In vitro binding of H1 histone subtypes to nucleosomal organized mouse mammary tumor virus long terminal repeat promotor.
about
H1 family histones in the nucleus. Control of binding and localization by the C-terminal domainHILS1 is a spermatid-specific linker histone H1-like protein implicated in chromatin remodeling during mammalian spermiogenesisHistone variants: are they functionally heterogeneous?H1 histones: current perspectives and challengesThe histone H1 family: specific members, specific functions?The preferential binding of histone H1 to DNA scaffold-associated regions is determined by its C-terminal domainDNA-induced secondary structure of the carboxyl-terminal domain of histone H1Differential affinity of mammalian histone H1 somatic subtypes for DNA and chromatin.Histone H1 subtypes differentially modulate chromatin condensation without preventing ATP-dependent remodeling by SWI/SNF or NURF.Histones: Controlling Tumor Signaling CircuitryHistone variants and histone modifications: a structural perspective.Chromatin condensing functions of the linker histone C-terminal domain are mediated by specific amino acid composition and intrinsic protein disorder.The H1 linker histones: multifunctional proteins beyond the nucleosomal core particle.Beyond the walls of the nucleus: the role of histones in cellular signaling and innate immunity.The dynamic mobility of histone H1 is regulated by cyclin/CDK phosphorylation.Profiling of linker histone variants in ovarian cancer.Structure of the H1 C-terminal domain and function in chromatin condensation.Molecular dynamics of histone H1.Open and closed: the roles of linker histones in plants and animals.Linker histone subtypes and their allelic variants.Role of H1 linker histones in mammalian development and stem cell differentiation.Modulation of chromatin function through linker histone H1 variants.Overproduction of histone H1 variants in vivo increases basal and induced activity of the mouse mammary tumor virus promoter.Rapid dephosphorylation of H1 histones after apoptosis induction.Regulation of Cellular Dynamics and Chromosomal Binding Site Preference of Linker Histones H1.0 and H1.X.Human linker histones: interplay between phosphorylation and O-β-GlcNAc to mediate chromatin structural modifications.Linker histones are mobilized during infection with herpes simplex virus type 1.Hyperphosphorylation of histone H2A.X and dephosphorylation of histone H1 subtypes in the course of apoptosis.Polymorphism in a histone H1 subtype with a short N-terminal domain in three legume species (Fabaceae, Fabaeae).Histone H5-chromatin interactions in situ are strongly modulated by H5 C-terminal phosphorylation.Mice with a targeted disruption of the H1t gene are fertile and undergo normal changes in structural chromosomal proteins during spermiogenesis.A K52Q substitution in the globular domain of histone H1t modulates its nucleosome binding properties
P2860
Q24303501-902CC5FE-4918-4199-8689-7ED40F333C3AQ24315894-0ED479CD-96DC-4A10-96A5-71F85647B097Q24793005-58B01D35-9167-4FE6-A8C1-ECC29F402903Q27023358-B87C785E-8707-472F-9754-72A8E9DA12EAQ28265464-DAC9B0C4-12EC-480F-B08B-E15809C1A871Q28507683-70B7F147-70AE-4552-8A8A-937DE9B68565Q28910207-6D518272-FB4C-4CE1-809B-74A6D898DC92Q33284453-882C001E-669B-48BD-BD57-23C7AEF4F6E7Q33507902-4E32E4D5-A971-4F7B-81C0-5A816B9BA409Q34109472-9E9454C7-D2DD-44B2-9120-056C061F8D9AQ34500001-239C9222-C34D-4A34-9E5D-36E547F40FD4Q34900589-E14C5AE4-96B2-4FCE-B50B-C5EC45810110Q36270852-58CA86AC-402A-446D-9B78-F59A30DEB460Q36579399-F584E8E8-B9BD-45CF-B333-A1341D27D221Q37061861-07D09894-6B48-47A8-A821-E182C75B451CQ37125546-A6C96C3D-A91C-44A5-992B-651EBC10909DQ37208591-3A5676E8-4E7E-44D7-BBC2-21A9D81C42F4Q37398631-8C543240-A7BC-4E76-92D4-582918685F51Q37615684-C60B9433-E673-4898-87B6-F130A5139626Q38052933-CA8F24C1-8D3D-4E05-9E34-A8111DF63FF7Q38675151-9A645C28-C45A-4AB4-9BAA-3401A6DDABF0Q38895906-DE3FEF5B-3ED3-4111-921E-9868C13EE9FEQ39728735-1E06B6F4-6EE8-45BF-8C3E-DE120BA530F1Q40870762-2F7206DC-3F29-434A-9301-49863928BEA1Q41461337-823F4BE0-8422-477B-8B2D-BDD7077BFABAQ41820513-473882EA-FAD5-4A3F-9283-0C7FF1160D35Q42407022-3EA01072-334E-478D-B82A-E85ACEFB4605Q42819537-40664CD1-99F7-4E56-897C-A9D20EEB78D3Q45958787-47C12186-DE3B-4844-A0F3-63F94874752FQ46445610-CD0BAE28-9CC3-4297-9879-F25E03B4E4B8Q52542019-8B7D2C87-AEF4-4AB3-B0CE-608D4DF6F275Q57038753-204148D5-0F7A-4528-B40A-0D48A553F2E2
P2860
In vitro binding of H1 histone subtypes to nucleosomal organized mouse mammary tumor virus long terminal repeat promotor.
description
1998 nî lūn-bûn
@nan
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
1998年论文
@zh
1998年论文
@zh-cn
name
In vitro binding of H1 histone ...... long terminal repeat promotor.
@en
In vitro binding of H1 histone ...... long terminal repeat promotor.
@nl
type
label
In vitro binding of H1 histone ...... long terminal repeat promotor.
@en
In vitro binding of H1 histone ...... long terminal repeat promotor.
@nl
prefLabel
In vitro binding of H1 histone ...... long terminal repeat promotor.
@en
In vitro binding of H1 histone ...... long terminal repeat promotor.
@nl
P2093
P2860
P356
P1476
In vitro binding of H1 histone ...... long terminal repeat promotor.
@en
P2093
Helliger W
Puschendorf B
Sapojnikova N
P2860
P304
32236-32243
P356
10.1074/JBC.273.48.32236
P407
P577
1998-11-01T00:00:00Z