Results 21 to 30 of about 19,683 (209)

Helicobacter hepaticus is required for immune targeting of bacterial heat shock protein 60 and fatal colitis in mice

open access: yesGut Microbes, 2021
Gut microbiota and the immune system are in constant exchange shaping both host immunity and microbial communities. Here, improper immune regulation can cause inflammatory bowel disease (IBD) and colitis. Antibody therapies blocking signaling through the
Verena Friedrich   +11 more
doaj   +1 more source

Роль ендокринних факторів та маркерів клітинного стресу у прогнозуванні ефективності лікування клімактеричного синдрому в період перименопаузи

open access: yesУкраїнський журнал Здоров'я жінки, 2022
Жiнки клiмактеричнoгo вiку становлять 10% популяції Землі, і наразі проблема патологічного клімактерію залишається актуальною. Причиною розвитку клімактерію вважається дефіцит естрогенів, тому використання замісної терапії є патогенетично обґрунтованим ...
I.V. Sokol, D.O. Govsieiev
doaj   +1 more source

GroEL and the maintenance of bacterial endosymbiosis [PDF]

open access: yesTrends in Genetics, 2004
Many eukaryotic organisms have symbiotic associations with obligate intracellular bacteria. The clonal transmission of endosymbionts between host generations should lead to the irreversible fixation of slightly deleterious mutations in their non-recombinant genome by genetic drift.
Fares, Mario Ali   +2 more
openaire   +3 more sources

GroEL‐Mediated protein folding [PDF]

open access: yesProtein Science, 1997
Abstract Architecture of GroEL and GroES and the reaction pathway Architecture of the chaperonins Reaction pathway of GroEL‐GroES‐mediated folding Polypeptide binding A parallel network of chaperones binding polypeptides in vivo Polypeptide binding in vitro Role of hydrophobicity in recognition Homologous proteins with differing recognition ...
W A, Fenton, A L, Horwich
openaire   +2 more sources

A structural model for the GroEL chaperonin [PDF]

open access: yesFEMS Microbiology Letters, 1993
Individual particle analysis of end views from negatively stained specimens of purified GroEL from Escherichia coli showed the presence of two different particle populations, those with a six-fold symmetry and those with a seven-fold symmetry, when studied at pH 7.7 and 5.0.
S, Marco   +5 more
openaire   +2 more sources

Porphyromonas gingivalis GroEL induces osteoclastogenesis of periodontal ligament cells and enhances alveolar bone resorption in rats. [PDF]

open access: yesPLoS ONE, 2014
Porphyromonas gingivalis is a major periodontal pathogen that contains a variety of virulence factors. The antibody titer to P. gingivalis GroEL, a homologue of HSP60, is significantly higher in periodontitis patients than in healthy control subjects ...
Feng-Yen Lin   +9 more
doaj   +1 more source

Stimulatory effects of Porphyromonas gingivalis GroEL protein on interleukin-6 and interleukin-8 in human osteoblasts

open access: yesJournal of the Formosan Medical Association, 2021
Background/Purpose: Porphyromonas gingivalis is an oral pathogen associated with periodontal diseases. P. gingivalis GroEL protein is a stimulator of inflammatory cytokines in macrophages. This study inspected effects of P.
Hsiu-Hui Lin   +5 more
doaj   +1 more source

In vivo activities of GroEL minichaperones

open access: yes, 1998
Fragments encompassing the apical domain of GroEL, called minichaperones, facilitate the refolding of several proteins in vitro without requiring GroES, ATP, or the cage-like structure of multimeric GroEL.
Hill, F   +3 more
core   +5 more sources

Characterization of Molecular Chaperone GroEL as a Potential Virulence Factor in Cronobacter sakazakii

open access: yesFoods, 2023
The molecular chaperone GroEL of C. sakazakii, a highly conserved protein encoded by the gene grol, has the basic function of responding to heat shock, thus enhancing the bacterium’s adaptation to dry and high-temperature environments, which poses a ...
Dongdong Zhu   +9 more
doaj   +1 more source

Dynamics of allosteric transitions in GroEL [PDF]

open access: yesProceedings of the National Academy of Sciences, 2006
The chaperonin GroEL-GroES, a machine that helps proteins to fold, cycles through a number of allosteric states, the T state, with high affinity for substrate proteins, the ATP-bound R state, and the R ″ (
Hyeon, Changbong   +2 more
openaire   +3 more sources

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