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Stephen W. Fesik

Researcher at Vanderbilt University

Publications -  298
Citations -  42613

Stephen W. Fesik is an academic researcher from Vanderbilt University. The author has contributed to research in topics: Nuclear magnetic resonance spectroscopy & Binding site. The author has an hindex of 95, co-authored 294 publications receiving 40006 citations. Previous affiliations of Stephen W. Fesik include Howard Hughes Medical Institute & Yale University.

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Regulation of the Apaf-1/caspase-9 apoptosome by caspase-3 and XIAP.

TL;DR: It is found that cleavage of procaspase-9 at Asp330 to generate p35, p 10 or p37, p10 forms resulted in a significant increase in apoptosome activity compared with p35/p12, and the significance of this increase was demonstrated by the near complete loss of apoptosomesome-mediated caspasing-3 activity.
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A Novel MCL1 Inhibitor Combined with Venetoclax Rescues Venetoclax-Resistant Acute Myelogenous Leukemia.

TL;DR: VU661013 is described, a novel, potent, selective MCL1 inhibitor that destabilizes BIM/MCL1 association, leads to apoptosis in AML, and is active in venetoclax-resistant cells and patient-derived xenografts.
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Solution structure of the cyclosporin A/cyclophilin complex by NMR

TL;DR: The solution structure of the cyclosporin A/cyclophilin complex obtained by heteronuclear three-dimensional NMR spectroscopy is presented and is analysed in terms of the binding interactions and structure/activity relationships for CsA analogues.
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Structure of the N-terminal RNA-binding domain of the SARS CoV nucleocapsid protein.

TL;DR: The three-dimensional structure of the N-terminal domain of the SARS coronavirus (CoV) nucleocapsid protein is described, which consists of a five-stranded beta sheet with a folding topology distinct from other RNA-binding proteins.
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Discovery of a Potent, Selective Protein Tyrosine Phosphatase 1B Inhibitor Using a Linked-Fragment Strategy

TL;DR: The modular approach to drug design described in this work should be applicable for the design of potent and selective inhibitors of other therapeutically relevant protein tyrosine phosphatases.