Document Detail


Histone-modifying enzymes: their role in the pathogenesis of acute leukemia and their therapeutic potential.
MedLine Citation:
PMID:  23288492     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Histone-modifying enzymes have recently been shown to play a central role in the regulation of both normal and malignant hematopoiesis. Post-translational modifications of histones and non-histone proteins underlies a regulatory complexity affecting numerous processes including transcriptional regulation, RNA processing and DNA damage response. Insights into the functions of these enzymes as well as their role in the epigenetic alterations found in leukemia will guide the development of novel therapeutic approaches. This review discusses examples of the proteins that have been implicated in the pathogenesis of leukemia, that may serve as potential therapeutic targets.
Authors:
Ly P Vu; Luisa Luciani; Stephen D Nimer
Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't; Review     Date:  2013-01-04
Journal Detail:
Title:  International journal of hematology     Volume:  97     ISSN:  1865-3774     ISO Abbreviation:  Int. J. Hematol.     Publication Date:  2013 Feb 
Date Detail:
Created Date:  2013-02-22     Completed Date:  2013-11-15     Revised Date:  2014-06-16    
Medline Journal Info:
Nlm Unique ID:  9111627     Medline TA:  Int J Hematol     Country:  Japan    
Other Details:
Languages:  eng     Pagination:  198-209     Citation Subset:  IM    
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MeSH Terms
Descriptor/Qualifier:
Animals
Histone Acetyltransferases / metabolism*
Histone Deacetylases / metabolism*
Histones / chemistry,  metabolism*
Humans
Leukemia / drug therapy,  enzymology,  metabolism
Methylation
Phosphorylation
Protein Interaction Domains and Motifs
Protein Methyltransferases / metabolism*
Grant Support
ID/Acronym/Agency:
R01//PHS HHS; R01 CA166835/CA/NCI NIH HHS
Chemical
Reg. No./Substance:
0/Histones; EC 2.1.1.-/Protein Methyltransferases; EC 2.3.1.48/Histone Acetyltransferases; EC 3.5.1.98/Histone Deacetylases

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


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