HCF-1 Is Cleaved in the Active Site of O-GlcNAc Transferase

scientific article

HCF-1 Is Cleaved in the Active Site of O-GlcNAc Transferase is …
instance of (P31):
scholarly articleQ13442814

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P356DOI10.1126/SCIENCE.1243990
P3181OpenCitations bibliographic resource ID4516611
P932PMC publication ID3930058
P698PubMed publication ID24311690

P50authorWinship HerrQ37382359
David J VocadloQ42410535
Michael B LazarusQ55404762
John JanetzkoQ58330914
Vaibhav KapuriaQ59698646
Tanja BhuiyanQ114423743
P2093author name stringJiaoyang Jiang
Suzanne Walker
Wesley F Zandberg
P2860cites workInteins: structure, function, and evolutionQ34762743
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Dynamic glycosylation of nuclear and cytosolic proteins. Cloning and characterization of a unique O-GlcNAc transferase with multiple tetratricopeptide repeatsQ24310656
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Structure of human O-GlcNAc transferase and its complex with a peptide substrateQ24337218
Crosstalk between O-GlcNAcylation and proteolytic cleavage regulates the host cell factor-1 maturation pathwayQ24338891
O-GlcNAc transferase catalyzes site-specific proteolysis of HCF-1Q24339060
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Structure of an O-GlcNAc transferase homolog provides insight into intracellular glycosylationQ27650768
Structural insights into mechanism and specificity of O-GlcNAc transferaseQ27652304
Structural snapshots of the reaction coordinate for O-GlcNAc transferaseQ27674735
O-GlcNAc transferase invokes nucleotide sugar pyrophosphate participation in catalysisQ27674743
A neutral diphosphate mimic crosslinks the active site of human O-GlcNAc transferaseQ27675565
Optimal description of a protein structure in terms of multiple groups undergoing TLS motionQ27860825
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Features and development of CootQ27861079
Scaling and assessment of data qualityQ27861107
Functional expression of O-linked GlcNAc transferase. Domain structure and substrate specificityQ28141169
The HCF repeat is an unusual proteolytic cleavage signalQ28291563
Cycling of O-linked beta-N-acetylglucosamine on nucleocytoplasmic proteinsQ28299550
Regulation of a cytosolic and nuclear O-GlcNAc transferase. Role of the tetratricopeptide repeatsQ28581400
Collaboration gets the most out of softwareQ28680770
electronic Ligand Builder and Optimization Workbench (eLBOW): a tool for ligand coordinate and restraint generationQ29617258
Glycosylation of nucleocytoplasmic proteins: signal transduction and O-GlcNAcQ33939701
Roles of the Tetratricopeptide Repeat Domain in O-GlcNAc Transferase Targeting and Protein Substrate SpecificityQ34193954
The herpes simplex virus VP16-induced complex: the makings of a regulatory switchQ34208918
The superhelical TPR-repeat domain of O-linked GlcNAc transferase exhibits structural similarities to importin alphaQ34347600
P433issue6163
P407language of work or nameEnglishQ1860
P1104number of pages5
P304page(s)1235-1239
P577publication date2013-12-01
P1433published inScienceQ192864
P1476titleHCF-1 is cleaved in the active site of O-GlcNAc transferase
P478volume342

Reverse relations

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