Results 11 to 20 of about 4,302 (172)
Current Opinion in Structural Biology, 1998 Molecular chaperones are essential to all living organisms. Their key role consists of mediating protein folding within the cell. Recent functional studies have provided more detailed information about the function and regulation of the chaperone network.
N A, Ranson, H E, White, H R, Saibil
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Editorial: Type I Chaperonins: Mechanism and Beyond
Frontiers in Molecular Biosciences, 2018 Adina Breiman +2 more
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The Possible Role of the Type I Chaperonins in Human Insulin Self-Association
Life, 2022 Insulin is a hormone that attends to energy metabolism by regulating glucose levels in the bloodstream. It is synthesised within pancreas beta-cells where, before being released into the serum, it is stored in granules as hexamers coordinated by Zn2+ and
Federica Pizzo +6 more
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Biomolecules, 2020 The main events in chaperone-assisted protein folding are the binding and ligand-induced release of substrate proteins. Here, we studied the location of denatured proteins previously bound to the GroEL chaperonin resulting from the action of the GroES co-
Victor Marchenkov +4 more
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Identification of elements that dictate the specificity of mitochondrial Hsp60 for its co-chaperonin. [PDF]
PLoS ONE, 2012 Type I chaperonins (cpn60/Hsp60) are essential proteins that mediate the folding of proteins in bacteria, chloroplast and mitochondria. Despite the high sequence homology among chaperonins, the mitochondrial chaperonin system has developed unique ...
Avital Parnas +8 more
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Microbiology Research, 2023 This review discusses a few examples of specific mechanisms mediating the contribution of the GIT microbiota to the development of amyloid neurodegenerative diseases caused by the pathologic transformation of prion protein, or alpha-synuclein. The effect
Vladimir I. Muronetz +3 more
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Cell Reports, 2020 Summary: Global warming and emerging plant diseases challenge agricultural food/feed production. We identify mechanism(s) regulating both plant thermotolerance and disease resistance.
Bikram Datt Pant +4 more
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CryoEM reveals the stochastic nature of individual ATP binding events in a group II chaperonin
Nature Communications, 2021 The mechanism by which chaperonins coordinate ATP utilization in their multiple subunits remains unclear. Here, the authors employ an approach that uses cryo-EM single particle analysis to track the number and distribution of nucleotides bound to each ...
Yanyan Zhao +3 more
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Functional divergence of chloroplast Cpn60α subunits during Arabidopsis embryo development. [PDF]
PLoS Genetics, 2017 Chaperonins are a class of molecular chaperones that assist in the folding and assembly of a wide range of substrates. In plants, chloroplast chaperonins are composed of two different types of subunits, Cpn60α and Cpn60β, and duplication of Cpn60α and ...
Xiaolong Ke +6 more
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Frontiers in Bioscience, 2009 Chaperonins are ubiquitous and essential protein folding machines. They have a striking structure, with two rings of seven, eight, or nine protomers forming a "double doughnut" complex, with the cavity in each ring being the likely site for protein folding to take place. The group I chaperonins, found in bacteria and the organelles descended from them,
Andrew T, Large, Peter A, Lund
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