Results 11 to 20 of about 31,985 (221)
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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Frontiers in Molecular Biosciences, 2022 The multi-subunit chaperonin containing TCP-1 (CCT) is an essential molecular chaperone that functions in the folding of key cellular proteins. This paper reviews the interactome of the eukaryotic chaperonin CCT and its primary clients, the ubiquitous ...
Mark D. Wilkinson +5 more
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Measuring protein stability in the GroEL chaperonin cage reveals massive destabilization
eLife, 2020 The thermodynamics of protein folding in bulk solution have been thoroughly investigated for decades. By contrast, measurements of protein substrate stability inside the GroEL/ES chaperonin cage have not been reported.
Ilia Korobko +3 more
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Polycomb Requires Chaperonin Containing TCP-1 Subunit 7 for Maintaining Gene Silencing in Drosophila
Frontiers in Cell and Developmental Biology, 2021 In metazoans, heritable states of cell type-specific gene expression patterns linked with specialization of various cell types constitute transcriptional cellular memory.
Najma Shaheen +7 more
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Curcumin affects HSP60 folding activity and levels in neuroblastoma cells [PDF]
, 2020 The fundamental challenge in fighting cancer is the development of protective agents able to interfere with the classical pathways of malignant transformation, such as extracellular matrix remodeling, epithelial\u2013mesenchymal transition and ...
Campanella C. +9 more
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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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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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Processes underlying the nutritional programming of embryonic development by iron deficiency in the rat [PDF]
, 2012 Peer reviewedPublisher ...
Gambling, Lorraine +5 more
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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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