Your browser doesn't support javascript.
loading
Multiple substitutions lead to increased loop flexibility and expanded specificity in Acinetobacter baumannii carbapenemase OXA-239.
Harper, Thomas M; June, Cynthia M; Taracila, Magdalena A; Bonomo, Robert A; Powers, Rachel A; Leonard, David A.
Affiliation
  • Harper TM; Department of Chemistry, Grand Valley State University, Allendale, MI 49401, U.S.A.
  • June CM; Department of Chemistry, Grand Valley State University, Allendale, MI 49401, U.S.A.
  • Taracila MA; Department of Medicine, Case Western Reserve University, Cleveland, OH 44106, U.S.A.
  • Bonomo RA; Research Service, Louis Stokes Veterans Affairs Medical Center, Cleveland, OH 44106, U.S.A.
  • Powers RA; Department of Medicine, Case Western Reserve University, Cleveland, OH 44106, U.S.A.
  • Leonard DA; Research Service, Louis Stokes Veterans Affairs Medical Center, Cleveland, OH 44106, U.S.A.
Biochem J ; 475(1): 273-288, 2018 01 11.
Article in En | MEDLINE | ID: mdl-29229762

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Bacterial Proteins / Beta-Lactamases / Carbapenems / Cefotaxime / Imipenem / Amino Acid Substitution / Acinetobacter baumannii Language: En Journal: Biochem J Year: 2018 Type: Article Affiliation country: United States

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Bacterial Proteins / Beta-Lactamases / Carbapenems / Cefotaxime / Imipenem / Amino Acid Substitution / Acinetobacter baumannii Language: En Journal: Biochem J Year: 2018 Type: Article Affiliation country: United States