Transmembrane orientation of the N-terminal and C-terminal ends of the ryanodine receptor in the sarcoplasmic reticulum of rabbit skeletal muscle
- 15 March 1994
- journal article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 298 (3) , 743-749
- https://doi.org/10.1042/bj2980743
Abstract
No abstract availableKeywords
This publication has 34 references indexed in Scilit:
- Primary structure and expression from complementary DNA of skeletal muscle ryanodine receptorNature, 1989
- TOPOGRAPHY OF MEMBRANE PROTEINSAnnual Review of Biochemistry, 1989
- Evidence for the cytoplasmic location of the N- and C-terminal segments of sarcoplasmic reticulum (Ca2+Mg2+)-ATPaseBiochemical and Biophysical Research Communications, 1989
- Three-dimensional architecture of the calcium channel/foot structure of sarcoplasmic reticulumNature, 1989
- Orientation of the N-terminal region of the membrane-bound ADP/ATP carrier protein explored by antipeptide antibodies and an arginine-specific endoprotease. Evidence that the accessibility of the N-terminal residues depends on the conformational state of the carrierBiochemistry, 1989
- Structural and Functional Correlation of the Trypsin-digested Ca2+ Release Channel of Skeletal Muscle Sarcoplasmic ReticulumJournal of Biological Chemistry, 1989
- Structural evidence for direct interaction between the molecular components of the transverse tubule/sarcoplasmic reticulum junction in skeletal muscle.The Journal of cell biology, 1988
- Trypsin destruction of the high affinity ryanodine binding sites of the junctional sarcoplasmic reticulum.Journal of Biological Chemistry, 1988
- Purification and reconstitution of the calcium release channel from skeletal muscleNature, 1988
- Purified ryanodine receptor from skeletal muscle sarcoplasmic reticulum is the Ca2+-permeable pore of the calcium release channel.Journal of Biological Chemistry, 1987