Solution structure of the antiapoptotic protein bcl-2 - Wikidata - awgldk - TriplyDB

Solution structure of the antiapoptotic protein bcl-2

Solution structure of the antiapoptotic protein bcl-2

http://www.wikidata.org/entity/Q27630598

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Tumor necrosis factor-alpha induces Bax-Bak interaction and apoptosis, which is inhibited by adenovirus E1B 19K Noxa/Bcl-2 protein interactions contribute to bortezomib resistance in human lymphoid cells Functional and structural studies of the vaccinia virus virulence factor N1 reveal a Bcl-2-like anti-apoptotic protein Identification of novel in vivo phosphorylation sites of the human proapoptotic protein BAD: pore-forming activity of BAD is regulated by phosphorylation Molecular basis of the interaction between the antiapoptotic Bcl-2 family proteins and the proapoptotic protein ASPP2 Paxillin comes of age The structure of Bcl-w reveals a role for the C-terminal residues in modulating biological activity A surface groove essential for viral Bcl-2 function during chronic infection in vivo.Extracellular BCL2 proteins are danger-associated molecular patterns that reduce tissue damage in murine models of ischemia-reperfusion injury Solution structure of a Bcl-2 homolog from Kaposi sarcoma virus.Solution structure of human BCL-w: modulation of ligand binding by the C-terminal helix Unique structural features of a BCL-2 family protein CED-9 and biophysical characterization of CED-9/EGL-1 interactions Structure of M11L: A myxoma virus structural homolog of the apoptosis inhibitor, Bcl-2 Structural insights into the degradation of Mcl-1 induced by BH3 domains Structural and Biochemical Bases for the Inhibition of Autophagy and Apoptosis by Viral BCL-2 of Murine γ-Herpesvirus 68 Mcl-1-Bim complexes accommodate surprising point mutations via minor structural changes Evidence that inhibition of BAX activation by BCL-2 involves its tight and preferential interaction with the BH3 domain of BAX ABT-199, a potent and selective BCL-2 inhibitor, achieves antitumor activity while sparing platelets Mitochondrial apoptosis and BH3 mimetics The proapoptotic BH3-only protein BAD transduces cell death signals independently of its interaction with Bcl-2 The flexible loop of Bcl-2 is required for molecular interaction with immunosuppressant FK-506 binding protein 38 (FKBP38)Critical upstream signals of cytochrome C release induced by a novel Bcl-2 inhibitor Building blocks of the apoptotic pore: how Bax and Bak are activated and oligomerize during apoptosis Regulation of the cell cycle and apoptosis by the oncogenes of adenovirus Bcl-XL is qualitatively different from and ten times more effective than Bcl-2 when expressed in a breast cancer cell line An inhibitor of Bcl-2 family proteins induces regression of solid tumours The FKBP38 catalytic domain binds to Bcl-2 via a charge-sensitive loop.The functional differences between pro-survival and pro-apoptotic B cell lymphoma 2 (Bcl-2) proteins depend on structural differences in their Bcl-2 homology 3 (BH3) domains.Mapping the intrinsically disordered properties of the flexible loop domain of Bcl-2: a molecular dynamics simulation study.Intrinsic disorder in spondins and some of their interacting partners.The use of therapeutic peptides to target and to kill cancer cells.Auto-activation of the apoptosis protein Bax increases mitochondrial membrane permeability and is inhibited by Bcl-2 Recent advances in the development of anticancer agents targeting cell death inhibitors in the Bcl-2 protein family.Genome-wide characterisation of the binding repertoire of small molecule drugs.Modulation of Nr-13 antideath activity by peptide aptamers.A novel Bcl-2-like inhibitor of apoptosis is encoded by the parapoxvirus ORF virus Assembling the puzzle: Oligomerization of α-pore forming proteins in membranes Reconstitution and engineering of apoptotic protein interactions on the bacterial cell surface.Oligomerization of membrane-bound Bcl-2 is involved in its pore formation induced by tBid.A survey of the anti-apoptotic Bcl-2 subfamily expression in cancer types provides a platform to predict the efficacy of Bcl-2 antagonists in cancer therapy.

P2860

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P2860

Solution structure of the antiapoptotic protein bcl-2

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Solution structure of the antiapoptotic protein bcl-2

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Solution structure of the antiapoptotic protein bcl-2

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Solution structure of the antiapoptotic protein bcl-2

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Solution structure of the antiapoptotic protein bcl-2

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Solution structure of the antiapoptotic protein bcl-2

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Solution structure of the antiapoptotic protein bcl-2

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Solution structure of the antiapoptotic protein bcl-2

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Solution structure of the antiapoptotic protein bcl-2

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Solution structure of the antiapoptotic protein bcl-2

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Proceedings of the National Academy of Sciences of the United States of America

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Solution structure of the antiapoptotic protein bcl-2

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Fesik SW

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Kim DH

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Matayoshi ED

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P2860

Dimerization properties of human BAD. Identification of a BH-3 domain and analysis of its binding to mutant BCL-2 and BCL-XL proteins

Bad, a heterodimeric partner for Bcl-XL and Bcl-2, displaces Bax and promotes cell death

bcl-x, a bcl-2-related gene that functions as a dominant regulator of apoptotic cell death

PROCHECK: a program to check the stereochemical quality of protein structures

Structure of Bax: coregulation of dimer formation and intracellular localization

X-ray and NMR structure of human Bcl-xL, an inhibitor of programmed cell death

Structure of Bcl-xL-Bak peptide complex: recognition between regulators of apoptosis

Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons

Protein backbone angle restraints from searching a database for chemical shift and sequence homology

Apoptosis in the pathogenesis and treatment of disease

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10.1073/PNAS.041619798

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6

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11248023

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apoptotic process

protein structure

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