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Charles S. Craik

Researcher at University of California, San Francisco

Publications -  452
Citations -  29993

Charles S. Craik is an academic researcher from University of California, San Francisco. The author has contributed to research in topics: Protease & Proteases. The author has an hindex of 84, co-authored 430 publications receiving 26509 citations. Previous affiliations of Charles S. Craik include Upjohn & University of California.

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A SARS-CoV-2 protein interaction map reveals targets for drug repurposing.

David E. Gordon, +128 more
- 30 Apr 2020 - 
TL;DR: A human–SARS-CoV-2 protein interaction map highlights cellular processes that are hijacked by the virus and that can be targeted by existing drugs, including inhibitors of mRNA translation and predicted regulators of the sigma receptors.
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Structural basis of substrate specificity in the serine proteases

TL;DR: Critical issues examined include the function of water molecules in providing strength and specificity of binding, the extent to which binding subsites are interdependent, and the roles of polypeptide chain flexibility and distal structural elements in contributing to specificity profiles.
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Global landscape of HIV-human protein complexes

TL;DR: The use of affinity tagging and purification mass spectrometry is reported to determine systematically the physical interactions of all 18 HIV-1 proteins and polyproteins with host proteins in two different human cell lines (HEK293 and Jurkat).
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Rapid and general profiling of protease specificity by using combinatorial fluorogenic substrate libraries

TL;DR: A method is presented for the preparation and use of fluorogenic peptide substrates that allows for the configuration of general substrate libraries to rapidly identify the primary and extended specificity of proteases to aid in the design of selective substrates and potent inhibitors.
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Cellular localization of membrane-type serine protease 1 and identification of protease-activated receptor-2 and single-chain urokinase-type plasminogen activator as substrates.

TL;DR: The membrane localization of MT-SP1 and its affinity for these key extracellular substrates suggests a role of the proteolytic activity in regulatory events.