Results 11 to 20 of about 24,211 (206)

DCAF12 Ubiquitin Ligase Promotes Lung Cancer Metastasis by Modulating the TRiC/CCT Chaperonin Complex. [PDF]

open access: yesAdv Sci (Weinh)
This study elucidates how DCAF12 facilitates non‐degradative ubiquitination to stabilize TRiC/CCT, thereby enhancing the folding capacity of chaperonins. This mechanism promotes the maturation of cytoskeletal proteins and activates key oncogenic drivers, including YAP, STAT3, and mTOR, ultimately driving metastatic progression in lung cancer.
Wang Z   +13 more
europepmc   +2 more sources

Heat shock protein 10 as a chaperone modulating α-synuclein amyloid fibril formation. [PDF]

open access: yesProtein Sci
Abstract HSP10 is a well‐known human co‐chaperone that interacts with HSP60 to comprise the HSP60/10 chaperonin complex which upholds mitochondrial proteostasis. HSP10 also demonstrates independent roles in binding to misfolded proteins and interacts with several amyloidogenic client proteins.
Larsson JNK   +5 more
europepmc   +2 more sources

The chop gene contains an element for the positive regulation of the mitochondrial unfolded protein response. [PDF]

open access: yesPLoS 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
doaj   +1 more source

Significance of chaperonin 10-mediated inhibition of ATP hydrolysis by chaperonin 60 [PDF]

open access: yesProceedings 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
openaire   +2 more sources

Crystal Structure of Chaperonin-60 from Paracoccus denitrificans [PDF]

open access: yesJournal 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
openaire   +2 more sources

Heat Shock Protein 60 (HSP60) detection by QCM Biosensor and Antibody Covered Gold Nanoparticles

open access: yesInternational 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
doaj   +1 more source

Epitopes of microbial and human heat shock protein 60 and their recognition in myalgic encephalomyelitis. [PDF]

open access: yesPLoS 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

Mycobacterium tuberculosis expresses two chaperonin-60 homologs. [PDF]

open access: yesProceedings 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
openaire   +2 more sources

The overview and role of heat shock proteins (HSP) especially HSP 60 and 70 in reproduction and other pathologies (a literature review)

open access: yesMedičnì Perspektivi, 2021
A search of peer-reviewed articles regarding heat shock proteins (HSP’s) especially HSP 60 and 70 was conducted in this review to understand its role in the development of various complications like miscarriage, preterm birth, tubal infertility and ...
V.O. Berestoviy   +6 more
doaj   +1 more source

Myelin pathology: Involvement of molecular chaperones and the promise of chaperonotherapy [PDF]

open access: yes, 2019
The process of axon myelination involves various proteins including molecular chaperones. Myelin alteration is a common feature in neurological diseases due to structural and functional abnormalities of one or more myelin proteins.
Cappello F.   +4 more
core   +1 more source

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