| http://purl.uniprot.org/citations/21454501 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/21454501 | http://www.w3.org/2000/01/rdf-schema#comment | "The ryanodine receptor type 1 (RyR1) is a homotetrameric Ca(2+) release channel located in the sarcoplasmic reticulum of skeletal muscle where it plays a role in the initiation of skeletal muscle contraction. A soluble, 6×-histidine affinity-tagged cytosolic fragment of RyR1 (amino acids 1-4243) was expressed in HEK-293 cells, and metal affinity chromatography under native conditions was used to purify the peptide together with interacting proteins. When analyzed by gel-free liquid chromatography mass spectrometry (LC-MS), 703 proteins were identified under all conditions. This group of proteins was filtered to identify putative RyR interacting proteins by removing those proteins found in only 1 RyR purification and proteins for which average spectral counts were enriched by less than 4-fold over control values. This resulted in 49 potential RyR1 interacting proteins, and 4 were selected for additional interaction studies: calcium homeostasis endoplasmic reticulum protein (CHERP), endoplasmic reticulum-Golgi intermediate compartment 53-kDa protein (LMAN1), T-complex protein, and phosphorylase kinase. Western blotting showed that only CHERP co-purified with affinity-tagged RyR1 and was eluted with imidazole. Immunofluorescence showed that endogenous CHERP co-localizes with endogenous RyR1 in the sarcoplasmic reticulum of rat soleus muscle. A combination of overexpression of RyR1 in HEK-293 cells with siRNA-mediated suppression of CHERP showed that CHERP affects Ca(2+) release from the ER via RyR1. Thus, we propose that CHERP is an RyR1 interacting protein that may be involved in the regulation of excitation-contraction coupling."xsd:string |
| http://purl.uniprot.org/citations/21454501 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m110.197186"xsd:string |
| http://purl.uniprot.org/citations/21454501 | http://purl.uniprot.org/core/author | "Sharma P."xsd:string |
| http://purl.uniprot.org/citations/21454501 | http://purl.uniprot.org/core/author | "Gramolini A.O."xsd:string |
| http://purl.uniprot.org/citations/21454501 | http://purl.uniprot.org/core/author | "MacLennan D.H."xsd:string |
| http://purl.uniprot.org/citations/21454501 | http://purl.uniprot.org/core/author | "Kislinger T."xsd:string |
| http://purl.uniprot.org/citations/21454501 | http://purl.uniprot.org/core/author | "Ignatchenko A."xsd:string |
| http://purl.uniprot.org/citations/21454501 | http://purl.uniprot.org/core/author | "Ryan T."xsd:string |
| http://purl.uniprot.org/citations/21454501 | http://purl.uniprot.org/core/date | "2011"xsd:gYear |
| http://purl.uniprot.org/citations/21454501 | http://purl.uniprot.org/core/name | "J Biol Chem"xsd:string |
| http://purl.uniprot.org/citations/21454501 | http://purl.uniprot.org/core/pages | "17060-17068"xsd:string |
| http://purl.uniprot.org/citations/21454501 | http://purl.uniprot.org/core/title | "Identification of novel ryanodine receptor 1 (RyR1) protein interaction with calcium homeostasis endoplasmic reticulum protein (CHERP)."xsd:string |
| http://purl.uniprot.org/citations/21454501 | http://purl.uniprot.org/core/volume | "286"xsd:string |
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