FK-binding Protein Is Associated with the Ryanodine Receptor of Skeletal Muscle in Vertebrate Animals
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference28 articles.
1. Chemistry and Biology of the Immunophilins and Their Immunosuppressive Ligands
2. The cytosolic-binding protein for the immunosuppressant FK-506 is both a ubiquitous and highly conserved peptidyl-prolyl cis-trans isomerase.
3. FK506 binding protein associated with the calcium release channel (ryanodine receptor).
4. The calcium release channel of sarcoplasmic reticulum is modulated by FK-506-binding protein. Dissociation and reconstitution of FKBP-12 to the calcium release channel of skeletal muscle sarcoplasmic reticulum.
5. The calcium release channel of sarcoplasmic reticulum is modulated by FK-506 binding protein: Effect of FKBP-12 on single channel activity of the skeletal muscle ryanodine receptor
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1. FKBP12 binds to the cardiac ryanodine receptor with negative cooperativity: implications for heart muscle physiology in health and disease;Philosophical Transactions of the Royal Society B: Biological Sciences;2023-05
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3. Ryanodine receptor dysfunction in human disorders;Biochimica et Biophysica Acta (BBA) - Molecular Cell Research;2018-11
4. Ryanodine receptor and FK506 binding protein 1 in the Atlantic killifish (Fundulus heteroclitus): A phylogenetic and population-based comparison;Aquatic Toxicology;2017-11
5. PEP-1-FK506BP12 inhibits matrix metalloproteinase expression in human articular chondrocytes and in a mouse carrageenan-induced arthritis model;BMB Reports;2015-07-31
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