Probing the Interaction of Aspergillomarasmine A with Metallo-β-lactamases NDM-1, VIM-2, and IMP-7

ACS Infectious Diseases

Volumn 4, Issue 2, 2018, Pages 135-145

  Bergstrom, Alexander ^a   Katko, Andrew ^a   Adkins, Zach ^a   Hill, Jessica ^a   Cheng, Zishuo ^a   Burnett, Mia ^a   Yang, Hao ^a   Aitha, Mahesh ^a   Mehaffey, M Rachel ^b   Brodbelt, Jennifer S ^b   Tehrani, Kamaleddin H M E ^c   Martin, Nathaniel I ^c   Bonomo, Robert A ^d   Page, Richard C ^a   Tierney, David L ^a   Fast, Walter ^e   Wright, Gerard D ^f   Crowder, Michael W ^a  

^a MIAMI UNIVERSITY   (United States)

^b University of Texas at Austin   (United States)

^c UTRECHT UNIVERSITY   (Netherlands)

^d LOUIS STOKES CLEVELAND VA MEDICAL CENTER   (United States)

^e UNIVERSITY OF TEXAS AT AUSTIN   (United States)

^f MCMASTER UNIVERSITY   (Canada)

Author keywords

antibiotic resistance; aspergillomarasmine A; IMP 7; metallo lactamase; NDM 1; VIM 2

Indexed keywords

ASPERGILLOMARASMINE A; BETA LACTAMASE INHIBITOR; COBALT; METALLO BETA LACTAMASE; METALLO BETA LACTAMASE IMP 7; METALLO BETA LACTAMASE NDM 1; METALLO BETA LACTAMASE VIM 2; UNCLASSIFIED DRUG; ASPARTIC ACID; BETA LACTAMASE; BETA-LACTAMASE NDM-1; BIOLOGICAL PRODUCT; PROTEIN BINDING; VIM-2 BETA-LACTAMASE; ZINC;

ARTICLE; ATOMIC EMISSION SPECTROMETRY; CONTROLLED STUDY; DRUG MECHANISM; DRUG PROTEIN BINDING; EQUILIBRIUM DIALYSIS; NONHUMAN; PRIORITY JOURNAL; PROTON NUCLEAR MAGNETIC RESONANCE; ANALOGS AND DERIVATIVES; CHEMICAL STRUCTURE; CHEMISTRY; DRUG EFFECT; ENZYME ACTIVATION; KINETICS; METABOLISM; MOLECULAR MODEL; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; QUANTITATIVE STRUCTURE ACTIVITY RELATION;

ASPARTIC ACID; BETA-LACTAMASE INHIBITORS; BETA-LACTAMASES; BIOLOGICAL PRODUCTS; COBALT; ENZYME ACTIVATION; KINETICS; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, MOLECULAR; MOLECULAR STRUCTURE; PROTEIN BINDING; QUANTITATIVE STRUCTURE-ACTIVITY RELATIONSHIP; ZINC;

EID: 85041713470     PISSN: None     EISSN: 23738227     Source Type: Journal    
DOI: 10.1021/acsinfecdis.7b00106     Document Type: Article

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