Results 181 to 190 of about 24,211 (206)

Deficiency of chaperonin 60 in Down's syndrome

Journal of Alzheimer's Disease, 2002
Patients with Down syndrome (DS) and Alzheimer's disease (AD) share a number of characteristic neuropathologic lesions. Several lines of evidence suggest that mitochondria and the oxidative stress response are involved in the pathogenesis of both conditions.
Peter, Bozner, G Lee, Wilson, Nadya M, Druzhyna, Tara K, Bryant-Thomas, Susan P, LeDoux, Glenn L, Wilson, Miguel A, Pappolla   +6 more
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Purification and characterization of the chaperonin 10 and chaperonin 60 proteins from Rhodobacter sphaeroides

Biochemistry, 1991
Two heat-shock proteins that show high identity with the Escherichia coli chaperonin 60 (groEL) and chaperonin 10 (groES) chaperonin proteins were purified and characterized from photolithoautotrophically grown Rhodobacter sphaeroides. The proteins were purified by using sucrose density gradient centrifugation and Mono-Q anion-exchange chromatography ...
K C, Terlesky, F R, Tabita
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Reconstitution and function of Tetragenococcus halophila chaperonin 60 tetradecamer

Journal of Bioscience and Bioengineering, 2005
Tetragenococcus halophila originally isolated from soy sauce is a halophilic lactic acid bacterium which can grow under 4 M sodium chloride. T. halophila chaperonin composed of a core moiety of chaperonin 60 (cpn60) and a lid moiety of chaperonin 10 (cpn10), is thought to contribute to host halotolerant capability.
Amonlaya, Tosukhowong, Jiro, Nakayama, Yoshimitsu, Mizunoe, Shinya, Sugimoto, Daisuke, Fukuda, Kenji, Sonomoto   +5 more
openaire   +2 more sources

Cloning, expression and purification of three Chaperonin 60 homologues

Journal of Chromatography B, 2003
The Chaperonin 60 (Cpn60) proteins have, in addition to their well-known functions of protein folding and protection, a range of intercellular signalling activities. As part of a study to investigate the biological activity of the Cpn60 proteins, particularly from pathogenic organisms, we have cloned and expressed three Cpn60 proteins from Homo sapiens,
Maria, Maguire, Anthony R M, Coates, Brian, Henderson   +2 more
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Human chaperonin 60 (Hsp60) stimulates bone resorption: structure/function relationships

Bone, 2003
It is established that the molecular chaperone, chaperonin 60, from various bacteria and from Homo sapiens has cell-cell signalling activity and is able to induce proinflammatory cytokine synthesis. We previously reported that chaperonin 60 proteins from Gram-negative bacteria, but not mycobacteria, have the capacity to resorb cultured murine calvarial
S, Meghji, M, Lillicrap, M, Maguire, P, Tabona, J S H, Gaston, S, Poole, B, Henderson   +6 more
openaire   +2 more sources

Purification and characterization of chaperonin 60 and chaperonin 10 from the anaerobic thermophile Thermoanaerobacter brockii

European Journal of Biochemistry, 1994
Chaperonin 60 and chaperonin 10 (GroEL and GroES homologues, respectively) have been isolated from extracts of the anaerobic thermophile Thermoanaerobacter brockii. A simple and rapid purification for chaperonin 60 made use of hydrophobic and anion‐exchange chromatographies, and could be readily scaled up; approximately 2 mg pure chaperonin 60 was ...
Truscott, KN, Hoj, PB, Scopes, RK
openaire   +3 more sources

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, Ana, Cehovin, Yanmin, Hu   +2 more
openaire   +1 more source

Chaperonin-facilitated refolding of ribulose bisphosphate carboxylase and ATP hydrolysis by chaperonin 60 (groEL) are potassium dependent

Biochemistry, 1990
Both the chaperonin- and MgATP-dependent reconstitution of unfolded ribulosebisphosphate carboxylase (Rubisco) and the uncoupled ATPase activity of chaperonin 60 (groEL) require ionic potassium. The spontaneous, chaperonin-independent reconstitution of Rubisco, observed at 15 but not at 25 degrees C, requires no K+ and is actually inhibited by ...
P V, Viitanen, T H, Lubben, J, Reed, P, Goloubinoff, D P, O'Keefe, G H, Lorimer   +5 more
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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, G K, Donaldson, G H, Lorimer, T H, Lubben, A A, Gatenby   +4 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, G, Egerton, A, Ball, R M, Tanguay, A E, Bianco   +4 more
openaire   +2 more sources