Results 31 to 40 of about 21,272 (221)
Heat Shock Protein 60 in Hepatocellular Carcinoma: Insights and Perspectives
Frontiers in Molecular Biosciences, 2020 Heat shock protein 60 (HSP60) is a mitochondrial chaperone that is implicated in physiological and pathological processes. For instance, it contributes to protein folding and stability, translocation of mitochondrial proteins, and apoptosis.
Abdullah Hoter +3 more
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The TRiCky Business of Protein Folding in Health and Disease
Frontiers in Cell and Developmental Biology, 2022 Maintenance of the cellular proteome or proteostasis is an essential process that when deregulated leads to diseases like neurological disorders and cancer.
Heba Ghozlan +5 more
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Proteome-Wide Analyis of Chaperonin-Dependent Protein Folding in Escherichia coli [PDF]
, 2006 In Escherichia coli, the cylindrical chaperonin GroEL and its cofactor GroES promote the folding of a fraction of newly synthesized polypeptide chains by acting as an Anfinsen cage.
Maier, T., Maier, Tobias
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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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Reconstitution of Pure Chaperonin Hetero-Oligomer Preparations in Vitro by Temperature Modulation
Frontiers in Molecular Biosciences, 2018 Chaperonins are large, essential, oligomers that facilitate protein folding in chloroplasts, mitochondria, and eubacteria. Plant chloroplast chaperonins are comprised of multiple homologous subunits that exhibit unique properties.
Anna Vitlin Gruber +3 more
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Frontiers in Genetics, 2020 Chaperonin containing tailless complex polypeptide 1 (CCT) or tailless complex polypeptide 1 ring complex (TRiC) is an essential eukaryotic molecular chaperone. It is a multi-subunit oligomer of two rings of eight individual protein subunits.
Julie Grantham
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GroEL—A Versatile Chaperone for Engineering and a Plethora of Applications
Biomolecules, 2022 Chaperones play a vital role in the life of cells by facilitating the correct folding of other proteins and maintaining them in a functional state, being themselves, as a rule, more stable than the rest of cell proteins.
Maria S. Yurkova, Alexey N. Fedorov
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Identification of a chaperonin-10 homologue in plant mitochondria [PDF]
, 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.
Leaver, C.J. +3 more
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Rubisco Assembly in the Chloroplast
Frontiers in Molecular Biosciences, 2018 Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) catalyzes the rate-limiting step in the Calvin-Benson cycle, which transforms atmospheric carbon into a biologically useful carbon source.
Anna Vitlin Gruber, Leila Feiz
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Molecules, 2022 The Escherichia coli chaperonin GroEL/ES (GroE) is one of the most extensively studied molecular chaperones. So far, ~80 proteins in E. coli are identified as GroE substrates that obligately require GroE for folding in vivo. In GroE-depleted cells, these
Tatsuya Niwa +2 more
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