Results 11 to 20 of about 18,538 (219)
Ligands regulate GroEL thermostability
FEBS Letters, 1997 Escherichia coli heat‐shock proteins GroEL and GroES stimulate (in an ATP‐dependent manner) the folding of various proteins. In this study scanning microcalorimetry was applied to investigate GroEL thermostability in the presence of its ligands. Mg2+ and K+ ions stabilize while ADP destabilizes the GroEL molecule against the action of temperature ...
Surin, A.K +5 more
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Structural and Computational Study of the GroEL–Prion Protein Complex
Biomedicines, 2021 The molecular chaperone GroEL is designed to promote protein folding and prevent aggregation. However, the interaction between GroEL and the prion protein, PrPC, could lead to pathogenic transformation of the latter to the aggregation-prone PrPSc form ...
Aleksandra A. Mamchur +8 more
doaj +2 more sources
In vivo activities of GroEL minichaperones [PDF]
Proceedings of the National Academy of Sciences, 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. We have identified the smallest minichaperone that is active in vitro in chaperoning ...
J, Chatellier +3 more
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Symmetric GroEL‐GroES complexes can contain substrate simultaneously in both GroEL rings [PDF]
FEBS Letters, 1997 © 1997 Federation of European Biochemical Societies.
Llorca, Oscar +3 more
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The Chaperonin GroEL: A Versatile Tool for Applied Biotechnology Platforms
Frontiers in Molecular Biosciences, 2018 The nucleotide-free chaperonin GroEL is capable of capturing transient unfolded or partially unfolded states that flicker in and out of existence due to large-scale protein dynamic vibrational modes.
Pierce T. O'Neil +10 more
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The Unfolding Action of GroEL on a Protein Substrate [PDF]
Biophysical Journal, 2004 A molecular dynamics simulation of the active unfolding of denatured rhodanese by the chaperone GroEL is presented. The compact denatured protein is bound initially to the cis cavity and forms stable contacts with several of the subunits. As the cis ring apical domains of GroEL undergo the transition from the closed to the more open (ATP-bound) state ...
van der Vaart, Arjan +2 more
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Dynamics of allosteric transitions in GroEL [PDF]
Proceedings 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 ″ ( GroEL – ADP –
Hyeon, Changbong +2 more
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Porphyromonas gingivalis GroEL induces osteoclastogenesis of periodontal ligament cells and enhances alveolar bone resorption in rats. [PDF]
PLoS 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
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Foods, 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
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GroEL and the maintenance of bacterial endosymbiosis [PDF]
Trends 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
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