Results 171 to 180 of about 18,538 (219)

Comparison of Diagnostic Performance of Commercially Available Serological and Molecular Tests for Detection of <i>Orientia tsutsugamushi</i> in South Korea: A Single-Center Prospective Study. [PDF]

J Clin Med
Kim S, Kim MG, Jang J, Lee J, Kim N, Yu Y, Kim AR, Lim S, Shin Y, Bae M.   +9 more
europepmc   +1 more source

Ancestral Chaperonins Provide the First Structural Glimpse into Early Multimeric Protein Evolution. [PDF]

Mol Biol Evol
Severino R, Cuéllar J, Gutiérrez-Seijo J, Maestro-López M, Sánchez-Pulido L, Santiago C, Moreno-Paz M, Valpuesta JM, Parro V.   +8 more
europepmc   +1 more source

Systematic Review of Mendelian Randomization Studies on <i>Helicobacter pylori</i>-Associated Health Outcomes. [PDF]

Interdiscip Perspect Infect Dis
Kato I, Canzian F, Rizzato C, Rodriguez A, Torres J.   +4 more
europepmc   +1 more source

Mechanism of substrate recognition by the chaperonin GroEL

Biochemistry and Cell Biology, 2001
The bacterial chaperonin GroEL functions with its cofactor GroES in assisting the folding of a wide range of proteins in an ATP-dependent manner. GroEL–GroES constitute one of the main chaperone systems in the Escherichia coli cytoplasm. The chaperonin facilitates protein folding by enclosing substrate proteins in a cage defined by the GroEL cylinder ...
Walid A Houry
openaire   +3 more sources

Lactobacillus stress protein GroEL prevents colonic inflammation [PDF]

Journal of Gastroenterology, 2021
International audienceBACKGROUND: We previously showed that supernatants of Lactobacillus biofilms induced an anti-inflammatory response by affecting the secretion of macrophage-derived cytokines, which was abrogated upon immunodepletion of the stress ...
François Hermetet, Sébastien Causse, Aurélie Rieu   +2 more
exaly   +2 more sources

Functional Differences between E. coli and ESKAPE Pathogen GroES/GroEL

MBio, 2021
As the GroES/GroEL chaperonin system is the only bacterial chaperone that is essential under all conditions, we have been interested in the development of GroES/GroEL inhibitors as potential antibiotics. Using Escherichia coli GroES/GroEL as a surrogate,
Jared Sivinski, Andrew J Ambrose, Christopher J Zerio   +2 more
exaly   +2 more sources

GroEL Ring Separation and Exchange in the Chaperonin Reaction

Cell, 2018
The bacterial chaperonin GroEL and its cofactor, GroES, form a nano-cage for a single molecule of substrate protein (SP) to fold in isolation. GroEL and GroES undergo an ATP-regulated interaction cycle to close and open the folding cage.
Andreas Bracher, F Ulrich Hartl, Manajit Hayer-Hartl   +2 more
exaly   +2 more sources

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Transmission Electron Microscopy of GroEL, GroES, and the Symmetrical GroEL/ES Complex

Journal of Structural Biology, 1994
Two new 2-D crystal forms of the Escherichia coli chaperone GroEL (cpn60) 2 x 7-mer have been produced using the negative staining-carbon film (NS-CF) technique. These 2-D crystals, which contain the cylindrical GroEL in side-on and end-on orientations, both possess p21 symmetry, with two molecules in the respective unit cells. The crystallographically
J R, Harris, A, Plückthun, R, Zahn
openaire   +2 more sources

Structure and Allostery of the Chaperonin GroEL

Journal of Molecular Biology, 2013
Chaperonins are intricate allosteric machines formed of two back-to-back, stacked rings of subunits presenting end cavities lined with hydrophobic binding sites for nonnative polypeptides. Once bound, substrates are subjected to forceful, concerted movements that result in their ejection from the binding surface and simultaneous encapsulation inside a ...
Helen R, Saibil, Wayne A, Fenton, Daniel K, Clare, Arthur L, Horwich   +3 more
openaire   +2 more sources