His primary areas of study are Biochemistry, Bacteria, Microbiology, Antibacterial agent and Antibiotics. His work carried out in the field of Biochemistry brings together such families of science as Zinc, Moiety, Crystal structure, Molecule and Hydroxide. His studies deal with areas such as Enzyme inhibitor and Enzyme as well as Bacteria.
His work in the fields of Enzyme, such as Biosynthesis, overlaps with other areas such as Clavulanic acid. His studies examine the connections between Antibacterial agent and genetics, as well as such issues in Staphylococcus aureus, with regards to Reductase. His studies in Antibiotics integrate themes in fields like Escherichia coli Proteins, Bacterial protein, Histidine kinase and Virulence.
The scientist’s investigation covers issues in Biochemistry, Microbiology, Enzyme, Stereochemistry and Staphylococcus aureus. His work on Antibiotics, Bacteroides fragilis and Beta-Lactamase Inhibitors is typically connected to Clavulanic acid as part of general Microbiology study, connecting several disciplines of science. His Antibiotics study incorporates themes from Biotechnology and Intensive care medicine.
His Biotechnology research incorporates elements of Risk analysis and Antibacterial drug. His Enzyme research includes elements of Escherichia coli, Imipenem and Bacteria. His Stereochemistry research integrates issues from Serine, Oxidoreductase, Active site, Bacillus cereus and Enterobacter cloacae.
His primary areas of investigation include Antibiotics, Biotechnology, Risk analysis, Antibacterial drug and Computational biology. His Antibiotics study combines topics in areas such as Histidine kinase, Escherichia coli Proteins, Bacterial protein, Bacteria and Virulence. His study in the fields of Biotechnology industry under the domain of Biotechnology overlaps with other disciplines such as Portfolio, Phase, Modern medicine and Active engagement.
His work on Antibacterial drug is being expanded to include thematically relevant topics such as Intensive care. His work in Computational biology is not limited to one particular discipline; it also encompasses Antibacterial activity. His research integrates issues of High plasma and Chemical space, Drug discovery, Bioinformatics in his study of Antibiotic resistance.
This overview was generated by a machine learning system which analysed the scientist’s body of work. If you have any feedback, you can contact us here.
Drugs for bad bugs: confronting the challenges of antibacterial discovery
David J. Payne;Michael N. Gwynn;David J. Holmes;David L. Pompliano.
Nature Reviews Drug Discovery (2007)
Alternatives to antibiotics—a pipeline portfolio review
Lloyd Czaplewski;Richard Bax;Martha Clokie;Mike Dawson.
Lancet Infectious Diseases (2016)
Crystal structure of the IMP-1 metallo beta-lactamase from Pseudomonas aeruginosa and its complex with a mercaptocarboxylate inhibitor: binding determinants of a potent, broad-spectrum inhibitor.
Néstor O. Concha;Cheryl A. Janson;Pam Rowling;Stewart Pearson.
Biochemistry (2000)
Desperately Seeking New Antibiotics
David J. Payne.
Science (2008)
Challenges of antibacterial discovery revisited
Michael N. Gwynn;Alison Portnoy;Stephen F. Rittenhouse;David J. Payne.
Annals of the New York Academy of Sciences (2010)
Comparative activities of clavulanic acid, sulbactam, and tazobactam against clinically important beta-lactamases.
D. J. Payne;R. Cramp;D. J. Winstanley;D. J. C. Knowles.
Antimicrobial Agents and Chemotherapy (1994)
Bacterial fatty-acid biosynthesis: a genomics-driven target for antibacterial drug discovery
David J Payne;Patrick V Warren;David J Holmes;Yinduo Ji.
Drug Discovery Today (2001)
Discovery of a Novel and Potent Class of FabI-Directed Antibacterial Agents
David J. Payne;William H. Miller;Valerie Berry;John Brosky.
Antimicrobial Agents and Chemotherapy (2002)
Inhibition of metallo-beta-lactamases by a series of mercaptoacetic acid thiol ester derivatives.
DJ Payne;JH Bateson;BC Gasson;D Proctor.
Antimicrobial Agents and Chemotherapy (1997)
Indole naphthyridinones as inhibitors of bacterial enoyl-ACP reductases FabI and FabK.
Mark A. Seefeld;William H. Miller;Kenneth A. Newlander;Walter J. Burgess.
Journal of Medicinal Chemistry (2003)
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