Results 11 to 20 of about 34,485 (247)
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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Ubiquitination-Driven Reprogramming of Proteostasis in Metastasis. [PDF]
Adv Sci (Weinh)The DCAF12–TRiC/CCT axis is a key regulator of metastasis in cancer. By reprogramming proteostasis to ensure efficient protein folding, it drives progression through a dual mechanism: enhancing cancer cell motility and invasiveness while concurrently activating pro‐growth and survival pathways.
Wei D, Chen J, Xu Y.
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cpnDB: A Chaperonin Sequence Database [PDF]
Genome Research, 2004 Type I chaperonins are molecular chaperones present in virtually all bacteria, some archaea and the plastids and mitochondria of eukaryotes. Sequences of cpn60 genes, encoding 60-kDa chaperonin protein subunits (CPN60, also known as GroEL or HSP60), are useful for phylogenetic studies and as targets for detection and identification of organisms ...
Janet E. Hill +4 more
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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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ZNRD2 Mediated Nucleoprotein Aggregation Impairs Respiratory Syncytial Virus Replication. [PDF]
Adv Sci (Weinh)During RSV infection, nucleoprotein (N) forms RNA‐bound oligomers. The host protein ZNRD2 binds to these oligomers, promoting their transition into insoluble aggregates. These aggregates simultaneously sequester functional N to restrict viral production and disrupt chaperonin assembly quality control by interfering with ZNRD2's role as an adaptor ...
Zhou H +8 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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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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