Proapoptotic BH3-only proteins trigger membrane integration of prosurvival Bcl-w and neutralize its activity - Wikidata - thesis-toulmin - TriplyDB

Proapoptotic BH3-only proteins trigger membrane integration of prosurvival Bcl-w and neutralize its activity

Proapoptotic BH3-only proteins trigger membrane integration of prosurvival Bcl-w and neutralize its activity

http://www.wikidata.org/entity/Q24675444

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Bcl-x(L) sequesters its C-terminal membrane anchor in soluble, cytosolic homodimers Evidence that Ser87 of BimEL is phosphorylated by Akt and regulates BimEL apoptotic function Proapoptotic Bak is sequestered by Mcl-1 and Bcl-xL, but not Bcl-2, until displaced by BH3-only proteins.Ankyrin repeat and suppressors of cytokine signaling box protein asb-9 targets creatine kinase B for degradation An internal EELD domain facilitates mitochondrial targeting of Mcl-1 via a Tom70-dependent pathway Structural Basis for Apoptosis Inhibition by Epstein-Barr Virus BHRF1 The restricted binding repertoire of Bcl-B leaves Bim as the universal BH3-only prosurvival Bcl-2 protein antagonist A1/Bfl-1 in leukocyte development and cell death Integral membrane proteins in the mitochondrial outer membrane of Saccharomyces cerevisiae.Building blocks of the apoptotic pore: how Bax and Bak are activated and oligomerize during apoptosis FNDC3A is required for adhesion between spermatids and Sertoli cells Bcl-XL is qualitatively different from and ten times more effective than Bcl-2 when expressed in a breast cancer cell line Intrinsically disordered proteins in bcl-2 regulated apoptosis.An imbalance between apoptosis and proliferation contributes to follicular persistence in polycystic ovaries in rats Auto-activation of the apoptosis protein Bax increases mitochondrial membrane permeability and is inhibited by Bcl-2 A novel Bcl-2-like inhibitor of apoptosis is encoded by the parapoxvirus ORF virus Bcl-XL inhibits membrane permeabilization by competing with Bax.Determination of cell survival by RING-mediated regulation of inhibitor of apoptosis (IAP) protein abundance ROS production is essential for the apoptotic function of E2F1 in pheochromocytoma and neuroblastoma cell lines.The Bcl-2 family: roles in cell survival and oncogenesis.Ligand binding and membrane insertion compete with oligomerization of the BclXL apoptotic repressor Bcl-w protects hippocampus during experimental status epilepticus.Mitochondrial permeabilization relies on BH3 ligands engaging multiple prosurvival Bcl-2 relatives, not Bak.BCL2 family of apoptosis-related genes: functions and clinical implications in cancer.Exploring the contribution of estrogen to amyloid-Beta regulation: a novel multifactorial computational modeling approach.Direct activation of full-length proapoptotic BAK Chelerythrine induces apoptosis through a Bax/Bak-independent mitochondrial mechanism.Embedded together: the life and death consequences of interaction of the Bcl-2 family with membranes.Yeast techniques for modeling drugs targeting Bcl-2 and caspase family members.Mechanisms of action of Bcl-2 family proteins Blood-stage Plasmodium infection induces CD8+ T lymphocytes to parasite-expressed antigens, largely regulated by CD8alpha+ dendritic cells.Bim regulation may determine hippocampal vulnerability after injurious seizures and in temporal lobe epilepsy.C-terminal residues regulate localization and function of the antiapoptotic protein Bfl-1.Molecular basis for Bcl-2 homology 3 domain recognition in the Bcl-2 protein family: identification of conserved hot spot interactions.Structural biology of the intrinsic cell death pathway: what do we know and what is missing?In vivo contributions of BH3-only proteins to neuronal death following seizures, ischemia, and traumatic brain injury.How vaccinia virus has evolved to subvert the host immune response.The Bcl-2 family: structures, interactions and targets for drug discovery.The use of a neutral peptide aptamer scaffold to anchor BH3 peptides constitutes a viable approach to studying their function BAX to basics: How the BCL2 gene family controls the death of retinal ganglion cells.

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P2860

Proapoptotic BH3-only proteins trigger membrane integration of prosurvival Bcl-w and neutralize its activity

http://www.wikidata.org/entity/Q24675444

description

2003 nî lūn-bûn

@nan

2003 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

@hyw

2003 թվականի սեպտեմբերին հրատարակված գիտական հոդված

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2003年の論文

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2003年論文

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2003年論文

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2003年論文

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2003年論文

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2003年論文

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2003年论文

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name

Proapoptotic BH3-only proteins ...... -w and neutralize its activity

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Proapoptotic BH3-only proteins ...... -w and neutralize its activity

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Proapoptotic BH3-only proteins ...... -w and neutralize its activity

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type

label

Proapoptotic BH3-only proteins ...... -w and neutralize its activity

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Proapoptotic BH3-only proteins ...... -w and neutralize its activity

@en

Proapoptotic BH3-only proteins ...... -w and neutralize its activity

@nl

prefLabel

Proapoptotic BH3-only proteins ...... -w and neutralize its activity

@ast

Proapoptotic BH3-only proteins ...... -w and neutralize its activity

@en

Proapoptotic BH3-only proteins ...... -w and neutralize its activity

@nl

P1433

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P1433

Journal of Cell Biology

P1476

Proapoptotic BH3-only proteins ...... -w and neutralize its activity

@en

P2093

David C S Huang

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

George Hausmann

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

Jennifer G Beaumont

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

Jerry M Adams

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

Julie Wilson-Annan

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

Lin Chen

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

Loes P Parma

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

Lorraine A O'Reilly

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

Mark G Hinds

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

Martin Lackmann

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

P2860

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

Bmf: a proapoptotic BH3-only protein regulated by interaction with the myosin V actin motor complex, activated by anoikis

The conserved N-terminal BH4 domain of Bcl-2 homologues is essential for inhibition of apoptosis and interaction with CED-4

Investigation of the subcellular distribution of the bcl-2 oncoprotein: residence in the nuclear envelope, endoplasmic reticulum, and outer mitochondrial membranes

Bim: a novel member of the Bcl-2 family that promotes apoptosis

Conformation of the Bax C-terminus regulates subcellular location and cell death

Cytosol-to-membrane redistribution of Bax and Bcl-X(L) during apoptosis

Rationale for Bcl-xL/Bad peptide complex formation from structure, mutagenesis, and biophysical studies

Movement of Bax from the cytosol to mitochondria during apoptosis

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

P304

877-87

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scholarly article

P356

10.1083/JCB.200302144

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P407

P433

5

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P478

162

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P50

Catherine L. Day

P577

2003-09-01T00:00:00Z

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P5875

10585040

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P698

12952938

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P921

apoptotic process

P932

2172834

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