Interaction partners of Dlk/ZIP kinase: co-expression of Dlk/ZIP kinase and Par-4 results in cytoplasmic retention and apoptosis
about
ZIPK: a unique case of murine-specific divergence of a conserved vertebrate geneAATF inhibits aberrant production of amyloid beta peptide 1-42 by interacting directly with Par-4ZIP kinase triggers apoptosis from nuclear PML oncogenic domainsPar-4 inhibits Akt and suppresses Ras-induced lung tumorigenesisThe tumor suppressor Par-4 activates an extrinsic pathway for apoptosisNovel mitosis-specific phosphorylation of histone H3 at Thr11 mediated by Dlk/ZIP kinaseIdentification of a new form of death-associated protein kinase that promotes cell survivalIdentification of a unique core domain of par-4 sufficient for selective apoptosis induction in cancer cellsDe Novo Fragment Design for Drug Discovery and Chemical BiologyATF-7, a novel bZIP protein, interacts with the PRL-1 protein-tyrosine phosphataseDlk/ZIP kinase-induced apoptosis in human medulloblastoma cells: requirement of the mitochondrial apoptosis pathwayCharacterization of rat BLOS2/Ceap, a putative yeast She3 homolog, as interaction partner of apoptosis antagonizing transcription factor/Che-1Par-4: a new activator of myosin phosphataseDAP-like kinase interacts with the rat homolog of Schizosaccharomyces pombe CDC5 protein, a factor involved in pre-mRNA splicing and required for G2/M phase transition.Phosphorylation-dependent control of ZIPK nuclear import is species specificProstate apoptosis response protein 4 sensitizes human colon cancer cells to chemotherapeutic 5-FU through mediation of an NF kappaB and microRNA network.Prostate apoptosis response-4 is expressed in normal cholangiocytes, is down-regulated in human cholangiocarcinoma, and promotes apoptosis of neoplastic cholangiocytes when induced pharmacologicallyPar-4 transcriptionally regulates Bcl-2 through a WT1-binding site on the bcl-2 promoter.The DAP kinase family of pro-apoptotic proteins: novel players in the apoptotic game.DAP-kinase: from functional gene cloning to establishment of its role in apoptosis and cancer.Prostate apoptosis response 4 (Par-4), a novel substrate of caspase-3 during apoptosis activation.Zipper-interacting protein kinase promotes epithelial-mesenchymal transition, invasion and metastasis through AKT and NF-kB signaling and is associated with metastasis and poor prognosis in gastric cancer patients.Par-4 downregulation promotes breast cancer recurrence by preventing multinucleation following targeted therapy.Apoptosis and tumor resistance conferred by Par-4The Par-4/PTEN connection in tumor suppression.Cancer-selective apoptotic effects of extracellular and intracellular Par-4.Zipper interacting protein kinase (ZIPK): function and signaling.The DAPK family: a structure-function analysis.pH-induced folding of an apoptotic coiled coil.Caspase-8-mediated PAR-4 cleavage is required for TNFα-induced apoptosis.Reovirus-induced alteration in expression of apoptosis and DNA repair genes with potential roles in viral pathogenesis.Death-associated protein kinase phosphorylates ZIP kinase, forming a unique kinase hierarchy to activate its cell death functions.C-terminal truncation of Dlk/ZIP kinase leads to abrogation of nuclear transport and high apoptotic activity.Structural basis for the regulatory interactions of proapoptotic Par-4.Stabilization of a pH-sensitive apoptosis-linked coiled coil through single point mutationsCloning, expression, purification, crystallization and preliminary crystallographic analysis of the C-terminal domain of Par-4 (PAWR).Par-4 is an essential downstream target of DAP-like kinase (Dlk) in Dlk/Par-4-mediated apoptosis.The pro-apoptotic protein Par-4 facilitates vascular contractility by cytoskeletal targeting of ZIPK.HeLa ZIP kinase induces diphosphorylation of myosin II regulatory light chain and reorganization of actin filaments in nonmuscle cells.ZIP kinase plays a crucial role in androgen receptor-mediated transcription.
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P2860
Interaction partners of Dlk/ZIP kinase: co-expression of Dlk/ZIP kinase and Par-4 results in cytoplasmic retention and apoptosis
description
1999 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
artículu científicu espublizáu en 1999
@ast
im Dezember 1999 veröffentlichter wissenschaftlicher Artikel
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scientific journal article
@en
vedecký článok (publikovaný 1999/12/02)
@sk
vědecký článek publikovaný v roce 1999
@cs
wetenschappelijk artikel (gepubliceerd op 1999/12/02)
@nl
наукова стаття, опублікована в грудні 1999
@uk
مقالة علمية (نشرت في 2-12-1999)
@ar
name
Interaction partners of Dlk/ZI ...... lasmic retention and apoptosis
@ast
Interaction partners of Dlk/ZI ...... lasmic retention and apoptosis
@en
Interaction partners of Dlk/ZI ...... lasmic retention and apoptosis
@nl
type
label
Interaction partners of Dlk/ZI ...... lasmic retention and apoptosis
@ast
Interaction partners of Dlk/ZI ...... lasmic retention and apoptosis
@en
Interaction partners of Dlk/ZI ...... lasmic retention and apoptosis
@nl
prefLabel
Interaction partners of Dlk/ZI ...... lasmic retention and apoptosis
@ast
Interaction partners of Dlk/ZI ...... lasmic retention and apoptosis
@en
Interaction partners of Dlk/ZI ...... lasmic retention and apoptosis
@nl
P2093
P2860
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P1433
P1476
Interaction partners of Dlk/ZI ...... lasmic retention and apoptosis
@en
P2093
K. H. Scheidtmann
V. Rangnekar
P2860
P2888
P304
P356
10.1038/SJ.ONC.1203170
P407
P577
1999-12-02T00:00:00Z
P5875
P6179
1053099685