Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Robert L. Kimble"'
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
Autor:
Zishuo Cheng, Caitlyn A. Thomas, Adam R. Joyner, Robert L. Kimble, Aidan M. Sturgill, Nhu-Y Tran, Maya R. Vulcan, Spencer A. Klinsky, Diego J. Orea, Cody R. Platt, Fanpu Cao, Bo Li, Qilin Yang, Cole J. Yurkiewicz, Walter Fast, Michael W. Crowder
Publikováno v:
Biomolecules, Vol 10, Iss 3, p 459 (2020)
In an effort to facilitate the discovery of new, improved inhibitors of the metallo-β-lactamases (MBLs), a new, interactive website called MBLinhibitors.com was developed. Despite considerable efforts from the science community, there are no clinica
Externí odkaz:
https://doaj.org/article/12023965576442398009cfa250409433
Autor:
Fanpu Cao, Maya R. Vulcan, Cole J. Yurkiewicz, Cody R. Platt, Caitlyn A. Thomas, Nhu-Y Tran, Spencer A. Klinsky, Aidan M. Sturgill, Robert L. Kimble, Zishuo Cheng, Michael W. Crowder, Bo Li, Diego J. Orea, Qilin Yang, Adam R. Joyner, Walter Fast
Publikováno v:
Biomolecules, Vol 10, Iss 3, p 459 (2020)
Biomolecules
Biomolecules
In an effort to facilitate the discovery of new, improved inhibitors of the metallo-β-lactamases (MBLs), a new, interactive website called MBLinhibitors.com was developed. Despite considerable efforts from the science community, there are no clinica
Autor:
Michael W. Crowder, Zishuo Cheng, Steven H. Marshall, Matthew Orischak, Ben A. Shurina, Pei W. Thomas, Walter Fast, Robert A. Bonomo, Kundi Yang, David L. Tierney, Robert L. Kimble, Jay C. Nix, Caitlyn A. Thomas, Jonathan Montgomery, Richard C. Page, Christopher R. Bethel, Jordan L. Tennenbaum, Callie M. Miller
Publikováno v:
mBio, Vol 10, Iss 6, p e02412-19 (2019)
mBio
mBio, Vol 10, Iss 6 (2019)
mBio
mBio, Vol 10, Iss 6 (2019)
Antibiotic resistance is a growing clinical threat. One of the most serious areas of concern is the ability of some bacteria to degrade carbapenems, drugs that are often reserved as last-resort antibiotics. Resistance to carbapenems can be conferred
Autor:
Erin Cumming, Callie Miller, Robert L. Kimble, Alexander Bergstrom, Kelly Mason, Richard C. Page, David L. Tierney, Stacey Lowery Bretz, Christopher R. Bethel, Jay C. Nix, Robert A. Bonomo, Huan Zhang, Andrew Katko, Jamie VanPelt, Zishuo Cheng, Sarah Fullington, Michael W. Crowder
In an effort to evaluate whether a recently reported putative metallo-β-lactamase (MβL) contains a novel MβL active site, SPS-1 from Sediminispirochaeta smaragdinae was over-expressed, purified, and characterized using spectroscopic and crystallog
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::33a12437a4d0d6eb858c5b1cc88996a1
https://europepmc.org/articles/PMC6314204/
https://europepmc.org/articles/PMC6314204/
Autor:
Alexander Bergstrom, Jamie VanPelt, Sarah Fullington, Michael W. Crowder, Robert A. Bonomo, Callie Miller, David L. Tierney, Robert L. Kimble, Richard C. Page, Zishuo Cheng, Erin Cumming, Jay C. Nix, Stacey Lowery Bretz, Huan Zhang, Kelly Mason, Christopher R. Bethel, Andrew Katko
In an effort to evaluate whether a recently reported putative metallo-β-lactamase (MβL) contains a novel MβL active site, SPS-1 from Sediminispirochaeta smaragdinae was over-expressed, purified, and characterized using spectroscopic and crystallog
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b971658684db81e4685d2663bdeb0d63
https://doi.org/10.1101/336024
https://doi.org/10.1101/336024