GroEL—A Versatile Chaperone for Engineering and a Plethora of Applications
Biomolecules, 2022 Chaperones play a vital role in the life of cells by facilitating the correct folding of other proteins and maintaining them in a functional state, being themselves, as a rule, more stable than the rest of cell proteins.
Maria S. Yurkova, Alexey N. Fedorov
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The Streptomyces coelicolor small ORF trpM stimulates growth and morphological development and exerts opposite effects on actinorhodin and calcium-dependent antibiotic production [PDF]
, 2020 In actinomycetes, antibiotic production is often associated with a morpho-physiological differentiation program that is regulated by complex molecular and metabolic networks. Many aspects of these regulatory circuits have been already elucidated and many
Alberto Vassallo +7 more
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Deletion of heat shock protein 60 in adult mouse cardiomyocytes perturbs mitochondrial protein homeostasis and causes heart failure. [PDF]
, 2020 To maintain healthy mitochondrial enzyme content and function, mitochondria possess a complex protein quality control system, which is composed of different endogenous sets of chaperones and proteases.
Chen, Ju +13 more
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Curcumin affects HSP60 folding activity and levels in neuroblastoma cells [PDF]
, 2020 The fundamental challenge in fighting cancer is the development of protective agents able to interfere with the classical pathways of malignant transformation, such as extracellular matrix remodeling, epithelial\u2013mesenchymal transition and ...
Campanella C. +9 more
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Rubisco Assembly in the Chloroplast
Frontiers in Molecular Biosciences, 2018 Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) catalyzes the rate-limiting step in the Calvin-Benson cycle, which transforms atmospheric carbon into a biologically useful carbon source.
Anna Vitlin Gruber, Leila Feiz
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Molecules, 2022 The Escherichia coli chaperonin GroEL/ES (GroE) is one of the most extensively studied molecular chaperones. So far, ~80 proteins in E. coli are identified as GroE substrates that obligately require GroE for folding in vivo. In GroE-depleted cells, these
Tatsuya Niwa +2 more
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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
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Production of a recombinant form of early pregnancy factor that can prolong allogeneic skin graft survival time in rats [PDF]
, 2000 Early pregnancy factor (EPF), an extracellular chaperonin 10 homologue, has immunosuppressive and growth factor properties. In order to carry out more extensive studies on the in vivo characteristics of EPF, a recombinant form of the molecule has been ...
Cassady, A I +7 more
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Biomedical and Biotechnology Research Journal, 2021 Background: The role of Lactobacillus casei on human health is well documented. However, little is known about their protein effects on food digestion. Therefore, in the present study, we aimed to investigate the efficacy of three proteins of L. casei on
Golgis Karimi +4 more
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ATP dependent rotational motion of group II chaperonin observed by X-ray single molecule tracking. [PDF]
PLoS ONE, 2013 Group II chaperonins play important roles in protein homeostasis in the eukaryotic cytosol and in Archaea. These proteins assist in the folding of nascent polypeptides and also refold unfolded proteins in an ATP-dependent manner.
Hiroshi Sekiguchi +10 more
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