The N-terminal tail of histone H2A binds to two distinct sites within the nucleosome core.
about
Structural analysis and DNA binding of the HMG domains of the human mitochondrial transcription factor AHigh-resolution mapping of changes in histone-DNA contacts of nucleosomes remodeled by ISW2The effect of epigenetic modifications on the secondary structures and possible binding positions of the N-terminal tail of histone H3 in the nucleosome: a computational studyHistone tails modulate nucleosome mobility and regulate ATP-dependent nucleosome sliding by NURFHistones: at the crossroads of peptide and protein chemistry.Histone tails and the H3 alphaN helix regulate nucleosome mobility and stability.Coupling between Histone Conformations and DNA Geometry in Nucleosomes on a Microsecond Timescale: Atomistic Insights into Nucleosome FunctionsInternucleosomal interactions mediated by histone tails allow distant communication in chromatinA brief review of nucleosome structureStructural features of transcription factor IIIA bound to a nucleosome in solution.Preferential interaction of the core histone tail domains with linker DNA.Histone H2A variants in nucleosomes and chromatin: more or less stable?Physical methods used to study core histone tail structures and interactions in solution.Histone N-terminal tails interfere with nucleosome traversal by RNA polymerase II.Intra- and inter-nucleosome interactions of the core histone tail domains in higher-order chromatin structure.Site-specific binding affinities within the H2B tail domain indicate specific effects of lysine acetylation.SWI/SNF- and RSC-catalyzed nucleosome mobilization requires internal DNA loop translocation within nucleosomes.The H3-H4 N-terminal tail domains are the primary mediators of transcription factor IIIA access to 5S DNA within a nucleosome.Nucleosome remodeling by the human SWI/SNF complex requires transient global disruption of histone-DNA interactionshSWI/SNF-catalyzed nucleosome sliding does not occur solely via a twist-diffusion mechanism.The core histone tail domains contribute to sequence-dependent nucleosome positioning.
P2860
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P2860
The N-terminal tail of histone H2A binds to two distinct sites within the nucleosome core.
description
1997 nî lūn-bûn
@nan
1997年の論文
@ja
1997年論文
@yue
1997年論文
@zh-hant
1997年論文
@zh-hk
1997年論文
@zh-mo
1997年論文
@zh-tw
1997年论文
@wuu
1997年论文
@zh
1997年论文
@zh-cn
name
The N-terminal tail of histone ...... es within the nucleosome core.
@ast
The N-terminal tail of histone ...... es within the nucleosome core.
@en
type
label
The N-terminal tail of histone ...... es within the nucleosome core.
@ast
The N-terminal tail of histone ...... es within the nucleosome core.
@en
prefLabel
The N-terminal tail of histone ...... es within the nucleosome core.
@ast
The N-terminal tail of histone ...... es within the nucleosome core.
@en
P2860
P356
P1476
The N-terminal tail of histone ...... es within the nucleosome core.
@en
P2093
P2860
P304
P356
10.1073/PNAS.94.17.8959
P407
P577
1997-08-01T00:00:00Z