Results 11 to 20 of about 20,108 (219)
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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Scientific Reports, 2021 Plasmodium falciparum harbors group 1 and group 2 chaperonin systems to mediate the folding of cellular proteins in different cellular locations. Two distinct group 1 chaperonins operate in the organelles of mitochondria and apicoplasts, while group 2 ...
Brian Nguyen +4 more
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Emerging Roles of the Unique Molecular Chaperone Cosmc in the Regulation of Health and Disease
Biomolecules, 2022 The core-1 β1-3galactosyltransferase-specific chaperone 1 (Cosmc) is a unique molecular chaperone of core-1 β1-3galactosyltransferase(C1GALT1), which typically functions inside the endoplasmic reticulum (ER).
Ting Xiang +4 more
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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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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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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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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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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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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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Chaperonin-encapsulation of proteins for NMR. [PDF]
, 2010 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 ...
Dixon, Nicholas E +5 more
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