Search Results - "Newton, Salete M.C."

Evidence of Ball-and-chain Transport of Ferric Enterobactin through FepA by Ma, Li, Kaserer, Wallace, Annamalai, Rajasekeran, Scott, Daniel C., Jin, Bo, Jiang, Xiaoxu, Xiao, Qiaobin, Maymani, Hossein, Massis, Liliana Moura, Ferreira, Luiz C.S., Newton, Salete M.C., Klebba, Phillip E.

“…The Escherichia coli iron transporter, FepA, has a globular N terminus that resides within a transmembrane β-barrel formed by its C terminus. We engineered 25…”
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Fluoresceination of FepA during colicin B killing: effects of temperature, toxin and TonB by Smallwood, Chuck R, Marco, Amparo Gala, Xiao, Qiaobin, Trinh, Vy, Newton, Salete M.C, Klebba, Phillip E

“…We studied the reactivity of 35 genetically engineered Cys sulphydryl groups at different locations in Escherichia coli FepA. Modification of surface loop…”
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Iron Acquisition Systems of Gram-negative Bacterial Pathogens Define TonB-Dependent Pathways to Novel Antibiotics by Klebba, Phillip E, Newton, Salete M. C, Six, David A, Kumar, Ashish, Yang, Taihao, Nairn, Brittany L, Munger, Colton, Chakravorty, Somnath

“…Iron is an indispensable metabolic cofactor in both pro- and eukaryotes, which engenders a natural competition for the metal between bacterial pathogens and…”
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Ligand-Specific Opening of a Gated-Porin Channel in the Outer Membrane of Living Bacteria by Jiang, Xunqing, Payne, Marvin A., Cao, Zhenghua, Foster, Samuel B., Feix, Jimmy B., Salete M. C. Newton, Klebba, Phillip E.

“…Ligand-gated membrane channels selectively facilitate the entry of iron into prokaryotic cells. The essential role of iron in metabolism makes its acquisition…”
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Biphasic Binding Kinetics between FepA and Its Ligands by Payne, Marvin A., Igo, John D., Cao, Zhenghua, Foster, Samuel B., Newton, Salete M.C., Klebba, Phillip E.

“…The Escherichia coli FepA protein is an energy- and TonB-dependent, ligand-binding porin that functions as a receptor for the siderophore ferric enterobactin…”
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Immune Response to Cholera Toxin Epitope Inserted in Salmonella Flagellin by Salete M. C. Newton, Jacob, Chaim O., Bruce A. D. Stocker

“…Bacterial flagella are potent immunogens and aromatic-dependent (aro) Salmonella as live vaccines evoke humoral and cellular immune responses. Such strains…”
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Mechanism of Transport of Ferric Enterobactin through FepA in Gram Negative Bacteria by Majumdar, Aritri, Trinh, Vy, Moore, Kyle J., Smallwood, Chuck R., Newton, Salete M.C., Klebba, Phillip E.

“…Abstract only…”
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Site Directed Crosslinking Studies of the FepA Transport Mechanism by Moore, Kyle J., Newton, Salete M.C., Klebba, Phillip E.

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Concerted loop motion triggers induced fit of FepA to ferric enterobactin by Smallwood, Chuck R, Jordan, Lorne, Trinh, Vy, Schuerch, Daniel W, Gala, Amparo, Hanson, Mathew, Hanson, Matthew, Shipelskiy, Yan, Majumdar, Aritri, Newton, Salete M C, Klebba, Phillip E

“…Spectroscopic analyses of fluorophore-labeled Escherichia coli FepA described dynamic actions of its surface loops during binding and transport of ferric…”
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Flagellar Display of Bone-Protein-Derived Peptides for Studying Peptide-Mediated Biomineralization by Li, Dong, Newton, Salete M. C, Klebba, Philip E, Mao, Chuanbin

“…A bacterial flagellum is self-assembled primarily from thousands of flagellin (FliC), a protein subunit. A foreign peptide can be fully displayed on the…”
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Concerted loop motion triggers induced fit of FepA to ferric enterobactin by Smallwood, Chuck R., Jordan, Lorne, Trinh, Vy, Schuerch, Daniel W., Gala, Amparo, Hanson, Mathew, Shipelskiy, Yan, Majumdar, Aritri, Newton, Salete M.C., Klebba, Phillip E.

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FepA- and TonB-Dependent Bacteriophage H8: Receptor Binding and Genomic Sequence by Rabsch, Wolfgang, Ma, Li, Wiley, Graham, Najar, Fares Z, Kaserer, Wallace, Schuerch, Daniel W, Klebba, Joseph E, Roe, Bruce A, Laverde Gomez, Jenny A, Schallmey, Marcus, Newton, Salete M C, Klebba, Phillip E

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Iron acquisition systems for ferric hydroxamates, haemin and haemoglobin in Listeria monocytogenes by Jin, Bo, Newton, Salete M. C., Shao, Yi, Jiang, Xiaoxu, Charbit, Alain, Klebba, Phillip E.

“…Summary Listeria monocytogenes is a Gram‐positive bacterium that causes severe opportunistic infections in humans and animals. We biochemically characterized,…”
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Insight from TonB Hybrid Proteins into the Mechanism of Iron Transport through the Outer Membrane by KASERER, Wallace A, XIAOXU JIANG, QIAOBIN XIAO, SCOTT, Daniel C, BAULER, Matthew, COPELAND, Daniel, NEWTON, Salete M. C, KLEBBA, Phillip E

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Recognition of Ferric Catecholates by FepA by ANNAMALAI, Rajasekaran, BO JIN, ZHENGHUA CAO, NEWTON, Salete M. C, KLEBBA, Phillip E

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The svpA‐srtB locus of Listeria monocytogenes: Fur‐mediated iron regulation and effect on virulence by Newton, Salete M. C., Klebba, Phillip E., Raynaud, Catherine, Shao, Yi, Jiang, Xiaoxu, Dubail, Iharilalao, Archer, Crystal, Frehel, Claude, Charbit, Alain

“…Summary In Listeria monocytogenes the promoter region of the svpA‐srtB locus contains a well‐conserved Fur box. We characterized the iron‐regulation of this…”
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Ferric enterobactin binding and utilization by Neisseria gonorrhoeae by Carson, S D, Klebba, P E, Newton, S M, Sparling, P F

“…FetA, formerly designated FrpB, an iron-regulated, 76-kDa neisserial outer membrane protein, shows sequence homology to the TonB-dependent family of receptors…”
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Exchangeability of N termini in the ligand-gated porins of Escherichia coli by Scott, D C, Cao, Z, Qi, Z, Bauler, M, Igo, J D, Newton, S M, Klebba, P E

“…The ferric siderophore transporters of the Gram-negative bacterial outer membrane manifest a unique architecture: Their N termini fold into a globular domain…”
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Effect of loop deletions on the binding and transport of ferric enterobactin by FepA by Newton, Salete M. C., Igo, John D., Scott, Daniel C., Klebba, Phillip E.

“…The siderophore ferric enterobactin enters Escherichia coli through the outer membrane (OM) porin FepA, which contains an aqueous transmembrane channel that is…”
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Mechanisms of solute transport through outer membrane porins: burning down the house by Klebba, Phillip E, Newton, Salete MC

“…Porins mediate the uptake of nutrients across the outer membrane of Gram-negative bacteria. For general porins like OmpF, electrophysicoloigcal experiments now…”
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