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Robert C. Cooksey

Researcher at Centers for Disease Control and Prevention

Publications -  51
Citations -  3616

Robert C. Cooksey is an academic researcher from Centers for Disease Control and Prevention. The author has contributed to research in topics: Mycobacterium tuberculosis & rpoB. The author has an hindex of 32, co-authored 51 publications receiving 3501 citations.

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Characterization of glycopeptide-resistant enterococci from U.S. hospitals.

TL;DR: Pulsed-field gel electrophoresis demonstrated both intrahospital and interhospital diversity among Vmr enterococci in the United States and was more useful than plasmid analysis for epidemiologic studies.
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Snapshot of Moving and Expanding Clones of Mycobacterium tuberculosis and Their Global Distribution Assessed by Spoligotyping in an International Study

TL;DR: To facilitate the analysis of hundreds of spoligotypes each made up of a binary succession of 43 bits of information, a number of major and minor visual rules were also defined to define 36 major clades (or families) of M. tuberculosis.
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ethA, inhA, and katG Loci of Ethionamide-Resistant Clinical Mycobacterium tuberculosis Isolates

TL;DR: In this paper, the authors sequenced the entire ethA structural gene of 41 ETH-resistant Mycobacterium tuberculosis isolates and determined the MICs of these MICs in order to associate the mutations identified with a resistance phenotype.
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Global distribution of Mycobacterium tuberculosis spoligotypes.

TL;DR: This global distribution was defined by data-mining of an international spoligotyping database, SpolDB3, which contains 11,708 patterns from as many clinical isolates originating from more than 90 countries.
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Antimicrobial susceptibility patterns of common and unusual species of enterococci causing infections in the United States. Enterococcal Study Group.

TL;DR: Antimicrobial susceptibility patterns vary among species of enterococci, and these organisms, while commonly resistant to high-level aminoglycosides, can also acquire resistance to vancomycin or the ability to produce beta-lactamase.