The chaperonin TRiC component Cct3 is required for axonal transport, myelination, and neuromuscular junction refinement [PDF]
Cell Death and DiseaseTRiCopathies are recently discovered neurodevelopmental diseases caused by pathogenic variants in components of the chaperonin tailless complex polypeptide 1 ring complex (TRiC).
Xiaomeng Zhang +7 more
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Correlation of the expression of tumor necrosis factor-alpha in chronic periapical lesions with the expression of bacterial chaperonin 60 [PDF]
Vojnosanitetski Pregled, 2022 Background/Aim. Chronic microbial infections of the root canal are a common issue. This process very often causes an immune reaction in the root canal system that results in forming of chronic periapical lesions (PLs).
Stanišić-Zindović Jelena +7 more
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Biomolecules, 2021 Group I chaperonins are a highly conserved family of essential proteins that self-assemble into molecular nanoboxes that mediate the folding of cytoplasmic proteins in bacteria and organelles.
Karla N. Valenzuela-Valderas +3 more
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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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Disruption of actin dynamics induces autophagy of the eukaryotic chaperonin TRiC/CCT
Cell Death Discovery, 2022 Autophagy plays important role in the intracellular protein quality control system by degrading abnormal organelles and proteins, including large protein complexes such as ribosomes.
Yuki Date +2 more
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Frontiers in Endocrinology, 2022 BackgroundLaryngeal cancer (LC) is a prevalent head and neck malignancy; however, the essential pathophysiological mechanism underlying its tumorigenesis and progression remains elusive.
Bing Liu +17 more
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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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Asymmetry in the function and dynamics of the cytosolic group II chaperonin CCT/TRiC. [PDF]
PLoS ONE, 2017 The eukaryotic group II chaperonin, the chaperonin-containing t-complex polypeptide 1 (CCT), plays an important role in cytosolic proteostasis. It has been estimated that as much as 10% of cytosolic proteins interact with CCT during their folding process.
Yohei Y Yamamoto +8 more
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Comparative transcriptome analysis reveals genetic diversity in the endosymbiont Hamiltonella between native and exotic populations of Bemisia tabaci from Brazil. [PDF]
PLoS ONE, 2018 The whitefly, Bemisia tabaci, is a species complex of more than 40 cryptic species and a major agricultural pest. It causes extensive damage to plants mainly by transmitting plant viruses. There is still a lack of genomic data available for the different
Bruno Rossitto De Marchi +4 more
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Acta Pharmaceutica Sinica B, 2022 Unlike healthy, non-transformed cells, the proteostasis network of cancer cells is taxed to produce proteins involved in tumor development. Cancer cells have a higher dependency on molecular chaperones to maintain proteostasis.
Gan Wang +21 more
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