Building blocks of the apoptotic pore: how Bax and Bak are activated and oligomerize during apoptosis - Wikidata - awgldk - TriplyDB

Building blocks of the apoptotic pore: how Bax and Bak are activated and oligomerize during apoptosis

Building blocks of the apoptotic pore: how Bax and Bak are activated and oligomerize during apoptosis

http://www.wikidata.org/entity/Q28300914

about

Mitochondria, cholesterol and cancer cell metabolism DNA repair and aging: the impact of the p53 family Getting TRAIL back on track for cancer therapy The Janus Face of Death Receptor Signaling during Tumor Immunoediting Minimalist Model Systems Reveal Similarities and Differences between Membrane Interaction Modes of MCL1 and BAK Synthetic Antibodies Inhibit Bcl-2-associated X Protein (BAX) through Blockade of the N-terminal Activation Site.Leptin is an anti-apoptotic effector in placental cells involving p53 downregulation.Release of Cytochrome C from Bax Pores at the Mitochondrial Membrane.Apoptotic pore formation is associated with in-plane insertion of Bak or Bax central helices into the mitochondrial outer membrane Conformational rearrangements in the pro-apoptotic protein, Bax, as it inserts into mitochondria: a cellular death switch.Visual and functional demonstration of growing Bax-induced pores in mitochondrial outer membranes.Mitochondria and apoptosis: emerging concepts.Structural transition in Bcl-xL and its potential association with mitochondrial calcium ion transport Obatoclax is a direct and potent antagonist of membrane-restricted Mcl-1 and is synthetic lethal with treatment that induces Bim.Programmed cell death in aging.Chorein addiction in VPS13A overexpressing rhabdomyosarcoma cells Apoptosis-Related Factors in the Luteal Phase of the Domestic Cat and Their Involvement in the Persistence of Corpora Lutea in Lynx.An interconnected hierarchical model of cell death regulation by the BCL-2 family XIAP-targeting drugs re-sensitize PIK3CA-mutated colorectal cancer cells for death receptor-induced apoptosis.Time-course gene profiling and networks in demethylated retinoblastoma cell line.BH3-in-groove dimerization initiates and helix 9 dimerization expands Bax pore assembly in membranes An FGF3-BMP Signaling Axis Regulates Caudal Neural Tube Closure, Neural Crest Specification and Anterior-Posterior Axis Extension.Bcl-xL Is Essential for the Survival and Function of Differentiated Neurons in the Cortex That Control Complex Behaviors.Identification of an activation site in Bak and mitochondrial Bax triggered by antibodies.In Situ Characterization of Bak Clusters Responsible for Cell Death Using Single Molecule Localization Microscopy.Conformational Heterogeneity of Bax Helix 9 Dimer for Apoptotic Pore Formation Oncogenic Mutations Differentially Affect Bax Monomer, Dimer, and Oligomeric Pore Formation in the Membrane.Redefining the BH3 Death Domain as a 'Short Linear Motif'.Impact of loss of BH3-only proteins on the development and treatment of MLL-fusion gene-driven AML in mice.Preclinical Studies of a Kidney Safe Iodinated Contrast Agent.Cytosolic Ku70 regulates Bax-mediated cell death.Bax/Bak activation in the absence of Bid, Bim, Puma, and p53.Hypoxia regulates TRAIL sensitivity of colorectal cancer cells through mitochondrial autophagy.Cancer chemoresistance and BAK The Bcl-2 family: structures, interactions and targets for drug discovery.Discoveries and controversies in BCL-2 protein-mediated apoptosis.Perioperative "remote" acute lung injury: recent update.Computational studies of peptide-induced membrane pore formation.Ceramide channels and mitochondrial outer membrane permeability.Apoptosis induced by a snake venom metalloproteinase from Bothrops alternatus venom in C2C12 muscle cells.

P2860

Q26741708-54EE11A1-ED20-43DC-A6A5-3673E33D2519 Q26775866-9BECF965-1095-4309-A347-1E0547D9555B Q27027460-E7EF3E61-FFEB-4A2F-A065-BEC6B28630DB Q28070036-0A731022-969F-4040-929F-B9186BB8A131 Q28383717-C0AC4FA1-2788-498A-B7F8-D8B88E32C8FF Q30381337-32AB3551-2075-445E-B817-F9E2B55B8494 Q33749053-6FD4B98B-7E66-4F31-BA5E-F436691D0BF6 Q33752784-AACB82CF-E7E5-466F-9436-69C6FFCFA962 Q34314503-BBB7A845-0CC9-46D8-A9EE-2D6B5887E3C9 Q34552749-B75EEF43-B7A1-4B21-AF5C-1681AE56416E Q34960771-2FB8838A-7D24-449D-80FC-056A2ECB367E Q35659301-9931F0B7-118A-4EC3-95B1-26509E444D57 Q35663795-6CE0598E-3176-4CC2-B180-6EE10D588B66 Q35731554-75F17F4A-091D-4F59-92ED-4FCEC85DE7B5 Q35779447-7B4244B0-D214-4D39-8A57-EB7F8827F777 Q35832986-D55160B9-ADE8-4746-887D-983D1715CBD0 Q35850308-20E89F03-3BFF-4276-B9AA-947DD970FEC0 Q36109186-2E6D564E-3C95-41A1-8957-F8EFCDB1F4B3 Q36292020-7D5CF606-432D-46B0-ACF3-66484C3AD197 Q36414265-FA7F708B-2B0E-4933-A0D7-3A03853FB902 Q36478810-B1CC7109-2B61-4744-995D-C44F069AAFE4 Q36868683-088B525E-0754-4512-8932-9D732A08DABE Q36914292-4B841A61-0348-4B9A-9C08-BCB22608703D Q36960198-8B015F47-E016-4D7C-94B4-68ADC15624E3 Q36996518-6B8B1165-4E88-45D0-865D-2A4863E5B544 Q37067833-841A37AD-E83B-45AE-BED0-87E8383C842B Q37257680-5693FE9B-71E0-4B57-B82E-1A0819FFE6A4 Q37324058-8BE7DC8C-63AA-41BC-9E7E-E9BA55FCDF18 Q37330840-D2789941-D414-418A-842C-D167121E82CB Q37375593-EC412A41-F6B7-484C-B417-F36D77D2B8F7 Q37396048-F2E2B797-E17F-43B8-8E85-EFA86146DF30 Q37482805-4E13E909-BEB9-4857-9736-EE9619D4BDB6 Q37520269-7D4B5C88-832E-4F75-B7AC-ADA8AA36948E Q38259648-5A449670-9256-42FA-B650-D191D7D0C859 Q38268329-80B0E136-AB47-40AC-B3DE-51E225A0EBBB Q38593940-B1195E7A-98B9-4573-8988-D67255EF7F05 Q38642506-9F526740-7514-47AA-8E4A-0210FAD369A9 Q38669154-D1E7C46C-3F02-4718-9ED9-563B8D1734BF Q38708390-CE6AC175-4224-49D2-B7AE-240FFD10767D Q38716227-07ADBD92-81A6-46B9-89CB-06711FF87E5A

P2860

Building blocks of the apoptotic pore: how Bax and Bak are activated and oligomerize during apoptosis

http://www.wikidata.org/entity/Q28300914

description

2014 nî lūn-bûn

@nan

2014 թուականի Փետրուարին հրատարակուած գիտական յօդուած

@hyw

2014 թվականի փետրվարին հրատարակված գիտական հոդված

@hy

2014年の論文

@ja

2014年論文

@yue

2014年論文

@zh-hant

2014年論文

@zh-hk

2014年論文

@zh-mo

2014年論文

@zh-tw

2014年论文

@wuu

name

Building blocks of the apoptot ...... d oligomerize during apoptosis

@ast

Building blocks of the apoptot ...... d oligomerize during apoptosis

@en

Building blocks of the apoptot ...... d oligomerize during apoptosis

@nl

type

label

Building blocks of the apoptot ...... d oligomerize during apoptosis

@ast

Building blocks of the apoptot ...... d oligomerize during apoptosis

@en

Building blocks of the apoptot ...... d oligomerize during apoptosis

@nl

prefLabel

Building blocks of the apoptot ...... d oligomerize during apoptosis

@ast

Building blocks of the apoptot ...... d oligomerize during apoptosis

@en

Building blocks of the apoptot ...... d oligomerize during apoptosis

@nl

P1433

Q28300914-646971B2-4760-4988-A999-5EABE4ADF6CA

P1476

Q28300914-3F86035E-0664-4C28-A849-4F26AA366650

P2093

Q28300914-52805C6C-15CF-4D69-A39D-39C3AFA46F73

Q28300914-EE27D569-4344-459A-BE5D-F737B9E762AE

P2860

Q28300914-03C4AC93-F039-4BFD-9A2C-471C8170A63E

Q28300914-051414DB-26B6-4C56-A2E6-8E6FFEF3E584

Q28300914-069D4A65-EFD8-48AC-96F0-02C218548944

Q28300914-07D5860B-9108-4346-AE9E-AD8716644329

Q28300914-09A89B8C-1EBF-4391-B22B-659FD442E316

Q28300914-09C92F91-45B0-49DA-B633-9FFA7691D3B1

Q28300914-0BCB7BB8-2E56-4C44-BC30-6EA0A68CA207

Q28300914-0D2D7D1C-CD76-4DD6-8279-CF3B4D2996EA

Q28300914-1062317F-69DD-4986-8126-958C73245F6B

Q28300914-18057126-CDFA-41ED-B596-A7CA38ABE3F0

P2888

Q28300914-FBFC59C4-D95B-49C8-94F0-7E97DB3E3FF9

P304

Q28300914-8D83BC0E-DB2A-4290-9DAA-679DF1BF76C0

P31

Q28300914-1E751DC5-E6B3-4BEA-AAD3-7BB5B1BB01E2

P3181

Q28300914-7BD98F91-5AB6-42E1-971F-5266C3F10C40

P356

Q28300914-AC6548F4-9ABD-403B-8426-E0A97CEE5770

P407

Q28300914-6431791C-ABF5-426D-92A6-C32076A7E668

P433

Q28300914-30071C28-E620-4D92-8BF3-50A639C42700

P478

Q28300914-102FF909-0360-4B58-A5A7-5130A4A3FA2E

P50

Q28300914-5A640CAF-236F-42A7-9F31-667A369BCC9A

P577

Q28300914-597097D6-99E3-4C5E-A724-52D2928E989B

P5875

Q28300914-59BC59C5-63B9-4D20-BDD7-BD2AB367DC82

P698

Q28300914-A3A7E459-A2D3-45FC-8F71-167C1D3CF2FD

P921

Q28300914-A970C393-254E-4972-9E10-D6CB4CB9998A

Q28300914-B06E11E9-9AD5-4F19-92A2-FBDFCB9EE747

P932

Q28300914-5C6DDA12-D017-473E-AF75-4E290B64B02D

P3181

P356

P1433

Cell Death & Differentiation

P1476

Building blocks of the apoptot ...... d oligomerize during apoptosis

@en

P2093

D Westphal

http://www.w3.org/2001/XMLSchema#string

G Dewson

http://www.w3.org/2001/XMLSchema#string

P2860

tBID, a membrane-targeted death ligand, oligomerizes BAK to release cytochrome c

tBid undergoes multiple conformational changes at the membrane required for Bax activation

Apoptosis initiated when BH3 ligands engage multiple Bcl-2 homologs, not Bax or Bak

Interaction with a membrane surface triggers a reversible conformational change in Bax normally associated with induction of apoptosis

Bcl-x(L) retrotranslocates Bax from the mitochondria into the cytosol

Membrane remodeling induced by the dynamin-related protein Drp1 stimulates Bax oligomerization

Proapoptotic Bak is sequestered by Mcl-1 and Bcl-xL, but not Bcl-2, until displaced by BH3-only proteins.

IBRDC2, an IBR-type E3 ubiquitin ligase, is a regulatory factor for Bax and apoptosis activation

BH3 domains other than Bim and Bid can directly activate Bax/Bak

A stapled BID BH3 helix directly binds and activates BAX

P2888

P304

196-205

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P3181

228629

http://www.w3.org/2001/XMLSchema#string

P356

10.1038/CDD.2013.139

http://www.w3.org/2001/XMLSchema#string

P407

P433

2

http://www.w3.org/2001/XMLSchema#string

P478

21

http://www.w3.org/2001/XMLSchema#string

P50

P577

2013-10-25T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

258103469

http://www.w3.org/2001/XMLSchema#string

P698

24162660

http://www.w3.org/2001/XMLSchema#string

P921

apoptotic process

P932

3890949

http://www.w3.org/2001/XMLSchema#string