{"doi":"10.1007/978-3-030-67696-4_3","title":"The Role of Endoplasmic Reticulum Chaperones in Protein Folding and Quality Control","abstract":null,"journal":"Progress in Molecular and Subcellular Biology","year":2021,"id":599081,"datarank":0.5289540786924243,"base_score":3.5263605246161616,"endowment":3.5263605246161616,"self_citation_contribution":0.5289540786924243,"citation_network_contribution":0.0,"self_endowment_contribution":0.5289540786924243,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":33,"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":321954,"name":"Nathan P. Canniff","orcid":null,"position":1,"is_corresponding":false},{"id":320511,"name":"Kevin P. Guay","orcid":"0000-0002-3468-942X","position":2,"is_corresponding":false},{"id":320512,"name":"Daniel N. Hebert","orcid":"0000-0003-1537-4446","position":3,"is_corresponding":false},{"id":320510,"name":"Benjamin M. Adams","orcid":"0000-0002-9980-5321","position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"The Role of Endoplasmic Reticulum Chaperones in Protein Folding and Quality Control","abstract":"Molecular chaperones assist the folding of nascent chains in the cell. Chaperones also aid in quality control decisions as persistent chaperone binding can help to sort terminal misfolded proteins for degradation. There are two major molecular chaperone families in the endoplasmic reticulum (ER) that assist proteins in reaching their native structure and evaluating the fidelity of the maturation process. The ER Hsp70 chaperone, BiP, supports adenine nucleotide-regulated binding to non-native proteins that possess exposed hydrophobic regions. In contrast, the carbohydrate-dependent chaperone system involving the membrane protein calnexin and its soluble paralogue calreticulin recognize a specific glycoform of an exposed hydrophilic protein modification for which the composition is controlled by a series of glycosidases and transferases. Here, we compare and contrast the properties, mechanisms of action and functions of these different chaperones systems that work in parallel, as well as together, to assist a large variety of substrates that traverse the eukaryotic secretory pathway.","is_dataset_classified":null,"base_score":3.4965075614664802,"endowment":3.4965075614664802,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"34050861","pmcid":"PMC9185992","openalex_id":"https://openalex.org/W3165347333","authors":[],"funders":[{"funder_name":"NIGMS NIH HHS","grant_id":"T32 GM008515","title":null},{"funder_name":"NIGMS NIH HHS","grant_id":"R01 GM086874","title":null}],"total_grants":2,"fwci":11.4387,"citation_percentile":0.98859316,"influential_citations":0,"citation_trend":[{"year":2021,"count":1},{"year":2022,"count":5},{"year":2023,"count":3},{"year":2024,"count":9},{"year":2025,"count":11},{"year":2026,"count":3}],"oa_status":"green","license":"https://www.springer.com/tdm","oa_locations":[{"url":"https://www.ncbi.nlm.nih.gov/pmc/articles/9185992","host_type":"repository"},{"url":"https://www.ncbi.nlm.nih.gov/pmc/articles/9185992","host_type":"repository"},{"url":"https://link.springer.com/content/pdf/10.1007/978-3-030-67696-4_3","host_type":"publisher"},{"url":"https://doi.org/10.1007/978-3-030-67696-4_3","host_type":"book series"},{"url":"https://pubmed.ncbi.nlm.nih.gov/34050861","host_type":"repository"}],"fields_of_study":["Endoplasmic Reticulum Stress and Disease","Heat shock proteins research","Iron Metabolism and Disorders","Calnexin","Endoplasmic Reticulum","Molecular Chaperones","Protein Folding","Quality Control"],"mesh_terms":["Endoplasmic Reticulum","Quality Control","Protein Folding","Molecular Chaperones","Calnexin"],"keywords":["Calnexin","Endoplasmic reticulum","Chaperone (clinical)","Protein folding","Co-chaperone","Calreticulin","Biology","Foldase","Chemical chaperone","Cell biology","Biochemistry","Translocon","Secretory pathway","Protein targeting","Unfolded protein response","Membrane protein","Hsp70","Heat shock protein","Membrane","Quality control","Molecular chaperones"],"sdg_mappings":[{"sdg_number":0,"sdg_label":"Life in Land"}],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[{"name":"pdb"}],"source":"live","citation_network_status":"fetched"},"created_at":"2026-07-28T18:00:25.403998Z","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":[]}