Document Detail


Expanding chemical biology of 2-oxoglutarate oxygenases.
MedLine Citation:
PMID:  18277970     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Beyond established roles in collagen biosynthesis, hypoxic signaling and fatty acid metabolism, recent reports have now revealed roles for human 2-oxoglutarate-dependent oxygenases in histone and nucleic acid demethylation and in signaling protein hydroxylation. The emerging role of these oxygenases in enabling a multiplicity of histone modifications has some analogy with their role in enabling structural diversity in secondary metabolism.
Authors:
Christoph Loenarz; Christopher J Schofield
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Nature chemical biology     Volume:  4     ISSN:  1552-4469     ISO Abbreviation:  Nat. Chem. Biol.     Publication Date:  2008 Mar 
Date Detail:
Created Date:  2008-02-18     Completed Date:  2008-09-02     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  101231976     Medline TA:  Nat Chem Biol     Country:  United States    
Other Details:
Languages:  eng     Pagination:  152-6     Citation Subset:  IM    
Affiliation:
Chemistry Research Laboratory and the Oxford Centre for Integrative Systems Biology, Mansfield Road, Oxford OX1 3TA, UK. christopher.schofield@chem.ox.ac.uk
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MeSH Terms
Descriptor/Qualifier:
Animals
Catalysis
Histones / chemistry,  physiology
Humans
Hydroxylation
Ketoglutaric Acids / metabolism*
Methylation
Models, Molecular
Nucleic Acids / chemical synthesis,  chemistry
Oxidation-Reduction
Oxygenases / chemistry*,  physiology*
Proteins / chemistry,  physiology
Signal Transduction / physiology
Stereoisomerism
Grant Support
ID/Acronym/Agency:
//Wellcome Trust
Chemical
Reg. No./Substance:
0/Histones; 0/Ketoglutaric Acids; 0/Nucleic Acids; 0/Proteins; 328-50-7/alpha-ketoglutaric acid; EC 1.13.-/Oxygenases

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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