Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Stewart C, Pearson"'
Autor:
William H. Miller, Catherine C.K. Yuan, Kalindi Vaidya, Brian J. Polizzi, Dennis T. Takata, Rebecca Claire Greenwood, Dirk A. Heerding, Mark A. Seefeld, Scott B. Winram, Valerie Berry, Martha S. Head, Walter J. Burgess, Andrew P. Fosberry, Nicola G. Wallis, David J. Payne, Stephen Rittenhouse, William F. Huffman, Paul M. Keller, Kevin L. Salyers, Manley Peter J, Kenneth A. Newlander, Deborah Dee Jaworski, Courtney Slater-Radosti, Cheryl A. Janson, Walter E. DeWolf, Irene N. Uzinskas, John Brosky, Stewart C. Pearson, Xiayang Qiu, Emile Chen, Terrance D. Moore, Martin G. Smyth
Publikováno v:
Antimicrobial Agents and Chemotherapy. 46:3118-3124
Bacterial enoyl-acyl carrier protein (ACP) reductase (FabI) catalyzes the final step in each elongation cycle of bacterial fatty acid biosynthesis and is an attractive target for the development of new antibacterial agents. High-throughput screening
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::997a68e3d46cb5b0dd9196003827969e
https://doi.org/10.1128/aac.46.10.3118-3124.2002
https://doi.org/10.1128/aac.46.10.3118-3124.2002
Autor:
William F. Huffman, Paul M. Keller, Valerie Berry, Walter E. DeWolf, William H. Miller, Catherine C.K. Yuan, Mark A. Seefeld, Stephen Rittenhouse, Brian J. Polizzi, Stewart C. Pearson, Cheryl A. Janson, Dirk A. Heerding, Walter J. Burgess, Martha S. Head, Terrance D. Moore, Kenneth A. Newlander, Xiayang Qiu, Irene N. Uzinskas, David J. Payne
Publikováno v:
Journal of Medicinal Chemistry. 45:3246-3256
Bacterial enoyl-ACP reductase (FabI) catalyzes the final step in each cycle of bacterial fatty acid biosynthesis and is an attractive target for the development of new antibacterial agents. Our eff...
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ac5be10717eef2aed6ee5bf83df2f1ef
https://doi.org/10.1021/jm020050+
https://doi.org/10.1021/jm020050+
Autor:
David G. Tew, Alfonso Rivera-Sagredo, Paloma Perez, Cheryl A. Janson, Nestor O. Concha, Martin Gilpin, Juan A. Hueso-Rodríguez, Michael Rees, John H. Bateson, Jesús Ángel de la Fuente, Helen F. Boyd, Niconovich Nancy, Stewart C. Pearson, Christy Cheever, David J. Payne, E. Diez, Stephen Rittenhouse
Publikováno v:
Antimicrobial Agents and Chemotherapy. 46:1880-1886
Metallo-β-lactamases provide bacteria with an efficient and effective way of mediating resistance to β-lactam-based antibacterial agents. More significantly, they confer resistance to carbapenems. Therefore, if metallo-β-lactamases increase in pre
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e9aa937c16cee0ca888b0a557de1cdef
https://doi.org/10.1128/aac.46.6.1880-1886.2002
https://doi.org/10.1128/aac.46.6.1880-1886.2002
Autor:
Brian Peter SmithKline Beecham Pharm Clarke, Moreno Galleni, David J. Payne, Bateson John Hargreaves, Ceri Lewis, Christy A. Cheever, Sherin S. Abdel-Meguid, Pam Rowling, Nestor O. Concha, Stewart C. Pearson, Jean-Marie Frere, Cheryl A. Janson
Publikováno v:
Biochemistry. 39:4288-4298
Metallo beta-lactamase enzymes confer antibiotic resistance to bacteria by catalyzing the hydrolysis of beta-lactam antibiotics. This relatively new form of resistance is spreading unchallenged as there is a current lack of potent and selective inhib
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bebe1f86d57c55a7dc16223592ffa7dd
https://doi.org/10.1021/bi992569m
https://doi.org/10.1021/bi992569m
Autor:
William H, Miller, Mark A, Seefeld, Kenneth A, Newlander, Irene N, Uzinskas, Walter J, Burgess, Dirk A, Heerding, Catherine C K, Yuan, Martha S, Head, David J, Payne, Stephen F, Rittenhouse, Terrance D, Moore, Stewart C, Pearson, Valerie, Berry, Walter E, DeWolf, Paul M, Keller, Brian J, Polizzi, Xiayang, Qiu, Cheryl A, Janson, William F, Huffman
Publikováno v:
Journal of medicinal chemistry. 45(15)
Bacterial enoyl-ACP reductase (FabI) catalyzes the final step in each cycle of bacterial fatty acid biosynthesis and is an attractive target for the development of new antibacterial agents. Our efforts to identify potent, selective FabI inhibitors be
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::88457e027bb10a51dc01df9d68bcf47b
https://pubmed.ncbi.nlm.nih.gov/12109908
https://pubmed.ncbi.nlm.nih.gov/12109908
Autor:
Alison F, Chalker, Karen A, Ingraham, R Dwayne, Lunsford, Alexander P, Bryant, Joanna, Bryant, Nicola G, Wallis, John P, Broskey, Stewart C, Pearson, David J, Holmes
Publikováno v:
Microbiology (Reading, England). 146
Homologues of Escherichia coli bacA, encoding extremely hydrophobic proteins, were identified in the genomes of Staphylococcus aureus and Streptococcus pneumoniae. Allelic replacement mutagenesis demonstrated that the gene is not essential for in vit
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::6c8f161e56df74522f9f7af6cf856ebb
https://pubmed.ncbi.nlm.nih.gov/10878119
https://pubmed.ncbi.nlm.nih.gov/10878119
Autor:
Stewart C. Pearson, David Proctor, Robert Reid, Teresa Khushi, Bateson John Hargreaves, David J. Payne, Brian Charles Gasson
Publikováno v:
FEMS microbiology letters. 157(1)
A series of mercaptophenylacetic acid thiol esters bearing a phenyl substituent adjacent to the carboxylic acid function has been shown to be inhibitors of metallo-beta-lactamases. The inhibition of the Bacteroides fragilis CfiA and Bacillus cereus I
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::eb09cfa321807f92e482bc7c8bf9bbe6
https://pubmed.ncbi.nlm.nih.gov/9418252
https://pubmed.ncbi.nlm.nih.gov/9418252
Publikováno v:
Microscopy and Microanalysis. 5:1138-1139
Clofoctol [2-(2,4-dichlorobenzyl)-4-(tetramethyl-l,l,3,3-butyl) phenol] is a synthetic antibacterial compound with activity against both Gram-positive1 and Gram-negative2 microorganisms. Although the specific mechanism of Clofoctol action has not bee
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::aa9a6a4175a18356751d8b3fdd992fa1
https://doi.org/10.1017/s1431927600019012
https://doi.org/10.1017/s1431927600019012