The VHL tumor suppressor at the crossroad of protein folding, aggregation, and cancer. [PDF]
Mol OncolMutations, environmental stress, and chaperone dysfunction can destabilize pVHL, promoting its conversion from the native folded state into amyloid‐like assemblies. This transition may contribute to protein storage, cell dormancy, survival, and drug resistance.
Abad L, Tosatto SCE, Leonardi E.
europepmc +2 more sources
Phage Display Selection and In Silico Characterization of Peptides as Potential GroEL Modulators [PDF]
PharmaceuticsBackground/Objectives. Antibiotic resistance is an escalating global health concern, highlighting the need for innovative antibacterial strategies beyond traditional drugs.
Stefania Olla +4 more
doaj +2 more sources
Gene expression asymmetry in Parkinson’s disease: variation of CCT gene expression is correlated with hemisphere specific severity [PDF]
Frontiers in Molecular NeuroscienceParkinson’s disease (PD) symptom onset is typically unilateral, which may be related to molecular differences underlying hemispheric vulnerability. Here we sampled prefrontal cortex bilaterally from people with PD and healthy controls and performed RNA ...
Steven E. Pierce +6 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
doaj +1 more source
P. falciparum cpn20 is a bona fide co-chaperonin that can replace GroES in E. coli. [PDF]
PLoS ONE, 2013 Human malaria is among the most ubiquitous and destructive tropical, parasitic diseases in the world today. The causative agent, Plasmodium falciparum, contains an unusual, essential organelle known as the apicoplast.
Anna Vitlin Gruber +6 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
doaj +1 more source
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
doaj +1 more source
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
doaj +1 more source
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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