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.
europepmc +2 more sources
Ectopic CH60 mediates HAPLN1-induced cell survival signaling in multiple myeloma
Life Science Alliance, 2023 This study defines ectopic mitochondrial chaperonin 60 (CH60) on the multiple myeloma cell surface as a HAPLN1 matrikine receptor that signals via TLR4 to induce NF-κB signaling and drug resistance.
Debayan De Bakshi +7 more
doaj +1 more source
The chop gene contains an element for the positive regulation of the mitochondrial unfolded protein response. [PDF]
PLoS ONE, 2007 We have previously reported on the discovery of a mitochondrial specific unfolded protein response (mtUPR) in mammalian cells, in which the accumulation of unfolded protein within the mitochondrial matrix results in the transcriptional activation of ...
Tomohisa Horibe, Nicholas J Hoogenraad
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Significance of chaperonin 10-mediated inhibition of ATP hydrolysis by chaperonin 60 [PDF]
Proceedings of the National Academy of Sciences, 1997 Chaperonins are essential for the folding of proteins in bacteria, mitochondria, and chloroplasts. We have functionally characterized the yeast mitochondrial chaperonins hsp60 and hsp10. In the presence of ADP, one molecule of hsp10 binds to hsp60 with an apparent K d of 0.9 nM and a second molecule of ...
Y, Dubaquié, R, Looser, S, Rospert
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Crystal Structure of Chaperonin-60 from Paracoccus denitrificans [PDF]
Journal of Molecular Biology, 2001 The crystal structure of chaperonin-60 from Paracoccus denitrificans (P.cpn60) has been determined at 3.2 A resolution by the molecular replacement method. Two heptameric rings of identical subunits of P.cpn60 in adjacent asymmetric units are stacked in a back-to-back manner and form a cylinder, as found in GroEL, cpn60 from Escherichia coli.
Fukami, T. A. +4 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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Heat Shock Protein 60 (HSP60) detection by QCM Biosensor and Antibody Covered Gold Nanoparticles
International Journal of Electrochemical Science, 2021 Heat Shock Protein 60 (HSP60) is a 60 kDa weighting chaperonin that is an evolutionary conserved protein occurring in a wide number of organisms. It can serve as a plasma or blood serum biomarker of serious pathologies including cancer.
Miroslav Pohanka
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Mycobacterium tuberculosis expresses two chaperonin-60 homologs. [PDF]
Proceedings of the National Academy of Sciences, 1993 A 65-kDa protein and a 10-kDa protein are two of the more strongly immunoreactive components of Mycobacterium tuberculosis, the causative agent of tuberculosis. The 65-kDa antigen has homology with members of the GroEL or chaperonin-60 (Cpn60) family of heat shock proteins.
T H, Kong +4 more
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Epitopes of microbial and human heat shock protein 60 and their recognition in myalgic encephalomyelitis. [PDF]
PLoS ONE, 2013 Myalgic encephalomyelitis (ME, also called Chronic Fatigue Syndrome), a common disease with chronic fatigability, cognitive dysfunction and myalgia of unknown etiology, often starts with an infection.
Amal Elfaitouri +8 more
doaj +1 more source
Overexpression of a Prefoldin β subunit gene reduces biomass recalcitrance in the bioenergy crop Populus. [PDF]
, 2020 Prefoldin (PFD) is a group II chaperonin that is ubiquitously present in the eukaryotic kingdom. Six subunits (PFD1-6) form a jellyfish-like heterohexameric PFD complex and function in protein folding and cytoskeleton organization.
Barry, Kerrie +20 more
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