The Aggregation State of Rhodanese during Folding Influences the Ability of GroEL to Assist Reactivation
Open Access
- 1 August 2001
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 276 (31) , 28739-28743
- https://doi.org/10.1074/jbc.m102500200
Abstract
No abstract availableKeywords
This publication has 29 references indexed in Scilit:
- Alteration Around the Active Site of Rhodanese during Urea-induced Denaturation and Its Implications for FoldingJournal of Biological Chemistry, 2000
- Determination of Regions in the Dihydrofolate Reductase Structure That Interact with the Molecular Chaperonin GroELBiochemistry, 1996
- The stability and hydrophobicity of cytosolic and mitochondrial malate dehydrogenases and their relation to chaperonin‐assisted foldingFEBS Letters, 1994
- The mechanism of protein folding. Implications of in vitro refolding models for de novo protein folding and translocation in the cellBiochemistry, 1990
- Role of diffusion in the folding of the .alpha. subunit of tryptophan synthase from Escherichia coliBiochemistry, 1990
- Polypeptide chain binding proteins: Catalysts of protein folding and related processes in cellsCell, 1989
- Protein folding in mitochondria requires complex formation with hsp60 and ATP hydrolysisNature, 1989
- Folding and association of proteinsProgress in Biophysics and Molecular Biology, 1987
- The covalent and tertiary structure of bovine liver rhodaneseNature, 1978
- Crystalline Rhodanese. I. Purification and Physicochemical Examination.Acta Chemica Scandinavica, 1953