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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
25
|
pubmed:dateCreated |
1992-12-8
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pubmed:abstractText |
The numbers of the arginine residues involved in strong histone-DNA interactions to fold DNA into a nucleosome core particle were determined for each of the four core histones, by kinetic studies of chemical modification of the residues in the nucleosome core particle. It was suggested that the arginines in the globular region of H3 histone make major contributions to the strong binding of the octameric histones to the core DNA.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:issn |
0261-3166
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pubmed:author | |
pubmed:issnType |
Print
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
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pubmed:pagination |
33-4
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pubmed:dateRevised |
2003-11-14
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pubmed:meshHeading |
pubmed-meshheading:1842084-Animals,
pubmed-meshheading:1842084-Arginine,
pubmed-meshheading:1842084-Chickens,
pubmed-meshheading:1842084-DNA,
pubmed-meshheading:1842084-Histones,
pubmed-meshheading:1842084-Kinetics,
pubmed-meshheading:1842084-Nucleic Acid Conformation,
pubmed-meshheading:1842084-Nucleosomes
|
pubmed:year |
1991
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pubmed:articleTitle |
Arginine residues involved in strong histone--DNA interactions to fold DNA into the nucleosome core particle.
|
pubmed:affiliation |
Division of Biology, National Institute of Radiological Sciences, Chiba-shi, Japan.
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pubmed:publicationType |
Journal Article
|