Intracellular Proteolytic Cleavage of 9-cis-Retinoic Acid Receptor α by Cathepsin L-type Protease Is a Potential Mechanism for Modulating Thyroid Hormone Action
Open Access
- 1 December 1998
- journal article
- Published by Elsevier
- Vol. 273 (50) , 33166-33173
- https://doi.org/10.1074/jbc.273.50.33166
Abstract
No abstract availableKeywords
This publication has 42 references indexed in Scilit:
- Heterodimerization Preferences of Thyroid Hormone Receptor α IsoformsBiochemical and Biophysical Research Communications, 1996
- Selective uptake and degradation of c-Fos and v-Fos by rat liver lysosomesFEBS Letters, 1996
- Proteolytic processing of nuclear factor κB by calpain in vitroFEBS Letters, 1996
- The Molecular Biology of Thyroid Hormone ActionAnnals of the New York Academy of Sciences, 1995
- Importance of cell aggregation for expression of liver functions and regeneration demonstrated with primary cultured hepatocytesJournal of Cellular Physiology, 1993
- Regulation of the Synthesis and Secretion of Transferrin and Cyclic Protein-2/Cathepsin L by Mature Rat Sertoli Cells in Culture1Biology of Reproduction, 1992
- Retinoid X receptor interacts with nuclear receptors in retinoic acid, thyroid hormone and vitamin D3 signallingNature, 1992
- Retinoid X receptor is an auxiliary protein for thyroid hormone and retinoic acid receptorsNature, 1992
- Novel epoxysuccinyl peptides A selective inhibitor of cathepsin B, in vivoFEBS Letters, 1991
- Gene structure and 5'‐upstream sequence of rat cathepsin LFEBS Letters, 1989