about
HERF1, a novel hematopoiesis-specific RING finger protein, is required for terminal differentiation of erythroid cellsPML nuclear bodiesSequestration and inhibition of Daxx-mediated transcriptional repression by PMLPromyelocytic leukemia protein (PML) and Daxx participate in a novel nuclear pathway for apoptosisNuclear structure in normal and Bloom syndrome cellsPotentiation of GATA-2 activity through interactions with the promyelocytic leukemia protein (PML) and the t(15;17)-generated PML-retinoic acid receptor alpha oncoproteinAtrophin-1, the dentato-rubral and pallido-luysian atrophy gene product, interacts with ETO/MTG8 in the nuclear matrix and represses transcriptionFIST/HIPK3: a Fas/FADD-interacting serine/threonine kinase that induces FADD phosphorylation and inhibits fas-mediated Jun NH(2)-terminal kinase activationRegulation of p53 activity in nuclear bodies by a specific PML isoformThe growth suppressor PML represses transcription by functionally and physically interacting with histone deacetylasesA new spectrin, beta IV, has a major truncated isoform that associates with promyelocytic leukemia protein nuclear bodies and the nuclear matrixRegulation and localization of the Bloom syndrome protein in response to DNA damageThe tripartite motif family identifies cell compartments.Coordinated regulation of p53 apoptotic targets BAX and PUMA by SMAR1 through an identical MAR elementDaxx silencing sensitizes cells to multiple apoptotic pathwaysHuman SIR2 deacetylates p53 and antagonizes PML/p53-induced cellular senescence.PML inhibits HIF-1alpha translation and neoangiogenesis through repression of mTORPML colocalizes with and stabilizes the DNA damage response protein TopBP1AXIN is an essential co-activator for the promyelocytic leukemia protein in p53 activationThe Cullin 3 substrate adaptor KLHL20 mediates DAPK ubiquitination to control interferon responsesPML-dependent apoptosis after DNA damage is regulated by the checkpoint kinase hCds1/Chk2ZIP kinase triggers apoptosis from nuclear PML oncogenic domainsModulation of M2-type pyruvate kinase activity by the cytoplasmic PML tumor suppressor proteinPMLRARα binds to Fas and suppresses Fas-mediated apoptosis through recruiting c-FLIP in vivoThe interferon stimulated gene 54 promotes apoptosisThe promyelocytic leukemia protein PML regulates c-Jun function in response to DNA damageViral immediate-early proteins abrogate the modification by SUMO-1 of PML and Sp100 proteins, correlating with nuclear body disruptionEpstein-barr virus immediate-early protein BZLF1 is SUMO-1 modified and disrupts promyelocytic leukemia bodiesSp110 localizes to the PML-Sp100 nuclear body and may function as a nuclear hormone receptor transcriptional coactivatorAbility of the human cytomegalovirus IE1 protein to modulate sumoylation of PML correlates with its functional activities in transcriptional regulation and infectivity in cultured fibroblast cellsRepression of PML nuclear body-associated transcription by oxidative stress-activated Bach2PML is critical for ND10 formation and recruits the PML-interacting protein daxx to this nuclear structure when modified by SUMO-1The C-terminal domain of the Bloom syndrome DNA helicase is essential for genomic stabilityThe function, regulation and therapeutic implications of the tumor suppressor protein, PMLDual effect of oxidative stress on leukemia cancer induction and treatmentContributions of Epstein-Barr nuclear antigen 1 (EBNA1) to cell immortalization and survivalThe Ret finger protein induces apoptosis via its RING finger-B box-coiled-coil motifThe 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 proteasomeFunctional interaction of p53 and BLM DNA helicase in apoptosisPhysical and functional interactions between PML and MDM2
P2860
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P2860
description
1998 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
articolo scientifico
@it
artículu científicu espublizáu en 1998
@ast
im November 1998 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 1998/11/01)
@sk
vědecký článek publikovaný v roce 1998
@cs
wetenschappelijk artikel (gepubliceerd op 1998/11/01)
@nl
наукова стаття, опублікована в листопаді 1998
@uk
name
PML is essential for multiple apoptotic pathways
@ast
PML is essential for multiple apoptotic pathways
@en
PML is essential for multiple apoptotic pathways
@nl
type
label
PML is essential for multiple apoptotic pathways
@ast
PML is essential for multiple apoptotic pathways
@en
PML is essential for multiple apoptotic pathways
@nl
prefLabel
PML is essential for multiple apoptotic pathways
@ast
PML is essential for multiple apoptotic pathways
@en
PML is essential for multiple apoptotic pathways
@nl
P2093
P3181
P356
P1433
P1476
PML is essential for multiple apoptotic pathways
@en
P2093
P2888
P304
P3181
P356
10.1038/3073
P407
P577
1998-11-01T00:00:00Z