Human Daxx regulates Fas-induced apoptosis from nuclear PML oncogenic domains (PODs).
about
PML nuclear bodiesInhibition of Daxx-mediated apoptosis by heat shock protein 27FIST/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 isoformCommon properties of nuclear body protein SP100 and TIF1alpha chromatin factor: role of SUMO modificationApoptosis signal-regulating kinase 1 controls the proapoptotic function of death-associated protein (Daxx) in the cytoplasmThe interaction of Pax5 (BSAP) with Daxx can result in transcriptional activation in B cellsHomeodomain-interacting protein kinase 1 modulates Daxx localization, phosphorylation, and transcriptional activity.Essential role of the 58-kDa microspherule protein in the modulation of Daxx-dependent transcriptional repression as revealed by nucleolar sequestrationDaxx silencing sensitizes cells to multiple apoptotic pathwaysPhysical and functional interactions between Daxx and STAT3Daxx is reciprocally regulated by Mdm2 and HauspDefects in death-inducing signalling complex formation prevent JNK activation and Fas-mediated apoptosis in DU 145 prostate carcinoma cellsFas-associated death domain protein interacts with methyl-CpG binding domain protein 4: a potential link between genome surveillance and apoptosisThe death domain-associated protein modulates activity of the transcription co-factor Skip/NcoA62Negative regulation of p53 functions by Daxx and the involvement of MDM2Interaction of DJ-1 with Daxx inhibits apoptosis signal-regulating kinase 1 activity and cell deathPhysiological and functional interactions between Tcf4 and Daxx in colon cancer cellsZIP kinase triggers apoptosis from nuclear PML oncogenic domainsThe ATRX syndrome protein forms a chromatin-remodeling complex with Daxx and localizes in promyelocytic leukemia nuclear bodiesEpstein-barr virus immediate-early protein BZLF1 is SUMO-1 modified and disrupts promyelocytic leukemia bodiesGranuphilin modulates the exocytosis of secretory granules through interaction with syntaxin 1aThe Rab27a/granuphilin complex regulates the exocytosis of insulin-containing dense-core granulesThe chromatin-remodeling protein ATRX is critical for neuronal survival during corticogenesisCell death and diseases related to oxidative stress: 4-hydroxynonenal (HNE) in the balanceMechanistic insights into the oncolytic activity of vesicular stomatitis virus in cancer immunotherapyDAXX interacts with heat shock factor 1 during stress activation and enhances its transcriptional activityDegradation of nucleosome-associated centromeric histone H3-like protein CENP-A induced by herpes simplex virus type 1 protein ICP0The transcriptional role of PML and the nuclear bodyThe insulin-sensitive glucose transporter, GLUT4, interacts physically with Daxx. Two proteins with capacity to bind Ubc9 and conjugated to SUMO1Regulation of Pax3 transcriptional activity by SUMO-1-modified PMLPML interaction with p53 and its role in apoptosis and replicative senescenceThe promyelocytic leukemia protein represses A20-mediated transcriptionPromyelocytic leukemia protein (PML) functions as a glucocorticoid receptor co-activator by sequestering Daxx to the PML oncogenic domains (PODs) to enhance its transactivation potentialNuclear-cytoplasmic shuttling of a RING-IBR protein RBCK1 and its functional interaction with nuclear body proteinsPromyelocytic leukemia is a direct inhibitor of SAPK2/p38 mitogen-activated protein kinaseRole of promyelocytic leukemia (PML) sumolation in nuclear body formation, 11S proteasome recruitment, and As2O3-induced PML or PML/retinoic acid receptor alpha degradationSubcellular localization of Daxx determines its opposing functions in ischemic cell deathSubcellular location and expression pattern of autoimmune regulator (Aire), the mouse orthologue for human gene defective in autoimmune polyendocrinopathy candidiasis ectodermal dystrophy (APECED)Immediate early gene X1 (IEX-1) is organized in subnuclear structures and partially co-localizes with promyelocytic leukemia protein in HeLa cells.
P2860
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P2860
Human Daxx regulates Fas-induced apoptosis from nuclear PML oncogenic domains (PODs).
description
1999 nî lūn-bûn
@nan
1999年の論文
@ja
1999年学术文章
@wuu
1999年学术文章
@zh-cn
1999年学术文章
@zh-hans
1999年学术文章
@zh-my
1999年学术文章
@zh-sg
1999年學術文章
@yue
1999年學術文章
@zh
1999年學術文章
@zh-hant
name
Human Daxx regulates Fas-induced apoptosis from nuclear PML oncogenic domains (PODs).
@en
type
label
Human Daxx regulates Fas-induced apoptosis from nuclear PML oncogenic domains (PODs).
@en
prefLabel
Human Daxx regulates Fas-induced apoptosis from nuclear PML oncogenic domains (PODs).
@en
P2093
P356
P1433
P1476
Human Daxx regulates Fas-induced apoptosis from nuclear PML oncogenic domains (PODs)
@en
P2093
P304
P356
10.1093/EMBOJ/18.21.6037
P407
P577
1999-11-01T00:00:00Z