Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
2005-11-3
pubmed:abstractText
The "histone code" is comprised of the covalent modifications of histone tails that function to regulate gene transcription. The post-translational modifications that occur in histones within the regulatory regions of genes include acetylation, methylation, phosphorylation, ubiquitination, sumoylation, and ADP-ribosylation. These modifications serve to alter chromatin structure and accessibility, and to act as docking sites for transcription factors or other histone modifying enzymes. Several of the factors that are disrupted by chromosomal translocations associated with hematological malignancies can alter the histone code in a gene-specific manner. Here, we discuss how the histone code may be disrupted by chromosomal translocations, either directly by altering the activity of histone modifying enzymes, or indirectly by recruitment of this type of enzyme by oncogenic transcription factors. These alterations in the histone code may alter gene expression pattern to set the stage for leukemogenesis.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0730-2312
pubmed:author
pubmed:copyrightInfo
2005 Wiley-Liss, Inc.
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
96
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
938-50
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:16167339-Amino Acid Motifs, pubmed-meshheading:16167339-Amino Acid Sequence, pubmed-meshheading:16167339-Animals, pubmed-meshheading:16167339-Chromatin, pubmed-meshheading:16167339-Chromosomes, pubmed-meshheading:16167339-Core Binding Factor Alpha 2 Subunit, pubmed-meshheading:16167339-DNA-Binding Proteins, pubmed-meshheading:16167339-Histone Acetyltransferases, pubmed-meshheading:16167339-Histone Deacetylases, pubmed-meshheading:16167339-Histones, pubmed-meshheading:16167339-Humans, pubmed-meshheading:16167339-Leukemia, pubmed-meshheading:16167339-Models, Biological, pubmed-meshheading:16167339-Models, Molecular, pubmed-meshheading:16167339-Molecular Sequence Data, pubmed-meshheading:16167339-Protein Structure, Tertiary, pubmed-meshheading:16167339-Recombinant Fusion Proteins, pubmed-meshheading:16167339-Translocation, Genetic
pubmed:year
2005
pubmed:articleTitle
Translating the histone code into leukemia.
pubmed:affiliation
Department of Biochemistry, Vanderbilt University School of Medicine, Nashville, Tennessee 37232, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, Non-P.H.S., Review, Research Support, Non-U.S. Gov't, Research Support, N.I.H., Extramural