Structural insights into mechanism and specificity of O-GlcNAc transferase - Wikidata - awgldk - TriplyDB

Structural insights into mechanism and specificity of O-GlcNAc transferase

Structural insights into mechanism and specificity of O-GlcNAc transferase

http://www.wikidata.org/entity/Q27652304

about

TET2 promotes histone O-GlcNAcylation during gene transcription Structure of human O-GlcNAc transferase and its complex with a peptide substrate Glycosyltransferase-mediated Sweet Modification in Oral Streptococci Proteolysis of HCF-1 by Ser/Thr glycosylation-incompetent O-GlcNAc transferase:UDP-GlcNAc complexes.Substrate and product analogues as human O-GlcNAc transferase inhibitors Human OGA binds substrates in a conserved peptide recognition groove Structural and Functional Analysis of a New Subfamily of Glycosyltransferases Required for Glycosylation of Serine-rich Streptococcal Adhesins Structural Insights into the Glycosyltransferase Activity of the Actinobacillus pleuropneumoniae HMW1C-like Protein O-GlcNAc transferase invokes nucleotide sugar pyrophosphate participation in catalysis Synergy of Peptide and Sugar in O-GlcNAcase Substrate Recognition Structure of a bacterial putative acetyltransferase defines the fold of the human O-GlcNAcase C-terminal domain HCF-1 Is Cleaved in the Active Site of O-GlcNAc Transferase Structure of a Novel O -Linked N -Acetyl-d-glucosamine ( O -GlcNAc) Transferase, GtfA, Reveals Insights into the Glycosylation of Pneumococcal Serine-rich Repeat Adhesins Glycomimetics Targeting Glycosyltransferases: Synthetic, Computational and Structural Studies of Less-Polar Conjugates A molecular description of cellulose biosynthesis.Evidence for a Functional O-Linked N-Acetylglucosamine (O-GlcNAc) System in the Thermophilic Bacterium Thermobaculum terrenum The putative eukaryote-like O-GlcNAc transferase of the cyanobacterium Synechococcus elongatus PCC 7942 hydrolyzes UDP-GlcNAc and is involved in multiple cellular processes.Regulation of calcium/calmodulin-dependent kinase IV by O-GlcNAc modification.Mechanistic study of CMP-Neu5Ac hydrolysis by α2,3-sialyltransferase from Pasteurella dagmatis.The hexosamine signaling pathway: O-GlcNAc cycling in feast or famine O-linked beta-N-acetylglucosamine (O-GlcNAc): Extensive crosstalk with phosphorylation to regulate signaling and transcription in response to nutrients and stress O-GlcNAc protein modification in plants: Evolution and function.The Actinobacillus pleuropneumoniae HMW1C-like glycosyltransferase mediates N-linked glycosylation of the Haemophilus influenzae HMW1 adhesin.Identification of O-GlcNAc sites within peptides of the Tau protein and their impact on phosphorylation.A novel deconvolution method for modeling UDP-N-acetyl-D-glucosamine biosynthetic pathways based on (13)C mass isotopologue profiles under non-steady-state conditions The making of a sweet modification: structure and function of O-GlcNAc transferase.Substrate specificity provides insights into the sugar donor recognition mechanism of O-GlcNAc transferase (OGT).Polycomb repressive complex 2 is necessary for the normal site-specific O-GlcNAc distribution in mouse embryonic stem cells.Cytoplasmic N-glycosyltransferase of Actinobacillus pleuropneumoniae is an inverting enzyme and recognizes the NX(S/T) consensus sequence.The active site of O-GlcNAc transferase imposes constraints on substrate sequence Cross talk between O-GlcNAcylation and phosphorylation: roles in signaling, transcription, and chronic disease.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.The roles of O-linked β-N-acetylglucosamine in cardiovascular physiology and disease.Undetectable histone O-GlcNAcylation in mammalian cells Production of homogeneous glycoprotein with multisite modifications by an engineered N-glycosyltransferase mutant.Dual functionality of O-GlcNAc transferase is required for Drosophila development.Chemical approaches to study O-GlcNAcylation.Protein O-GlcNAcylation: a new signaling paradigm for the cardiovascular system.O-GlcNAc cycling: implications for neurodegenerative disorders.The alpha,alpha-difluorinated phosphonate L-pSer-analogue: an accessible chemical tool for studying kinase-dependent signal transduction.

P2860

Q24305451-CB0E6ED5-F0AA-4D23-B7E1-11BC2A78059F Q24337218-7EFB07E1-D9E5-4203-ACBD-326F997BDE96 Q26823901-FA782D4E-0C61-415A-8493-DC51DACD7C85 Q27322397-C8BF6C60-B92E-49BD-B914-B9FAE53D0A56 Q27663568-E898FC23-EA92-46D4-99D8-F3911475F7F8 Q27664652-FE4116AD-F6C2-4185-BEC0-04AF4AC5548B Q27666270-E53F9DB6-3367-4D8C-91B9-F43BCC4B35E4 Q27673698-E76C67F5-5989-47A8-BE95-80DC114CCAEB Q27674743-A0ED7CD7-8D99-4085-8AC6-A21E1E9265FF Q27677479-B80E66F4-52E7-4719-BC1C-B45C00C84704 Q27680132-AB363BE1-4FDE-46C2-B3AE-CEF1C3119353 Q27680781-5CC2F8C6-CDBC-443F-988F-264CFD6B7F08 Q27684362-CE9E03FF-88E8-4D90-8DEA-16612EFA17AB Q27704561-218B4520-40B3-4BE9-A164-8770858DF053 Q28084652-082ADDDD-DB6D-4F29-9B1B-77E9B8D74F9A Q30380552-C5E81A60-0464-4A62-A25C-2EF5C7E248C6 Q30407892-25A89E19-DB96-48FC-B28D-FA186252F1CF Q30490721-71901E02-188A-4300-8C69-2160C546C6D2 Q30832222-7EA12F3D-74D2-4B52-AA4C-2D6B48235DAD Q33625053-6B6A0708-2647-4499-A0BD-BC337AC667D5 Q33625265-A42AAAD2-B7A3-4F86-98D8-A7F3910A9C18 Q33625578-BF325962-C594-43C9-86DD-25B119DAAAE0 Q33786797-823C26ED-F82C-4F60-A3F2-DEA904E84CFE Q33822354-6C10030B-15D0-4026-B333-46BB75DD9C69 Q33917561-CBC2C5DF-4D29-4C77-9730-8289D8A231D1 Q34683020-56D3C567-2F16-47E9-A766-6B4C3AEF4F6B Q34735104-46E1EB77-A0FD-480D-A7E5-C4E3522F71DC Q35035129-A9139A6C-65B4-4C07-A645-65E72AB4199F Q35266458-9546A9FD-8AD7-4B2B-A771-5454F586DB08 Q35735257-3F0F6BCF-F746-4A29-9A08-9CEF011C7988 Q35804446-646891F2-A413-40C7-8D94-01377A4A46CF Q35939748-D88E02FE-D4D2-4852-B864-26B5961FF311 Q35994096-42871912-84BB-4FF1-9478-D2009F379DEC Q36213044-E35ECD9F-8B13-40DF-A13D-95E534C6B755 Q36337312-BBC4362B-0DC7-4AFF-A5AA-E48AE06EE7F5 Q36435554-BC98FA5D-F245-4413-97F5-F95CC8A3898F Q36809063-26F77E8B-2CB9-4000-A6C4-EF146EBE349C Q37088282-3D867980-7635-4A40-AFA2-CECDFE9342C8 Q37376816-B8978BEE-6ED1-46F8-80CC-CE116904E8C3 Q37602835-53187006-8A9E-4E96-8A45-F7A2DB98F0EF

P2860

Structural insights into mechanism and specificity of O-GlcNAc transferase

http://www.wikidata.org/entity/Q27652304

description

2008 nî lūn-bûn

@nan

2008 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

@hyw

2008 թվականի սեպտեմբերին հրատարակված գիտական հոդված

@hy

2008年の論文

@ja

2008年論文

@yue

2008年論文

@zh-hant

2008年論文

@zh-hk

2008年論文

@zh-mo

2008年論文

@zh-tw

2008年论文

@wuu

name

Structural insights into mechanism and specificity of O-GlcNAc transferase

@ast

Structural insights into mechanism and specificity of O-GlcNAc transferase

@en

Structural insights into mechanism and specificity of O-GlcNAc transferase

@nl

type

label

Structural insights into mechanism and specificity of O-GlcNAc transferase

@ast

Structural insights into mechanism and specificity of O-GlcNAc transferase

@en

Structural insights into mechanism and specificity of O-GlcNAc transferase

@nl

prefLabel

Structural insights into mechanism and specificity of O-GlcNAc transferase

@ast

Structural insights into mechanism and specificity of O-GlcNAc transferase

@en

Structural insights into mechanism and specificity of O-GlcNAc transferase

@nl

P1433

Q27652304-021F6D06-CB10-4980-A2A7-B1A6C1CD96FF

P1476

Q27652304-BA25BE09-3A25-49CE-BE87-5E902928E81C

P2093

Q27652304-2139D835-E3F8-41F7-8F1D-DDA7F685A7BE

Q27652304-2A34CDB8-DAD7-448E-99DC-04B7C76FCAF0

Q27652304-3258280B-4DD6-4520-96DA-2766344190CA

Q27652304-32C2D3CA-C4FA-412C-B556-A0B9A2E6AE1D

Q27652304-9E2D5D15-20CC-48DA-A779-7B29FAA2449E

Q27652304-A7761CE9-7D5C-45AD-BCE4-24DC3785BB0B

Q27652304-BEA1D6D4-BB53-4085-BCC4-8CC8A6487AA4

Q27652304-D935D236-FDBC-4E50-8317-34BA167D38EB

P2860

Q27652304-09A1564B-7FA1-4CEF-8F0D-7512C03799ED

Q27652304-0D4BB5F6-8E93-471D-87EE-C6D3D3C4E7B0

Q27652304-17364437-B01E-4CC4-9EDD-4E9C755257D9

Q27652304-1ADD5790-3EFB-4BE3-A1C7-0B5A395EABB2

Q27652304-1C6E4623-593B-45C2-A632-3B026147E9C9

Q27652304-202BE1E6-BE2E-4B9E-8357-7BCC788AA256

Q27652304-2A56D051-7B81-400D-AD20-B4DD99FBABFA

Q27652304-30E14532-D8A8-434E-8356-D7FD3ADFA0F6

Q27652304-42E35583-3A4B-46B4-9F59-97D248343F7A

Q27652304-44AB0742-C049-450F-8211-5CE4740749C7

P304

Q27652304-773F89C2-09A3-4DC3-A94C-48DFCA959D88

P31

Q27652304-DF1754F4-E8DC-4716-8AB7-3BB38C221CFA

P356

Q27652304-C11BD381-0DA6-4455-8C9A-9D29DD13ABA9

P407

Q27652304-B7B49295-6274-4D0D-ADD4-C2A1097FD9B4

P433

Q27652304-8F85BC9A-1906-4C8A-9746-E8DBD8DFEEEA

P478

Q27652304-0B1084C6-321A-440B-8BD9-DB2F965BFA1B

P50

Q27652304-7A041B7C-3F8B-437B-BEA0-A89138691F81

P577

Q27652304-9E91DA7A-970F-4425-BFF5-46483057B9B7

P5875

Q27652304-285972DB-AFFE-401A-BC50-2331CA15B927

P698

Q27652304-1909D203-2C73-4A71-9880-3F56401DF268

P932

Q27652304-C9FF2460-43B5-49DE-98CA-14462BB86997

P356

P1433

The EMBO Journal

P1476

Structural insights into mechanism and specificity of O-GlcNAc transferase

@en

P2093

Adel F M Ibrahim

http://www.w3.org/2001/XMLSchema#string

Alexander W Schüttelkopf

http://www.w3.org/2001/XMLSchema#string

Andrew J Clarke

http://www.w3.org/2001/XMLSchema#string

Daan M F van Aalten

http://www.w3.org/2001/XMLSchema#string

Ramon Hurtado-Guerrero

http://www.w3.org/2001/XMLSchema#string

Shalini Pathak

http://www.w3.org/2001/XMLSchema#string

Sharon M Shepherd

http://www.w3.org/2001/XMLSchema#string

Vladimir Borodkin

http://www.w3.org/2001/XMLSchema#string

P2860

Dynamic O-glycosylation of nuclear and cytosolic proteins: cloning and characterization of a neutral, cytosolic beta-N-acetylglucosaminidase from human brain

Dynamic glycosylation of nuclear and cytosolic proteins. Cloning and characterization of a unique O-GlcNAc transferase with multiple tetratricopeptide repeats

O-Linked GlcNAc transferase is a conserved nucleocytoplasmic protein containing tetratricopeptide repeats

Phosphoinositide signalling links O-GlcNAc transferase to insulin resistance

Crystal structure of the MurG:UDP-GlcNAc complex reveals common structural principles of a superfamily of glycosyltransferases

Crystal structures of the T4 phage beta-glucosyltransferase and the D100A mutant in complex with UDP-glucose: glucose binding and identification of the catalytic base for a direct displacement mechanism

SOLVE and RESOLVE: automated structure solution and density modification

Coot: model-building tools for molecular graphics

Protein structure comparison by alignment of distance matrices

Refinement of macromolecular structures by the maximum-likelihood method

P304

2780-2788

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1038/EMBOJ.2008.186

http://www.w3.org/2001/XMLSchema#string

P407

P433

20

http://www.w3.org/2001/XMLSchema#string

P478

27

http://www.w3.org/2001/XMLSchema#string

P50

Ramon Hurtado-Guerrero

P577

2008-09-25T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

23281909

http://www.w3.org/2001/XMLSchema#string

P698

18818698

http://www.w3.org/2001/XMLSchema#string

P932

2556091

http://www.w3.org/2001/XMLSchema#string