Zobrazeno 1 - 10
of 40
pro vyhledávání: '"Pei W. Thomas"'
Autor:
Cory T. Reidl, Romila Mascarenhas, Thahani S. Habeeb Mohammad, Marlon R. Lutz, Pei W. Thomas, Walter Fast, Dali Liu, Daniel P. Becker
Publikováno v:
ACS Omega, Vol 6, Iss 21, Pp 13567-13578 (2021)
Externí odkaz:
https://doaj.org/article/a768cfe8f3ae44a7826846aca78995dc
Autor:
Zishuo Cheng, Ben A. Shurina, Christopher R. Bethel, Pei W. Thomas, Steven H. Marshall, Caitlyn A. Thomas, Kundi Yang, Robert L. Kimble, Jonathan S. Montgomery, Matthew G. Orischak, Callie M. Miller, Jordan L. Tennenbaum, Jay C. Nix, David L. Tierney, Walter Fast, Robert A. Bonomo, Richard C. Page, Michael W. Crowder
Publikováno v:
mBio, Vol 10, Iss 6 (2019)
ABSTRACT To understand the evolution of Verona integron-encoded metallo-β-lactamase (VIM) genes (blaVIM) and their clinical impact, microbiological, biochemical, and structural studies were conducted. Forty-five clinically derived VIM variants engin
Externí odkaz:
https://doaj.org/article/456a2252f5b9467492680466c100f2cc
Discovery of an Effective Small-Molecule Allosteric Inhibitor of New Delhi Metallo-β-lactamase (NDM)
Autor:
Pei W. Thomas, Eun Jeong Cho, Christopher R. Bethel, Thomas Smisek, Yeong-Chan Ahn, John M. Schroeder, Caitlyn A. Thomas, Kevin N. Dalby, Josh T. Beckham, Michael W. Crowder, Robert A. Bonomo, Walter Fast
Publikováno v:
ACS Infectious Diseases. 8:811-824
To identify novel inhibitors of the carbapenemase New Delhi metallo-β-lactamase (NDM) as possible therapeutic compounds, we conducted a high-throughput screen of a 43,358-compound library. One of these compounds, a 2-quinazolinone linked through a d
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ddb67a67c07ab43dc1326f73bfe7fdaf
https://doi.org/10.1021/acsinfecdis.1c00577
https://doi.org/10.1021/acsinfecdis.1c00577
Autor:
Dali Liu, Walter Fast, Pei W. Thomas, Thahani S. Habeeb Mohammad, Daniel P. Becker, Cory T. Reidl, Romila Mascarenhas, Marlon R. Lutz
Publikováno v:
ACS Omega, Vol 6, Iss 21, Pp 13567-13578 (2021)
ACS Omega
ACS Omega
An α-amido cyclobutanone possessing a C10 hydrocarbon tail was designed as a potential transition-state mimetic for the quorum-quenching metallo-γ-lactonase autoinducer inactivator A (AiiA) with the support of in-house modeling techniques and found
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e6f38f623ca17073633f05157a53427f
https://doaj.org/article/a768cfe8f3ae44a7826846aca78995dc
https://doaj.org/article/a768cfe8f3ae44a7826846aca78995dc
Autor:
Caitlyn A. Thomas, Kundi Yang, Walter Fast, Zishuo Cheng, Seth M. Cohen, Michael W. Crowder, Allie Y. Chen, Pei W. Thomas
Publikováno v:
ChemMedChem
The fungal natural product Aspergillomarasmine A (AMA) has been identified as a non-competitive inhibitor of New Delhi Metallo-β-lactamase-1 (NDM-1) that inhibits via active site Zn(II) removal. The non-selective metal-chelating properties and the d
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fbd5f29c9ff1aa0d1020e736f12ce455
https://doi.org/10.1002/cmdc.202000123
https://doi.org/10.1002/cmdc.202000123
Autor:
Jennifer S. Brodbelt, Dann D Rivera, R. F. Pratt, Pei W. Thomas, Michael W. Crowder, Zishuo Cheng, M. Rachel Mehaffey, Yeong-Chan Ahn, Walter Fast
Publikováno v:
Chemical Science
We use mass spectrometry (MS), under denaturing and non-denaturing solution conditions, along with ultraviolet photodissociation (UVPD) to characterize structural variations in New Delhi metallo-β-lactamase (NDM) upon perturbation by ligands or muta
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::66c4f1c2beb8aedeb4642d902a849ac5
https://doi.org/10.1039/d0sc02503h
https://doi.org/10.1039/d0sc02503h
Autor:
Sky Price, Radhika Mehta, Dominique Tan, Abigail Hinojosa, Pei W. Thomas, Tawanda Cummings, Walter Fast, Emily L. Que
Publikováno v:
SSRN Electronic Journal.
Metallo-β-lactamases (MBLs) are enzymes that are capable of hydrolyzing most β-lactam antibiotics and all clinically relevant carbapenems. We developed a library of reversible fluorescent turn-on probes that are designed to directly bind to the diz
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::abda00428b7f086a5122f7121c79ce9c
https://doi.org/10.2139/ssrn.4032579
https://doi.org/10.2139/ssrn.4032579
Autor:
Dominique Tan, Alesha C. Stewart, Caitlyn A. Thomas, Dann D Rivera, Pei W. Thomas, Radhika Mehta, Zishuo Cheng, Abigail Hinojosa, David J. Reilley, Emily L. Que, Anastassia N. Alexandrova, Michael W. Crowder, Walter Fast
Publikováno v:
Journal of the American Chemical Society, vol 143, iss 22
J Am Chem Soc
J Am Chem Soc
New Delhi metallo-β-lactamase (NDM) grants resistance to a broad spectrum of β-lactam antibiotics, including last-resort carbapenems, and is emerging as a global antibiotic resistance threat. Limited zinc availability adversely impacts the ability
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4dddee04f76dcee299e12974660e593a
https://escholarship.org/uc/item/7q31084r
https://escholarship.org/uc/item/7q31084r
Autor:
Zishuo Cheng, Walter Fast, Allie Y. Chen, Michael W. Crowder, Seth M. Cohen, David L. Tierney, Pei W. Thomas, Nasa Y. Xu
Publikováno v:
ChemMedChem
New Delhi Metallo-β-lactamase-1 (NDM-1) poses an immediate threat to our most effective and widely prescribed drugs, the β-lactam containing class of antibiotics. There are no clinically relevant inhibitors to combat NDM-1, despite significant effo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::805baf8645594413368818155a53375a
https://doi.org/10.1002/cmdc.201900172
https://doi.org/10.1002/cmdc.201900172
Autor:
Aidan M. Sturgill, Michael W. Crowder, Kundi Yang, Ben A. Shurina, Zishuo Cheng, Richard C. Page, Robert A. Bonomo, Walter Fast, Pei W. Thomas, Christopher R. Bethel, Huan Zhang, Steven H. Marshall, John-Paul Alao, Andrea N. Kravats, Caitlyn A. Thomas
Publikováno v:
Antimicrob Agents Chemother
Metallo-β-lactamases (MBLs) are a growing clinical threat because they inactivate nearly all β-lactam-containing antibiotics, and there are no clinically available inhibitors. A significant number of variants have already emerged for each MBL subfa
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::15e989d702cb28a7d29900daa21b2392
https://doi.org/10.1128/aac.01714-20
https://doi.org/10.1128/aac.01714-20