Identification of Triadin 1 as the Predominant Triadin Isoform Expressed in Mammalian Myocardium
Open Access
- 1 October 1999
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 274 (40) , 28660-28668
- https://doi.org/10.1074/jbc.274.40.28660
Abstract
No abstract availableKeywords
This publication has 21 references indexed in Scilit:
- A new scorpion toxin (BmK-PL) stimulates Ca2+-release channel activity of the skeletal-muscle ryanodine receptor by an indirect mechanismBiochemical Journal, 1999
- Dual Regulation of the Skeletal Muscle Ryanodine Receptor by Triadin and CalsequestrinBiochemistry, 1998
- Regulation of Ca2+ signaling in transgenic mouse cardiac myocytes overexpressing calsequestrin.Journal of Clinical Investigation, 1998
- Disulfide bonds, N-glycosylation and transmembrane topology of skeletal muscle triadinBiochemistry, 1995
- Immunolocalization of sarcolemmal dihydropyridine receptor and sarcoplasmic reticular triadin and ryanodine receptor in rabbit ventricle and atrium.The Journal of cell biology, 1995
- Association of Triadin with the Ryanodine Receptor and Calsequestrin in the Lumen of the Sarcoplasmic ReticulumJournal of Biological Chemistry, 1995
- Functional Reconstitution of Recombinant Phospholamban with Rabbit Skeletal Ca2+-ATPasePublished by Elsevier ,1995
- Localization and partial characterization of the oligomeric disulfide-linked molecular weight 95,000 protein (triadin) which binds the ryanodine and dihydropyridine receptors in skeletal muscle triadic vesiclesBiochemistry, 1991
- Isolation of a terminal cisterna protein which may link the dihydropyridine receptor to the junctional foot protein in skeletal muscleBiochemistry, 1990
- Biochemistry and Biophysics of Excitation-Contraction CouplingAnnual Review of Biophysics, 1989