{"doi":"10.1021/bi001049k","title":"Regulatory Role of Phospholamban in the Efficiency of Cardiac Sarcoplasmic Reticulum Ca<sup>2+</sup> Transport","abstract":null,"journal":"Biochemistry","year":2000,"id":638274,"datarank":0.5495342469194471,"base_score":3.6635616461296463,"endowment":3.6635616461296463,"self_citation_contribution":0.5495342469194471,"citation_network_contribution":0.0,"self_endowment_contribution":0.5495342469194471,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":38,"citer_count":0,"citers_with_citation_signal":0,"citers_with_endowment":0,"datacite_reuse_total":0,"is_dataset":false,"is_dataset_confidence":null,"is_data_producer":false,"deposit_databanks":null,"is_oa":false,"file_count":0,"downloads":0,"has_version_chain":false,"published_date":null,"fair_score":null,"fair_percentile":null,"algorithm_id":"datarank_citation_only_1hop_v6","ranking_scope":"data_only","authors":[{"id":1657710,"name":"Carola Tilgmann","orcid":null,"position":1,"is_corresponding":false},{"id":914649,"name":"Thomas R. Shannon","orcid":"0009-0002-5806-5037","position":2,"is_corresponding":false},{"id":229037,"name":"Donald M. Bers","orcid":"0000-0002-2237-9483","position":3,"is_corresponding":false},{"id":408804,"name":"Evangelia G. Kranias","orcid":"0000-0002-4621-6179","position":4,"is_corresponding":false},{"id":1657709,"name":"Konrad Frank","orcid":null,"position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"Regulatory Role of Phospholamban in the Efficiency of Cardiac Sarcoplasmic Reticulum Ca<sup>2+</sup> Transport","abstract":"Phospholamban is an inhibitor of the sarcoplasmic reticulum Ca(2+) transport apparent affinity for Ca(2+) in cardiac muscle. This inhibitory effect of phospholamban can be relieved through its phosphorylation or ablation. To better characterize the regulatory mechanism of phospholamban, we examined the initial rates of Ca(2+)-uptake and Ca(2+)-ATPase activity under identical conditions, using sarcoplasmic reticulum-enriched preparations from phospholamban-deficient and wild-type hearts. The apparent coupling ratio, calculated by dividing the initial rates of Ca(2+) transport by ATP hydrolysis, appeared to increase with increasing [Ca(2+)] in wild-type hearts. However, in the phospholamban-deficient hearts, this ratio was constant, and it was similar to the value obtained at high [Ca(2+)] in wild-type hearts. Phosphorylation of phospholamban by the catalytic subunit of protein kinase A in wild-type sarcoplasmic reticulum also resulted in a constant value of the apparent ratio of Ca(2+) transported per ATP hydrolyzed, which was similar to that present in phospholamban-deficient hearts. Thus, the inhibitory effects of dephosphorylated phospholamban involve decreases in the apparent affinity of sarcoplasmic reticulum Ca(2+) transport for Ca(2+) and the efficiency of this transport system at low [Ca(2+)], both leading to prolonged relaxation in myocytes.","is_dataset_classified":null,"base_score":3.6635616461296463,"endowment":3.6635616461296463,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"11087366","pmcid":null,"openalex_id":"https://openalex.org/W2070631962","authors":[],"funders":[{"funder_name":"NHLBI NIH HHS","grant_id":"HL-52318","title":null},{"funder_name":"NCRR NIH HHS","grant_id":"P40RR12358","title":null},{"funder_name":"NHLBI NIH HHS","grant_id":"HL-26057","title":null}],"total_grants":3,"fwci":1.7352,"citation_percentile":0.8585076,"influential_citations":0,"citation_trend":[{"year":2013,"count":5},{"year":2014,"count":1},{"year":2015,"count":2},{"year":2018,"count":1},{"year":2019,"count":1},{"year":2020,"count":1}],"oa_status":"closed","license":null,"oa_locations":[{"url":"https://doi.org/10.1021/bi001049k","host_type":"journal"},{"url":"https://pubmed.ncbi.nlm.nih.gov/11087366","host_type":"repository"},{"url":"https://lup.lub.lu.se/record/b1d4e674-9b77-4425-a496-40193a14b5f7","host_type":"repository"}],"fields_of_study":["Cardiac electrophysiology and arrhythmias","Ion channel regulation and function","Cardiomyopathy and Myosin Studies"],"mesh_terms":["Phospholamban","Calcium-Transporting ATPases","Adenosine Triphosphate","Animals","Biological Transport","Calcium","Calcium-Binding Proteins","Enzyme Activation","Hydrolysis","Intracellular Membranes","Microsomes","Myocardium","Phosphorylation","Ruthenium Red","Sarcoplasmic Reticulum","Calcium Channels","Cyclic AMP-Dependent Protein Kinases","Thapsigargin","Catalytic Domain","Mice"],"keywords":["Phospholamban","Endoplasmic reticulum","Chemistry","Phosphorylation","Myocyte","Biophysics","ATP hydrolysis","Internal medicine","ATPase","Endocrinology","Biochemistry","Biology","Enzyme","Medicine"],"sdg_mappings":[],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[],"source":"live","citation_network_status":"fetched"},"created_at":"2026-08-06T20:24:13.886240Z","pmid":null,"pmcid":null,"fwci":null,"citation_percentile":null,"influential_citations":0,"oa_status":null,"license":null,"views":0,"total_file_size_bytes":0,"version_count":0,"fair_f":null,"fair_a":null,"fair_i":null,"fair_r":null,"fair_zscore":null,"fair_rationale":null,"fair_model":null,"fair_agent_version":null,"fair_fulltext_source":null,"fair_has_llm":null,"fair_computed_at":null,"clinical_trials":[],"software_tools":[],"db_accessions":[],"linked_datasets":[],"topics":[]}