BCL2 associated X, apoptosis regulator

BCL2 associated X, apoptosis regulator

Item
http://www.wikidata.org/entity/Q408476
Q21111616
sameAs
BAX
P688
Bax interacts with the permeability transition pore to induce permeability transition and cytochrome c release in isolated mitochondriaIdentification and characterization of baxepsilon, a novel bax variant missing the BH2 and the transmembrane domainsBax oligomerization is required for channel-forming activity in liposomes and to trigger cytochrome c release from mitochondriaDeficiency of caspase-3 in MCF7 cells blocks Bax-mediated nuclear fragmentation but not cell deathThe expression of a new variant of the pro-apoptotic molecule Bax, Baxpsi, is correlated with an increased survival of glioblastoma multiforme patientsCytosolic accumulation of HSP60 during apoptosis with or without apparent mitochondrial release: evidence that its pro-apoptotic or pro-survival functions involve differential interactions with caspase-3Involvement of Noxa in cellular apoptotic responses to interferon, double-stranded RNA, and virus infectionApoptosis initiated when BH3 ligands engage multiple Bcl-2 homologs, not Bax or BakInteraction with a membrane surface triggers a reversible conformational change in Bax normally associated with induction of apoptosisT-2 toxin induces apoptosis, and selenium partly blocks, T-2 toxin induced apoptosis in chondrocytes through modulation of the Bax/Bcl-2 ratioApoptosis via the B cell antigen receptor requires Bax translocation and involves mitochondrial depolarization, cytochrome C release, and caspase-9 activationMembrane remodeling induced by the dynamin-related protein Drp1 stimulates Bax oligomerizationThe cytosolic domain of human Tom22 modulates human Bax mitochondrial translocation and conformation in yeastThe endoplasmic reticulum is a key component of the plasma cell death pathwayInhibition of Bax activity is crucial for the antiapoptotic function of the human papillomavirus E6 oncoproteinViral apoptosis is induced by IRF-3-mediated activation of BaxDifferential contribution of Puma and Noxa in dual regulation of p53-mediated apoptotic pathwaysQuantitation of mitochondrial dynamics by photolabeling of individual organelles shows that mitochondrial fusion is blocked during the Bax activation phase of apoptosisA stapled BID BH3 helix directly binds and activates BAXDirect activation of Bax by p53 mediates mitochondrial membrane permeabilization and apoptosisDimerization properties of human BAD. Identification of a BH-3 domain and analysis of its binding to mutant BCL-2 and BCL-XL proteinsBax crystal structures reveal how BH3 domains activate Bax and nucleate its oligomerization to induce apoptosisA common binding site mediates heterodimerization and homodimerization of Bcl-2 family membersBax inhibitor-1, a mammalian apoptosis suppressor identified by functional screening in yeastPUMA Dissociates Bax and Bcl-X(L) to induce apoptosis in colon cancer cellsHepatitis C virus NS5A as a potential viral Bcl-2 homologue interacts with Bax and inhibits apoptosis in hepatocellular carcinomaClusterin inhibits apoptosis by interacting with activated BaxInhibition of Bax channel-forming activity by Bcl-2A novel pro-apoptotic function of RACK1: suppression of Src activity in the intrinsic and Akt pathwaysA short Nur77-derived peptide converts Bcl-2 from a protector to a killerRACK1 promotes Bax oligomerization and dissociates the interaction of Bax and Bcl-XLHematopoietic malignancies demonstrate loss-of-function mutations of BAXProapoptotic BAX and BAK modulate the unfolded protein response by a direct interaction with IRE1alphaBax activates endophilin B1 oligomerization and lipid membrane vesiculationMutation to Bax beyond the BH3 domain disrupts interactions with pro-survival proteins and promotes apoptosisMembrane binding by tBid initiates an ordered series of events culminating in membrane permeabilization by BaxProtein kinase C-epsilon protects MCF-7 cells from TNF-mediated cell death by inhibiting Bax translocationEndophilin B1/Bif-1 stimulates BAX activation independently from its capacity to produce large scale membrane morphological rearrangementsMAP-1 is a mitochondrial effector of Bax.Spatial and temporal association of Bax with mitochondrial fission sites, Drp1, and Mfn2 during apoptosis
P921
Q22008484-C75F0410-B99F-4712-BA0E-4A6E0A547C6BQ22008718-40D873A4-D9AA-4B98-8D88-3B3B071720FDQ22011013-0CC90076-5ABC-49F5-9832-79705529ADCBQ24291223-DE64E64D-3BAE-4BB2-BD43-4AE8765C5596Q24292678-B359EEF5-24ED-438C-902C-8A3CFBAB3192Q24292978-34F9C9D3-B939-40FA-BDB3-A08B643E9A86Q24294698-936F5BA9-5E73-4836-B8AB-3889BAEA95C4Q24296478-01E7339A-19FA-40CF-91B1-4BA9349A889AQ24296781-684B9423-85FE-4713-96E9-75645698C0BDQ24296958-AAB813C2-9069-41DD-BB49-7329B90F60ABQ24297540-4A37DBAA-3566-4A35-85D9-0C6DE0E7AEA2Q24300125-36E61BDF-B5ED-457F-86BD-74BFB84757D3Q24300635-83599904-80F5-4D19-A34E-0182A395018AQ24301496-058C7802-6CEB-4957-9DC1-628AF3A8BA31Q24303964-F5C841B8-00DB-47CC-B32B-91BEE0F1C1F5Q24305369-84F8DDD6-B912-4D09-A28B-13B15C174999Q24306130-B8044594-FA87-4C47-ADB9-4413BB48CF57Q24307662-BAEE7335-53D2-4F97-8A3B-6797E95FDD20Q24307663-19E24AF8-2609-43E5-84B1-E955A1F9A2D7Q24307994-471FE80D-CD7E-4F53-93A0-F2852DAAEEEAQ24310631-07E804B8-4A25-4923-9ED8-AFA85C3BC5A9Q24313049-4BC22422-1481-49EE-A3C6-463F6BDCA0F3Q24314405-A5131F2A-0C53-4253-A3AA-0866C1DFB520Q24314476-478BD06C-E3AA-497B-8EB2-15980EEDABF1Q24316443-61A136AA-E780-4CA5-A581-2F54D02FD680Q24316497-12629400-4528-47AD-BFE2-0CF119B74190Q24316499-2E790321-D412-45BF-8EF5-5F239513FDFBQ24317099-B4789D00-BCA6-401E-B43A-357AE366E628Q24317698-8D83299D-AF98-4147-AF41-35E8FA4856EFQ24319007-51FC0EEC-A5D9-42F3-BDF1-599F8A524EBDQ24319133-38C1D841-BC27-4A84-A4C2-ED5B67730EECQ24321995-73FD8313-A2FD-4DED-AE19-BE17C72B9D72Q24322072-E9552684-BA2E-4FEE-9B01-C0F20E4FA1F3Q24322581-BD4CC254-C092-4AEC-A734-9B860BE8842BQ24322798-459506AD-7B82-4E5A-BBF8-A026BE086075Q24323186-24A79E5B-A2CE-432D-897A-8464481AAEA0Q24324334-E4536416-0AA9-4D8F-8C79-9756A2D916D1Q24324817-5D00DFBF-5C04-4520-95F0-4ED60C92C88EQ24337383-24136F5B-34C3-458F-9EFB-7059CC01F289Q24337576-D924595E-15DF-4F48-A26D-4C9FC444BE49
P921

BCL2 associated X, apoptosis regulator

Item
http://www.wikidata.org/entity/Q408476
description
Protein in Homo sapiens
@de
mammalian protein found in Homo sapiens
@en
protein
@id
protein
@sv
proteinë
@sq
proteïne in BCL2 associated X, apoptosis regulator
@nl
protèin
@ace
protéine
@fr
بروتين في الإنسان العاقل
@ar
name
BAX
@cy
BAX
@uk
BCL2 associated X, apoptosis regulator
@en
BCL2 associated X, apoptosis regulator
@nl
Bax
@de
Bax
@pl
Bax
@tr
Bcl-2–associated X protein
@fr
Bcl-2結合Xタンパク質
@ja
Proteína X associada a BCL-2
@pt
type
label
BAX
@cy
BAX
@uk
BCL2 associated X, apoptosis regulator
@en
BCL2 associated X, apoptosis regulator
@nl
Bax
@de
Bax
@pl
Bax
@tr
Bcl-2–associated X protein
@fr
Bcl-2結合Xタンパク質
@ja
Proteína X associada a BCL-2
@pt
altLabel
BAX
@en
BCL2 associated X protein
@en
BCL2-associated X protein omega
@en
Bax
@fr
Baxdelta2G9
@en
Baxdelta2G9omega
@en
Baxdelta2omega
@en
Bcl-2-associated X protein
@fr
apoptosis regulator BAX
@en
bcl-2-like protein 4
@en
prefLabel
BAX
@cy
BAX
@uk
BCL2 associated X, apoptosis regulator
@en
BCL2 associated X, apoptosis regulator
@nl
Bax
@de
Bax
@pl
Bax
@tr
Bcl-2–associated X protein
@fr
Bcl-2結合Xタンパク質
@ja
Proteína X associada a BCL-2
@pt
P2888
P31
P352
P361
P486
P527
P6366
P637
P638
P646
P680
P681
P682
P692
P702
P703
P705
P7260
P352
P486
P6366
P637
P638
P646
P2888
P31
P352
P361
P486
P527
P6366
P637
P638
P646
P680
P681
P682
P692
P702
P703
P705
P7260