Results 141 to 150 of about 13,221 (182)
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Chaperonin 60 and macrophage activation.

Novartis Foundation symposium, 2008
Eukaryotic and prokaryotic chaperonin 60s (Cpn60s) activate macrophages to produce pro-inflammatory cytokines. CD14 and TLR4 have been proposed as potential Cpn receptors. In addition, Cpn60s can block LPS-induced activation. This is a dose-related effect, low concentrations block, and high concentrations activate.
Anthony R M, Coates   +2 more
openaire   +1 more source

The genes encoding mammalian chaperonin 60 and chaperonin 10 are linked head-to-head and share a bidirectional promoter

Gene, 1997
Chaperonins are a class of stress-inducible molecular chaperones involved in protein folding. We report the cloning, sequencing and characterisation of the rat mitochondrial chaperonin 60 and chaperonin 10 genes. The two genes are arranged in a head-to-head configuration and together comprise 14 kb and contain 14 introns.
Ryan, Michael T.   +5 more
openaire   +5 more sources

Chaperonin 60 and mitochondrial disease in Dictyostelium.

Journal of muscle research and cell motility, 2003
The single Dictyostelium chaperonin 60 gene, hspA, was cloned, sequenced and characterized. Sequence comparisons and a three-dimensional model for the structure of the encoded protein showed that it exhibits the conserved sequence and structural features expected for its role as the Dictyostelium mitochondrial chaperonin 60. Dictyostelium hspA contains
Kotsifas, Martha.   +4 more
openaire   +1 more source

The Chaperonin 60 Gene in Dictyostelium discoideum

2001
Submitted to the Dept. of Microbiology, Faculty of Science, Technology and Engineering.; Thesis (Ph.D.)-La Trobe University, 2001.
openaire   +1 more source

Complex interactions between the chaperonin 60 molecular chaperone and dihydrofolate reductase

Biochemistry, 1991
The spontaneous refolding of chemically denatured dihydrofolate reductase (DHFR) is completely arrested by chaperonin 60 (GroEL). This inhibition presumably results from the formation of a stable complex between chaperonin 60 and one or more intermediates in the folding pathway. While sequestered on chaperonin 60, DHFR is considerably more sensitive to
P V, Viitanen   +4 more
openaire   +2 more sources

Chaperonin 60 regulation of SOX9 ubiquitination mitigates the development of knee osteoarthritis

Journal of Molecular Medicine, 2016
Articular cartilage integrity loss is a prominently deleterious feature of osteoarthritis (OA). The mechanistic underlying the development of OA warrants characterization. Heat shock proteins (HSPs), members of the chaperone family, reportedly orchestrate tissue homeostasis and remodeling in response to detrimental stress.
Jih-Yang, Ko   +3 more
openaire   +2 more sources

Characterization of the heat-shock protein 60 chaperonin from Onchocerca volvulus☆

Molecular and Biochemical Parasitology, 2000
Chaperonin 60 (cpn60) belongs to the group of ubiquitous molecular chaperones that comprise the heat shock proteins, nucleoplasmins and chaperonins. Antibodies to recombinant CPN60 from humans was used to screen a cDNA library of Onchocerca volvulus and antigen-positive clones were selected.
Y, Wu   +4 more
openaire   +2 more sources

Occurrence of Chaperonin 60 and Chaperonin 10 in primary and secondary bacterial symbionts of aphids: Implications for the evolution of an endosymbiotic system in aphids

Journal of Molecular Evolution, 1993
All aphids harbor symbiotrophic prokaryotes ("primary symbionts") in a specialized-abdominal cell, the bacteriocyte. Chaperonin 60 (Cpn60, symbionin) and chaperonin 10 (Cpn10), which are high and low molecular weight heatshock proteins, were sought in tissues of more than 60 aphid species.
T, Fukatsu, H, Ishikawa
openaire   +2 more sources

Histoplasma capsulatum Chaperonin 60: A Novel Adhesin and Vaccine Candidate

2013
HSP60 has a key role in immunoregulation and the abundance of HSP60 proteins in mammalian and microbial cells impacts diverse biological functions in both. Therefore, it may be essential for innate immune cells to distinguish HSP60 proteins by their endogenous or infectious origin.
Joshua Daniel Nosanchuk   +1 more
openaire   +1 more source

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