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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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Antibiotics For Emerging Pathogens

TL;DR: The emergence of multidrug resistance among the latest generation of pathogens suggests that the discovery of new scaffolds should be a priority, and promising approaches to scaffold discovery are emerging.
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Ribosomally synthesized and post-translationally modified peptide natural products: Overview and recommendations for a universal nomenclature

Paul G. Arnison, +65 more
TL;DR: This review presents recommended nomenclature for the biosynthesis of ribosomally synthesized and post-translationally modified peptides (RiPPs), a rapidly growing class of natural products.
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Molecular mechanisms that confer antibacterial drug resistance

TL;DR: The authors live in an era when antibiotic resistance has spread at an alarming rate and dire predictions concerning the lack of effective antibacterial drugs occur with increasing frequency, so it is apposite to ask a few simple questions about these life-saving molecules.
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Assembly-line enzymology for polyketide and nonribosomal Peptide antibiotics: logic, machinery, and mechanisms.

TL;DR: Christopher T. Walsh is the Hamilton Kuhn Professor of Biological Chemistry and Molecular Pharmacology (BCMP) at Harvard Medical School and has had extensive experience in academic administration, including Chairmanship of the MIT Chemistry Department and the HMS Biological Chemistry & molecular Pharmacology Department.
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Protein posttranslational modifications: the chemistry of proteome diversifications.

TL;DR: An understanding of the scope and pattern of the many posttranslational modifications in eukaryotic cells provides insight into the function and dynamics of proteome compositions.