C
Christopher T. Walsh
Researcher at Stanford University
Publications - 841
Citations - 79830
Christopher T. Walsh is an academic researcher from Stanford University. The author has contributed to research in topics: Nonribosomal peptide & Active site. The author has an hindex of 139, co-authored 819 publications receiving 74314 citations. Previous affiliations of Christopher T. Walsh include Florida State University & Massachusetts Institute of Technology.
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Phosphotyrosine-independent binding of a 62-kDa protein to the src homology 2 (SH2) domain of p56lck and its regulation by phosphorylation of Ser-59 in the lck unique N-terminal region
Indal Park,Jongkyong Chung,Christopher T. Walsh,Yungdae Yun,Jack L. Strominger,Jaekyoon Shin +5 more
TL;DR: Phosphotyrosine-independent binding of p62 to the p56lck SH2 domain appears to provide an alternative pathway for p 56lck signaling that is regulated by Ser-59 phosphorylation.
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How Nature Morphs Peptide Scaffolds into Antibiotics
TL;DR: The conventional notion that peptides are poor candidates for orally available drugs because of protease‐sensitive peptide bonds, intrinsic hydrophilicity, and ionic charges contrasts with the diversity of antibiotic natural products with peptide‐based frameworks that are synthesized and utilized by Nature.
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Organomercurial lyase and mercuric ion reductase: nature's mercury detoxification catalysts
Melissa J. Moore,Melissa J. Moore,Mark D. Distefano,Mark D. Distefano,Lynne D. Zydowsky,Richard T. Cummings,Christopher T. Walsh +6 more
TL;DR: In this article, the authors studied the mechanisms by which bacteria cope with increased heavy metal burdens in the food chain and found that organometallics are especially toxic to higher organisms, whose lipophilic nature gives them a strong tendency toward bioaccumulation.
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Mechanistic studies of a protonolytic organomercurial cleaving enzyme: bacterial organomercurial lyase.
TL;DR: As the first well-characterized enzymatic reaction of an organometallic substrate and the first example of an enzyme-mediated SE2 reaction the organomercurial lyase catalyzed carbon-mercury bond cleavage provides an arena for investigating novel enzyme structure-function relationships.
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The residual enzymatic phosphorylation activity of hexokinase II mutants is correlated with glucose repression in Saccharomyces cerevisiae.
TL;DR: The results strongly support the hypothesis that the phosphorylation activity of hexokinase II is correlated with glucose repression.