Results 21 to 30 of about 31,985 (221)
Myelin pathology: Involvement of molecular chaperones and the promise of chaperonotherapy [PDF]
, 2019 The process of axon myelination involves various proteins including molecular chaperones. Myelin alteration is a common feature in neurological diseases due to structural and functional abnormalities of one or more myelin proteins.
Cappello F. +4 more
core +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
Antifolding activity of hsp60 couples protein import into the mitochondrial matrix with export to the intermembrane space [PDF]
, 1992 Cytochrome b2 reaches the intermembrane space of mitochondria by transport into the matrix followed by export across the inner membrane. While in the matrix, the protein interacts with hsp60, which arrests its folding prior to export.
Guiard, Bernard +6 more
core +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
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
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
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
Chaperonin GroEL Reassembly: An Effect of Protein Ligands and Solvent Composition
Biomolecules, 2014 Chaperonin GroEL is a complex oligomeric heat shock protein (Hsp60) assisting the correct folding and assembly of other proteins in the cell. An intriguing question is how GroEL folds itself.
Nataliya Ryabova +3 more
doaj +1 more source