Results 171 to 180 of about 13,634 (224)
Heat shock protein 10 as a chaperone modulating α-synuclein amyloid fibril formation. [PDF]
Larsson JNK +5 more
europepmc +1 more source
A nuclear TRiC/CCT chaperonin assembles meiotic HORMAD proteins into chromosome axes competent for crossing over. [PDF]
Zetka M +5 more
europepmc +1 more source
Origin of chaperone dependence and assembly complexity in Rubisco’s biogenesis
Ng JZY +7 more
europepmc +1 more source
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 +6 more sources
Chaperonin 60 is the prototypic molecular chaperone, an essential protein in eukaryotes and prokaryotes, whose sequence conservation provides an excellent basis for phylogenetic analysis.
Mario A Fares, Peter A Lund
exaly +2 more sources
The mitochondrial chaperonin system consists of chaperonin 60 (also termed hsp60), which is homologous to E. coli groEL, and chaperonin 10, which is homologous to E. coli groES.
Tina Junne, Benjamin S Glick, G Schatz
exaly +2 more sources
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The search for the chaperonin 60 receptors
Methods, 2007Chaperonin (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
openaire +2 more sources
Deficiency of chaperonin 60 in Down's syndrome
Journal of Alzheimer's Disease, 2002Patients 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 +6 more
openaire +2 more sources
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
openaire +2 more sources
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
openaire +2 more sources
Reconstitution and function of Tetragenococcus halophila chaperonin 60 tetradecamer
Journal of Bioscience and Bioengineering, 2005Tetragenococcus 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 +5 more
openaire +2 more sources

