T
Travis J. Barnard
Researcher at National Institutes of Health
Publications - 15
Citations - 1856
Travis J. Barnard is an academic researcher from National Institutes of Health. The author has contributed to research in topics: Bacterial outer membrane & Autotransporters. The author has an hindex of 13, co-authored 15 publications receiving 1622 citations. Previous affiliations of Travis J. Barnard include Laboratory of Molecular Biology.
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Journal ArticleDOI
TonB-Dependent Transporters: Regulation, Structure, and Function
TL;DR: Recent progress in understanding regulation, structure, and function in TBDTs is summarized and questions remaining to be answered are summarized.
Journal ArticleDOI
Autotransporter structure reveals intra-barrel cleavage followed by conformational changes.
TL;DR: X-ray crystallography solves the 2.7-Å structure of the post-cleavage state of the β-domain of EspP, an autotransporter produced by Escherichia coli strain O157:H7 and reveals an unprecedented intra-barrel cleavage mechanism and suggests that two conformational changes occur in theβ-domain after cleavage.
Journal ArticleDOI
Structural insight into the role of the Ton complex in energy transduction
Herve Celia,Nicholas Noinaj,Stanislav D. Zakharov,Enrica Bordignon,Istvan Botos,Monica Santamaria,Travis J. Barnard,William A. Cramer,Roland Lloubès,Susan K. Buchanan +9 more
TL;DR: Electrophysiology studies show that the Ton subcomplex forms pH-sensitive cation-selective channels and provide insight into the mechanism by which it may harness the proton motive force to produce energy.
Journal ArticleDOI
Structural engineering of a phage lysin that targets Gram-negative pathogens
Petra Lukacik,Travis J. Barnard,Paul W. Keller,Kaveri S. Chaturvedi,Nadir Seddiki,James W. Fairman,Nicholas Noinaj,Tara L. Kirby,Jeffrey P. Henderson,Alasdair C. Steven,B. Joseph Hinnebusch,Susan K. Buchanan +11 more
TL;DR: This work solved the crystal structures of a Yersinia pestis outer membrane transporter called FyuA and a bacterial toxin called pesticin that targets this transporter and designs a phage therapy reagent comprised of the F RyuA binding domain of pesticin fused to the N-terminus of T4 lysozyme.
Journal ArticleDOI
Efficient secretion of a folded protein domain by a monomeric bacterial autotransporter.
Kristen M. Skillman,Travis J. Barnard,Janine H. Peterson,Rodolfo Ghirlando,Harris D. Bernstein +4 more
TL;DR: It is proposed that the EspP β domain functions primarily to target and anchor the protein and that an external factor transports the passenger domain across the OM.