The BH3 mimetic ABT-737 targets selective Bcl-2 proteins and efficiently induces apoptosis via Bak/Bax if Mcl-1 is neutralized. - Wikidata - wikimedia - TriplyDB

The BH3 mimetic ABT-737 targets selective Bcl-2 proteins and efficiently induces apoptosis via Bak/Bax if Mcl-1 is neutralized.

The BH3 mimetic ABT-737 targets selective Bcl-2 proteins and efficiently induces apoptosis via Bak/Bax if Mcl-1 is neutralized.

http://www.wikidata.org/entity/Q42064781

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Two independent positive feedbacks and bistability in the Bcl-2 apoptotic switch Use of human cancer cell lines mitochondria to explore the mechanisms of BH3 peptides and ABT-737-induced mitochondrial membrane permeabilization Human nuclear clusterin mediates apoptosis by interacting with Bcl-XL through C-terminal coiled coil domain Functional and physical interaction between Bcl-X(L) and a BH3-like domain in Beclin-1 Heterodimerization of BAK and MCL-1 activated by detergent micelles BH3 domains other than Bim and Bid can directly activate Bax/Bak ATM-dependent expression of IEX-1 controls nuclear accumulation of Mcl-1 and the DNA damage response Chemical genomics identifies small-molecule MCL1 repressors and BCL-xL as a predictor of MCL1 dependency A novel pro-apoptotic function of RACK1: suppression of Src activity in the intrinsic and Akt pathways Mutation to Bax beyond the BH3 domain disrupts interactions with pro-survival proteins and promotes apoptosis Taspase1 functions as a non-oncogene addiction protease that coordinates cancer cell proliferation and apoptosis The Bcl-2 apoptotic switch in cancer development and therapy PUMA, a potent killer with or without p53 Bcl-2 inhibitors: targeting mitochondrial apoptotic pathways in cancer therapy Small-molecule Bcl-2 antagonists as targeted therapy in oncology BH3 mimetics to improve cancer therapy; mechanisms and examples Mitochondria, cholesterol and cancer cell metabolism The biology of DHX9 and its potential as a therapeutic target Targeting Cell Survival Proteins for Cancer Cell Death Bcl-2 antagonists: a proof of concept for CLL therapy Chloroquine and hydroxychloroquine for cancer therapy Targeting BCL2-Proteins for the Treatment of Solid Tumours Targeting the Bcl-2 family for cancer therapy Structural insights into the transcription-independent apoptotic pathway of p53 The BCL2 Family: Key Mediators of the Apoptotic Response to Targeted Anticancer Therapeutics Targeting Mcl-1 for the therapy of cancer Apoptotic agents Targeting the apoptosis pathway in hematologic malignancies Genetic ablation of Bcl-x attenuates invasiveness without affecting apoptosis or tumor growth in a mouse model of pancreatic neuroendocrine cancer Structural insights into the degradation of Mcl-1 induced by BH3 domains A novel BH3 ligand that selectively targets Mcl-1 reveals that apoptosis can proceed without Mcl-1 degradation 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 The MCL-1 BH3 helix is an exclusive MCL-1 inhibitor and apoptosis sensitizer Structural Basis for Apoptosis Inhibition by Epstein-Barr Virus BHRF1 Rational Design of Proteolytically Stable, Cell-Permeable Peptide-Based Selective Mcl-1 Inhibitors The restricted binding repertoire of Bcl-B leaves Bim as the universal BH3-only prosurvival Bcl-2 protein antagonist Discovery of Potent Myeloid Cell Leukemia 1 (Mcl-1) Inhibitors Using Fragment-Based Methods and Structure-Based Design Discovery of 2-Indole-acylsulfonamide Myeloid Cell Leukemia 1 (Mcl-1) Inhibitors Using Fragment-Based Methods

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The BH3 mimetic ABT-737 targets selective Bcl-2 proteins and efficiently induces apoptosis via Bak/Bax if Mcl-1 is neutralized.

http://www.wikidata.org/entity/Q42064781

description

2006 nî lūn-bûn

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2006年の論文

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name

The BH3 mimetic ABT-737 target ...... k/Bax if Mcl-1 is neutralized.

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The BH3 mimetic ABT-737 target ...... k/Bax if Mcl-1 is neutralized.

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type

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The BH3 mimetic ABT-737 target ...... k/Bax if Mcl-1 is neutralized.

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The BH3 mimetic ABT-737 target ...... k/Bax if Mcl-1 is neutralized.

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The BH3 mimetic ABT-737 target ...... k/Bax if Mcl-1 is neutralized.

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The BH3 mimetic ABT-737 target ...... k/Bax if Mcl-1 is neutralized.

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J.CCR.2006.08.027

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The BH3 mimetic ABT-737 target ...... ak/Bax if Mcl-1 is neutralized

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Andrew H Wei

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Cassandra J Vandenberg

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Clare L Scott

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Lin Chen

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Peter E Czabotar

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Simon N Willis

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The Hallmarks of Cancer

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.

Mule/ARF-BP1, a BH3-only E3 ubiquitin ligase, catalyzes the polyubiquitination of Mcl-1 and regulates apoptosis

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

Activation of apoptosis in vivo by a hydrocarbon-stapled BH3 helix.

MCL1, a gene expressed in programmed myeloid cell differentiation, has sequence similarity to BCL2

Seliciclib (CYC202 or R-roscovitine), a small-molecule cyclin-dependent kinase inhibitor, mediates activity via down-regulation of Mcl-1 in multiple myeloma

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

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389-399

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10.1016/J.CCR.2006.08.027

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5

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10

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Catherine L. Day

Andrew W Roberts

Mark F van Delft

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2006-11-01T00:00:00Z

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6699037

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17097561

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2953559

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