Two distinct mechanisms operate in the reactivation of heat-denatured proteins by the mitochondrial Hsp70/Mdj1p/Yge1p chaperone system
- 19 February 1999
- journal article
- research article
- Published by Elsevier BV in Journal of Molecular Biology
- Vol. 286 (2), 447-464
- https://doi.org/10.1006/jmbi.1998.2465
Abstract
No abstract availableKeywords
This publication has 29 references indexed in Scilit:
- Purification and Biochemical Properties of Saccharomyces cerevisiae Mdj1p, the Mitochondrial DnaJ HomologueJournal of Biological Chemistry, 1997
- The Mitochondrial hsp70 Chaperone SystemJournal of Biological Chemistry, 1997
- Role of mitochondrial GrpE and phosphate in the ATPase cycle of matrix Hsp70Journal of Molecular Biology, 1997
- Purification and Biochemical Properties of Saccharomyces cerevisiae's Mge1p, the Mitochondrial Cochaperone of Ssc1pPublished by Elsevier BV ,1996
- Molecular chaperones in cellular protein foldingNature, 1996
- Binding of Mitochondrial Presequences to Yeast Cytosolic Heat Shock Protein 70 Depends on the Amphiphilicity of the PresequencePublished by Elsevier BV ,1996
- Mitochondrial presequences can induce aggregation of unfolded proteinsFEBS Letters, 1995
- Three-dimensional structure of the ATPase fragment of a 70K heat-shock cognate proteinNature, 1990
- SSC1, an essential member of the yeast HSP70 multigene family, encodes a mitochondrial protein.Molecular and Cellular Biology, 1989
- Transcription antitermination by bacteriophage lambda N gene productJournal of Molecular Biology, 1980