Measuring protein stability in the GroEL chaperonin cage reveals massive destabilization
eLife, 2020 The thermodynamics of protein folding in bulk solution have been thoroughly investigated for decades. By contrast, measurements of protein substrate stability inside the GroEL/ES chaperonin cage have not been reported.
Ilia Korobko +3 more
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Chloroplast Chaperonin: An Intricate Protein Folding Machine for Photosynthesis
Frontiers in Molecular Biosciences, 2018 Group I chaperonins are large cylindrical-shaped nano-machines that function as a central hub in the protein quality control system in the bacterial cytosol, mitochondria and chloroplasts.
Qian Zhao, Qian Zhao, Cuimin Liu
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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
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Dynamic complexes in the chaperonin-mediated protein folding cycle
Frontiers in Molecular Biosciences, 2016 The GroEL-GroES chaperonin system is probably one of the most studied chaperone systems at the level of the molecular mechanism. Since the first reports of a bacterial gene involved in phage morphogenesis in 1972, these proteins have stimulated ...
Celeste Weiss +3 more
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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
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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
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Frontiers in Molecular Biosciences, 2016 Heat shock protein 60 (HSP60) forms together with heat shock protein 10 (HSP10) double-barrel chaperonin complexes that are essential for folding to the native state of proteins in the mitochondrial matrix space.
Peter Bross, Paula Fernandez-Guerra
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Abstract P-45: Structure of the Bacteriophage AR9 Bacillus Subtilis Chaperonin According to Cryo-Electron Microscopy [PDF]
International Journal of Biomedicine, 2021 Background: Chaperonins are a family of molecular chaperones Hsp60 (heat shock proteins 60). GroEL is a bacterial chaperonin. It ensures the correct folding of proteins, using the energy of ATP hydrolysis.
Ekaterina S. Maslova +4 more
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mTORC1-chaperonin CCT signaling regulates m6A RNA methylation to suppress autophagy
Proceedings of the National Academy of Sciences of the United States of America, 2021 Significance N6-methyladenosine (m6A) is the most prevalent modification in eukaryotic messenger RNA (mRNA) and affects RNA metabolism including splicing, stability, and translation.
Hong-Wen Tang +16 more
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Bardet–Biedl syndrome: The pleiotropic role of the chaperonin‐like BBS6, 10, and 12 proteins
American Journal of Medical Genetics. Part C, Seminars in Medical Genetics, 2022 Bardet–Biedl syndrome (BBS) is a rare pleiotropic disorder known as a ciliopathy. Despite significant genetic heterogeneity, BBS1 and BBS10 are responsible for major diagnosis in western countries.
Neha Gupta +4 more
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