Results 21 to 30 of about 21,272 (221)
Journal of Extracellular Vesicles, 2023 Cell proteostasis includes gene transcription, protein translation, folding of de novo proteins, post‐translational modifications, secretion, degradation and recycling. By profiling the proteome of extracellular vesicles (EVs) from T cells, we have found
Amelia Rojas‐Gómez +17 more
doaj +1 more source
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
Frontiers in Microbiology, 2016 Antibiotic resistance is an increasing challenge to modern healthcare. Aminoglycoside antiobiotics cause translation corruption and protein misfolding and aggregation in Escherichia coli.
Lise eGoltermann +2 more
doaj +1 more source
Chaperonins: Nanocarriers with Biotechnological Applications [PDF]
Nanomaterials, 2021 Chaperonins are molecular chaperones found in all kingdoms of life, and as such they assist in the folding of other proteins. Structurally, chaperonins are cylinders composed of two back-to-back rings, each of which is an oligomer of ~60-kDa proteins.
Sergio Pipaón +7 more
openaire +6 more sources
Production of a recombinant form of early pregnancy factor that can prolong allogeneic skin graft survival time in rats [PDF]
, 2000 Early pregnancy factor (EPF), an extracellular chaperonin 10 homologue, has immunosuppressive and growth factor properties. In order to carry out more extensive studies on the in vivo characteristics of EPF, a recombinant form of the molecule has been ...
Murphy, R M +7 more
core +1 more source
Cation-mediated interplay of loops in chaperonin-10
, 2006 The ubiquitously occurring chaperonins consist of a large tetradecameric Chaperonin-60, forming a cylindrical assembly, and a smaller heptameric Chaperonin-10.
Sen, Ranjan +4 more
core +3 more sources
Biomolecules, 2014 Numerous human diseases are caused by protein folding defects where the protein may become more susceptible to degradation or aggregation. Aberrant protein folding can affect the kinetic stability of the proteins even if these proteins appear to be ...
Ana R. Correia +3 more
doaj +1 more source
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 +26 more
doaj +1 more source
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
doaj +1 more source
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