2022 - Research.com Best Scientist Award
2017 - Robert Koch Gold Medal
2014 - Benjamin Franklin Medal, Franklin Institute
2007 - Murray Goodman Memorial Prize, American Chemical Society (ACS)
2004 - Promega Biotechnology Research Award, American Society for Microbiology
1989 - Member of the National Academy of Sciences
1989 - Member of the National Academy of Medicine (NAM)
1987 - Centenary Prize, Royal Society of Chemistry (UK)
1985 - Fellow of the American Academy of Arts and Sciences
1975 - Fellow of Alfred P. Sloan Foundation
Christopher T. Walsh mainly focuses on Biochemistry, Stereochemistry, Enzyme, Nonribosomal peptide and Biosynthesis. Biochemistry is a component of his Escherichia coli, Peptide, Peptide sequence, Serine and Enterobactin studies. His studies examine the connections between Stereochemistry and genetics, as well as such issues in Thioesterase, with regards to Cyclic peptide.
His study connects In vitro and Enzyme. His Nonribosomal peptide study combines topics from a wide range of disciplines, such as Polyketide synthase, Polyketide, Peptide Synthases and Yersiniabactin. His study explores the link between Polyketide and topics such as Gene cluster that cross with problems in Bacillus subtilis and Microbiology.
Christopher T. Walsh focuses on Biochemistry, Stereochemistry, Enzyme, Biosynthesis and Nonribosomal peptide. Many of his studies involve connections with topics such as Molecular biology and Biochemistry. Christopher T. Walsh works mostly in the field of Stereochemistry, limiting it down to topics relating to Cofactor and, in certain cases, Flavin group, as a part of the same area of interest.
His studies in Enzyme integrate themes in fields like Catalysis and Bacteria. His Biosynthesis research incorporates elements of Natural product and Gene cluster. His Nonribosomal peptide study integrates concerns from other disciplines, such as Thioesterase, Adenylylation, Polyketide synthase, Polyketide and Peptide Synthases.
His main research concerns Biochemistry, Stereochemistry, Biosynthesis, Enzyme and Amino acid. His Biochemistry study focuses mostly on Nonribosomal peptide, Gene cluster, Peptide sequence, Peptide and Gene. His Nonribosomal peptide research is multidisciplinary, relying on both Peptide Synthases and Fungal protein.
His Stereochemistry research is multidisciplinary, incorporating perspectives in Protein structure, Dipeptide, Alanine and Tryptophan. His Biosynthesis course of study focuses on Antibiotics and Bacteria. His studies deal with areas such as Oxygenase, Polyketide, Substrate and Flavin group as well as Amino acid.
His primary areas of investigation include Biochemistry, Stereochemistry, Nonribosomal peptide, Biosynthesis and Amino acid. His study in Peptide sequence, Peptide, Gene cluster, Gene and Enzyme falls within the category of Biochemistry. His work on Oxygenase as part of general Enzyme research is frequently linked to Translocase, bridging the gap between disciplines.
Christopher T. Walsh works mostly in the field of Stereochemistry, limiting it down to topics relating to Polyketide and, in certain cases, Multienzyme complexes. His Nonribosomal peptide research incorporates themes from Adenylylation, Acylation, Protein structure, Peptide Synthases and Fungal protein. The various areas that he examines in his Biosynthesis study include In vitro, Differentiation-inducing factor, Bacteria, Natural product and Morphogen.
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Antibiotics For Emerging Pathogens
Michael A. Fischbach;Christopher T. Walsh.
Molecular mechanisms that confer antibacterial drug resistance
Enzymatic Reaction Mechanisms
Antibiotics: Actions, Origins, Resistance
Protein posttranslational modifications: the chemistry of proteome diversifications.
Christopher T. Walsh;Sylvie Garneau‐Tsodikova;Gregory J. Gatto.
Angewandte Chemie (2005)
Assembly-line enzymology for polyketide and nonribosomal Peptide antibiotics: logic, machinery, and mechanisms.
Michael A. Fischbach;Christopher T. Walsh.
Chemical Reviews (2006)
Lessons from natural molecules
Jon Clardy;Christopher Walsh.
Ribosomally synthesized and post-translationally modified peptide natural products: Overview and recommendations for a universal nomenclature
Paul G. Arnison;Mervyn J. Bibb;Gabriele Bierbaum;Albert Alexander Bowers.
Natural Product Reports (2013)
The Behavior and Significance of Slow-Binding Enzyme Inhibitors
John F. Morrison;Christopher T. Walsh.
Advances in Enzymology and Related Areas of Molecular Biology (1988)
A new enzyme superfamily — the phosphopantetheinyl transferases
Ralph H. Lambalot;Amy M. Gehring;Roger S. Flugel;Peter Zuber.
Chemistry & Biology (1996)
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