Articles - 2cbi mentioned but not cited (3)
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- Synthesis of New Hydrophilic and Hydrophobic Cobinamides as NO-Independent sGC Activators. Proinsias KÓ, Giedyk M, Sharina IG, Martin E, Gryko D. ACS Med Chem Lett 3 476-479 (2012)
Reviews citing this publication (30)
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- Molecular mechanisms of O-GlcNAcylation. Hurtado-Guerrero R, Dorfmueller HC, van Aalten DM. Curr. Opin. Struct. Biol. 18 551-557 (2008)
- O-GlcNAc transferase and O-GlcNAcase: achieving target substrate specificity. Nagel AK, Ball LE. Amino Acids 46 2305-2316 (2014)
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- Chemical approaches to study O-GlcNAcylation. Banerjee PS, Hart GW, Cho JW. Chem Soc Rev 42 4345-4357 (2013)
- Deciphering the Functions of Protein O-GlcNAcylation with Chemistry. Worth M, Li H, Jiang J. ACS Chem Biol 12 326-335 (2017)
- Chemical tools to probe cellular O-GlcNAc signalling. Ostrowski A, van Aalten DM. Biochem. J. 456 1-12 (2013)
- Tools for probing and perturbing O-GlcNAc in cells and in vivo. Cecioni S, Vocadlo DJ. Curr Opin Chem Biol 17 719-728 (2013)
- O-GlcNAcase: promiscuous hexosaminidase or key regulator of O-GlcNAc signaling? Alonso J, Schimpl M, van Aalten DM. J. Biol. Chem. 289 34433-34439 (2014)
- Chemical arsenal for the study of O-GlcNAc. Kim EJ. Molecules 16 1987-2022 (2011)
- Structural characterization of the O-GlcNAc cycling enzymes: insights into substrate recognition and catalytic mechanisms. Joiner CM, Li H, Jiang J, Walker S. Curr Opin Struct Biol 56 97-106 (2019)
- Critical observations that shaped our understanding of the function(s) of intracellular glycosylation (O-GlcNAc). Zachara NE. FEBS Lett. 592 3950-3975 (2018)
- Molecular Interrogation to Crack the Case of O-GlcNAc. Estevez A, Zhu D, Blankenship C, Jiang J. Chemistry 26 12086-12100 (2020)
- Tools for functional dissection of site-specific O-GlcNAcylation. Gorelik A, van Aalten DMF. RSC Chem Biol 1 98-109 (2020)
- Demystifying O-GlcNAcylation: hints from peptide substrates. Shi J, Ruijtenbeek R, Pieters RJ. Glycobiology 28 814-824 (2018)
- In Vitro Biochemical Assays for O-GlcNAc-Processing Enzymes. Kim EJ. Chembiochem 18 1462-1472 (2017)
- Integration of O-GlcNAc into Stress Response Pathways. Fahie KMM, Papanicolaou KN, Zachara NE. Cells 11 3509 (2022)
- Role and Function of O-GlcNAcylation in Cancer. Lee JB, Pyo KH, Kim HR. Cancers (Basel) 13 5365 (2021)
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Articles citing this publication (86)
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- The permeability of reconstituted nuclear pores provides direct evidence for the selective phase model. Hülsmann BB, Labokha AA, Görlich D. Cell 150 738-751 (2012)
- Structure and mechanism of a bacterial beta-glucosaminidase having O-GlcNAcase activity. Dennis RJ, Taylor EJ, Macauley MS, Stubbs KA, Turkenburg JP, Hart SJ, Black GN, Vocadlo DJ, Davies GJ. Nat. Struct. Mol. Biol. 13 365-371 (2006)
- GlcNAcstatin: a picomolar, selective O-GlcNAcase inhibitor that modulates intracellular O-glcNAcylation levels. Dorfmueller HC, Borodkin VS, Schimpl M, Shepherd SM, Shpiro NA, van Aalten DM. J Am Chem Soc 128 16484-16485 (2006)
- Elevation of global O-GlcNAc levels in 3T3-L1 adipocytes by selective inhibition of O-GlcNAcase does not induce insulin resistance. Macauley MS, Bubb AK, Martinez-Fleites C, Davies GJ, Vocadlo DJ. J. Biol. Chem. 283 34687-34695 (2008)
- Glucose and glutamine fuel protein O-GlcNAcylation to control T cell self-renewal and malignancy. Swamy M, Pathak S, Grzes KM, Damerow S, Sinclair LV, van Aalten DM, Cantrell DA. Nat. Immunol. 17 712-720 (2016)
- O-GlcNAcylation of TAB1 modulates TAK1-mediated cytokine release. Pathak S, Borodkin VS, Albarbarawi O, Campbell DG, Ibrahim A, van Aalten DM. EMBO J. 31 1394-1404 (2012)
- A lipid-droplet-targeted O-GlcNAcase isoform is a key regulator of the proteasome. Keembiyehetty CN, Krzeslak A, Love DC, Hanover JA. J. Cell. Sci. 124 2851-2860 (2011)
- Insights into O-linked N-acetylglucosamine ([0-9]O-GlcNAc) processing and dynamics through kinetic analysis of O-GlcNAc transferase and O-GlcNAcase activity on protein substrates. Shen DL, Gloster TM, Yuzwa SA, Vocadlo DJ. J. Biol. Chem. 287 15395-15408 (2012)
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- Structural determinants of an insect beta-N-Acetyl-D-hexosaminidase specialized as a chitinolytic enzyme. Liu T, Zhang H, Liu F, Wu Q, Shen X, Yang Q. J. Biol. Chem. 286 4049-4058 (2011)
- Nutrient-driven O-GlcNAc cycling - think globally but act locally. Harwood KR, Hanover JA. J. Cell. Sci. 127 1857-1867 (2014)
- Removal of Abnormal Myofilament O-GlcNAcylation Restores Ca2+ Sensitivity in Diabetic Cardiac Muscle. Ramirez-Correa GA, Ma J, Slawson C, Zeidan Q, Lugo-Fagundo NS, Xu M, Shen X, Gao WD, Caceres V, Chakir K, DeVine L, Cole RN, Marchionni L, Paolocci N, Hart GW, Murphy AM. Diabetes 64 3573-3587 (2015)
- Human OGA binds substrates in a conserved peptide recognition groove. Schimpl M, Schüttelkopf AW, Borodkin VS, van Aalten DM. Biochem. J. 432 1-7 (2010)
- Insight into a strategy for attenuating AmpC-mediated beta-lactam resistance: structural basis for selective inhibition of the glycoside hydrolase NagZ. Balcewich MD, Stubbs KA, He Y, James TW, Davies GJ, Vocadlo DJ, Mark BL. Protein Sci. 18 1541-1551 (2009)
- Structure of N-acetyl-beta-D-glucosaminidase (GcnA) from the endocarditis pathogen Streptococcus gordonii and its complex with the mechanism-based inhibitor NAG-thiazoline. Langley DB, Harty DW, Jacques NA, Hunter N, Guss JM, Collyer CA. J. Mol. Biol. 377 104-116 (2008)
- Synergy of peptide and sugar in O-GlcNAcase substrate recognition. Schimpl M, Borodkin VS, Gray LJ, van Aalten DM. Chem. Biol. 19 173-178 (2012)
- Functional analysis of a group A streptococcal glycoside hydrolase Spy1600 from family 84 reveals it is a beta-N-acetylglucosaminidase and not a hyaluronidase. Sheldon WL, Macauley MS, Taylor EJ, Robinson CE, Charnock SJ, Davies GJ, Vocadlo DJ, Black GW. Biochem. J. 399 241-247 (2006)
- Mechanism, Structure, and Inhibition of O-GlcNAc Processing Enzymes. Gloster TM, Vocadlo DJ. Curr Signal Transduct Ther 5 74-91 (2010)
- Substrate and product analogues as human O-GlcNAc transferase inhibitors. Dorfmueller HC, Borodkin VS, Blair DE, Pathak S, Navratilova I, van Aalten DM. Amino Acids 40 781-792 (2011)
- Comparative Proteomics Reveals Dysregulated Mitochondrial O-GlcNAcylation in Diabetic Hearts. Ma J, Banerjee P, Whelan SA, Liu T, Wei AC, Ramirez-Correa G, McComb ME, Costello CE, O'Rourke B, Murphy A, Hart GW. J Proteome Res 15 2254-2264 (2016)
- Chemical dissection of the link between streptozotocin, O-GlcNAc, and pancreatic cell death. Pathak S, Dorfmueller HC, Borodkin VS, van Aalten DM. Chem. Biol. 15 799-807 (2008)
- Inhibition of O-GlcNAcase by a gluco-configured nagstatin and a PUGNAc-imidazole hybrid inhibitor. Shanmugasundaram B, Debowski AW, Dennis RJ, Davies GJ, Vocadlo DJ, Vasella A. Chem. Commun. (Camb.) 4372-4374 (2006)
- Sph3 Is a Glycoside Hydrolase Required for the Biosynthesis of Galactosaminogalactan in Aspergillus fumigatus. Bamford NC, Snarr BD, Gravelat FN, Little DJ, Lee MJ, Zacharias CA, Chabot JC, Geller AM, Baptista SD, Baker P, Robinson H, Howell PL, Sheppard DC. J. Biol. Chem. 290 27438-27450 (2015)
- Structure of a bacterial putative acetyltransferase defines the fold of the human O-GlcNAcase C-terminal domain. Rao FV, Schüttelkopf AW, Dorfmueller HC, Ferenbach AT, Navratilova I, van Aalten DM. Open Biol 3 130021 (2013)
- Gaining insight into the inhibition of glycoside hydrolase family 20 exo-β-N-acetylhexosaminidases using a structural approach. Sumida T, Stubbs KA, Ito M, Yokoyama S. Org. Biomol. Chem. 10 2607-2612 (2012)
- N-acetylglucosamine recognition by a family 32 carbohydrate-binding module from Clostridium perfringens NagH. Ficko-Blean E, Boraston AB. J. Mol. Biol. 390 208-220 (2009)
- Active-pocket size differentiating insectile from bacterial chitinolytic β-N-acetyl-D-hexosaminidases. Liu T, Zhang H, Liu F, Chen L, Shen X, Yang Q. Biochem. J. 438 467-474 (2011)
- Portrait of an enzyme, a complete structural analysis of a multimodular {beta}-N-acetylglucosaminidase from Clostridium perfringens. Ficko-Blean E, Gregg KJ, Adams JJ, Hehemann JH, Czjzek M, Smith SP, Boraston AB. J. Biol. Chem. 284 9876-9884 (2009)
- Cloning and comparison of phylogenetically related chitinases from Listeria monocytogenes EGD and Enterococcus faecalis V583. Leisner JJ, Larsen MH, Ingmer H, Petersen BO, Duus JØ, Palcic MM. J. Appl. Microbiol. 107 2080-2087 (2009)
- Structural and functional insight into human O-GlcNAcase. Roth C, Chan S, Offen WA, Hemsworth GR, Willems LI, King DT, Varghese V, Britton R, Vocadlo DJ, Davies GJ. Nat. Chem. Biol. 13 610-612 (2017)
- A 1-acetamido derivative of 6-epi-valienamine: an inhibitor of a diverse group of beta-N-acetylglucosaminidases. Scaffidi A, Stubbs KA, Dennis RJ, Taylor EJ, Davies GJ, Vocadlo DJ, Stick RV. Org. Biomol. Chem. 5 3013-3019 (2007)
- Three-dimensional structure of a putative non-cellulosomal cohesin module from a Clostridium perfringens family 84 glycoside hydrolase. Chitayat S, Gregg K, Adams JJ, Ficko-Blean E, Bayer EA, Boraston AB, Smith SP. J. Mol. Biol. 375 20-28 (2008)
- Crystal structures of a glycoside hydrolase family 20 lacto-N-biosidase from Bifidobacterium bifidum. Ito T, Katayama T, Hattie M, Sakurama H, Wada J, Suzuki R, Ashida H, Wakagi T, Yamamoto K, Stubbs KA, Fushinobu S. J. Biol. Chem. 288 11795-11806 (2013)
- Insights into activity and inhibition from the crystal structure of human O-GlcNAcase. Elsen NL, Patel SB, Ford RE, Hall DL, Hess F, Kandula H, Kornienko M, Reid J, Selnick H, Shipman JM, Sharma S, Lumb KJ, Soisson SM, Klein DJ. Nat. Chem. Biol. 13 613-615 (2017)
- Structures of human O-GlcNAcase and its complexes reveal a new substrate recognition mode. Li B, Li H, Lu L, Jiang J. Nat. Struct. Mol. Biol. 24 362-369 (2017)
- Dual functionality of O-GlcNAc transferase is required for Drosophila development. Mariappa D, Zheng X, Schimpl M, Raimi O, Ferenbach AT, Müller HA, van Aalten DM. Open Biol 5 150234 (2015)
- A mutant O-GlcNAcase enriches Drosophila developmental regulators. Selvan N, Williamson R, Mariappa D, Campbell DG, Gourlay R, Ferenbach AT, Aristotelous T, Hopkins-Navratilova I, Trost M, van Aalten DMF. Nat. Chem. Biol. 13 882-887 (2017)
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- Metabolism of vertebrate amino sugars with N-glycolyl groups: intracellular β-O-linked N-glycolylglucosamine (GlcNGc), UDP-GlcNGc, and the biochemical and structural rationale for the substrate tolerance of β-O-linked β-N-acetylglucosaminidase. Macauley MS, Chan J, Zandberg WF, He Y, Whitworth GE, Stubbs KA, Yuzwa SA, Bennet AJ, Varki A, Davies GJ, Vocadlo DJ. J. Biol. Chem. 287 28882-28897 (2012)
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- Evidence for a Functional O-Linked N-Acetylglucosamine (O-GlcNAc) System in the Thermophilic Bacterium Thermobaculum terrenum. Ostrowski A, Gundogdu M, Ferenbach AT, Lebedev AA, van Aalten DM. J. Biol. Chem. 290 30291-30305 (2015)
- Expression, characterization and homology modeling of a novel eukaryotic GH84 β-N-acetylglucosaminidase from Penicillium chrysogenum. Slámová K, Kulik N, Fiala M, Krejzová-Hofmeisterová J, Ettrich R, Křen V. Protein Expr. Purif. 95 204-210 (2014)
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- Synthesis of 2-amido, 2-amino, and 2-azido derivatives of the nitrogen analogue of the naturally occurring glycosidase inhibitor salacinol and their inhibitory activities against O-GlcNAcase and NagZ enzymes. Choubdar N, Bhat RG, Stubbs KA, Yuzwa S, Pinto BM. Carbohydr. Res. 343 1766-1777 (2008)
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- Probing the Catalytic Mechanism of Vibrio harveyi GH20 β-N-Acetylglucosaminidase by Chemical Rescue. Meekrathok P, Suginta W. PLoS ONE 11 e0149228 (2016)
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- Type II Secretion Substrates of Legionella pneumophila Translocate Out of the Pathogen-Occupied Vacuole via a Semipermeable Membrane. Truchan HK, Christman HD, White RC, Rutledge NS, Cianciotto NP. MBio 8 (2017)
- Gaining insight into the catalysis by GH20 lacto-N-biosidase using small molecule inhibitors and structural analysis. Hattie M, Ito T, Debowski AW, Arakawa T, Katayama T, Yamamoto K, Fushinobu S, Stubbs KA. Chem. Commun. (Camb.) 51 15008-15011 (2015)
- Loss of O-GlcNAcase catalytic activity leads to defects in mouse embryogenesis. Muha V, Authier F, Szoke-Kovacs Z, Johnson S, Gallagher J, McNeilly A, McCrimmon RJ, Teboul L, van Aalten DMF. J Biol Chem 296 100439 (2021)
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- O-GlcNAcase Fragment Discovery with Fluorescence Polarimetry. Borodkin VS, Rafie K, Selvan N, Aristotelous T, Navratilova I, Ferenbach AT, van Aalten DMF. ACS Chem Biol 13 1353-1360 (2018)
- Protein-ligand interaction study of CpOGA in complex with GlcNAcstatin. Sousa PR, de Alencar NA, Lima AH, Lameira J, Alves CN. Chem Biol Drug Des 81 284-290 (2013)
- Recognition of diazirine-modified O-GlcNAc by human O-GlcNAcase. Rodriguez AC, Kohler JJ. Medchemcomm 5 1227-1234 (2014)
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- Defining the structural origin of the substrate sequence independence of O-GlcNAcase using a combination of molecular docking and dynamics simulation. Martin JC, Fadda E, Ito K, Woods RJ. Glycobiology 24 85-96 (2014)
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- Dual-specificity RNA aptamers enable manipulation of target-specific O-GlcNAcylation and unveil functions of O-GlcNAc on β-catenin. Zhu Y, Hart GW. Cell 186 428-445.e27 (2023)
- Dynamic changes in O-GlcNAcylation regulate osteoclast differentiation and bone loss via nucleoporin 153. Li YN, Chen CW, Trinh-Minh T, Zhu H, Matei AE, Györfi AH, Kuwert F, Hubel P, Ding X, Manh CT, Xu X, Liebel C, Fedorchenko V, Liang R, Huang K, Pfannstiel J, Huang MC, Lin NY, Ramming A, Schett G, Distler JHW. Bone Res 10 51 (2022)
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- Identification of a specific inhibitor of nOGA - a caspase-3 cleaved O-GlcNAcase variant during apoptosis. Li J, Li Z, Li T, Lin L, Zhang Y, Guo L, Xu Y, Zhao W, Wang P. Biochemistry Mosc. 77 194-200 (2012)
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- O-GlcNAcase contributes to cognitive function in Drosophila. Muha V, Fenckova M, Ferenbach AT, Catinozzi M, Eidhof I, Storkebaum E, Schenck A, van Aalten DMF. J Biol Chem 295 8636-8646 (2020)
- Analysis of transition state mimicry by tight binding aminothiazoline inhibitors provides insight into catalysis by human O-GlcNAcase. Cekic N, Heinonen JE, Stubbs KA, Roth C, He Y, Bennet AJ, McEachern EJ, Davies GJ, Vocadlo DJ. Chem Sci 7 3742-3750 (2016)
- Characterization of a phospholipid-regulated β-galactosidase from Akkermansia muciniphila involved in mucin degradation. Kosciow K, Deppenmeier U. Microbiologyopen 8 e00796 (2019)
- Computational Studies on the Potency and Selectivity of PUGNAc Derivatives Against GH3, GH20, and GH84 β-N-acetyl-D-hexosaminidases. Dong L, Shen S, Xu Y, Wang L, Feng R, Zhang J, Lu H. Front Chem 7 235 (2019)
- Loss of CRMP2 O-GlcNAcylation leads to reduced novel object recognition performance in mice. Muha V, Williamson R, Hills R, McNeilly AD, McWilliams TG, Alonso J, Schimpl M, Leney AC, Heck AJR, Sutherland C, Read KD, McCrimmon RJ, Brooks SP, van Aalten DMF. Open Biol 9 190192 (2019)
- Native detection of protein O-GlcNAcylation by gel electrophoresis. Fu C, van Aalten DMF. Analyst 145 6826-6830 (2020)
- O-GlcNAc transferase promotes the nuclear localization of the focal adhesion-associated protein Zyxin to regulate UV-induced cell death. Zhao Y, Yue S, Zhou X, Guo J, Ma S, Chen Q. J Biol Chem 298 101776 (2022)
- Structural and functional characterization of a multi-domain GH92 α-1,2-mannosidase from Neobacillus novalis. Kołaczkowski BM, Moroz OV, Blagova E, Davies GJ, Møller MS, Meyer AS, Westh P, Jensen K, Wilson KS, Krogh KBRM. Acta Crystallogr D Struct Biol 79 387-400 (2023)
- Structural insights of the enzymes from the chitin utilization locus of Flavobacterium johnsoniae. Mazurkewich S, Helland R, Mackenzie A, Eijsink VGH, Pope PB, Brändén G, Larsbrink J. Sci Rep 10 13775 (2020)