Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Andrew C. Goodrich"'
Publikováno v:
Journal of Biological Chemistry. 292:10002-10013
Nonribosomal peptide synthesis involves the interplay between covalent protein modifications, conformational fluctuations, catalysis, and transient protein-protein interactions. Delineating the mechanisms involved in orchestrating these various proce
Autor:
Valarie Del Rio, Tiffany A. Lu, P Rogelio Escamilla, James F. Reuther, Eric V. Anslyn, Bryan William Davies, Andrew C. Goodrich
Publikováno v:
Journal of the American Chemical Society. 140(10)
Peptide oligomers offer versatile scaffolds for the formation of potent antimicrobial agents due to their high sequence versatility, inherent biocompatibility, and chemical tunability. Though many methods exist for the formation of peptide-based macr
Publikováno v:
Journal of the American Chemical Society. 137(37)
Nonribosomal peptide synthetases (NRPSs) are microbial enzymes that produce a wealth of important natural products by condensing substrates in an assembly line manner. The proper sequence of substrates is obtained by tethering them to phosphopantethe
Autor:
Andrew C. Goodrich, Dominique P. Frueh
Publikováno v:
Biochemistry. 54(5)
Carrier proteins (CPs) play a central role in nonribosomal peptide synthetases (NRPSs) as they shuttle covalently attached substrates between active sites. Understanding how the covalent attachment of a substrate (loading) influences the molecular pr
Publikováno v:
Current opinion in structural biology. 23(5)
NMR structural studies of large monomeric and multimeric proteins face distinct challenges. In large monomeric proteins, the common occurrence of frequency degeneracies between residues impedes unambiguous assignment of NMR signals. To overcome this
Autor:
Dominique P. Frueh, Andrew C. Goodrich, Bradley J. Harden, Subrata H. Mishra, Scott R. Nichols
Publikováno v:
Biophysical Journal. 108:58a
Nonribosomal peptide synthetases (NRPSs) are modular, multi-domain, enzymatic assembly lines that combine simple substrates to synthesize complex natural products (e.g. penicillin, bacitracin, yersiniabactin). Substrates are each covalently attached
Autor:
Andrew C. Goodrich, Bradley J. Harden, Dominique P. Frueh, Scott R. Nichols, Subrata H. Mishra
Publikováno v:
Biophysical Journal. (2):180a
Non-ribosomal peptide synthetases (NRPSs) are enzymatic systems that synthesize important natural products in bacteria and fungi, often with pharmaceutical applications (antibiotics, antitumor agents or immunosuppressants). NRPSs use a series of doma
Autor:
Andrew C. Goodrich, Dominique P. Frueh
Publikováno v:
Biophysical Journal. (2):510a
Nonribosomal peptide synthetases (NRPSs) are modular enzymatic systems responsible for the production of complex secondary metabolites in bacteria and fungi. Each module is comprised of (at least) three core domains whose combined action leads to the
Conference
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