Results 11 to 20 of about 15,061 (184)
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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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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Journal 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
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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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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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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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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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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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Putting handcuffs on the chaperonin GroEL [PDF]
Proceedings of the National Academy of Sciences, 2013 Oligomeric, ring-shaped nano-machines that are fueled by ATP are ubiquitous in all three kingdoms of life and are involved in a wide range of processes that include, for example, protein folding, protein degradation, DNA and RNA remodeling, and protein insertion into membranes (for review, see ref. 1).
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BMC Evolutionary Biology, 2007 Background Heat-shock proteins are specialized molecules performing different and essential roles in the cell including protein degradation, folding and trafficking.
Fares Mario A, McNally David
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