Results 31 to 40 of about 20,108 (219)

Muscle Histopathological Abnormalities in a Patient With a CCT5 Mutation Predicted to Affect the Apical Domain of the Chaperonin Subunit

Frontiers in Molecular Biosciences, 2022
Recognition of diseases associated with mutations of the chaperone system genes, e.g., chaperonopathies, is on the rise. Hereditary and clinical aspects are established, but the impact of the mutation on the chaperone molecule and the mechanisms ...
Federica Scalia, Federica Scalia, Rosario Barone, Francesca Rappa, Antonella Marino Gammazza, Fabrizio Lo Celso, Fabrizio Lo Celso, Giosuè Lo Bosco, Giosuè Lo Bosco, Giampaolo Barone, Vincenzo Antona, Maria Vadalà, Maria Vadalà, Alessandra Maria Vitale, Alessandra Maria Vitale, Giuseppe Donato Mangano, Domenico Amato, Giusy Sentiero, Giusy Sentiero, Filippo Macaluso, Kathryn H. Myburgh, Everly Conway de Macario, Alberto J. L. Macario, Alberto J. L. Macario, Mario Giuffrè, Francesco Cappello, Francesco Cappello   +26 more
doaj   +1 more source

Archaeal chaperonins

Frontiers in Bioscience, 2009
Chaperonins are ubiquitous and essential protein folding machines. They have a striking structure, with two rings of seven, eight, or nine protomers forming a "double doughnut" complex, with the cavity in each ring being the likely site for protein folding to take place. The group I chaperonins, found in bacteria and the organelles descended from them,
Andrew T, Large, Peter A, Lund
openaire   +2 more sources

Chaperonin-co-chaperonin interactions measured by SPR. [PDF]

, 2012
Association and dissociation patterns of 10 µM of the indicated chaperonin to immobilized (A) GroES (∼ 600 Relative Units-RU) or (B) mHsp10 (∼ 800 RU) in the presence of 2 mM ATP.
Galit Levy-Rimler (115146), Shahar Nisemblat (104049), Celeste Weiss (104056), Amir Pri-Or (115148), Peter A. Lund (115152), Peter Bross (115155), Abdussalam Azem (17943), Avital Parnas (104053), Tsaffrir Zor (115150)   +8 more
core   +1 more source

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., Burt, W.J.E., W.J.E. Burt, C.J. Leaver   +3 more
core   +1 more source

In vivo client proteins of the chaperonin GroEL-GroES provide insight into the role of chaperones in protein evolution

Frontiers in Molecular Biosciences, 2023
Protein folding is often hampered by intermolecular protein aggregation, which can be prevented by a variety of chaperones in the cell. Bacterial chaperonin GroEL is a ring-shaped chaperone that forms complexes with its cochaperonin GroES, creating ...
Hideki Taguchi, Ayumi Koike-Takeshita
doaj   +1 more source

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, Abdullah Hoter, Sandra Rizk, Hassan Y. Naim   +3 more
doaj   +1 more source

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, Heba Ghozlan, Amanda Cox, Daniel Nierenberg, Stephen King, Annette R. Khaled   +5 more
doaj   +1 more source

The Functional Differences between the GroEL Chaperonin of Escherichia coli and the HtpB Chaperonin of Legionella pneumophila Can Be Mapped to Specific Amino Acid Residues

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, Gabriel Moreno-Hagelsieb, John R. Rohde, Rafael A. Garduño   +3 more
doaj   +1 more source

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, Milena Vugman, Abdussalam Azem, Celeste E. Weiss   +3 more
doaj   +1 more source

The Molecular Chaperone CCT/TRiC: An Essential Component of Proteostasis and a Potential Modulator of Protein Aggregation

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
doaj   +1 more source