Beyond Antibodies: Development of a Novel Protein Scaffold Based on Human Chaperonin 10. [PDF]
Sci Rep, 2016 AbstractHuman Chaperonin 10 (hCpn10) was utilised as a novel scaffold for presenting peptides of therapeutic and diagnostic significance. Molecular dynamic simulations and protein sizing analyses identified a peptide linker (P1) optimal for the formation of the quarternary hCpn10 heptamer structure.
Alsultan AM +5 more
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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
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 ...
Dubaquié Y, Looser R, Rospert S
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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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Identification of a chaperonin‐10 homologue in plant mitochondria [PDF]
FEBS Letters, 1994 Chaperonin‐60 and chaperonin‐10 form stable binary complexes in the presence of ATP. This phenomenon has been used as the basis for the identification of a chaperonin‐10 homologue in potato (Solanum tuberosum L.) mitochondria. ATP‐dependent binary complexes formed between chaperonin‐60 and chaperonin‐10 in potato mitochondrial extracts were isolated by
Burt, W.J.E., Leaver, C.J.
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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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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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