights into function.
  Trends Biochem Sci, 31, 445-454.  
16326917 E.Gross, D.Q.Peng, S.L.Hazen, and J.D.Smith (2006).
A novel folding intermediate state for apolipoprotein A-I: role of the amino and carboxy termini.
  Biophys J, 90, 1362-1370.  
16430220 I.N.Gorshkova, T.Liu, H.Y.Kan, A.Chroni, V.I.Zannis, and D.Atkinson (2006).
Structure and stability of apolipoprotein a-I in solution and in discoidal high-density lipoprotein probed by double charge ablation and deletion mutation.
  Biochemistry, 45, 1242-1254.  
17107880 L.Obici, G.Franceschini, L.Calabresi, S.Giorgetti, M.Stoppini, G.Merlini, and V.Bellotti (2006).
Structure, function and amyloidogenic propensity of apolipoprotein A-I.
  Amyloid, 13, 191-205.  
16680024 M.J.Thomas, S.Bhat, and M.G.Sorci-Thomas (2006).
The use of chemical cross-linking and mass spectrometry to elucidate the tertiary conformation of lipid-bound apolipoprotein A-I.
  Curr Opin Lipidol, 17, 214-220.  
16905105 N.Furnham, A.S.Doré, D.Y.Chirgadze, P.I.de Bakker, M.A.Depristo, and T.L.Blundell (2006).
Knowledge-based real-space explorations for low-resolution structure determination.
  Structure, 14, 1313-1320.  
16501936 V.I.Zannis, A.Chroni, and M.Krieger (2006).
Role of apoA-I, ABCA1, LCAT, and SR-BI in the biogenesis of HDL.
  J Mol Med, 84, 276-294.  
16905610 Y.Li, A.Z.Kijac, S.G.Sligar, and C.M.Rienstra (2006).
Structural analysis of nanoscale self-assembled discoidal lipid bilayers by solid-state NMR spectroscopy.
  Biophys J, 91, 3819-3828.  
15533924 A.Y.Shih, I.G.Denisov, J.C.Phillips, S.G.Sligar, and K.Schulten (2005).
Molecular dynamics simulations of discoidal bilayers assembled from truncated human lipoproteins.
  Biophys J, 88, 548-556.  
16852976 I.G.Denisov, M.A.McLean, A.W.Shaw, Y.V.Grinkova, and S.G.Sligar (2005).
Thermotropic phase transition in soluble nanoscale lipid bilayers.
  J Phys Chem B, 109, 15580-15588.  
15891389 O.Gursky (2005).
Apolipoprotein structure and dynamics.
  Curr Opin Lipidol, 16, 287-294.  
15891390 W.S.Davidson, and R.A.Silva (2005).
Apolipoprotein structural organization in high density lipoproteins: belts, bundles, hinges and hairpins.
  Curr Opin Lipidol, 16, 295-300.  
15558533 C.L.Murphy, S.Wang, K.Weaver, M.A.Gertz, D.T.Weiss, and A.Solomon (2004).
Renal apolipoprotein A-I amyloidosis associated with a novel mutant Leu64Pro.
  Am J Kidney Dis, 44, 1103-1109.  
15272303 E.Papagrigoriou, A.R.Gingras, I.L.Barsukov, N.Bate, I.J.Fillingham, B.Patel, R.Frank, W.H.Ziegler, G.C.Roberts, D.R.Critchley, and J.Emsley (2004).
Activation of a vinculin-binding site in the talin rod involves rearrangement of a five-helix bundle.
  EMBO J, 23, 2942-2951.
PDB codes: 1sj7 1sj8 1t01
15678758 F.J.Stevens (2004).
Amyloid formation: an emulation of matrix protein assembly?
  Amyloid, 11, 232-244.  
15234552 H.Saito, S.Lund-Katz, and M.C.Phillips (2004).
Contributions of domain structure and lipid interaction to the functionality of exchangeable human apolipoproteins.
  Prog Lipid Res, 43, 350-380.  
15333941 L.R.Alves, P.L.Oliveira, J.A.Barbosa, B.G.Guimarães, and F.J.Medrano (2004).
Crystallization and preliminary X-ray diffraction analysis of HeLp, a heme lipoprotein from the hemolymph of the cattle tick Boophilus microplus.
  Acta Crystallogr D Biol Crystallogr, 60, 1639-1640.  
15098021 M.Harel, A.Aharoni, L.Gaidukov, B.Brumshtein, O.Khersonsky, R.Meged, H.Dvir, R.B.Ravelli, A.McCarthy, L.Toker, I.Silman, J.L.Sussman, and D.S.Tawfik (2004).
Structure and evolution of the serum paraoxonase family of detoxifying and anti-atherosclerotic enzymes.
  Nat Struct Mol Biol, 11, 412-419.
PDB code: 1v04
12819519 C.Alonso-Villaverde, T.Segues, B.Coll-Crespo, R.Pérez-Bernalte, A.Rabassa, M.Gomila, S.Parra, M.A.Gozález-Esteban, M.J.Jiménez-Expósito, and L.Masana (2003).
High-density lipoprotein concentrations relate to the clinical course of HIV viral load in patients undergoing antiretroviral therapy.
  AIDS, 17, 1173-1178.  
  14986480 D.Coriu, A.Dispenzieri, F.J.Stevens, C.L.Murphy, S.Wang, D.T.Weiss, and A.Solomon (2003).
Hepatic amyloidosis resulting from deposition of the apolipoprotein A-I variant Leu75Pro.
  Amyloid, 10, 215-223.  
12754494 M.N.Oda, T.M.Forte, R.O.Ryan, and J.C.Voss (2003).
The C-terminal domain of apolipoprotein A-I contains a lipid-sensitive conformational trigger.
  Nat Struct Biol, 10, 455-460.  
12642783 Y.L.Marcel, and R.S.Kiss (2003).
Structure-function relationships of apolipoprotein A-I: a flexible protein with dynamic lipid associations.
  Curr Opin Lipidol, 14, 151-157.  
11818551 J.Wang, B.D.Sykes, and R.O.Ryan (2002).
Structural basis for the conformational adaptability of apolipophorin III, a helix-bundle exchangeable apolipoprotein.
  Proc Natl Acad Sci U S A, 99, 1188-1193.
PDB code: 1eq1
11988467 R.J.Cushley, and M.Okon (2002).
NMR studies of lipoprotein structure.
  Annu Rev Biophys Biomol Struct, 31, 177-206.  
11959505 S.Pokutta, and W.I.Weis (2002).
The cytoplasmic face of cell contact sites.
  Curr Opin Struct Biol, 12, 255-262.  
11278170 C.G.Brouillette, G.M.Anantharamaiah, J.A.Engler, and D.W.Borhani (2001).
Structural models of human apolipoprotein A-I: a critical analysis and review.
  Biochim Biophys Acta, 1531, 4.  
11266606 P.Mangione, M.Sunde, S.Giorgetti, M.Stoppini, G.Esposito, L.Gianelli, L.Obici, L.Asti, A.Andreola, P.Viglino, G.Merlini, and V.Bellotti (2001).
Amyloid fibrils derived from the apolipoprotein A1 Leu174Ser variant contain elements of ordered helical structure.
  Protein Sci, 10, 187-199.  
11325616 R.S.Kiss, R.O.Ryan, and G.A.Francis (2001).
Functional similarities of human and chicken apolipoprotein A-I: dependence on secondary and tertiary rather than primary structure.
  Biochim Biophys Acta, 1531, 251-259.  
10969027 A.E.Klon, M.K.Jones, J.P.Segrest, and S.C.Harvey (2000).
Molecular belt models for the apolipoprotein A-I Paris and Milano mutations.
  Biophys J, 79, 1679-1685.  
10828977 D.Sahoo, V.Narayanaswami, C.M.Kay, and R.O.Ryan (2000).
Pyrene excimer fluorescence: a spatially sensitive probe to monitor lipid-induced helical rearrangement of apolipophorin III.
  Biochemistry, 39, 6594-6601.  
10787171 J.P.Segrest, L.Li, G.M.Anantharamaiah, S.C.Harvey, K.N.Liadaki, and V.Zannis (2000).
Structure and function of apolipoprotein A-I and high-density lipoprotein.
  Curr Opin Lipidol, 11, 105-115.  
11087425 M.A.Tricerri, A.K.Behling Agree, S.A.Sanchez, and A.Jonas (2000).
Characterization of apolipoprotein A-I structure using a cysteine-specific fluorescence probe.
  Biochemistry, 39, 14682-14691.  
  10854214 M.M.de Sousa, C.Vital, D.Ostler, R.Fernandes, J.Pouget-Abadie, D.Carles, and M.J.Saraiva (2000).
Apolipoprotein AI and transthyretin as components of amyloid fibrils in a kindred with apoAI Leu178His amyloidosis.
  Am J Pathol, 156, 1911-1917.  
10841768 P.M.Weers, E.J.Prenner, C.Kay, and R.O.Ryan (2000).
Lipid binding of the exchangeable apolipoprotein apolipophorin III induces major changes in fluorescence properties of tryptophans 115 and 130.
  Biochemistry, 39, 6874-6880.  
10601693 V.Narayanaswami, and R.O.Ryan (2000).
Molecular basis of exchangeable apolipoprotein function.
  Biochim Biophys Acta, 1483, 15-36.  
10049304 C.Sheldahl, and S.C.Harvey (1999).
Molecular dynamics on a model for nascent high-density lipoprotein: role of salt bridges.
  Biophys J, 76, 1190-1198.  
10026251 D.L.Sparks, P.G.Frank, S.Braschi, T.A.Neville, and Y.L.Marcel (1999).
Effect of apolipoprotein A-I lipidation on the formation and function of pre-beta and alpha-migrating LpA-I particles.
  Biochemistry, 38, 1727-1735.  
10489452 D.W.Borhani, J.A.Engler, and C.G.Brouillette (1999).
Crystallization of truncated human apolipoprotein A-I in a novel conformation.
  Acta Crystallogr D Biol Crystallogr, 55, 1578-1583.  
10666577 D.W.Borhani, J.A.Engler, and C.G.Brouillette (1999).
Human apolipoprotein A-I: structure determination and analysis of unusual diffraction characteristics.
  Acta Crystallogr D Biol Crystallogr, 55, 2013-2021.  
  10487826 L.Obici, V.Bellotti, P.Mangione, M.Stoppini, E.Arbustini, L.Verga, I.Zorzoli, E.Anesi, G.Zanotti, C.Campana, M.Viganò, and G.Merlini (1999).
The new apolipoprotein A-I variant leu(174) --> Ser causes hereditary cardiac amyloidosis, and the amyloid fibrils are constituted by the 93-residue N-terminal polypeptide.
  Am J Pathol, 155, 695-702.  
  10548051 O.Gursky (1999).
Probing the conformation of a human apolipoprotein C-1 by amino acid substitutions and trimethylamine-N-oxide.
  Protein Sci, 8, 2055-2064.  
10194351 R.S.Kiss, C.M.Kay, and R.O.Ryan (1999).
Amphipathic alpha-helix bundle organization of lipid-free chicken apolipoprotein A-I.
  Biochemistry, 38, 4327-4334.  
10357827 T.Ahola, A.Lampio, P.Auvinen, and L.Kääriäinen (1999).
Semliki Forest virus mRNA capping enzyme requires association with anionic membrane phospholipids for activity.
  EMBO J, 18, 3164-3172.  
10572013 W.S.Davidson, K.Arnvig-McGuire, A.Kennedy, J.Kosman, T.L.Hazlett, and A.Jonas (1999).
Structural organization of the N-terminal domain of apolipoprotein A-I: studies of tryptophan mutants.
  Biochemistry, 38, 14387-14395.  
10089535 A.Saxena, A.Gries, R.Schwarzenbacher, G.M.Kostner, P.Laggner, and R.Prassl (1998).
Crystallization and preliminary X-ray crystallographic studies on apolipoprotein H (beta2-glycoprotein-I) from human plasma.
  Acta Crystallogr D Biol Crystallogr, 54, 1450-1452.  
9914209 C.H.Cheng (1998).
Evolution of the diverse antifreeze proteins.
  Curr Opin Genet Dev, 8, 715-720.  
9819208 M.F.Lecompte, A.C.Bras, N.Dousset, I.Portas, R.Salvayre, and M.Ayrault-Jarrier (1998).
Binding steps of apolipoprotein A-I with phospholipid monolayers: adsorption and penetration.
  Biochemistry, 37, 16165-16171.  
9753480 P.G.Frank, D.N'Guyen, V.Franklin, T.Neville, M.Desforges, E.Rassart, D.L.Sparks, and Y.L.Marcel (1998).
Importance of central alpha-helices of human apolipoprotein A-I in the maturation of high-density lipoproteins.
  Biochemistry, 37, 13902-13909.  
9665740 V.K.Mishra, M.N.Palgunachari, G.Datta, M.C.Phillips, S.Lund-Katz, S.O.Adeyeye, J.P.Segrest, and G.M.Anantharamaiah (1998).
Studies of synthetic peptides of human apolipoprotein A-I containing tandem amphipathic alpha-helixes.
  Biochemistry, 37, 10313-10324.  
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