Rearrangement of the histone H2A C-terminal domain in the nucleosome.
about
Distinct Roles of Histone H3 and H2A Tails in Nucleosome Stability.Structure and organization of chromatin fiber in the nucleusPersistent interactions of core histone tails with nucleosomal DNA following acetylation and transcription factor bindingDisruption of higher-order folding by core histone acetylation dramatically enhances transcription of nucleosomal arrays by RNA polymerase IIIElectrostatic mechanism of nucleosomal array folding revealed by computer simulation.Histone acetylation facilitates RNA polymerase II transcription of the Drosophila hsp26 gene in chromatin.Role of histone acetylation in the assembly and modulation of chromatin structures.Chromatin modification and diseaseHistone variants and histone modifications: a structural perspective.Properties of ets-1 binding to chromatin and its effect on platelet factor 4 gene expressionSubnucleosomal structures and nucleosome asymmetry across a genomeThe elusive structural role of ubiquitinated histones.The nonessential H2A N-terminal tail can function as an essential charge patch on the H2A.Z variant N-terminal tailContribution of the serine 129 of histone H2A to chromatin structure.Reconstitution of hyperacetylated, DNase I-sensitive chromatin characterized by high conformational flexibility of nucleosomal DNA.Preferential interaction of the core histone tail domains with linker DNA.Histone H2A variants in nucleosomes and chromatin: more or less stable?The N-terminal tail of histone H2A binds to two distinct sites within the nucleosome core.Physical methods used to study core histone tail structures and interactions in solution.Truncation of histone H2A's C-terminal tail, as is typical for Ni(II)-assisted specific peptide bond hydrolysis, has gene expression altering effectsIntra- and inter-nucleosome interactions of the core histone tail domains in higher-order chromatin structure.Chromosome condensation induced by fostriecin does not require p34cdc2 kinase activity and histone H1 hyperphosphorylation, but is associated with enhanced histone H2A and H3 phosphorylation.Site-specific binding affinities within the H2B tail domain indicate specific effects of lysine acetylation.Regulation of ISW2 by concerted action of histone H4 tail and extranucleosomal DNA.Nucleosome positioning properties of the albumin transcriptional enhancer.Human DNA ligase I efficiently seals nicks in nucleosomesNucleosome-driven autoimmune response in lupus. Pathogenic T helper cell epitopes and costimulatory signals.Effect of in vivo histone hyperacetylation on the state of chromatin fibers.Multiscale modeling of nucleosome dynamics.Characterization of mussel H2A.Z.2: a new H2A.Z variant preferentially expressed in germinal tissues from Mytilus.Gcn5p, a Transcription-related Histone Acetyltransferase, Acetylates Nucleosomes and Folded Nucleosomal Arrays in the Absence of Other Protein Subunits
P2860
Q27318120-BCCE1757-F7BA-4199-8A55-7F31DDE65491Q28080958-62A5289A-6715-4830-8007-B3A6D86F0BA5Q31998516-C29B4F70-1832-4373-804A-D6D2F46D624AQ33775383-2673EC1B-B6D3-49A7-AB68-D4A6259DDAC8Q33836463-9D29CB27-F318-4C7A-8C8C-D20A41370C53Q33888854-7126E3D8-CE06-47D4-83F1-5F23278FD68EQ34093176-2784A3BE-50C6-4E3D-BA2D-43DA750837B5Q34098840-909B7934-71FB-4D26-84B8-9A75C2042A31Q34500001-7C278BF2-7E3B-45EB-A950-1E6623536728Q34550215-BDE2D0B7-ACE5-43BD-A90F-488F43E3C6E7Q34645082-1507488D-B89A-484B-A942-780682B955D9Q34746899-F9F10F61-FC1B-490E-8837-1AB766D3BC61Q34889008-26D28CA1-9486-4142-AD27-C9A95443AF70Q35856903-06862408-F586-458B-8679-CB16DCFAA4DFQ35871435-4D7400A1-E1C6-46CD-90B0-BBA2A056BEEDQ36228515-382D41EC-CD74-485E-A46E-E5A78E7F8484Q36435083-BDDAE719-4AF0-4C16-9D56-DC49BA71E35EQ36544944-33BE84F9-6FCD-44D4-85AB-B49E85B867EDQ36579395-FE743F67-AD7B-466C-80C2-67E9477B361FQ37409379-A328B30F-F64A-4F22-A138-96F8DE904E21Q37610823-A027A48F-48EE-4C06-959D-5187FBB463B2Q37694723-9BD7D3ED-B611-481A-BE1E-A0E80B146C55Q38299037-F22ABE7E-E0FF-4D33-94D0-80675260AB20Q39129726-1D952ABB-DE3C-4F76-8576-F83461F0B742Q39715428-E6CC18EE-E2FB-4B1A-ADD9-13C5F3C4E30AQ40430379-824CF33E-4DA5-41D2-BF4E-AC284413159BQ41500830-520B9DB0-3DFD-4C8A-8479-A9F9CA4E4D90Q41924069-043B3D02-1AF9-4695-81A6-4367E189C41BQ42957995-D1E3C051-4624-4047-84F8-732B29343C5EQ51518774-9B175977-34C2-4A44-9D41-1F1096D361AEQ58514612-1EF6C480-59FB-48C9-8F0A-D9D1E4ED5D4C
P2860
Rearrangement of the histone H2A C-terminal domain in the nucleosome.
description
1994 nî lūn-bûn
@nan
1994年の論文
@ja
1994年論文
@yue
1994年論文
@zh-hant
1994年論文
@zh-hk
1994年論文
@zh-mo
1994年論文
@zh-tw
1994年论文
@wuu
1994年论文
@zh
1994年论文
@zh-cn
name
Rearrangement of the histone H2A C-terminal domain in the nucleosome.
@ast
Rearrangement of the histone H2A C-terminal domain in the nucleosome.
@en
type
label
Rearrangement of the histone H2A C-terminal domain in the nucleosome.
@ast
Rearrangement of the histone H2A C-terminal domain in the nucleosome.
@en
prefLabel
Rearrangement of the histone H2A C-terminal domain in the nucleosome.
@ast
Rearrangement of the histone H2A C-terminal domain in the nucleosome.
@en
P2093
P2860
P356
P1476
Rearrangement of the histone H2A C-terminal domain in the nucleosome.
@en
P2093
E M Bradbury
S G Bavykin
S I Usachenko
P2860
P304
P356
10.1073/PNAS.91.15.6845
P407
P577
1994-07-01T00:00:00Z