Increased Efficiency of GroE-assisted Protein Folding by Manganese Ions
Open Access
- 1 November 1995
- journal article
- research article
- Published by Elsevier
- Vol. 270 (47) , 28387-28391
- https://doi.org/10.1074/jbc.270.47.28387
Abstract
No abstract availableKeywords
This publication has 21 references indexed in Scilit:
- Effect of Free and ATP-bound Magnesium and Manganese Ions on the ATPase Activity of Chaperonin GroEL14Biochemistry, 1995
- Residues in chaperonin GroEL required for polypeptide binding and releaseNature, 1994
- Characterization of a Functional GroEL 14 (GroES 7 ) 2 Chaperonin Hetero-OligomerScience, 1994
- Effect of Divalent Cations on the Molecular Structure of the GroEL OligomerBiochemistry, 1994
- Folding in vivo of bacterial cytoplasmic proteins: Role of GroELCell, 1993
- GroE facilitates refolding of citrate synthase by suppressing aggregationBiochemistry, 1991
- Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfolded state depends on two chaperonin proteins and Mg-ATPNature, 1989
- GroE heat-shock proteins promote assembly of foreign prokaryotic ribulose bisphosphate carboxylase oligomers in Escherichia coliNature, 1989
- Purification and properties of groE, a host protein involved in bacteriophage assemblyJournal of Molecular Biology, 1979
- A rapid and sensitive radiometric assay for adenosine triphosphatase activity using Cerenkov radiationAnalytical Biochemistry, 1975