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Protein folding and chaperonins
Plant Molecular Biology, 1992The folding of polypeptide chains in cells, following either translation or translocation through membranes, must take place under conditions of extremely high protein concentrations. In addition, folding into a correct structure must occur in the presence of other rapidly folding species, and at temperatures known to destabilize aggregation-prone ...
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GroEL Ring Separation and Exchange in the Chaperonin Reaction
Cell, 2018Andreas Bracher +2 more
exaly
Mammalian cytosolic chaperonin.
Methods in enzymology, 1998Cytosolic chaperonin, the eukaryotic cytosolic homolog of GroEL, has certain unusual features that make it uniquely useful for studying the mechanism of chaperonin action. It is of particular interest as an essential component in the generation of native actin and tubulin in vivo. We describe a method for the purification of mammalian c-cpn from rabbit
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Pathway of Actin Folding Directed by the Eukaryotic Chaperonin TRiC
Cell, 2018David Balchin +2 more
exaly
Seminars in cell biology, 1991
The discovery and properties of the plastid chaperonin are described. This chaperonin is implicated in the folding and assembly of the enzyme ribulose bisphosphate carboxylase-oxygenase and in the folding of proteins imported into plastids from the cytosol.
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The discovery and properties of the plastid chaperonin are described. This chaperonin is implicated in the folding and assembly of the enzyme ribulose bisphosphate carboxylase-oxygenase and in the folding of proteins imported into plastids from the cytosol.
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