about
P688
tBID, a membrane-targeted death ligand, oligomerizes BAK to release cytochrome cProapoptotic BAX and BAK control multiple initiator caspasesProapoptotic Bak is sequestered by Mcl-1 and Bcl-xL, but not Bcl-2, until displaced by BH3-only proteins.BH3 domains other than Bim and Bid can directly activate Bax/BakIL-6 protects against hyperoxia-induced mitochondrial damage via Bcl-2-induced Bak interactions with mitofusinsProapoptotic BAX and BAK modulate the unfolded protein response by a direct interaction with IRE1alphaStructural plasticity underpins promiscuous binding of the prosurvival protein A1Intrinsic and extrinsic pathway signaling during neuronal apoptosis: lessons from the analysis of mutant miceProapoptotic BAX and BAK regulate the type 1 inositol trisphosphate receptor and calcium leak from the endoplasmic reticulumBax and Bak independently promote cytochrome C release from mitochondriaCell death provoked by loss of interleukin-3 signaling is independent of Bad, Bim, and PI3 kinase, but depends in part on PumaTemporal profiles of the subcellular localization of Bim, a BH3-only protein, during middle cerebral artery occlusion in miceThe mitochondrial protein Bak is pivotal for gliotoxin-induced apoptosis and a critical host factor of Aspergillus fumigatus virulence in miceThe combined functions of proapoptotic Bcl-2 family members bak and bax are essential for normal development of multiple tissuesEssential role of BAX,BAK in B cell homeostasis and prevention of autoimmune diseaseRadiation-induced gastric epithelial apoptosis occurs in the proliferative zone and is regulated by p53, bak, bax, and bcl-2Combined loss of proapoptotic genes Bak or Bax with Bim synergizes to cause defects in hematopoiesis and in thymocyte apoptosisBax and Bak can localize to the endoplasmic reticulum to initiate apoptosisGrowth factor regulation of autophagy and cell survival in the absence of apoptosisPersistent fetal ocular vasculature in mice deficient in bax and bakRole of Bax and Bak in mitochondrial morphogenesisExpression of Bcl-2 family during liver regeneration and identification of Bcl-x as a delayed early response geneBOK Is a Non-canonical BCL-2 Family Effector of Apoptosis Regulated by ER-Associated DegradationVDAC2 inhibits BAK activation and mitochondrial apoptosisBak regulates mitochondrial morphology and pathology during apoptosis by interacting with mitofusins.
P921
Q24290118-53BB80F5-5DA5-4DF4-B07C-F5FEF471787CQ24298402-669B1C5F-F618-4469-A1D2-27036C520F92Q24302494-29405767-D26C-46E7-AE27-CA1108D1DF0EQ24305138-4144A410-52E3-43B4-868C-D779634DBFCFQ24322036-18B2DAB6-D3AF-4FD7-ACEE-04789F701C2EQ24322072-D84CEDEC-03E1-4B57-B88F-18E2AC1A1387Q27650558-557397D6-B1A3-4175-9330-ECA14FE690BBQ28504500-0513AAEB-CFDB-4209-81F4-083109688A3DQ28506206-28396E93-C2A3-496A-A916-4E512FCC5B90Q28507634-2C2ECE46-CCCF-41AE-A54B-7195896B254EQ28507857-4D486439-A4C2-4195-9C8A-64E243F9D130Q28508507-D6DC03B5-0EC6-4D7F-9BC7-9F4CEE7D8F46Q28511677-8D2BCC35-3ADF-45D8-9DB2-7F717CE93E3BQ28512628-8971BB66-1BE7-43C4-B45B-2E44E2F38F32Q28513752-974A6296-3DB5-4A3E-9FC7-8FE2D9CE6B05Q28584915-BBBCBE34-0930-4307-AD7D-31DA998E78C2Q28587336-B10FE7D2-8D24-48CA-89B1-051C3065BD35Q28588618-9F9DBB21-65CC-4317-9625-FFF6B4384265Q28588809-7362C113-7761-4158-8B39-F53B5E1C5BBAQ28589564-4D111F0F-7581-43D0-8184-834D2862CC15Q28591724-98DFD7C6-3427-4EDF-8B0D-378507981501Q28593316-632813A9-262C-4E16-83DD-6078EDD4D6C4Q28593563-5D1966F4-A93B-43C9-B724-A8C8CC95AAD4Q28594000-7ED0C683-54F1-4058-AFD4-A2B317C50887Q35880175-A77061A9-18D6-429B-8931-544C85A1FD0A
P921
description
mammalian protein found in Mus musculus
@en
protein
@id
proteinë
@sq
proteïne in BCL2-antagonist/killer 1
@nl
protèin
@ace
بروتين في فأر المنازل
@ar
name
BCL2-antagonist/killer 1
@en
BCL2-antagonist/killer 1
@nl
type
label
BCL2-antagonist/killer 1
@en
BCL2-antagonist/killer 1
@nl
altLabel
Bak1
@en
Bcl2 homologous antagonist/killer
@en
apoptosis regulator BAK
@en
bcl-2 homologous antagonist/killer
@en
prefLabel
BCL2-antagonist/killer 1
@en
BCL2-antagonist/killer 1
@nl