Journal ArticleDOI
Reactivation of denatured fungal glucose 6-phosphate dehydrogenase and E. coli alkaline phosphatase with E. coli ribosome.
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TLDR
Almost total recovery of the activities of completely inactivated enzymes was obtained when 70S ribosome was present at about equimolar concentration with the enzyme molecules at 37C and 50C, respectively.About:
This article is published in Biochemical and Biophysical Research Communications.The article was published on 1992-03-16. It has received 44 citations till now. The article focuses on the topics: Alkaline phosphatase & Enzyme.read more
Citations
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Journal ArticleDOI
Protein folding at the exit tunnel.
TL;DR: This review focuses on the current state of knowledge in protein folding in the cell with emphasis on the early stage of a protein's life, as the nascent polypeptide traverses and emerges from the ribosomal tunnel.
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Ribosomes and ribosomal RNA as chaperones for folding of proteins
TL;DR: Large subunits of E. coli ribosomes, specifically 23S rRNA, have the capacity to mediate refolding of denatured rhodanese and this activity is related to the state or conformation of ribosome that is promoted by EF-G.
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Protein folding and aggregation in bacteria.
TL;DR: Overall, this review illustrates how prokaryotic organisms might provide the bedrock on which to understand the complexity of protein folding and aggregation in the cell.
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In vitro protein folding by ribosomes from Escherichia coli, wheat germ and rat liver: the role of the 50S particle and its 23S rRNA
TL;DR: Observations on the refolding of denatured lactate dehydrogenase from rabbit muscle and glucose-6-phosphate dehydration from baker's yeast by ribosomes from E. coli, wheat germ and rat liver show loss of tertiary structure inhibited the protein-folding activity of 23S rRNA.
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Reactivation of denatured proteins by 23S ribosomal RNA: role of domain V.
TL;DR: Domain V of 23S rRNA appears to play a crucial role in reactivation of denatured proteins in E. coli.
References
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Journal ArticleDOI
Principles that Govern the Folding of Protein Chains
TL;DR: Anfinsen as discussed by the authors provided a sketch of the rich history of research that provided the foundation for his work on protein folding and the Thermodynamic Hypothesis, and outlined potential avenues of current and future scientific exploration.
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Homologous plant and bacterial proteins chaperone oligomeric protein assembly
Sean M. Hemmingsen,Carol A. Woolford,Saskia M. van der Vies,Kit Tilly,David T. Dennis,Costa Georgopoulos,Roger W. Hendrix,R. John Ellis +7 more
TL;DR: Chaperonins comprise a class of molecular chaperones that are found in chloroplasts, mitochondria and prokaryotes and are implicated in the assembly of the oligomeric enzyme ribulose bisphosphate carboxylase-oxygenase, which catalyses photosynthetic CO2-fixation in higher plants.
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Further studies on the properties and assay of glucose 6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase of rat liver.
TL;DR: The significance of this pathway in animal tissues, its physiological control and the relative importance of the direct oxidative and glycolytic routes of carbohydrate metabolism are still, however, chiefly matters of conjecture.
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Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfolded state depends on two chaperonin proteins and Mg-ATP
TL;DR: In vitro reconstitution of active ribulose bisphosphate carboxylase (Rubisco) from unfolded poly-peptides is facilitated by the molecular chaperones: chaperonin-60 from Escherichia coli, yeast mitochondria or chloroplasts, together with chaper onin-10 from E coli, and Mg-ATP.
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Molecular chaperones: proteins essential for the biogenesis of some macromolecular structures
R. John Ellis,Sean M. Hemmingsen +1 more
TL;DR: The effect that the recognition of the essential roles played by these proteins in assembly processes may have on the principle of spontaneous self-assembly is discussed.