Results 11 to 20 of about 5,379 (199)
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 ...
Juan García-Bernalt Diego +2 more
exaly +10 more sources
Biopolymers and Cell, 2001 Обзор посвящен последним достижениям в понимании основных механизмов посттрансляционной сборки белков у бактерий. Особое внимание уделено роли шаперонинов, их структуре и механизму работы при облегчении сборки белков.
Ерко, В.Н.
core +4 more sources
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
doaj +2 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 ...
Large, Andrew, Lund, Peter
core +3 more sources
Friends in need: How chaperonins recognize and remodel proteins that require folding assistance [PDF]
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
doaj +2 more sources
Single-Ring Intermediates Are Essential for Some Chaperonins
Frontiers in Molecular Biosciences, 2018 Chaperonins are macromolecular complexes found throughout all kingdoms of life that assist unfolded proteins reach a biologically active state. Historically, chaperonins have been classified into two groups based on sequence, subunit structure, and the ...
Jay M. Bhatt +6 more
doaj +2 more sources
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.
Mohammed Y. Ansari, Shekhar C. Mande
doaj +2 more sources
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
doaj +2 more sources
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
doaj +2 more sources
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
doaj +2 more sources