Results 51 to 60 of about 8,317 (219)

Chloroplast Chaperonin: An Intricate Protein Folding Machine for Photosynthesis

open access: yesFrontiers in Molecular Biosciences, 2018
Group I chaperonins are large cylindrical-shaped nano-machines that function as a central hub in the protein quality control system in the bacterial cytosol, mitochondria and chloroplasts.
Qian Zhao, Qian Zhao, Cuimin Liu
doaj   +1 more source

OsCPN10a, cooperating with OsCPN20 and OsHSP60‐3B negatively regulate ABA signaling and enhance seed storability in rice

open access: yesJournal of Integrative Plant Biology, EarlyView.
Abscisic acid signaling homeostasis is essential for seed storability. The molecular chaperone OsCPN10a enhances rice seed storability by forming a trimeric chaperone complex with OsCPN20‐OsHSP60‐3B that attenuates abscisic acid signaling via direct interaction with OsPYL10‐OsABIL1, thereby maintaining starch integrity and offering a promising target ...
Sufeng Liao   +13 more
wiley   +1 more source

Single-molecule fluorescence polarization study of conformational change in archaeal group II chaperonin. [PDF]

open access: yesPLoS ONE, 2011
Group II chaperonins found in archaea and in eukaryotic cytosol mediate protein folding without a GroES-like cofactor. The function of the cofactor is substituted by the helical protrusion at the tip of the apical domain, which forms a built-in lid on ...
Ryo Iizuka   +3 more
doaj   +1 more source

The refolding of recombinant human liver methylmalonyl-CoA mutase from inclusion bodies produced in Escherichia coli : a thesis presented in partial fulfilment of the requirements for the degree of Master of Science in Biochemistry at Massey University [PDF]

open access: yes, 1998
Human methylmalonyl-CoA mutase (hMCM) is an adenosylcobalamin-dependent enzyme that catalyses the structural rearrangement of (R)-methylmalonyl-CoA to succinyl-CoA as pan of the catabolism of the branched chain amino acids valine, leucine and isoleucine,
Hayes, Michelle Marie
core  

A multi‐omics investigation of sarcopenia and frailty: Integrating genomic, epigenomic and telomere length data

open access: yesExperimental Physiology, EarlyView.
Abstract Sarcopenia and frailty are complex geriatric syndromes influenced by a combination of genetic and environmental factors. Recent studies suggest that specific genetic variants, DNA methylation patterns and shortened telomeres are associated with age‐related diseases and might contribute to the development of both sarcopenia and frailty. In this
Valentina Ginevičienė   +10 more
wiley   +1 more source

A comprehensive analysis of prefoldins and their implication in cancer

open access: yesiScience, 2021
Summary: Prefoldins (PFDNs) are evolutionary conserved co-chaperones, initially discovered in archaea but universally present in eukaryotes. PFDNs are prevalently organized into hetero-hexameric complexes.
Irene Herranz-Montoya   +2 more
doaj   +1 more source

Traversing the effects of ploidy changes in different Eragrostis curvula genotypes through high‐throughput RNA sequencing

open access: yesThe Plant Genome, Volume 19, Issue 2, June 2026.
Abstract Polyploidization has played a key role in plant genome evolution. Eragrostis curvula (Schrad.) Ness, a perennial forage grass species of the Poaceae family, is an excellent model for investigating genome duplication due to its natural variation in ploidy levels.
D. F. Santoro   +5 more
wiley   +1 more source

Dissecting intrinsic chaperonin activity [PDF]

open access: yesProceedings of the National Academy of Sciences, 1997
It has long been known that the linear sequence of amino acids along the polypeptide chains contains all the necessary information required to determine the correct three-dimensional structure of a protein (1). Indeed, a large number of proteins have been shown to refold spontaneously in vitro from an unfolded denatured state to the native folded state
G M, Clore, A M, Gronenborn
openaire   +2 more sources

Structural and mechanistic characterization of an archaeal-like chaperonin from a thermophilic bacterium

open access: yesNature Communications, 2017
Chaperonins (CPNs) are ATP-dependent protein-folding machines. Here the authors present the open and closed crystal structures of a Group III CPN from the thermophilic bacterium Carboxydothermus hydrogenoformans, discuss its mechanism and structurally ...
Young Jun An   +8 more
doaj   +1 more source

The Molecular Anatomy of Human Hsp60 and its Similarity with that of Bacterial Orthologs and Acetylcholine Receptor Reveal a Potential Pathogenetic Role of Anti-Chaperonin Immunity in Myasthenia Gravis. [PDF]

open access: yes, 2012
Heat-shock protein 60 (Hsp60) is ubiquitous and highly conserved being present in eukaryotes and prokaryotes, including pathogens. This chaperonin, although typically a mitochondrial protein, can also be found in other intracellular sites ...
BENIGNO, Arcangelo   +7 more
core   +1 more source

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