{"doi":"10.1016/s1672-0229(03)01002-7","title":"Advances in the Study of SR Protein Family","abstract":"<jats:title>Abstract</jats:title>\n               <jats:p>The name of SR proteins is derived from their typical RS domain that is rich in serine (Ser, S) and arginine (Arg, R). They are conserved in evolution. Up to now, 10 members of the SR protein family have been identified in humans. SR proteins contain one or two RNA binding motifs aside from the RS domain, and also possess special biochemical and immunological features. As to the functions of SR proteins, they facilitate the recruitment of the components of splicesome via protein-protein interaction to prompt the assembly of early splicesome; while in alternative splicing, tissue-specifically expressed SR protein along with the relative ratio of SR protein and heterogeneous nuclear ribonucleoprotein (hnRNP) is composed of two main regulative mechanisms for alternative splicing. Almost all of the biochemical functions are regulated by reversible phosphorylation.</jats:p>","journal":"Genomics, Proteomics &amp; Bioinformatics","year":2003,"id":34445,"datarank":0.8056215670592382,"base_score":2.70805020110221,"endowment":2.70805020110221,"self_citation_contribution":0.40620753016533157,"citation_network_contribution":0.3994140368939066,"self_endowment_contribution":0.40620753016533157,"citer_contribution":0.3994140368939066,"corpus_percentile":null,"corpus_rank":null,"citation_count":14,"citer_count":14,"citers_with_citation_signal":14,"citers_with_endowment":14,"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":148297,"name":"Fuchu He","orcid":null,"position":1,"is_corresponding":false},{"id":178367,"name":"Xiaoyun Ma","orcid":null,"position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"base_score":2.70805020110221,"endowment":2.70805020110221,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"15626328","pmcid":"PMC5172405","openalex_id":"https://openalex.org/W2417100554","authors":[],"funders":[{"funder_name":"National Natural Science Foundation of China","grant_id":"30070285","title":null}],"total_grants":1,"fwci":0.1145,"citation_percentile":0.49873791,"influential_citations":1,"citation_trend":[{"year":2013,"count":1},{"year":2015,"count":1},{"year":2017,"count":1},{"year":2021,"count":1},{"year":2022,"count":3},{"year":2024,"count":3},{"year":2025,"count":1},{"year":2026,"count":1}],"oa_status":"gold","license":"cc-by","oa_locations":[{"url":"https://doi.org/10.1016/s1672-0229(03)01002-7","host_type":"journal"},{"url":"https://doi.org/10.1016/s1672-0229(03)01002-7","host_type":"GOLD"},{"url":"https://doi.org/10.1016/s1672-0229(03)01002-7","host_type":"publisher"},{"url":"https://api.elsevier.com/content/article/PII:S1672022903010027?httpAccept=text/xml","host_type":"publisher"},{"url":"https://api.elsevier.com/content/article/PII:S1672022903010027?httpAccept=text/plain","host_type":"publisher"},{"url":"https://academic.oup.com/gpb/article-pdf/1/1/2/57482014/gpb_1_1_2.pdf","host_type":"publisher"},{"url":"https://pubmed.ncbi.nlm.nih.gov/15626328","host_type":"repository"},{"url":"https://www.ncbi.nlm.nih.gov/pmc/articles/5172405","host_type":"repository"},{"url":"https://europepmc.org/articles/PMC5172405","host_type":"Europe_PMC"},{"url":"https://europepmc.org/articles/PMC5172405?pdf=render","host_type":"Europe_PMC"}],"fields_of_study":["RNA Research and Splicing","RNA modifications and cancer","RNA and protein synthesis mechanisms","Biology","Medicine","Alternative Splicing","Amino Acid Motifs","Evolution, Molecular","Heterogeneous-Nuclear Ribonucleoproteins","Humans","Phosphorylation","Protein Binding","Protein Conformation","Protein Structure, Tertiary","Proteomics","RNA","Spliceosomes"],"mesh_terms":["Humans","Phosphorylation","Protein Binding","Protein Conformation","RNA","Spliceosomes","Alternative Splicing","Protein Structure, Tertiary","Evolution, Molecular","Amino Acid Motifs","Heterogeneous-Nuclear Ribonucleoproteins","Proteomics"],"keywords":["Computational biology","Computer science","Biology"],"sdg_mappings":[],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[],"source":"live","citation_network_status":"fetched"},"created_at":"2026-06-09T18:42:11.388494Z","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":[]}