{"doi":"10.1139/o98-091","title":"Calreticulin, a multifunctional Ca<sup>2+</sup> binding chaperone of the endoplasmic reticulum","abstract":"<jats:p> Calreticulin is a ubiquitous endoplasmic reticulum Ca<jats:sup>2+</jats:sup> binding chaperone. The protein has been implicated in a variety of diverse functions. Calreticulin is a lectin-like chaperone and, together with calnexin, it plays an important role in quality control during protein synthesis, folding, and posttranslational modification. Calreticulin binds Ca<jats:sup>2+</jats:sup> and affects cellular Ca<jats:sup>2+</jats:sup> homeostasis. The protein increases the Ca<jats:sup>2+</jats:sup> storage capacity of the endoplasmic reticulum and modulates the function of endoplasmic reticulum Ca<jats:sup>2+</jats:sup>-ATPase. Calreticulin also plays a role in the control of cell adhesion and steroid-sensitive gene expression. Recently, the protein has been identified and characterized in higher plants but its precise role in plant cells awaits further investigation.Key words: calreticulin, endoplasmic reticulum, chaperone, Ca<jats:sup>2+</jats:sup> binding protein. </jats:p>","journal":"Biochemistry and Cell Biology","year":1998,"id":589059,"datarank":2.1279101148416855,"base_score":3.784189633918261,"endowment":3.784189633918261,"self_citation_contribution":0.5676284450877392,"citation_network_contribution":1.560281669753946,"self_endowment_contribution":0.5676284450877392,"citer_contribution":1.560281669753946,"corpus_percentile":null,"corpus_rank":null,"citation_count":43,"citer_count":36,"citers_with_citation_signal":35,"citers_with_endowment":35,"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":1507070,"name":"Paola Mariani","orcid":null,"position":1,"is_corresponding":false},{"id":188517,"name":"Michal Opas","orcid":null,"position":2,"is_corresponding":false},{"id":163711,"name":"Marek Michalak","orcid":null,"position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"Calreticulin, a multifunctional Ca<sup>2+</sup> binding chaperone of the endoplasmic reticulum","abstract":"<jats:p> Calreticulin is a ubiquitous endoplasmic reticulum Ca<jats:sup>2+</jats:sup> binding chaperone. The protein has been implicated in a variety of diverse functions. Calreticulin is a lectin-like chaperone and, together with calnexin, it plays an important role in quality control during protein synthesis, folding, and posttranslational modification. Calreticulin binds Ca<jats:sup>2+</jats:sup> and affects cellular Ca<jats:sup>2+</jats:sup> homeostasis. The protein increases the Ca<jats:sup>2+</jats:sup> storage capacity of the endoplasmic reticulum and modulates the function of endoplasmic reticulum Ca<jats:sup>2+</jats:sup>-ATPase. Calreticulin also plays a role in the control of cell adhesion and steroid-sensitive gene expression. Recently, the protein has been identified and characterized in higher plants but its precise role in plant cells awaits further investigation.Key words: calreticulin, endoplasmic reticulum, chaperone, Ca<jats:sup>2+</jats:sup> binding protein. </jats:p>","is_dataset_classified":null,"base_score":3.6888794541139363,"endowment":3.6888794541139363,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"26657633","pmcid":null,"openalex_id":"https://openalex.org/W4253673657","authors":[],"funders":[],"total_grants":0,"fwci":0.4667,"citation_percentile":0.65261236,"influential_citations":0,"citation_trend":[{"year":2012,"count":1},{"year":2013,"count":1},{"year":2014,"count":1},{"year":2015,"count":2},{"year":2018,"count":1},{"year":2019,"count":2},{"year":2020,"count":3},{"year":2021,"count":2},{"year":2022,"count":2},{"year":2024,"count":2}],"oa_status":"closed","license":"http://www.nrcresearchpress.com/page/about/CorporateTextAndDataMining","oa_locations":[{"url":"https://cdnsciencepub.com/doi/pdf/10.1139/o98-091","host_type":"publisher"},{"url":"https://doi.org/10.1139/o98-091","host_type":"journal"}],"fields_of_study":["Endoplasmic Reticulum Stress and Disease"],"mesh_terms":[],"keywords":["Calreticulin","Endoplasmic reticulum","Calnexin","Chaperone (clinical)","Cell biology","STIM1","Biology"],"sdg_mappings":[],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[],"source":"live","citation_network_status":"fetched"},"created_at":"2026-07-23T12:24:49.026211Z","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":[]}