Probing the Kinetic Stabilities of Friedreich’s Ataxia Clinical Variants Using a Solid Phase GroEL Chaperonin Capture Platform [PDF]
Biomolecules, 2014 Numerous human diseases are caused by protein folding defects where the protein may become more susceptible to degradation or aggregation. Aberrant protein folding can affect the kinetic stability of the proteins even if these proteins appear to be ...
Ana R. Correia +3 more
doaj +4 more sources
Role of the chaperonin TCP-1 ring complex in protein aggregation and neurodegeneration [PDF]
Frontiers in Molecular NeuroscienceThe chaperonin TCP-1 ring complex (TRiC), also known as chaperonin-containing TCP-1 (CCT) complex, plays a crucial role in protein folding and quality control within the cell.
Vanlalrinchhani Varte +3 more
doaj +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
doaj +2 more sources
The BBS/CCT chaperonin complex ensures the localization of the adhesion G protein-coupled receptor ADGRV1 to the base of primary cilia [PDF]
Frontiers in Cell and Developmental BiologyPrimary cilia are antenna-like sensory organelles present on almost all eukaryotic cells. Their sensory capacity relies on receptors, in particular G-protein-coupled receptors (GPCRs) which localize to the ciliary membrane.
Joshua Linnert +6 more
doaj +2 more sources
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
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
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
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
Oncogenic fusion protein BCR-FGFR1 requires the breakpoint cluster region-mediated oligomerization and chaperonin Hsp90 for activation. [PDF]
, 2020 Mutation and translocation of fibroblast growth factor receptors often lead to aberrant signaling and cancer. This work focuses on the t(8;22)(p11;q11) chromosomal translocation which creates the breakpoint cluster region (BCR) fibroblast growth factor ...
Bisom-Rapp, Ezra W +4 more
core +2 more sources