Crystal structure of ABT-737 complexed with Bcl-xL: implications for selectivity of antagonists of the Bcl-2 family - Wikidata - awgldk - TriplyDB

Crystal structure of ABT-737 complexed with Bcl-xL: implications for selectivity of antagonists of the Bcl-2 family

Crystal structure of ABT-737 complexed with Bcl-xL: implications for selectivity of antagonists of the Bcl-2 family

http://www.wikidata.org/entity/Q27645935

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Structural changes in the BH3 domain of SOUL protein upon interaction with the anti-apoptotic protein Bcl-xL Vaccinia virus anti-apoptotic F1L is a novel Bcl-2-like domain-swapped dimer that binds a highly selective subset of BH3-containing death ligands Mutation to Bax beyond the BH3 domain disrupts interactions with pro-survival proteins and promotes apoptosis Structural conservation of druggable hot spots in protein-protein interfaces BH3 mimetics to improve cancer therapy; mechanisms and examples A novel BH3 ligand that selectively targets Mcl-1 reveals that apoptosis can proceed without Mcl-1 degradation Completing the family portrait of the anti-apoptotic Bcl-2 proteins: crystal structure of human Bfl-1 in complex with Bim High-Resolution Structural Characterization of a Helical α/β-Peptide Foldamer Bound to the Anti-Apoptotic Protein Bcl-xL Conformational Changes in Bcl-2 Pro-survival Proteins Determine Their Capacity to Bind Ligands Mcl-1-Bim complexes accommodate surprising point mutations via minor structural changes Determinants of BH3 Binding Specificity for Mcl-1 versus Bcl-xL Design of Bcl-2 and Bcl-xL Inhibitors with Subnanomolar Binding Affinities Based upon a New Scaffold Structure-Guided Rational Design of α/β-Peptide Foldamers with High Affinity for BCL-2 Family Prosurvival Proteins ABT-199, a potent and selective BCL-2 inhibitor, achieves antitumor activity while sparing platelets The Role of the Acidity of N-Heteroaryl Sulfonamides as Inhibitors of Bcl-2 Family Protein–Protein Interactions Structure-Guided Rescaffolding of Selective Antagonists of BCL-X L What can we learn from the evolution of protein-ligand interactions to aid the design of new therapeutics?BcL-xL conformational changes upon fragment binding revealed by NMR Structure-based druggability assessment of the mammalian structural proteome with inclusion of light protein flexibility Synthesis and characterization of novel 2-amino-chromene-nitriles that target Bcl-2 in acute myeloid leukemia cell lines Evidence of conformational selection driving the formation of ligand binding sites in protein-protein interfaces Intrinsically disordered proteins in bcl-2 regulated apoptosis.Novel Bcl-2 homology-3 domain-like sequences identified from screening randomized peptide libraries for inhibitors of the pro-survival Bcl-2 proteins.A novel and efficient tool for locating and characterizing protein cavities and binding sites.Bcl-2 antagonists interact synergistically with bortezomib in DLBCL cells in association with JNK activation and induction of ER stress.Protein binding specificity versus promiscuity.Targeting protein-protein interactions as an anticancer strategy Conformational rearrangements in the pro-apoptotic protein, Bax, as it inserts into mitochondria: a cellular death switch.Molecular interactions of prodiginines with the BH3 domain of anti-apoptotic Bcl-2 family members Locating Herpesvirus Bcl-2 Homologs in the Specificity Landscape of Anti-Apoptotic Bcl-2 Proteins.Antagonism between granulocytic maturation and deacetylase inhibitor-induced apoptosis in acute promyelocytic leukaemia cells Small-Molecule and Peptide Inhibitors of the Pro-Survival Protein Mcl-1 Classification of scaffold-hopping approaches Small molecules, big targets: drug discovery faces the protein-protein interaction challenge.Dynamics of the BH3-Only Protein Binding Interface of Bcl-xL.An Integrated Bioinformatics and Computational Biology Approach Identifies New BH3-Only Protein Candidates Structure-based design of potent Bcl-2/Bcl-xL inhibitors with strong in vivo antitumor activity.Structure-based discovery of BM-957 as a potent small-molecule inhibitor of Bcl-2 and Bcl-xL capable of achieving complete tumor regression Predictive Bcl-2 family binding models rooted in experiment or structure.Physiological restraint of Bak by Bcl-xL is essential for cell survival.

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Crystal structure of ABT-737 complexed with Bcl-xL: implications for selectivity of antagonists of the Bcl-2 family

http://www.wikidata.org/entity/Q27645935

description

2007 nî lūn-bûn

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2007 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

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2007 թվականի սեպտեմբերին հրատարակված գիտական հոդված

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2007年論文

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Crystal structure of ABT-737 c ...... ntagonists of the Bcl-2 family

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Crystal structure of ABT-737 c ...... ntagonists of the Bcl-2 family

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Crystal structure of ABT-737 c ...... ntagonists of the Bcl-2 family

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Crystal structure of ABT-737 c ...... ntagonists of the Bcl-2 family

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Crystal structure of ABT-737 c ...... ntagonists of the Bcl-2 family

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Crystal structure of ABT-737 c ...... ntagonists of the Bcl-2 family

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Crystal structure of ABT-737 c ...... ntagonists of the Bcl-2 family

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Crystal structure of ABT-737 c ...... ntagonists of the Bcl-2 family

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Crystal structure of ABT-737 c ...... ntagonists of the Bcl-2 family

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Crystal structure of ABT-737 c ...... ntagonists of the Bcl-2 family

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K Deshayes

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K Zobel

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P E Czabotar

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P M Colman

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P2860

Differential targeting of prosurvival Bcl-2 proteins by their BH3-only ligands allows complementary apoptotic function

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

Mechanisms of apoptosis sensitivity and resistance to the BH3 mimetic ABT-737 in acute myeloid leukemia

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

The structure of a Bcl-xL/Bim fragment complex: implications for Bim function

Studies leading to potent, dual inhibitors of Bcl-2 and Bcl-xL

A structural viral mimic of prosurvival Bcl-2: a pivotal role for sequestering proapoptotic Bax and Bak

Structural insights into the degradation of Mcl-1 induced by BH3 domains

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

An inhibitor of Bcl-2 family proteins induces regression of solid tumours

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10.1038/SJ.CDD.4402178

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9

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14

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Walter D Fairlie

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6263794

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17572662

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crystal structure