Results 131 to 140 of about 13,221 (182)

Origin of chaperone dependence and assembly complexity in Rubisco’s biogenesis

Ng JZY, Wiens D, Schulz L, Hergenröder A, Küffner AM, Geil C, Erb TJ, Hochberg GKA.   +7 more
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The search for the chaperonin 60 receptors

Methods, 2007
Chaperonin (Cpn)60 proteins have the ability to activate human and murine myeloid cells. There is contradictory evidence that the receptor for this protein is either similar to that of lipopolysaccharide--CD14 and one or other toll-like receptor (e.g. TLR4) or is some other, undidentified, receptor.
Brian, Henderson, Jon, Mesher
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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
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Expression of chaperonin 60 in the hippocampus of the streptozotocin diabetic rat

NeuroReport, 2006
Mitochondrial dysfunction and oxidative stress are implicated in the pathological changes observed in the diabetic central nervous system. In this study, using the streptozotocin-induced diabetic rat model we document for the first time the over-expression of a mitochondrial specific stress protein (chaperonin 60) in the CA1/CA3 regions of the diabetic
Jiang, Yuan, Brian J, Young, Ryan D, Martinus   +2 more
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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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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
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Conformational states of ribulose bisphosphate carboxylase and their interaction with chaperonin 60

Biochemistry, 1992
Conformational states of ribulosebisphosphate carboxylase (Rubisco) from Rhodospirillum rubrum were examined by far-UV circular dichroism (CD), tryptophan fluorescence, and 1-anilino-naphthalenesulfonate (ANS) binding. At pH 2 and low ionic strength (I = 0.01), Rubisco adopts an unfolded, monomeric conformation (UA1 state) as judged by far-UV CD and ...
S M, van der Vies, P V, Viitanen, A A, Gatenby, G H, Lorimer, R, Jaenicke   +4 more
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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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