Structure of a bacterial putative acetyltransferase defines the fold of the human O-GlcNAcase C-terminal domain
Published 2013 View Full Article
- Home
- Publications
- Publication Search
- Publication Details
Title
Structure of a bacterial putative acetyltransferase defines the fold of the human O-GlcNAcase C-terminal domain
Authors
Keywords
-
Journal
Open Biology
Volume 3, Issue 10, Pages 130021-130021
Publisher
The Royal Society
Online
2013-10-03
DOI
10.1098/rsob.130021
References
Ask authors/readers for more resources
Related references
Note: Only part of the references are listed.- Synergy of Peptide and Sugar in O-GlcNAcase Substrate Recognition
- (2012) Marianne Schimpl et al. CHEMISTRY & BIOLOGY
- Structural snapshots of the reaction coordinate for O-GlcNAc transferase
- (2012) Michael B Lazarus et al. Nature Chemical Biology
- O-GlcNAc transferase invokes nucleotide sugar pyrophosphate participation in catalysis
- (2012) Marianne Schimpl et al. Nature Chemical Biology
- Overview of theCCP4 suite and current developments
- (2011) Martyn D. Winn et al. ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
- Structure of a Ternary Naa50p (NAT5/SAN) N-terminal Acetyltransferase Complex Reveals the Molecular Basis for Substrate-specific Acetylation
- (2011) Glen Liszczak et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Structure of human O-GlcNAc transferase and its complex with a peptide substrate
- (2011) Michael B. Lazarus et al. NATURE
- Experimental phasing withSHELXC/D/E: combining chain tracing with density modification
- (2010) George M. Sheldrick ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
- Features and development ofCoot
- (2010) P. Emsley et al. ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
- Exploring minimal biotinylation conditions for biosensor analysis using capture chips
- (2010) Giuseppe Papalia et al. ANALYTICAL BIOCHEMISTRY
- Human OGA binds substrates in a conserved peptide recognition groove
- (2010) Marianne Schimpl et al. BIOCHEMICAL JOURNAL
- -N-acetylglucosamine (O-GlcNAc) is part of the histone code
- (2010) K. Sakabe et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- ALINE: a WYSIWYG protein-sequence alignment editor for publication-quality alignments
- (2009) Charles Simon Bond et al. ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
- Structural insights into mechanism and specificity of O-GlcNAc transferase
- (2008) Andrew J Clarke et al. EMBO JOURNAL
- Characterization of β-N-Acetylglucosaminidase Cleavage by Caspase-3 during Apoptosis
- (2008) Chutikarn Butkinaree et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- A potent mechanism-inspired O-GlcNAcase inhibitor that blocks phosphorylation of tau in vivo
- (2008) Scott A Yuzwa et al. Nature Chemical Biology
- Automated macromolecular model building for X-ray crystallography using ARP/wARP version 7
- (2008) Gerrit Langer et al. Nature Protocols
- Structure of an O-GlcNAc transferase homolog provides insight into intracellular glycosylation
- (2008) Carlos Martinez-Fleites et al. NATURE STRUCTURAL & MOLECULAR BIOLOGY
- The Jpred 3 secondary structure prediction server
- (2008) C. Cole et al. NUCLEIC ACIDS RESEARCH
- The Carbohydrate-Active EnZymes database (CAZy): an expert resource for Glycogenomics
- (2008) B. L. Cantarel et al. NUCLEIC ACIDS RESEARCH
- Cross-talk between GlcNAcylation and phosphorylation: Site-specific phosphorylation dynamics in response to globally elevated O-GlcNAc
- (2008) Z. Wang et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Crystal structure of RimI fromSalmonella typhimurium LT2, the GNAT responsible for Nα-acetylation of ribosomal protein S18
- (2008) Matthew W. Vetting et al. PROTEIN SCIENCE
Create your own webinar
Interested in hosting your own webinar? Check the schedule and propose your idea to the Peeref Content Team.
Create NowAsk a Question. Answer a Question.
Quickly pose questions to the entire community. Debate answers and get clarity on the most important issues facing researchers.
Get Started