H
Helen I. Zgurskaya
Researcher at University of Oklahoma
Publications - 125
Citations - 7271
Helen I. Zgurskaya is an academic researcher from University of Oklahoma. The author has contributed to research in topics: Efflux & Bacterial outer membrane. The author has an hindex of 40, co-authored 101 publications receiving 6153 citations. Previous affiliations of Helen I. Zgurskaya include University of California, Berkeley & Russian Academy of Sciences.
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Journal ArticleDOI
Tackling antibiotic resistance
Karen Bush,Patrice Courvalin,Gautam Dantas,Julian Davies,Barry I. Eisenstein,Pentti Huovinen,George A. Jacoby,Roy Kishony,Barry N. Kreiswirth,Elizabeth Kutter,Stephen A. Lerner,Stuart B. Levy,Kim Lewis,Olga Lomovskaya,Jeffrey H Miller,Shahriar Mobashery,Laura J. V. Piddock,Steven J. Projan,Christopher M. Thomas,Alexander Tomasz,Paul M. Tulkens,Timothy R. Walsh,James D. Watson,Jan A. Witkowski,Wolfgang Witte,Gerry Wright,Pamela J. Yeh,Helen I. Zgurskaya +27 more
TL;DR: To explore how the problem of antibiotic resistance might best be addressed, a group of 30 scientists from academia and industry gathered at the Banbury Conference Centre in Cold Spring Harbor, New York, USA, from 16 to 18 May 2011.
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Multidrug resistance mechanisms: drug efflux across two membranes.
TL;DR: This review focuses on the structural features and the mechanism of major efflux pumps of Gram‐negative bacteria, which expel from the cells a remarkably broad range of antimicrobial compounds and produce the characteristic intrinsic resistance of these bacteria to antibiotics, detergents, dyes and organic solvents.
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Permeability Barrier of Gram-Negative Cell Envelopes and Approaches To Bypass It
TL;DR: Current advances in understanding the molecular bases of the low permeability barrier of Gram-negative pathogens, which is the major obstacle in discovery and development of antibiotics effective against such pathogens, are summarized.
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Bypassing the periplasm: Reconstitution of the AcrAB multidrug efflux pump of Escherichia coli
TL;DR: Results suggest that AcrA brings two membranes together, and under certain conditions may even cause the fusion of at least the outer leaflets of the membranes, contributing to the ability of the AcrAB-TolC system to pump drugs out directly into the medium.
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Structural basis of multiple drug-binding capacity of the AcrB multidrug efflux pump.
TL;DR: In this paper, the authors obtained x-ray crystallographic structures of the trimeric AcrB pump from Escherichia coli with four structurally diverse ligands, and showed that three molecules of ligands bind simultaneously to the extremely large central cavity of 5000 cubic angstroms, primarily by hydrophobic, aromatic stacking and van der Waals interactions.