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 Alcíbar +2 more
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Chaperonin in health and disease [PDF]
Molecular BiomedicineChaperonins, evolutionarily conserved heat shock proteins characterized by subunits of approximately 60 kDa, play indispensable roles in maintaining cellular homeostasis.
Pengfei Xu +8 more
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Myelin Pathology: Involvement of Molecular Chaperones and the Promise of Chaperonotherapy [PDF]
Brain Sciences, 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.
Federica Scalia +4 more
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A Glimpse Into the Structure and Function of Atypical Type I Chaperonins
Frontiers in Molecular Biosciences, 2018 Chaperonins are a subclass of molecular chaperones that assist cellular proteins to fold and assemble into their native shape. Much work has been done on Type I chaperonins, which has elucidated their elegant mechanism.
Shekhar C Mande
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Genetic and structural insights into the functional importance of the conserved gly-met-rich C-terminal tails in bacterial chaperonins [PDF]
Communications BiologyE. coli chaperonin GroEL forms nano-cages for protein folding. Although the chaperonin-mediated protein folding mechanism is well understood, the role of the conserved glycine and methionine-rich carboxy-terminal residues remains unclear.
C. M. Santosh Kumar +3 more
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The Passage of Chaperonins to Extracellular Locations in Legionella pneumophila Requires a Functional Dot/Icm System [PDF]
BiomoleculesHtpB, the chaperonin of the bacterial pathogen L. pneumophila, is found in extracellular locations, even the cytoplasm of host cells. Although chaperonins have an essential cytoplasmic function in protein folding, HtpB exits the cytoplasm to perform ...
Peter Robertson +2 more
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Increased expression and purification of soluble iron-regulatory protein 1 from Escherichia coli co-expressing chaperonins GroES and GroEL [PDF]
Brazilian Journal of Medical and Biological Research, 2008 Iron is an essential metal for all living organisms. However, iron homeostasis needs to be tightly controlled since iron can mediate the production of reactive oxygen species, which can damage cell components and compromise the integrity and/or cause DNA
H. Carvalho, R. Meneghini
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Compartmentalization of heme biosynthetic pathways into yeast mitochondria enhances heme production [PDF]
npj Science of FoodSaccharomyces cerevisiae is a generally recognized as safe (GRAS) workhorse strain widely used in the food industry for the cost-effective production of food ingredients. However, the heme production yield in yeast is significantly lower than in bacteria
Jae Yoon Won +4 more
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The BBS/CCT chaperonin complex ensures the localization of the adhesion G protein-coupled receptor ADGRV1 to the base of primary cilia [PDF]
Frontiers in Cell and Developmental BiologyPrimary cilia are antenna-like sensory organelles present on almost all eukaryotic cells. Their sensory capacity relies on receptors, in particular G-protein-coupled receptors (GPCRs) which localize to the ciliary membrane.
Joshua Linnert +6 more
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Friends in need: How chaperonins recognize and remodel proteins that require folding assistance
Frontiers in Molecular Biosciences, 2022 Chaperonins are biological nanomachines that help newly translated proteins to fold by rescuing them from kinetically trapped misfolded states. Protein folding assistance by the chaperonin machinery is obligatory in vivo for a subset of proteins in the ...
George Stan +3 more
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