Conformation of membrane-associated proapoptotic tBid. - Wikidata - awgldk - TriplyDB

Conformation of membrane-associated proapoptotic tBid.

Conformation of membrane-associated proapoptotic tBid.

http://www.wikidata.org/entity/Q34549543

about

Structural Insights of tBid, the Caspase-8-activated Bid, and Its BH3 Domain Active fragments from pro- and antiapoptotic BCL-2 proteins have distinct membrane behavior reflecting their functional divergence The rheostat in the membrane: BCL-2 family proteins and apoptosis Dynamic interaction of cBid with detergents, liposomes and mitochondria.Effect of hyperthermia in combination with TRAIL on the JNK-Bim signal transduction pathway and growth of xenograft tumors.Lung injury caused by high tidal volume mechanical ventilation and hyperoxia is dependent on oxidant-mediated c-Jun NH2-terminal kinase activation.Nur77 converts phenotype of Bcl-B, an antiapoptotic protein expressed in plasma cells and myeloma Phosphatidic acid mediates the targeting of tBid to induce lysosomal membrane permeabilization and apoptosis.Bid chimeras indicate that most BH3-only proteins can directly activate Bak and Bax, and show no preference for Bak versus Bax.Embedded together: the life and death consequences of interaction of the Bcl-2 family with membranes.Structure, topology, and tilt of cell-signaling peptides containing nuclear localization sequences in membrane bilayers determined by solid-state NMR and molecular dynamics simulation studies Mapping the interaction of pro-apoptotic tBID with pro-survival BCL-XL.Bid: a Bax-like BH3 protein.Discoveries and controversies in BCL-2 protein-mediated apoptosis.A179L, a viral Bcl-2 homologue, targets the core Bcl-2 apoptotic machinery and its upstream BH3 activators with selective binding restrictions for Bid and Noxa.Peptides derived from apoptotic Bax and Bid reproduce the poration activity of the parent full-length proteins Optimizing oriented planar-supported lipid samples for solid-state protein NMR.Molecular details of Bax activation, oligomerization, and membrane insertion.Inhibition of cytochrome c release by 10-N-nonyl acridine orange, a cardiolipin-specific dye, during myocardial ischemia-reperfusion in the rat.BIM and tBID are not mechanistically equivalent when assisting BAX to permeabilize bilayer membranes.

P2860

Q27680461-E88868A8-125E-4020-8757-157995F3DD1E Q28749082-A294A180-E036-44AF-90D8-894FB4690D13 Q34038716-E48E1600-0869-4F1B-B3F0-773DAEE4B9E5 Q34249427-420E2A19-2C6E-46FE-BD8A-EF4E449FB00C Q34257806-BAFF7EDC-6F0B-4F68-BE14-1E68C688B126 Q35562018-0D540B0D-8D18-4E9E-998E-78CE7E5592F2 Q35804409-2007CF6F-919F-4338-9512-2AC3B785B9E1 Q36213869-B639D2F3-9821-44E6-86BA-2353DBBF8C15 Q36293251-CB6AD2F2-4B5F-407C-A966-6458B9C4CD44 Q36799170-58967741-2386-4150-82A8-37534A230B09 Q36857817-8897ABA7-415A-4F90-9038-FBE50FAEA095 Q37389520-9FA1F72E-C2EB-4839-9DA3-21F1344E0E3A Q37566240-31237F6B-597E-40E7-9A84-CA5C420D84D0 Q38593940-3E7EAAF7-6D2B-49B0-A29B-3DD5B552AFC4 Q40004302-6093BB96-26C6-41CE-A0B8-8BF7F03FC874 Q40334590-68231943-85D7-44CE-BA61-D62A8189DB7C Q42121023-96A77C5C-86CD-44FC-A27E-DA2181F8CACD Q42910802-6C62B338-8BDA-417D-98DE-4C2CDFB23A3A Q43235366-F5CCFFC4-52DB-4EDA-85CD-22DFE49392DD Q46808299-6ECAF606-A3CF-4879-B834-FBEFE65EF3B0

P2860

Conformation of membrane-associated proapoptotic tBid.

http://www.wikidata.org/entity/Q34549543

description

2004 nî lūn-bûn

@nan

2004 թուականի Ապրիլին հրատարակուած գիտական յօդուած

@hyw

2004 թվականի ապրիլին հրատարակված գիտական հոդված

@hy

2004年の論文

@ja

2004年論文

@yue

2004年論文

@zh-hant

2004年論文

@zh-hk

2004年論文

@zh-mo

2004年論文

@zh-tw

2004年论文

@wuu

name

Conformation of membrane-associated proapoptotic tBid.

@ast

Conformation of membrane-associated proapoptotic tBid.

@en

Conformation of membrane-associated proapoptotic tBid.

@nl

type

label

Conformation of membrane-associated proapoptotic tBid.

@ast

Conformation of membrane-associated proapoptotic tBid.

@en

Conformation of membrane-associated proapoptotic tBid.

@nl

prefLabel

Conformation of membrane-associated proapoptotic tBid.

@ast

Conformation of membrane-associated proapoptotic tBid.

@en

Conformation of membrane-associated proapoptotic tBid.

@nl

P1433

Q34549543-BB646C88-9AFF-43EB-8A73-B9816813DDB8

P1476

Q34549543-1331531E-FF10-4985-8482-BE887CFF2EDA

P2093

Q34549543-027955F4-AF15-413A-9AD3-39A0126EA54E

Q34549543-11495006-B430-4F56-85B2-2CC761C70F62

Q34549543-142C0BA8-7718-4609-B4C4-A18155C04DBC

Q34549543-4B6D9B67-E77B-4445-80C9-2452359CFD8C

Q34549543-6D33711C-BB39-47D1-B9B4-D690781C989F

Q34549543-A7520489-46FF-42E7-95BA-E35037FC3BA6

P2860

Q34549543-02520BB4-FCD8-4615-8F6F-1422E609B4CA

Q34549543-04348D6A-5C0F-43CC-BBFD-9128A1F01850

Q34549543-05B4DD55-43A6-4DD3-ABAF-4DD1449B0DA7

Q34549543-091001AD-76CA-49CF-8621-290F6ECB2DF5

Q34549543-10349631-34A4-47F6-967F-358E34BF75D4

Q34549543-1036498F-D330-4C56-8BC9-F7E42FC70AF4

Q34549543-128C7DDA-1DD4-427A-B818-4BED3C20535F

Q34549543-19D7B3F8-721D-4C8D-9367-EB8DEE90FF53

Q34549543-1CEC500B-5E9B-4390-8F07-3EC9DE98574F

Q34549543-1DC56E44-8084-4C22-AAB9-078791E7F9DF

P304

Q34549543-5022AA99-7740-49C8-B077-EF0F2AD6D373

P31

Q34549543-9C42664B-AC49-49B3-8A5F-A6715211FDDB

P356

Q34549543-529BB8AC-853C-4A91-B851-C9529A75EBA4

P407

Q34549543-755A9BC9-0039-4AA7-A0E1-802A61D3D031

P433

Q34549543-233B206F-B7EE-4538-BC9C-C1875ACED6EA

P478

Q34549543-1CAC3EAA-355C-42DA-AE71-9C4A0DC022C5

P577

Q34549543-E0B8D3D1-7421-4770-95FC-0BAD5F410062

P698

Q34549543-937352DD-EA4A-4575-BA31-B627C7513E49

P932

Q34549543-FF5E7E17-8C1B-4A5C-B644-8ED69D9FC4A3

P356

P1433

Journal of Biological Chemistry

P1476

Conformation of membrane-associated proapoptotic tBid.

@en

P2093

Carla M Franzin

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

Dayong Zhai

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

Francesca M Marassi

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

John C Reed

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

Jungyuen Choi

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

Xiao-Min Gong

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

P2860

Humanin peptide suppresses apoptosis by interfering with Bax activation

Bid, a Bcl2 interacting protein, mediates cytochrome c release from mitochondria in response to activation of cell surface death receptors

Cleavage of BID by caspase 8 mediates the mitochondrial damage in the Fas pathway of apoptosis

BID: a novel BH3 domain-only death agonist

Structural basis for the conformational adaptability of apolipophorin III, a helix-bundle exchangeable apolipoprotein.

The structure of Bcl-w reveals a role for the C-terminal residues in modulating biological activity

Solution structure of BID, an intracellular amplifier of apoptotic signaling

Solution structure of the proapoptotic molecule BID: a structural basis for apoptotic agonists and antagonists

Structure of Bax: coregulation of dimer formation and intracellular localization

Solution structure of human BCL-w: modulation of ligand binding by the C-terminal helix

P304

28954-28960

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

P31

scholarly article

P356

10.1074/JBC.M403490200

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

P407

P433

28

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

P478

279

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

P577

2004-04-28T00:00:00Z

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

P698

15123718

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

P932

3033194

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