Results 11 to 20 of about 21,272 (221)
Chloroplast Chaperonin: An Intricate Protein Folding Machine for Photosynthesis
Frontiers in Molecular Biosciences, 2018 Group I chaperonins are large cylindrical-shaped nano-machines that function as a central hub in the protein quality control system in the bacterial cytosol, mitochondria and chloroplasts.
Qian Zhao, Qian Zhao, Cuimin Liu
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Chaperonin Abundance Enhances Bacterial Fitness [PDF]
Frontiers in Molecular Biosciences, 2021 The ability of chaperonins to buffer mutations that affect protein folding pathways suggests that their abundance should be evolutionarily advantageous. Here, we investigate the effect of chaperonin overproduction on cellular fitness in Escherichia coli.
C. M. Santosh Kumar +7 more
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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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Toxins, 2023 GroEL is a chaperonin that helps other proteins fold correctly. However, alternative activities, such as acting as an insect toxin, have also been discovered.
Abraham Rivera-Ramírez +5 more
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Biochemical Characterization of a Group-5 Soluble Diiron Monooxygenase Hydroxylase and Related Chaperonin-like Component [PDF]
, 2020 Recently, the functional expression of group-5 hydroxylase component (MimA and MimC) in Escherichia coli along with its related chaperonin-like component (MimG) was reported by Furuya and Kino. In this study, we report the purification via a heterologous
Chihiro, Inoue +2 more
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BMC Evolutionary Biology, 2010 Background Chaperonin proteins are well known for the critical role they play in protein folding and in disease. However, the recent identification of three diverged chaperonin paralogs associated with the human Bardet-Biedl and McKusick-Kaufman ...
Macario Alberto JL +3 more
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Hsp60 Post-translational Modifications: Functional and Pathological Consequences
Frontiers in Molecular Biosciences, 2020 Hsp60 is a chaperone belonging to the Chaperonins of Group I and typically functions inside mitochondria in which, together with the co-chaperonin Hsp10, maintains protein homeostasis.
Celeste Caruso Bavisotto +14 more
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Complex Destabilization in the Mitochondrial Chaperonin Hsp60 Leads to Disease
Frontiers in Molecular Biosciences, 2020 Several neurological disorders have been linked to mutations in chaperonin genes and more specifically to the HSPD1 gene. In humans, HSPD1 encodes the mitochondrial Heat Shock Protein 60 (mtHsp60) chaperonin, which carries out essential protein folding ...
Alejandro Rodriguez +3 more
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Folding for the Immune Synapse: CCT Chaperonin and the Cytoskeleton
Frontiers in Cell and Developmental Biology, 2021 Lymphocytes rearrange their shape, membrane receptors and organelles during cognate contacts with antigen-presenting cells (APCs). Activation of T cells by APCs through pMHC-TCR/CD3 interaction (peptide-major histocompatibility complex-T cell receptor ...
Noa Beatriz Martín-Cófreces +6 more
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Chaperonin-encapsulation of proteins for NMR [PDF]
, 2016 A novel chaperonin-encapsulation system for NMR measurements has been designed. The single-ring variant SR398 with an ATPase deficient mutation of GroEL, also known as chaperonin, bound co-chaperonin GroES irreversibly, forming a stable cage to ...
Tanaka, Shinji +5 more
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