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Journal Article|Research Support, N.I.H., Intramural|Research Support, Non-U.S. Gov't |
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41568 |
| issn |
0021-9258 |
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49 |
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41560-41568 |
| publicationName |
The Journal of biological chemistry |
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41560 |
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Polster A, Ohrtman JD, Beam KG, Papadopoulos S. Fluorescence Resonance Energy Transfer (FRET) Indicates That Association with the Type I Ryanodine Receptor (RyR1) Causes Reorientation of Multiple Cytoplasmic Domains of the Dihydropyridine Receptor (DHPR) α1S Subunit. Journal of Biological Chemistry. 2012 Nov;287(49):41560–8. doi: 10.1074/jbc.m112.404194. |
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| date |
2012-11-30-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| identifier |
https://doi.org/10.1074/jbc.m112.404194
https://pubmed.ncbi.nlm.nih.gov/23071115
https://pubmed.ncbi.nlm.nih.gov/PMC3510851 |
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| language |
English |
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https://www.crossref.org/
https://pubmed.ncbi.nlm.nih.gov/ |
| title |
Fluorescence resonance energy transfer (FRET) indicates that association with the type I ryanodine receptor (RyR1) causes reorientation of multiple cytoplasmic domains of the dihydropyridine receptor (DHPR) α(1S) subunit |
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