R. A. Powers

Publications85
h-index15
Citations911
Highly Influential Citations38
Claim Author Page
Author pages are created from data sourced from our academic publisher partnerships and public sources.

Recommended Authors

  • R. Bonomo
  • 650 Publications • 29,493 Citations
  • B. Shoichet
  • 289 Publications • 30,374 Citations
  • F. Prati
  • 178 Publications • 1,961 Citations
  • D. Leonard
  • 104 Publications • 945 Citations
  • Publications
  • Influence
The complexed structure and antimicrobial activity of a non‐β‐lactam inhibitor of AmpC β‐lactamase
β‐Lactamases are the major resistance mechanism to β‐lactam antibiotics and pose a growing threat to public health. Recently, bacteria have become resistant to β‐lactamase inhibitors, making this… Expand
  • 72
  • 7
  • PDF
Structures of the class D carbapenemase OXA-24 from Acinetobacter baumannii in complex with doripenem.
The emergence of class D β-lactamases with carbapenemase activity presents an enormous challenge to health practitioners, particularly with regard to the treatment of infections caused by… Expand
  • 57
  • 6
Structure-based approach for binding site identification on AmpC beta-lactamase.
Beta-lactamases are the most widespread resistance mechanism to beta-lactam antibiotics and are an increasing menace to public health. Several beta-lactamase structures have been determined, making… Expand
  • 115
  • 4
  • PDF
Structures of the Class D Carbapenemases OXA-23 and OXA-146: Mechanistic Basis of Activity against Carbapenems, Extended-Spectrum Cephalosporins, and Aztreonam
ABSTRACT Class D β-lactamases that hydrolyze carbapenems such as imipenem and doripenem are a recognized danger to the efficacy of these “last-resort” β-lactam antibiotics. Like all known class D… Expand
  • 50
  • 3
  • PDF
Multiple substitutions lead to increased loop flexibility and expanded specificity in Acinetobacter baumannii carbapenemase OXA-239.
OXA-239 is a class D carbapenemase isolated from an Acinetobacter baumannii strain found in Mexico. This enzyme is a variant of OXA-23 with three amino acid substitutions in or near the active site.… Expand
  • 9
  • 3
Structure-Based Discovery of a Novel, Noncovalent Inhibitor of AmpC β-Lactamase
beta-lactamases are the most widespread resistance mechanisms to beta-lactam antibiotics, and there is a pressing need for novel, non-beta-lactam drugs. A database of over 200,000 compounds was… Expand
  • 105
  • 2
Structures of ceftazidime and its transition-state analogue in complex with AmpC beta-lactamase: implications for resistance mutations and inhibitor design.
Third-generation cephalosporins are widely used beta-lactam antibiotics that resist hydrolysis by beta-lactamases. Recently, mutant beta-lactamases that rapidly inactivate these drugs have emerged.… Expand
  • 93
  • 2
  • PDF
The 1.4 A crystal structure of the class D beta-lactamase OXA-1 complexed with doripenem.
The clinical efficacy of carbapenem antibiotics depends on their resistance to the hydrolytic action of beta-lactamase enzymes. The structure of the class D beta-lactamase OXA-1 as an acyl complex… Expand
  • 51
  • 2
Biochemical and Structural Analysis of Inhibitors Targeting the ADC-7 Cephalosporinase of Acinetobacter baumannii
β-Lactam resistance in Acinetobacter baumannii presents one of the greatest challenges to contemporary antimicrobial chemotherapy. Much of this resistance to cephalosporins derives from the… Expand
  • 13
  • 2
Structural basis of activity against aztreonam and extended spectrum cephalosporins for two carbapenem-hydrolyzing class D β-lactamases from Acinetobacter baumannii.
The carbapenem-hydrolyzing class D β-lactamases OXA-23 and OXA-24/40 have emerged worldwide as causative agents for β-lactam antibiotic resistance in Acinetobacter species. Many variants of these… Expand
  • 17
  • 2
...
1
2
3
4
5
...