Zobrazeno 1 - 10
of 19
pro vyhledávání: '"Benjamin P. Duckworth"'
Autor:
Surendra Dawadi, Clifton E. Barry, Kathryn M. Nelson, Kishore Viswanathan, Benjamin P. Duckworth, Helena I. Boshoff, Courtney C. Aldrich
Publikováno v:
Journal of Medicinal Chemistry. 58:5459-5475
MbtA catalyzes the first committed biosynthetic step of the mycobactins, which are important virulence factors associated with iron acquisition in Mycobacterium tuberculosis. MbtA is a validated therapeutic target for antitubercular drug development.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4cf5b80ff1cf81ba2ea9cb14f445d94d
https://doi.org/10.1021/acs.jmedchem.5b00391
https://doi.org/10.1021/acs.jmedchem.5b00391
Autor:
Clifton E. Barry, Helena I. Boshoff, Courtney C. Aldrich, Benjamin P. Duckworth, Anja Meissner, Mahalakshmi Vasan
Publikováno v:
Bioorganic & Medicinal Chemistry. 21:6385-6397
A series of 2-aminothiazoles was synthesized based on a HTS scaffold from a whole-cell screen against Mycobacterium tuberculosis (Mtb). The SAR shows the central thiazole moiety and the 2-pyridyl moiety at C-4 of the thiazole are intolerant to modifi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::80bc71e35d4ea2b61b188fab237190c4
https://doi.org/10.1016/j.bmc.2013.08.048
https://doi.org/10.1016/j.bmc.2013.08.048
Publikováno v:
Methods in Molecular Biology ISBN: 9781493933730
Adenylation is a crucial enzymatic process in the biosynthesis of nonribosomal peptide synthetase (NRPS) derived natural products. Adenylation domains are considered the gatekeepers of NRPSs since they select, activate, and load the carboxylic acid s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5d7168997aa94a0b67b9e182c7a19105
https://pubmed.ncbi.nlm.nih.gov/26831700
https://pubmed.ncbi.nlm.nih.gov/26831700
Publikováno v:
Biochemistry. 49:9292-9305
The human pathogen Acinetobacter baumannii produces a siderophore called acinetobactin that is derived from one molecule each of threonine, histidine, and 2,3-dihydroxybenzoic acid (DHB). The activity of several non-ribosomal peptide synthetase (NRPS
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c2fa4b4960b81f470d80ea39e3b8849d
https://doi.org/10.1021/bi101226n
https://doi.org/10.1021/bi101226n
Publikováno v:
Analytical Biochemistry. 403:13-19
An alarming number of clinically relevant bacterial pathogens are becoming resistant to many antibiotics, thereby fueling intense research into the discovery of novel therapeutic targets. Phosphopantetheinyl transferases (PPTases) represent a promisi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0cb188b35ca49ac336c9f3516d7956e5
https://doi.org/10.1016/j.ab.2010.04.009
https://doi.org/10.1016/j.ab.2010.04.009
Autor:
Benjamin P. Duckworth, Yan Chen, James W. Wollack, Yuk Sham, Joachim D. Mueller, T. Andrew Taton, Mark D. Distefano
Publikováno v:
Angewandte Chemie. 119:8975-8978
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::55fb1a85522273e94fb8957a3ebfa686
https://doi.org/10.1002/ange.200701942
https://doi.org/10.1002/ange.200701942
Publikováno v:
Bioconjugate Chemistry. 17:967-974
Immobilized and site-specifically labeled proteins are becoming invaluable tools in proteomics. Here, we describe a strategy to attach a desired protein to a solid surface in a covalent, site-specific manner. This approach employs an enzymatic posttr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cc10b44e148ea6ac3800eae47a29fef0
https://doi.org/10.1021/bc060125e
https://doi.org/10.1021/bc060125e
Autor:
E. Christine Pietsch, Suzy V. Torti, Alan J. Townsend, Sandra Leone-Kabler, Allison L. Hurley, Elizabeth E. Scott, Mark E. Welker, Benjamin P. Duckworth, Frank M. Torti
Publikováno v:
Biochemical Pharmacology. 65:1261-1269
Compounds that induce the synthesis of cytoprotective phase II enzymes have shown promise as cancer chemopreventive agents. Although chemically diverse, phase II enzyme inducers are capable of participating in Michael reaction chemistry. We have synt
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3c6f13edf97438886cf6760453a197b8
https://doi.org/10.1016/s0006-2952(03)00081-9
https://doi.org/10.1016/s0006-2952(03)00081-9
Publikováno v:
Analytical biochemistry. 461
Tyrosine sulfurylation is a post-translational modification important for protein-protein interactions in the extracellular space that are instrumental in cell adhesion, cell signaling, immune responses, and pathogen recognition of host cells. Tyrosi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4afcbe98a37d10e78572e2d315f1be51
https://pubmed.ncbi.nlm.nih.gov/24909447
https://pubmed.ncbi.nlm.nih.gov/24909447
Autor:
Daniel J. Wilson, Helena I. Boshoff, Courtney C. Aldrich, Clifton E. Barry, Benjamin P. Duckworth, Kathryn M. Nelson
MbtA is an adenylating enzyme from Mycobacterium tuberculosis that catalyzes the first step in the biosynthesis of the mycobactins. A potent bisubstrate inhibitor (Sal-AMS) of MbtA was previously described that displays potent antitubercular activity
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e95df4eee6750233d72d43f0205b3c15
https://europepmc.org/articles/PMC3477287/
https://europepmc.org/articles/PMC3477287/
