Dual roles of p300 in chromatin assembly and transcriptional activation in cooperation with nucleosome assembly protein 1 in vitro.
about
The histone chaperone protein Nucleosome Assembly Protein-1 (hNAP-1) binds HIV-1 Tat and promotes viral transcriptionConditional knockout mice reveal distinct functions for the global transcriptional coactivators CBP and p300 in T-cell developmentDirect interaction between nucleosome assembly protein 1 and the papillomavirus E2 proteins involved in activation of transcriptionCatalysis and substrate selection by histone/protein lysine acetyltransferasesThe nucleosome assembly activity of NAP1 is enhanced by AlienRole of redox signaling in neuroinflammation and neurodegenerative diseasesMolecular functions of the histone acetyltransferase chaperone complex Rtt109-Vps75Nap1l2 promotes histone acetylation activity during neuronal differentiationCellular expression and localization of DGKζ-interacting NAP1-like proteins in the brain and functional implications under hypoxic stressThe nucleosome assembly protein TSPYL2 regulates the expression of NMDA receptor subunits GluN2A and GluN2B.Dynamic and selective nucleosome repositioning during endotoxin tolerance.Transcription coactivator CBP has direct DNA binding activity and stimulates transcription factor DNA binding through small domains.Nucleosome eviction and activated transcription require p300 acetylation of histone H3 lysine 14.HCMV IE2-mediated inhibition of HAT activity downregulates p53 function.Identification of novel imprinted genes in a genome-wide screen for maternal methylation.Tax recruitment of CBP/p300, via the KIX domain, reveals a potent requirement for acetyltransferase activity that is chromatin dependent and histone tail independentHistone chaperones, histone acetylation, and the fluidity of the chromogenomeInhibition of p53 acetylation by INHAT subunit SET/TAF-Iβ represses p53 activity.Enhancer of Acetyltransferase Chameau (EAChm) Is a Novel Transcriptional Co-ActivatorAssociation of GNLY genetic polymorphisms with chronic liver disease in a Korean population.Structure and function of nucleosome assembly proteins.TSPY is a cancer testis antigen expressed in human hepatocellular carcinoma.Nucleosome formation with the testis-specific histone H3 variant, H3t, by human nucleosome assembly proteins in vitro.The coactivators CBP/p300 and the histone chaperone NAP1 promote transcription-independent nucleosome eviction at the HTLV-1 promoterStructural evidence for Nap1-dependent H2A-H2B deposition and nucleosome assembly.NSBP-1 mediates the effects of cholesterol on insulin/IGF-1 signaling in Caenorhabditis elegans.Smad3 activates the Sox9-dependent transcription on chromatinUnderstanding histone acetyltransferase Rtt109 structure and function: how many chaperones does it take?Hepatitis C Virus NS5A Targets Nucleosome Assembly Protein NAP1L1 To Control the Innate Cellular Response.Sox9 and p300 cooperatively regulate chromatin-mediated transcription.Transcriptional co-activators CREB-binding protein and p300 regulate chondrocyte-specific gene expression via association with Sox9.A genome-wide role for CHD remodelling factors and Nap1 in nucleosome disassembly.Regulatory role for nucleosome assembly protein-1 in the proliferative and vasculogenic phenotype of pulmonary endothelium.Beyond the histone tail: acetylation at the nucleosome dyad commands transcription.Preferential binding of the histone (H3-H4)2 tetramer by NAP1 is mediated by the amino-terminal histone tails.Human accelerated regions and other human-specific sequence variations in the context of evolution and their relevance for brain development.Interacting proteins and differences in nuclear transport reveal specific functions for the NAP1 family proteins in plants.Smad3 induces chondrogenesis through the activation of SOX9 via CREB-binding protein/p300 recruitment.Developmentally controlled farnesylation modulates AtNAP1;1 function in cell proliferation and cell expansion during Arabidopsis leaf development.C-terminal acidic domain of histone chaperone human NAP1 is an efficient binding assistant for histone H2A-H2B, but not H3-H4.
P2860
Q24307870-C3C27A94-8867-4160-B51B-C149F9623816Q24537650-67E7F27C-FF22-4826-A938-DB3A125B7576Q24607374-6CF8CFC1-E847-4F68-9D65-CD11C08ADA8EQ24654957-998691EA-9F5E-41A8-AD1C-18AD9ED89808Q24683217-8E498529-80EF-4C10-ABA8-87F963612976Q27012569-AFBE48E5-00CE-438C-843C-B1FA991DA8E8Q27653529-7C53869A-CADB-4AFC-9406-C8014DF679BFQ28513497-6D079F56-0120-4744-B160-2728333863CFQ28567417-0B027515-1443-4E42-A1E8-5C5F1AA0EEADQ30564075-71B7B51F-A54D-4A58-A79D-68DFD0791FC5Q33569697-E84D892C-6778-445C-BBF9-B85362751BBEQ33598618-65B98C35-FADD-4E58-BCFA-4AB83DECAD10Q34320228-906D55E8-4214-478B-9658-8B164F22BFCBQ34348863-DA877A0B-88E8-4FD5-AF87-ADFDB4D0178DQ34994392-E8415536-7B04-4FC7-9E69-F1AA6279CE94Q35148532-C84E7301-500D-4C0E-9E5F-E051AD88CD77Q35253477-80CA49DF-23CA-45B0-8181-A8940C032F10Q35633551-A74BB6D8-4733-4734-AD13-BA6D9E70B915Q35837298-1DFB6EDA-3836-4B8A-8062-03DB71FC99E2Q36194159-B0D6E259-2E7D-4FB9-9BDE-B7288C80043CQ36579383-9E1EEEC3-817B-4580-B361-BF9B62703AC2Q36615203-6CEE34FB-5167-4A17-B399-F1D08FADF034Q36633206-27D476B7-9A09-44A9-AAA9-4D49C7D09764Q36725637-0F3A70D3-3228-4F09-AB85-A3F2C942A3B2Q37060824-3AFD43A0-1900-41CD-9D86-BA81FBFF043AQ37137329-062A03A5-41B9-4EFB-9C0D-C98FE0FFA272Q37172739-A1FB99D5-6C37-4D58-91B2-E3A63657FC58Q37949026-03B4F856-9FB1-41BE-B204-4C0057D25DF3Q40141993-79AEFB66-D9F5-45CA-A4D8-C55EE45652B9Q40383677-C5A8DC5F-28CF-498B-AD22-DAB767E71C64Q40649748-C87B211C-87A4-4E82-A070-CB87893EC648Q41928549-951D231E-A496-49FE-BAFC-E1B369F5D5B7Q42521174-974A0A31-6BCD-46F2-8F08-654F44CC6AACQ42736685-EFCA0228-1C4D-4530-8E66-21B6CCEB7FD7Q44556042-743F22A2-C9C9-4811-B58F-2234658B1FDCQ46259543-E4DDDAB2-69C9-41C8-BF60-CF23A90DF394Q46568314-A9317065-89B5-403E-B2AC-B39A4514EC96Q46780418-46E26728-6956-4516-BC16-1C0119EBF6B1Q50711734-CFF912DF-93EB-4A3F-B352-9EA6E7C640FFQ51536603-A6A0B1C4-35AF-4D16-9EA2-6D28B302E7C1
P2860
Dual roles of p300 in chromatin assembly and transcriptional activation in cooperation with nucleosome assembly protein 1 in vitro.
description
2002 nî lūn-bûn
@nan
2002 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2002年の論文
@ja
2002年論文
@yue
2002年論文
@zh-hant
2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
@zh-tw
2002年论文
@wuu
name
Dual roles of p300 in chromati ...... me assembly protein 1 in vitro
@nl
Dual roles of p300 in chromati ...... e assembly protein 1 in vitro.
@ast
Dual roles of p300 in chromati ...... e assembly protein 1 in vitro.
@en
Dual roles of p300 in chromati ...... e assembly protein 1 in vitro.
@en-gb
type
label
Dual roles of p300 in chromati ...... me assembly protein 1 in vitro
@nl
Dual roles of p300 in chromati ...... e assembly protein 1 in vitro.
@ast
Dual roles of p300 in chromati ...... e assembly protein 1 in vitro.
@en
Dual roles of p300 in chromati ...... e assembly protein 1 in vitro.
@en-gb
prefLabel
Dual roles of p300 in chromati ...... me assembly protein 1 in vitro
@nl
Dual roles of p300 in chromati ...... e assembly protein 1 in vitro.
@ast
Dual roles of p300 in chromati ...... e assembly protein 1 in vitro.
@en
Dual roles of p300 in chromati ...... e assembly protein 1 in vitro.
@en-gb
P2093
P2860
P1476
Dual roles of p300 in chromati ...... e assembly protein 1 in vitro.
@en
P2093
Fumiko Hirose
Hiroshi Asahara
Marc Montminy
Takashi Ito
Takeya Nakagawa
Tony Hunter
Tsuyoshi Ikehara
P2860
P304
P356
10.1128/MCB.22.9.2974-2983.2002
P407
P577
2002-05-01T00:00:00Z