The N-terminal tails of the H2A-H2B histones affect dimer structure and stability.
about
Disordered proteinaceous machinesDynamics of chromatin decondensation reveals the structural integrity of a mechanically prestressed nucleus.Deciphering the roles of the histone H2B N-terminal domain in genome-wide transcription.Histone tails and the H3 alphaN helix regulate nucleosome mobility and stability.Alanine or aspartic acid substitutions at serine23/24 of cardiac troponin I decrease thin filament activation, with no effect on crossbridge detachment kineticsThe H2A.Z/H2B dimer is unstable compared to the dimer containing the major H2A isoform.Folding mechanism of the (H3-H4)2 histone tetramer of the core nucleosome.The tropomyosin binding region of cardiac troponin T modulates crossbridge recruitment dynamics in rat cardiac muscle fibers.Structure Change from β-Strand and Turn to α-Helix in Histone H2A-H2B Induced by DNA Damage ResponseTruncation of histone H2A's C-terminal tail, as is typical for Ni(II)-assisted specific peptide bond hydrolysis, has gene expression altering effectsCompartmentalization and Functionality of Nuclear Disorder: Intrinsic Disorder and Protein-Protein Interactions in Intra-Nuclear Compartments.Mutational analysis of the stability of the H2A and H2B histone monomers.Intrinsically disordered proteins in the nucleus of human cells.H2A.Z and H2B.Z double-variant nucleosomes define intergenic regions and dynamically occupy var gene promoters in the malaria parasite Plasmodium falciparum.More than just tails: intrinsic disorder in histone proteins.
P2860
Q28652765-EA7A30CA-2E48-417E-A52B-18B53F4965E2Q33343962-0CB8259D-49A7-47D4-8081-4CBCE7F0F650Q34717455-A3616D65-A106-415F-98D6-157D764F2796Q35857015-164D1D95-84DB-4673-8331-0FF956FA16CCQ36117053-960C5786-500B-4CD4-B8B1-DF312227BAEDQ36476910-BE5894E5-019E-4529-ADD3-FF5CE55DB7A5Q36526594-4600024F-3E06-4E55-8DBD-2D427DA13C3AQ36788034-E905BD97-16D2-4795-9196-692D88F3B6E2Q37095471-55B39FD2-F3B2-4676-B1AC-FB6DDEB86BE3Q37409379-6E80BF33-FD3A-4ED8-8F81-32879C2DAF95Q40162990-C9A70B69-B43F-4607-9985-620F8D00D0AAQ42227728-16215C37-E4A3-491C-A77F-C1AC5B51C756Q47142042-B3F813E0-6601-47D0-A0CF-8E3E931201FFQ48032398-440ACE18-121A-442E-A793-975C3F380C9EQ48050089-E0155F59-F8B9-47E2-8BED-A94833CB90F0
P2860
The N-terminal tails of the H2A-H2B histones affect dimer structure and stability.
description
2002 nî lūn-bûn
@nan
2002年の論文
@ja
2002年学术文章
@wuu
2002年学术文章
@zh
2002年学术文章
@zh-cn
2002年学术文章
@zh-hans
2002年学术文章
@zh-my
2002年学术文章
@zh-sg
2002年學術文章
@yue
2002年學術文章
@zh-hant
name
The N-terminal tails of the H2A-H2B histones affect dimer structure and stability.
@en
The N-terminal tails of the H2A-H2B histones affect dimer structure and stability.
@nl
type
label
The N-terminal tails of the H2A-H2B histones affect dimer structure and stability.
@en
The N-terminal tails of the H2A-H2B histones affect dimer structure and stability.
@nl
prefLabel
The N-terminal tails of the H2A-H2B histones affect dimer structure and stability.
@en
The N-terminal tails of the H2A-H2B histones affect dimer structure and stability.
@nl
P356
P1433
P1476
The N-terminal tails of the H2A-H2B histones affect dimer structure and stability.
@en
P2093
Brandon J Placek
Lisa M Gloss
P304
14960-14968
P356
10.1021/BI026283K
P407
P577
2002-12-01T00:00:00Z