M
Michael S. Gilmore
Researcher at Massachusetts Eye and Ear Infirmary
Publications - 305
Citations - 21338
Michael S. Gilmore is an academic researcher from Massachusetts Eye and Ear Infirmary. The author has contributed to research in topics: Enterococcus faecalis & Virulence. The author has an hindex of 76, co-authored 296 publications receiving 18988 citations. Previous affiliations of Michael S. Gilmore include University of Oklahoma Health Sciences Center & Yale University.
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Virulence of enterococci.
TL;DR: The current understanding of enterococcal virulence relating to adherence to host tissues, invasion and abscess formation, factors potentially relevant to modulation of host inflammatory responses, and potentially toxic secreted products are discussed.
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Multiple-drug resistant enterococci: the nature of the problem and an agenda for the future.
TL;DR: Effective control of multiple-drug resistantEnterococci will require better understanding of the interaction between enterococci, the hospital environment, and humans, 2) prudent antibiotic use, 3) better contact isolation in hospitals and other patient care environments, and 4) improved surveillance.
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In vitro susceptibility studies of vancomycin-resistant Enterococcus faecalis.
TL;DR: Vancomycin resistance exhibited by E faecalis isolates V583, V586, and V587 is described in this article, where vancomycin MICs ranged from 32 to 64 micrograms/ml.
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Simplified agar plate method for quantifying viable bacteria
TL;DR: A track-dilution technique whereby six 10-fold serial dilutions of a sample containing an unknown quantity of bacteria are plated onto a single agar plate is developed, which reduces time and materials required and statistically analyzing the data for accuracy and reproducibility.
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Infection-Derived Enterococcus faecalis Strains Are Enriched in esp, a Gene Encoding a Novel Surface Protein
TL;DR: The deduced primary structure of the Esp protein from strain MMH594, inferred to be 1,873 amino acids with a predicted mass of ∼202 kDa, reveals a core region consisting of repeat units that make up 50% of the protein, which bears global organizational similarity to the Rib and C alpha proteins of group B streptococci.