Regulation of histone acetylation and transcription by INHAT, a human cellular complex containing the set oncoprotein
about
Granzyme A activates an endoplasmic reticulum-associated caspase-independent nuclease to induce single-stranded DNA nicksHMG2 interacts with the nucleosome assembly protein SET and is a target of the cytotoxic T-lymphocyte protease granzyme ADual roles of p300 in chromatin assembly and transcriptional activation in cooperation with nucleosome assembly protein 1 in vitro.Rac1-induced cell migration requires membrane recruitment of the nuclear oncogene SETA transcriptional inhibitor targeted by the atypical orphan nuclear receptor SHPNIR is a novel INHAT repressor that modulates the transcriptional activity of p53.NIR, an inhibitor of histone acetyltransferases, regulates transcription factor TAp63 and is controlled by the cell cycleInhibition of FoxO1 acetylation by INHAT subunit SET/TAF-Iβ induces p21 transcriptionAlpha-synuclein acts in the nucleus to inhibit histone acetylation and promote neurotoxicityCytoplasmic targeting of the proto-oncogene SET promotes cell spreading and migrationThe role of LANP and ataxin 1 in E4F-mediated transcriptional repressionFE65 binds Teashirt, inhibiting expression of the primate-specific caspase-4Neuroprotective actions of PIKE-L by inhibition of SET proteolytic degradation by asparagine endopeptidaseMechanism of inhibition of PP2A activity and abnormal hyperphosphorylation of tau by I2(PP2A)/SETCleaving the oxidative repair protein Ape1 enhances cell death mediated by granzyme AAnalysis of the adenovirus E1B-55K-anchored proteome reveals its link to ubiquitination machinery.MicroRNA-21 targets tumor suppressor genes ANP32A and SMARCA4Induced ncRNAs allosterically modify RNA-binding proteins in cis to inhibit transcriptionPositive and negative regulation of the cardiovascular transcription factor KLF5 by p300 and the oncogenic regulator SET through interaction and acetylation on the DNA-binding domainInhibition of p300/CBP by early B-cell factorProtein Phosphatase 2A as a Therapeutic Target in Acute Myeloid LeukemiaThe Rac1 hypervariable region in targeting and signaling: a tail of many storiesA peek into the complex realm of histone phosphorylationSister chromatid segregation in meiosis II: deprotection through phosphorylationRegulation of PP2A by Sphingolipid Metabolism and SignalingTargeted ANP32E mutant mice do not demonstrate obvious movement defectsRelationship between the structure of SET/TAF-I /INHAT and its histone chaperone activityMolecular functions of the histone acetyltransferase chaperone complex Rtt109-Vps75Anp32e, a higher eukaryotic histone chaperone directs preferential recognition for H2A.ZHistone chaperone specificity in Rtt109 activation.Chaperone control of the activity and specificity of the histone H3 acetyltransferase Rtt109.A nuclear FK506-binding protein is a histone chaperone regulating rDNA silencing.Mapmodulin/leucine-rich acidic nuclear protein binds the light chain of microtubule-associated protein 1B and modulates neuritogenesisThe protein SET binds the neuronal Cdk5 activator p35nck5a and modulates Cdk5/p35nck5a activityThe oncoprotein Set/TAF-1beta, an inhibitor of histone acetyltransferase, inhibits active demethylation of DNA, integrating DNA methylation and transcriptional silencingSignificance of the transcription factor KLF5 in cardiovascular remodelingThe transcriptional corepressor, PELP1, recruits HDAC2 and masks histones using two separate domainsRegulation of histone acetylation and nucleosome assembly by transcription factor JDP2Colorectal cancer derived organotypic spheroids maintain essential tissue characteristics but adapt their metabolism in culturepp32 (ANP32A) expression inhibits pancreatic cancer cell growth and induces gemcitabine resistance by disrupting HuR binding to mRNAs
P2860
Q24291688-9ADB6A7E-3722-484D-A773-BE2A6751017CQ24292517-0A57BDFB-34AA-486D-BCB6-54C87F1B9E2EQ24293575-4344C867-F0CA-45D6-B680-EC259ED3EDEDQ24294337-264136AD-DBFC-43D8-858D-DD8E3E5E7590Q24294778-70116075-E47C-452F-8D3C-7D3CBD97AE70Q24297694-FCF1884D-CB9F-4154-B997-A97B7828C87EQ24298090-BF19E6E0-3146-4F15-A607-E5576DE311B2Q24300174-7E13C610-11D1-42C4-BDBD-DFDFF0A25EB5Q24301946-DD05A1DB-FC65-4CC5-ADC5-9D9F3F6F88EDQ24305121-A34E5862-14B9-4A43-96D6-F115F63EB2D9Q24308036-4357292A-140C-4650-89E3-A5920A051B1FQ24312011-31BD2ABB-78D1-4319-9F3D-28F525DEE8C6Q24315618-4A57F636-630E-4562-BB32-0C97793B1200Q24318458-86DF5ADC-8CFF-4AEF-BDC1-CC465C88A6D6Q24338600-16F43845-F4B9-4A9D-8167-B4D63F3D0564Q24538586-ED52AB40-362D-4D45-B63D-2E6DCB4B962DQ24633718-B9451141-91EA-4865-B37D-6896F733FCF0Q24646744-098982A6-027F-431E-B146-CEA1A7313282Q24648562-477B4233-C0EF-465B-868B-22E8CB723BF7Q24673236-B43821ED-5056-4FA7-A468-6B5FBBAE7740Q26752430-6C13FA59-EB43-42F9-9B58-E7116A465090Q26864271-59B0E15A-A0BF-4EED-AF98-952A32006137Q26992357-7AF0ACA2-F793-4B99-A619-223979848CE1Q27008999-7AF5A56D-7B15-4B09-B12B-C726C0160617Q27026038-5D550343-B8E5-4D57-83BA-1A9D13BB1051Q27320069-FA366CE0-BBC5-4C80-9719-BD5073D85F91Q27644058-BC83F0AA-CAEA-4526-BFBD-971BF3D59E3DQ27653529-1FA3EE6A-BBE9-410E-A061-9D625915C15EQ27682061-EA7B3139-557C-4C49-8D21-1B1122FA0004Q27931083-CDFE3F50-E0B0-4BD6-A334-D6E2B211C33CQ27932154-0E60E6A1-E364-4ACE-B91F-F118CCBCA48BQ27937248-ABAF38B2-0EF0-470D-A105-608C9CCC1B02Q28179296-8A8B6ACE-14E3-4C21-BEBB-EEF453E31B78Q28210628-49F47616-8440-4F72-A990-9E405B1D5890Q28215929-504BAD7B-E164-4048-8582-6FF470079EBDQ28267393-BD71E0F5-CC8E-4FD5-95C3-31F8C735DA3BQ28285366-EE817617-7177-400C-A68F-5F460A2B5442Q28300507-7F3C4FB6-D81C-4146-980D-41AC57BDC3A1Q28391219-D816A012-34A5-4387-B28F-48954C6DDF55Q28476402-C1E939A0-7A30-44B7-B77E-32F3985CE98B
P2860
Regulation of histone acetylation and transcription by INHAT, a human cellular complex containing the set oncoprotein
description
2001 nî lūn-bûn
@nan
2001 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
Regulation of histone acetylat ...... containing the set oncoprotein
@ast
Regulation of histone acetylat ...... containing the set oncoprotein
@en
Regulation of histone acetylat ...... containing the set oncoprotein
@nl
type
label
Regulation of histone acetylat ...... containing the set oncoprotein
@ast
Regulation of histone acetylat ...... containing the set oncoprotein
@en
Regulation of histone acetylat ...... containing the set oncoprotein
@nl
prefLabel
Regulation of histone acetylat ...... containing the set oncoprotein
@ast
Regulation of histone acetylat ...... containing the set oncoprotein
@en
Regulation of histone acetylat ...... containing the set oncoprotein
@nl
P2093
P3181
P1433
P1476
Regulation of histone acetylat ...... containing the set oncoprotein
@en
P2093
P304
P3181
P356
10.1016/S0092-8674(01)00196-9
P407
P577
2001-01-12T00:00:00Z