GroEL‐Mediated protein folding [PDF]
Protein 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
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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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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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Exposure of Bifidobacterium longum subsp. infantis to Milk Oligosaccharides Increases Adhesion to Epithelial Cells and Induces a Substantial Transcriptional Response [PDF]
, 2013 Devon Kavanaugh is in receipt of a Teagasc Walsh Fellowship. The authors would also like to acknowledge the support of Science Foundation Ireland under Grant No.
Butto, Ludovica F. +8 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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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
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Cryo-EM map interpretation and protein model-building using iterative map segmentation. [PDF]
, 2020 A procedure for building protein chains into maps produced by single-particle electron cryo-microscopy (cryo-EM) is described. The procedure is similar to the way an experienced structural biologist might analyze a map, focusing first on secondary ...
Afonine PV +9 more
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A structural model for the GroEL chaperonin [PDF]
FEMS 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
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Borrelia burgdorferi Surface Exposed GroEL Is a Multifunctional Protein
Pathogens, 2021 The spirochete, Borrelia burgdorferi, has a large number of membrane proteins involved in a complex life cycle, that includes a tick vector and a vertebrate host.
Thomas Cafiero, Alvaro Toledo
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Structural Plasticity and Noncovalent Substrate Binding in the GroEL Apical Domain. A study using electrospray ionization mass spectrometry and fluorescence binding studies [PDF]
, 2002 Advances in understanding how GroEL binds to non-native proteins are reported. Conformational flexibility in the GroEL apical domain, which could account for the variety of substrates that GroEL binds, is illustrated by comparison of several independent ...
Adams +62 more
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