Results 31 to 40 of about 37,307 (249)
Overexpression of a Prefoldin β subunit gene reduces biomass recalcitrance in the bioenergy crop Populus. [PDF]
, 2020 Prefoldin (PFD) is a group II chaperonin that is ubiquitously present in the eukaryotic kingdom. Six subunits (PFD1-6) form a jellyfish-like heterohexameric PFD complex and function in protein folding and cytoskeleton organization.
Barry, Kerrie +20 more
core +1 more source
The chaperonin CCT controls T cell receptor–driven 3D configuration of centrioles
Science Advances, 2020 Eukaryotic chaperonin-containing TCP1 drives tubulin dynamics and centrosome structure at immune synaptic contacts. T lymphocyte activation requires the formation of immune synapses (IS) with antigen-presenting cells.
N. Martín-Cófreces +15 more
semanticscholar +1 more source
Complex Destabilization in the Mitochondrial Chaperonin Hsp60 Leads to Disease
Frontiers in Molecular Biosciences, 2020 Several neurological disorders have been linked to mutations in chaperonin genes and more specifically to the HSPD1 gene. In humans, HSPD1 encodes the mitochondrial Heat Shock Protein 60 (mtHsp60) chaperonin, which carries out essential protein folding ...
Alejandro Rodriguez +3 more
doaj +1 more source
Folding for the Immune Synapse: CCT Chaperonin and the Cytoskeleton
Frontiers in Cell and Developmental Biology, 2021 Lymphocytes rearrange their shape, membrane receptors and organelles during cognate contacts with antigen-presenting cells (APCs). Activation of T cells by APCs through pMHC-TCR/CD3 interaction (peptide-major histocompatibility complex-T cell receptor ...
Noa Beatriz Martín-Cófreces +6 more
doaj +1 more source
Postembryonic RNAi in Heterorhabditis bacteriophora: a nematode insect parasite and host for insect pathogenic symbionts [PDF]
, 2007 Background: Heterorhabditis bacteriophora is applied throughout the world for the biological control of insects and is an animal model to study interspecies interactions, e.g. mutualism, parasitism and vector-borne disease. H. bacteriophora nematodes are
Ciche, Todd A., Sternberg, Paul W.
core +4 more sources
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
Chaperonin-assisted protein folding: a chronologue
Quarterly Reviews of Biophysics (print), 2020 This chronologue seeks to document the discovery and development of an understanding of oligomeric ring protein assemblies known as chaperonins that assist protein folding in the cell.
A. Horwich, W. Fenton
semanticscholar +1 more source
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
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 +5 more sources