{"doi":"10.1038/ncb1201-1129","title":"Nicastrin is required for Presenilin-mediated transmembrane cleavage in Drosophila","abstract":null,"journal":"Nature Cell Biology","year":2001,"id":642172,"datarank":0.7535820781269416,"base_score":5.0238805208462765,"endowment":5.0238805208462765,"self_citation_contribution":0.7535820781269416,"citation_network_contribution":0.0,"self_endowment_contribution":0.7535820781269416,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":151,"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":356019,"name":"Gary Struhl","orcid":"0000-0002-0018-604X","position":1,"is_corresponding":false},{"id":1670099,"name":"Hui-Min Chung","orcid":null,"position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"Nicastrin is required for Presenilin-mediated transmembrane cleavage in Drosophila","abstract":"The transmembrane glycoprotein Nicastrin was identified in a complex with the multipass membrane protein Presenilin. Presenilin mediates transmembrane cleavage of single-pass transmembrane proteins with short extracellular domains, including the ligand-activated form of the receptor Notch and beta-amyloid precursor protein (beta-APP). Transmembrane cleavage of Notch is essential for signal transduction, and transmembrane cleavage of beta-APP generates pathogenic amyloid peptides implicated in Alzheimer's disease. Here, we investigate the requirement for Nicastrin in Presenilin-mediated transmembrane cleavage. We show that, in Drosophila, loss of Nicastrin activity blocks the accumulation of Presenilin associated with the apical plasma membrane, abolishes Presenilin-dependent cleavage of the transmembrane domains of Notch and beta-APP, and abrogates Notch signal transduction.","is_dataset_classified":null,"base_score":0.0,"endowment":0.0,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"11781576","pmcid":null,"openalex_id":null,"authors":[],"funders":[],"total_grants":0,"fwci":null,"citation_percentile":null,"influential_citations":0,"citation_trend":[],"oa_status":"closed","license":"http://www.springer.com/tdm","oa_locations":[{"url":"http://www.nature.com/articles/ncb1201-1129.pdf","host_type":"publisher"},{"url":"http://www.nature.com/articles/ncb1201-1129","host_type":"publisher"}],"fields_of_study":[],"mesh_terms":["Cell Membrane","Animals","Drosophila","Amyloid beta-Protein Precursor","Membrane Glycoproteins","Drosophila Proteins","Membrane Proteins","Signal Transduction","Mutation","Receptors, Notch","Amyloid Precursor Protein Secretases","Presenilin-1"],"keywords":[],"sdg_mappings":[],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[],"source":"live","citation_network_status":"fetched"},"created_at":"2026-08-07T21:47:16.015806Z","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":[]}