Possible Regulation of the Skeletal Muscle Ryanodine Receptor by a Polyubiquitin Binding Subunit of the 26S Proteasome
- 17 April 1998
- journal article
- Published by Elsevier in Biochemical and Biophysical Research Communications
- Vol. 245 (2) , 428-429
- https://doi.org/10.1006/bbrc.1998.8450
Abstract
No abstract availableKeywords
This publication has 13 references indexed in Scilit:
- Characterization of Type 3 Ryanodine Receptor (RyR3) of Sarcoplasmic Reticulum from Rabbit Skeletal MusclesJournal of Biological Chemistry, 1997
- Novel Regulation of the Helix-Loop-Helix Protein Id1 by S5a, a Subunit of the 26 S ProteasomePublished by Elsevier ,1997
- Angiotensin II-induced Down-regulation of Inositol Trisphosphate Receptors in WB Rat Liver Epithelial CellsPublished by Elsevier ,1997
- Ryanodine receptor Ca2+ release channels: does diversity in form equal diversity in function?Physiological Reviews, 1996
- Arabidopsis MBP1 gene encodes a conserved ubiquitin recognition component of the 26S proteasome.Proceedings of the National Academy of Sciences, 1996
- A Proteasome Activator Subunit Binds CalciumJournal of Biological Chemistry, 1995
- Molecular Cloning and Expression of a 26 S Protease Subunit Enriched in Dileucine RepeatsPublished by Elsevier ,1995
- Stabilization of calcium release channel (ryanodine receptor) function by FK506-binding proteinPublished by Elsevier ,1994
- Sequence analysis of the ryanodine receptor: Possible association with a 12K, FK506-binding immunophilin/protein kinase C inhibitorBiochemical and Biophysical Research Communications, 1991
- Molecular cloning and characterization of the ryanodine receptor/junctional channel complex cDNA from skeletal muscle sarcoplasmic reticulum.Proceedings of the National Academy of Sciences, 1989