Results 11 to 20 of about 13,634 (224)

Streptococcus suis Serotypes Characterized by Analysis of Chaperonin 60 Gene Sequences [PDF]

open access: yesApplied and Environmental Microbiology, 2001
ABSTRACT Streptococcus suis is an important pathogen of swine which occasionally infects humans as well. There are 35 serotypes known for this organism, and it would be desirable to develop rapid methods methods to identify and differentiate the strains of this species.
Brousseau, Ronald   +5 more
openaire   +4 more sources

Disease-associated mutations in the HSPD1 gene encoding the large subunit of the mitochondrial HSP60/HSP10 chaperonin complex

open access: yesFrontiers in Molecular Biosciences, 2016
Heat shock protein 60 (HSP60) forms together with heat shock protein 10 (HSP10) double-barrel chaperonin complexes that are essential for folding to the native state of proteins in the mitochondrial matrix space.
Peter Bross, Paula Fernandez-Guerra
doaj   +2 more sources

Significance of chaperonin 10-mediated inhibition of ATP hydrolysis by chaperonin 60 [PDF]

open access: yesProceedings of the National Academy of Sciences, 1997
Chaperonins are essential for the folding of proteins in bacteria, mitochondria, and chloroplasts. We have functionally characterized the yeast mitochondrial chaperonins hsp60 and hsp10. In the presence of ADP, one molecule of hsp10 binds to hsp60 with an apparent K d of 0.9 nM and a second molecule of ...
Dubaquié Y, Looser R, Rospert S
openaire   +3 more sources

The chop gene contains an element for the positive regulation of the mitochondrial unfolded protein response. [PDF]

open access: yesPLoS ONE, 2007
We have previously reported on the discovery of a mitochondrial specific unfolded protein response (mtUPR) in mammalian cells, in which the accumulation of unfolded protein within the mitochondrial matrix results in the transcriptional activation of ...
Tomohisa Horibe, Nicholas J Hoogenraad
doaj   +1 more source

Affinity of chaperonin-60 for a protein substrate and its modulation by nucleotides and chaperonin-10 [PDF]

open access: yesBiochemical Journal, 1994
The refolding of lactate dehydrogenase fully unfolded in 4 M guanidinium chloride was initiated by dilution into assay buffer, and the emergence of active enzyme was recorded. This was performed in the presence of the following chaperonin complexes in the refolding medium: chaperonin-60 (cpn60), cpn60-MgATP, cpn60-Mgp[NH]ppA, cpn60-MgADP in both the ...
Staniforth, RA   +3 more
openaire   +2 more sources

Heat Shock Protein 60 (HSP60) detection by QCM Biosensor and Antibody Covered Gold Nanoparticles

open access: yesInternational Journal of Electrochemical Science, 2021
Heat Shock Protein 60 (HSP60) is a 60 kDa weighting chaperonin that is an evolutionary conserved protein occurring in a wide number of organisms. It can serve as a plasma or blood serum biomarker of serious pathologies including cancer.
Miroslav Pohanka
doaj   +1 more source

The effect of nucleotides and mitochondrial chaperonin 10 on the structure and chaperone activity of mitochondrial chaperonin 60 [PDF]

open access: yesEuropean Journal of Biochemistry, 2001
Mitochondrial chaperonins are necessary for the folding of newly imported and stress‐denatured mitochondrial proteins. The goal of this study was to investigate the structure and function of the mammalian mitochondrial chaperonin system. We present evidence that the 60 kDa chaperonin (mt‐cpn60) exists in solution in dynamic equilibrium between monomers,
G, Levy-Rimler   +8 more
openaire   +2 more sources

Epitopes of microbial and human heat shock protein 60 and their recognition in myalgic encephalomyelitis. [PDF]

open access: yesPLoS ONE, 2013
Myalgic encephalomyelitis (ME, also called Chronic Fatigue Syndrome), a common disease with chronic fatigability, cognitive dysfunction and myalgia of unknown etiology, often starts with an infection.
Amal Elfaitouri   +8 more
doaj   +1 more source

Crystal Structure of Chaperonin-60 from Paracoccus denitrificans [PDF]

open access: yesJournal of Molecular Biology, 2001
The crystal structure of chaperonin-60 from Paracoccus denitrificans (P.cpn60) has been determined at 3.2 A resolution by the molecular replacement method. Two heptameric rings of identical subunits of P.cpn60 in adjacent asymmetric units are stacked in a back-to-back manner and form a cylinder, as found in GroEL, cpn60 from Escherichia coli.
Fukami, T. A.   +4 more
openaire   +2 more sources

The overview and role of heat shock proteins (HSP) especially HSP 60 and 70 in reproduction and other pathologies (a literature review)

open access: yesMedičnì Perspektivi, 2021
A search of peer-reviewed articles regarding heat shock proteins (HSP’s) especially HSP 60 and 70 was conducted in this review to understand its role in the development of various complications like miscarriage, preterm birth, tubal infertility and ...
V.O. Berestoviy   +6 more
doaj   +1 more source

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