Browsing by Subject "Escherichia coli Proteins"
Now showing items 1-14 of 14
-
A flexible statistical model for alignment of label-free proteomics data--incorporating ion mobility and product ion information.
(BMC Bioinformatics, 2013-12-16)BACKGROUND: The goal of many proteomics experiments is to determine the abundance of proteins in biological samples, and the variation thereof in various physiological conditions. High-throughput quantitative proteomics, ... -
Epigenetic regulation of the nitrosative stress response and intracellular macrophage survival by extraintestinal pathogenic Escherichia coli.
(2011)Escherichia coli is a typical constituent of the enteric tract in many animals, including humans. However, specialized extraintestinal pathogenic E. colistrains (ExPEC) may transition from benign occupation of the enteric ... -
Escherichia coli global gene expression in urine from women with urinary tract infection.
(PLoS pathogens, 2010-11)Murine models of urinary tract infection (UTI) have provided substantial data identifying uropathogenic E. coli (UPEC) virulence factors and assessing their expression in vivo. However, it is unclear how gene expression ... -
FtsZ at mid-cell is essential in Escherichia coli until the late stage of constriction.
(Microbiology (Reading, England), 2022-06)There has been recent debate as to the source of constriction force during cell division. FtsZ can generate a constriction force on tubular membranes in vitro, suggesting it may generate the constriction force in vivo. However, ... -
FtsZ Protofilament Curvature Is the Opposite of Tubulin Rings.
(Biochemistry, 2016-07)FtsZ protofilaments (pfs) form the bacterial cytokinetic Z ring. Previous work suggested that a conformational change from straight to curved pfs generated the constriction force. In the simplest model, the C-terminal membrane ... -
Heat-labile enterotoxin: beyond G(m1) binding.
(Toxins (Basel), 2010-06)Enterotoxigenic Escherichia coli (ETEC) is a significant source of morbidity and mortality worldwide. One major virulence factor released by ETEC is the heat-labile enterotoxin LT, which is structurally and functionally ... -
Modulation of bacterial outer membrane vesicle production by envelope structure and content.
(BMC Microbiol, 2014-12-21)BACKGROUND: Vesiculation is a ubiquitous secretion process of Gram-negative bacteria, where outer membrane vesicles (OMVs) are small spherical particles on the order of 50 to 250 nm composed of outer membrane (OM) and lumenal ... -
NlpI-mediated modulation of outer membrane vesicle production through peptidoglycan dynamics in Escherichia coli.
(Microbiologyopen, 2015-06)Outer membrane vesicles (OMVs) are ubiquitously secreted from the outer membrane (OM) of Gram-negative bacteria. These heterogeneous structures are composed of OM filled with periplasmic content from the site of budding. ... -
Polyethylene Glycol-conjugated L-asparaginase versus native L-asparaginase in combination with standard agents for children with acute lymphoblastic leukemia in second bone marrow relapse: a Children's Oncology Group Study (POG 8866).
(Journal of pediatric hematology/oncology, 2011-12)<h4>Background</h4>Administration of L-asparaginase is limited by hypersensitivity reactions mediated by anti-asparaginase antibodies. To overcome this problem, native Escherichia coli L-asparaginase was conjugated ... -
Release of outer membrane vesicles by Gram-negative bacteria is a novel envelope stress response.
(Mol Microbiol, 2007-01)Conditions that impair protein folding in the Gram-negative bacterial envelope cause stress. The destabilizing effects of stress in this compartment are recognized and countered by a number of signal transduction mechanisms. ... -
SulA inhibits assembly of FtsZ by a simple sequestration mechanism.
(Biochemistry, 2012-04)We have investigated the inhibition by SulA of the assembly of Escherichia coli FtsZ. Using quantitative GTPase and fluorescence assays, we found that SulA inhibition resulted in an increase in the apparent critical concentration ... -
The C-terminal linker of Escherichia coli FtsZ functions as an intrinsically disordered peptide.
(Molecular microbiology, 2013-07)The tubulin homologue FtsZ provides the cytoskeletal framework and constriction force for bacterial cell division. FtsZ has an 50-amino-acid (aa) linker between the protofilament-forming globular domain and the C-terminal ... -
Thermodynamic analysis of a molecular chaperone binding to unfolded protein substrates.
(Biochemistry, 2010-02-16)Molecular chaperones are a highly diverse group of proteins that recognize and bind unfolded proteins to facilitate protein folding and prevent nonspecific protein aggregation. The mechanisms by which chaperones bind their ... -
Thermodynamic analysis of ligand-induced changes in protein thermal unfolding applied to high-throughput determination of ligand affinities with extrinsic fluorescent dyes.
(Biochemistry, 2010-12-28)The quantification of protein-ligand interactions is essential for systems biology, drug discovery, and bioengineering. Ligand-induced changes in protein thermal stability provide a general, quantifiable signature of binding ...
