Results 41 to 50 of about 20,108 (219)
GroEL—A Versatile Chaperone for Engineering and a Plethora of Applications
Biomolecules, 2022 Chaperones play a vital role in the life of cells by facilitating the correct folding of other proteins and maintaining them in a functional state, being themselves, as a rule, more stable than the rest of cell proteins.
Maria S. Yurkova, Alexey N. Fedorov
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Molecules, 2022 The Escherichia coli chaperonin GroEL/ES (GroE) is one of the most extensively studied molecular chaperones. So far, ~80 proteins in E. coli are identified as GroE substrates that obligately require GroE for folding in vivo. In GroE-depleted cells, these
Tatsuya Niwa +2 more
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Inhibition of chaperonin ATPase activity by various co-chaperonins. [PDF]
, 2012 Steady-state ATPase activity was measured for each chaperonin. The T.O.N values (1/min) were 3.27±0.32, 0.83±0.14, 0.91±0.1 and 0.79±0.08 for GroEL, mHsp60, E321K and R264K/E358K, respectively. The percentage of ATPase inhibition by each co-chaperonin is
Galit Levy-Rimler (115146) +8 more
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Rubisco Assembly in the Chloroplast
Frontiers in Molecular Biosciences, 2018 Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) catalyzes the rate-limiting step in the Calvin-Benson cycle, which transforms atmospheric carbon into a biologically useful carbon source.
Anna Vitlin Gruber, Leila Feiz
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Chaperonin GroEL Reassembly: An Effect of Protein Ligands and Solvent Composition
Biomolecules, 2014 Chaperonin GroEL is a complex oligomeric heat shock protein (Hsp60) assisting the correct folding and assembly of other proteins in the cell. An intriguing question is how GroEL folds itself.
Nataliya Ryabova +3 more
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Biomedical and Biotechnology Research Journal, 2021 Background: The role of Lactobacillus casei on human health is well documented. However, little is known about their protein effects on food digestion. Therefore, in the present study, we aimed to investigate the efficacy of three proteins of L. casei on
Golgis Karimi +4 more
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Chaperonin filaments: The archael cytoskeleton [PDF]
, 1997 Chaperonins are multi-subunit double-ring complexed composed of 60-kDa proteins that are believed to mediate protein folding in vivo. The chaperonins in the hyperthermophilic archaeon Sulfolobus shibatae are composed of the organism`s two most abundant ...
Trent, Jonathan D. +4 more
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ATP dependent rotational motion of group II chaperonin observed by X-ray single molecule tracking. [PDF]
PLoS ONE, 2013 Group II chaperonins play important roles in protein homeostasis in the eukaryotic cytosol and in Archaea. These proteins assist in the folding of nascent polypeptides and also refold unfolded proteins in an ATP-dependent manner.
Hiroshi Sekiguchi +10 more
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Frontiers in Immunology, 2021 Recombinant human factor H (hFH) has potential for treating diseases linked to aberrant complement regulation including C3 glomerulopathy (C3G) and dry age-related macular degeneration.
Heather Kerr +18 more
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The genes encoding mammalian chaperonin 60 and chaperonin 10 are linked head-to-head and share a bidirectional promoter [PDF]
, 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.
Herd, Susanna M. +12 more
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