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Barbara E. Murray
Researcher at University of Texas at Austin
Publications - 235
Citations - 23158
Barbara E. Murray is an academic researcher from University of Texas at Austin. The author has contributed to research in topics: Enterococcus faecalis & Enterococcus faecium. The author has an hindex of 73, co-authored 232 publications receiving 21704 citations. Previous affiliations of Barbara E. Murray include Emerging Pathogens Institute & University of Texas Health Science Center at Houston.
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Journal ArticleDOI
Impact of Fluoroquinolones on the Gastrointestinal Flora
TL;DR: Several recent studies suggest that the effects of some fluoroquinolones on faecal anaerobes and Gram-positive cocci may be more profound in certain patient populations such as bone marrow transplant recipients and patients undergoing gastrointestinal surgery.
Journal ArticleDOI
Diversity of the fsr-gelE Region of the Enterococcus faecalis Genome but Conservation in Strains with Partial Deletions of the fsr Operon
TL;DR: The identity of fsrD despite high plasticity within the fsrC-EF_1841 region and the surrounding sequence is described, suggesting that the deletion may result from horizontal transfer and recombination.
Journal ArticleDOI
Comparative in vitro activity of DU-6859a, a new fluoroquinolone agent, against gram-positive cocci.
TL;DR: The bactericidal activity of DU was demonstrated by time-kill techniques against all ciprofloxacin-susceptible enterococci and shows promise for the treatment of infections with gram-positive cocci and warrants further evaluation by in vitro and in vivo studies.
Book ChapterDOI
Application of Molecular Techniques to the Study of Nosocomial Infections Caused by Enterococci
TL;DR: Concern that antibiotic resistance will continue to spread and will increasingly render conventional antimicrobial chemotherapy inadequate for serious enterococcal infections has stimulated interest in methods to improve the diagnosis and epi-demiologic investigation of infections caused by enterococci.
Journal ArticleDOI
Targeted Protein Engineering Provides Insights into Binding Mechanism and Affinities of Bacterial Collagen Adhesins
TL;DR: surface plasmon resonance-based binding analysis demonstrated that mutations that are predicted to alter the orientation of the Ace and Cna N1 and N2 subdomains significantly affect the interaction between the MSCRAMM (microbial surface components recognizing adhesive matrix molecule) and CI in vitro, including affinity, association/dissociation rates and binding ratio.