Intracellular localization of the BCL-2 family member BOK and functional implications
about
Bag6 complex contains a minimal tail-anchor-targeting module and a mock BAG domainThe Bcl-2 protein family member Bok binds to the coupling domain of inositol 1,4,5-trisphosphate receptors and protects them from proteolytic cleavageCell biology. Metabolic control of cell deathBCL-2 family member BOK promotes apoptosis in response to endoplasmic reticulum stressThe Stability and Expression Level of Bok Are Governed by Binding to Inositol 1,4,5-Trisphosphate ReceptorsBOK Is a Non-canonical BCL-2 Family Effector of Apoptosis Regulated by ER-Associated DegradationMitochondrial apoptosis is dispensable for NLRP3 inflammasome activation but non-apoptotic caspase-8 is required for inflammasome primingp53 at the endoplasmic reticulum regulates apoptosis in a Ca2+-dependent manner.Intravital imaging reveals p53-dependent cancer cell death induced by phototherapy via calcium signaling.Golgi fragmentation and sphingomyelin transport to Chlamydia trachomatis during penicillin-induced persistence do not depend on the cytosolic presence of the chlamydial protease CPAFFunctional conservation of the apoptotic machinery from coral to man: the diverse and complex Bcl-2 and caspase repertoires of Acropora millepora.Impact of the combined loss of BOK, BAX and BAK on the hematopoietic system is slightly more severe than compound loss of BAX and BAKInactivation of prosurvival Bcl-2 proteins activates Bax/Bak through the outer mitochondrial membrane.Consequences of the combined loss of BOK and BAK or BOK and BAX.Contribution of apoptosis-associated signaling pathways to epileptogenesis: lessons from Bcl-2 family knockouts.Structural biology of the Bcl-2 family and its mimicry by viral proteinsInterrogating the relevance of mitochondrial apoptosis for vertebrate development and postnatal tissue homeostasisPharmacological inhibition of Bcl-xL sensitizes osteosarcoma to doxorubicin.The mystery of BCL2 family: Bcl-2 proteins and apoptosis: an update.BOK displays cell death-independent tumor suppressor activity in non-small-cell lung carcinoma.Bcl-2 proteins and calcium signaling: complexity beneath the surface.Oncogenic and oncosuppressive signal transduction at mitochondria-associated endoplasmic reticulum membranesOverexpression of CREB protein protects from tunicamycin-induced apoptosis in various rat cell types.BCL-2 family: integrating stress responses at the ER to control cell demise.Is BOK required for apoptosis induced by endoplasmic reticulum stress?Reply to Fernandez-Marrero et al.: Role of BOK at the intersection of endoplasmic reticulum stress and apoptosis regulation.Monocytes enhance neutrophil-induced blister formation in an ex vivo model of bullous pemphigoid.Evidence for a role of eosinophils in blister formation in bullous pemphigoid.MOMP, cell suicide as a BCL-2 family business.Novel post-transcriptional and post-translational regulation of pro-apoptotic protein BOK and anti-apoptotic protein Mcl-1 determine the fate of breast cancer cells to survive or die.BOK promotes chemical-induced hepatocarcinogenesis in mice.Bax, Bak and beyond - mitochondrial performance in apoptosis.Molecular mechanisms of cell death: recommendations of the Nomenclature Committee on Cell Death 2018.The BAX/BAK-like protein BOK is a prognostic marker in colorectal cancer.The membrane activity of BOK involves formation of large, stable toroidal pores and is promoted by cBID.Ceramide-induced BOK promotes mitochondrial fission in preeclampsia.There is something about BOK we just don't get yet.Subcellular Localization and Dynamics of the Bcl-2 Family of Proteins.Targeting BCL-2 regulated apoptosis in cancer.Loss of BID Delays FASL-Induced Cell Death of Mouse Neutrophils and Aggravates DSS-Induced Weight Loss.
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P2860
Intracellular localization of the BCL-2 family member BOK and functional implications
description
2013 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2013 թվականի հունիսին հրատարակված գիտական հոդված
@hy
artículu científicu espublizáu en 2013
@ast
im Juni 2013 veröffentlichter wissenschaftlicher Artikel
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scientific journal article
@en
vedecký článok (publikovaný 2013/06/01)
@sk
vědecký článek publikovaný v roce 2013
@cs
wetenschappelijk artikel (gepubliceerd op 2013/06/01)
@nl
наукова стаття, опублікована в червні 2013
@uk
مقالة علمية (نشرت في يونيو 2013)
@ar
name
Intracellular localization of the BCL-2 family member BOK and functional implications
@ast
Intracellular localization of the BCL-2 family member BOK and functional implications
@en
Intracellular localization of the BCL-2 family member BOK and functional implications
@nl
type
label
Intracellular localization of the BCL-2 family member BOK and functional implications
@ast
Intracellular localization of the BCL-2 family member BOK and functional implications
@en
Intracellular localization of the BCL-2 family member BOK and functional implications
@nl
prefLabel
Intracellular localization of the BCL-2 family member BOK and functional implications
@ast
Intracellular localization of the BCL-2 family member BOK and functional implications
@en
Intracellular localization of the BCL-2 family member BOK and functional implications
@nl
P2093
P2860
P356
P1476
Intracellular localization of the BCL-2 family member BOK and functional implications
@en
P2093
D. Bachmann
H. U. Simon
N. Echeverry
P2860
P2888
P304
P356
10.1038/CDD.2013.10
P577
2013-06-01T00:00:00Z