Ubiquitin-dependent Degradation of Certain Protein Substrates in Vitro Requires the Molecular Chaperone Hsc70
Open Access
- 1 April 1997
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 272 (14) , 9002-9010
- https://doi.org/10.1074/jbc.272.14.9002
Abstract
No abstract availableKeywords
This publication has 48 references indexed in Scilit:
- Roles of molecular chaperones in protein degradation.The Journal of cell biology, 1996
- Mechanism of GroEL action: Productive release of polypeptide from a sequestered position under groesCell, 1995
- Ubiquitin-mediated Processing of NF-κB Transcriptional Activator Precursor p105Journal of Biological Chemistry, 1995
- The ubiquitin-proteasome proteolytic pathwayCell, 1994
- A 70‐kDa heat shock cognate protein suppresses the defects caused by a proteasome mutation in Saccharomyces cerevisiaeFEBS Letters, 1994
- Unfolded proteins stimulate molecular chaperone Hsc70 ATPase by accelerating ADP/ATP exchangeBiochemistry, 1992
- Uncoupling ubiquitin-protein conjugation from ubiquitin-dependent proteolysis by use of .beta.,.gamma.-nonhydrolyzable ATP analogsBiochemistry, 1991
- Secondary structure of the mammalian 70-kilodalton heat shock cognate protein analyzed by circular dichroism spectroscopy and secondary structure predictionBiochemistry, 1990
- Role of arginine-tRNA in protein degradation by the ubiquitin pathwayNature, 1987
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976