Characterization of a stable, reactivatable complex between chaperonin 60 and mitochondrial rhodanese.
Open Access
- 1 December 1992
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 267 (34) , 24648-24654
- https://doi.org/10.1016/s0021-9258(18)35813-7
Abstract
No abstract availableKeywords
This publication has 32 references indexed in Scilit:
- Protein folding in the cellNature, 1992
- Binding of a chaperonin to the folding intermediates of lactate dehydrogenaseBiochemistry, 1991
- The chaperonin GroEL binds a polypeptide in an .alpha.-helical conformationBiochemistry, 1991
- Chaperonin-mediated protein folding at the surface of groEL through a 'molten globule'-like intermediateNature, 1991
- Mitochondrial protein importBiochimica et Biophysica Acta (BBA) - Reviews on Biomembranes, 1989
- The high resolution three-dimensional structure of bovine liver rhodaneseFundamental and Applied Toxicology, 1983
- α‐lactalbumin: compact state with fluctuating tertiary structure?FEBS Letters, 1981
- Purification and properties of groE, a host protein involved in bacteriophage assemblyJournal of Molecular Biology, 1979
- The covalent and tertiary structure of bovine liver rhodaneseNature, 1978
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970