The growth suppressor PML represses transcription by functionally and physically interacting with histone deacetylases
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Human SIR2 deacetylates p53 and antagonizes PML/p53-induced cellular senescence.Evidence for a role of the cellular ND10 protein PML in mediating intrinsic immunity against human cytomegalovirus infectionsMageA2 restrains cellular senescence by targeting the function of PMLIV/p53 axis at the PML-NBsPML regulates PER2 nuclear localization and circadian functionPML colocalizes with and stabilizes the DNA damage response protein TopBP1Proteasome-independent disruption of PML oncogenic domains (PODs), but not covalent modification by SUMO-1, is required for human cytomegalovirus immediate-early protein IE1 to inhibit PML-mediated transcriptional repression.Physical and functional interactions of histone deacetylase 3 with TFII-I family proteins and PIASxbeta.PIASy, a nuclear matrix-associated SUMO E3 ligase, represses LEF1 activity by sequestration into nuclear bodiesHistone sumoylation is associated with transcriptional repressionRole of ND10 nuclear bodies in the chromatin repression of HSV-1The function, regulation and therapeutic implications of the tumor suppressor protein, PMLPML-nuclear bodies are involved in cellular serum responseThe coiled-coil domain is the structural determinant for mammalian homologues of Drosophila Sina-mediated degradation of promyelocytic leukemia protein and other tripartite motif proteins by the proteasomePromyelocytic leukemia protein PML inhibits Nur77-mediated transcription through specific functional interactionsPML protein isoforms and the RBCC/TRIM motifPML interaction with p53 and its role in apoptosis and replicative senescenceThe promyelocytic leukemia protein represses A20-mediated transcriptionChanging nuclear landscape and unique PML structures during early epigenetic transitions of human embryonic stem cells.Identification of a novel modulator of thyroid hormone receptor-mediated action.HDAC3 as a molecular chaperone for shuttling phosphorylated TR2 to PML: a novel deacetylase activity-independent function of HDAC3.The DEAD-box protein DP103 (Ddx20 or Gemin-3) represses orphan nuclear receptor activity via SUMO modification.Loss of the promyelocytic leukemia protein in gastric cancer: implications for IP-10 expression and tumor-infiltrating lymphocytes.Cellular proteins localized at and interacting within ND10/PML nuclear bodies/PODs suggest functions of a nuclear depot.Valproic acid induces differentiation and transient tumor regression, but spares leukemia-initiating activity in mouse models of APL.PML-mediated signaling and its role in cancer stem cells.SIRT1 and p53, effect on cancer, senescence and beyond.In vivo analysis of the molecular genetics of acute promyelocytic leukemia.Real-time transcriptional profiling of cellular and viral gene expression during lytic cytomegalovirus infectionSystematic analysis of time-series gene expression data on tumor cell-selective apoptotic responses to HDAC inhibitors.Transcriptional regulation in acute promyelocytic leukemia.PODs in the nuclear spot: enigmas in the magician's pot.The promyelocytic leukemia nuclear body: sites of activity?Determination of minimum herpes simplex virus type 1 components necessary to localize transcriptionally active DNA to ND10.Combining the differentiating effect of panobinostat with the apoptotic effect of arsenic trioxide leads to significant survival benefit in a model of t(8;21) acute myeloid leukemia.SIRT1 stabilizes PML promoting its sumoylationThe promyelocytic leukemia protein functions as a negative regulator of IFN-gamma signaling.Positive role of promyelocytic leukemia protein in type I interferon response and its regulation by human cytomegalovirus.Promyelocytic leukemia inhibits adipogenesis, and loss of promyelocytic leukemia results in fat accumulation in mice.PHA-4/FoxA cooperates with TAM-1/TRIM to regulate cell fate restriction in the C. elegans foregutDegradation of the tumor suppressor PML by Pin1 contributes to the cancer phenotype of breast cancer MDA-MB-231 cells.
P2860
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P2860
The growth suppressor PML represses transcription by functionally and physically interacting with histone deacetylases
description
2001 nî lūn-bûn
@nan
2001 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2001年の論文
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2001年学术文章
@wuu
2001年学术文章
@zh-cn
2001年学术文章
@zh-hans
2001年学术文章
@zh-my
2001年学术文章
@zh-sg
2001年學術文章
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name
The growth suppressor PML repr ...... ting with histone deacetylases
@ast
The growth suppressor PML repr ...... ting with histone deacetylases
@en
The growth suppressor PML repr ...... ting with histone deacetylases
@en-gb
The growth suppressor PML repr ...... ting with histone deacetylases
@nl
type
label
The growth suppressor PML repr ...... ting with histone deacetylases
@ast
The growth suppressor PML repr ...... ting with histone deacetylases
@en
The growth suppressor PML repr ...... ting with histone deacetylases
@en-gb
The growth suppressor PML repr ...... ting with histone deacetylases
@nl
prefLabel
The growth suppressor PML repr ...... ting with histone deacetylases
@ast
The growth suppressor PML repr ...... ting with histone deacetylases
@en
The growth suppressor PML repr ...... ting with histone deacetylases
@en-gb
The growth suppressor PML repr ...... ting with histone deacetylases
@nl
P2093
P2860
P3181
P1476
The growth suppressor PML repr ...... ting with histone deacetylases
@en
P2093
D Edmondson
P2860
P304
P3181
P356
10.1128/MCB.21.7.2259-2268.2001
P407
P577
2001-04-01T00:00:00Z