Purification, Primary Structure, and Immunological Characterization of the 26-kDa Calsequestrin Binding Protein (Junctin) from Cardiac Junctional Sarcoplasmic Reticulum
Open Access
- 1 December 1995
- journal article
- research article
- Published by Elsevier
- Vol. 270 (51) , 30787-30796
- https://doi.org/10.1074/jbc.270.51.30787
Abstract
No abstract availableKeywords
This publication has 42 references indexed in Scilit:
- Cloning and characterization of the human gene encoding aspartyl β-hydroxylaseGene, 1994
- Structural diversity of triadin in skeletal muscle and evidence of its existence in heartFEBS Letters, 1994
- The Ca2+-release channel/ryanodine receptor is localized in junctional and corbular sarcoplasmic reticulum in cardiac muscle.The Journal of cell biology, 1993
- Specific protein-protein interactions of calsequestrin with junctional sarcoplasmic reticulum of skeletal muscleBiochemical and Biophysical Research Communications, 1990
- The signal peptideThe Journal of Membrane Biology, 1990
- Characterization of the junctional face membrane from terminal cisternae of sarcoplasmic reticulum.The Journal of cell biology, 1986
- Evidence for the presence of calsequestrin in two structurally different regions of myocardial sarcoplasmic reticulum.The Journal of cell biology, 1984
- A simple method for displaying the hydropathic character of a proteinJournal of Molecular Biology, 1982
- “Western Blotting”: Electrophoretic transfer of proteins from sodium dodecyl sulfate-polyacrylamide gels to unmodified nitrocellulose and radiographic detection with antibody and radioiodinated protein AAnalytical Biochemistry, 1981
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970