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rdf:type |
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lifeskim:mentions |
umls-concept:C0008546,
umls-concept:C0026544,
umls-concept:C0040648,
umls-concept:C0430991,
umls-concept:C0740302,
umls-concept:C1167622,
umls-concept:C1257994,
umls-concept:C1366516,
umls-concept:C1538317,
umls-concept:C1706474,
umls-concept:C1709059,
umls-concept:C2603363
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pubmed:issue |
1-2
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pubmed:dateCreated |
2010-2-24
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pubmed:abstractText |
The orchestration of the events in the cell during the progression of the cell cycle is modulated by various phenomenon which are regulated by structural modules of the cell. The nucleus is a major hub for all these regulatory units which harbour the nuclear matrix, matrix proteins and chromatin. The histone modifications etch a complex code on the chromatin and the matrix proteins in consort with the histone code regulate the gene expression. SMAR1 is a matrix attachment region binding protein that interacts with chromatin modulators like HDAC1, Sin3A and causes chromatin condensation. SMAR1 modulates the chromatin at the Vbeta locus and plays a prominent role in V(D)J recombination. Such indispensable function of SMAR1 by the modulation of chromatin in the context of malignancy and V(D)J recombination emphasizes that MAR binding proteins regulate the complex events of the cell and perturbed expression causes disease conditions.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/BANP protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Cell Cycle Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Chromatin,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclin D1,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Histone Deacetylase 1,
http://linkedlifedata.com/resource/pubmed/chemical/Histones,
http://linkedlifedata.com/resource/pubmed/chemical/Matrix Attachment Region Binding...,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Matrix-Associated Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
1573-4919
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:volume |
336
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
75-84
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pubmed:meshHeading |
pubmed-meshheading:19802523-Acetylation,
pubmed-meshheading:19802523-Animals,
pubmed-meshheading:19802523-Cell Cycle Proteins,
pubmed-meshheading:19802523-Chromatin,
pubmed-meshheading:19802523-Cyclin D1,
pubmed-meshheading:19802523-DNA-Binding Proteins,
pubmed-meshheading:19802523-Gene Expression Regulation,
pubmed-meshheading:19802523-Histone Deacetylase 1,
pubmed-meshheading:19802523-Histones,
pubmed-meshheading:19802523-Humans,
pubmed-meshheading:19802523-Matrix Attachment Region Binding Proteins,
pubmed-meshheading:19802523-Matrix Attachment Regions,
pubmed-meshheading:19802523-Methylation,
pubmed-meshheading:19802523-Nuclear Matrix,
pubmed-meshheading:19802523-Nuclear Matrix-Associated Proteins,
pubmed-meshheading:19802523-Nuclear Proteins,
pubmed-meshheading:19802523-Phosphorylation,
pubmed-meshheading:19802523-Recombination, Genetic
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pubmed:year |
2010
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pubmed:articleTitle |
Modulation of chromatin by MARs and MAR binding oncogenic transcription factor SMAR1.
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pubmed:affiliation |
National Centre for Cell Science, Pune University Campus, Ganeshkhind, Pune, 411007, Maharashtra, India.
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pubmed:publicationType |
Journal Article
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