{"doi":"10.1016/j.jmb.2018.04.022","title":"Yeast Prions Compared to Functional Prions and Amyloids","abstract":null,"journal":"Journal of Molecular Biology","year":2018,"id":686982,"datarank":0.5533319181170905,"base_score":3.6888794541139363,"endowment":3.6888794541139363,"self_citation_contribution":0.5533319181170905,"citation_network_contribution":0.0,"self_endowment_contribution":0.5533319181170905,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":39,"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":776912,"name":"Herman K. Edskes","orcid":"0000-0002-2708-2961","position":1,"is_corresponding":false},{"id":370848,"name":"Moonil Son","orcid":"0000-0002-1325-2085","position":2,"is_corresponding":false},{"id":776914,"name":"Evgeny E. Bezsonov","orcid":"0000-0002-9382-8338","position":3,"is_corresponding":false},{"id":777572,"name":"Morgan DeWilde","orcid":null,"position":4,"is_corresponding":false},{"id":1794716,"name":"Mathieu Ducatez","orcid":null,"position":5,"is_corresponding":false},{"id":370849,"name":"Reed B. Wickner","orcid":"0000-0003-0273-8247","position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"Yeast Prions Compared to Functional Prions and Amyloids","abstract":"Saccharomyces cerevisiae is an occasional host to an array of prions, most based on self-propagating, self-templating amyloid filaments of a normally soluble protein. [URE3] is a prion of Ure2p, a regulator of nitrogen catabolism, while [PSI+] is a prion of Sup35p, a subunit of the translation termination factor Sup35p. In contrast to the functional prions, [Het-s] of Podospora anserina and [BETA] of yeast, the amyloid-based yeast prions are rare in wild strains, arise sporadically, have an array of prion variants for a single prion protein sequence, have a folded in-register parallel β-sheet amyloid architecture, are detrimental to their hosts, arouse a stress response in the host, and are subject to curing by various host anti-prion systems. These characteristics allow a logical basis for distinction between functional amyloids/prions and prion diseases. These infectious yeast amyloidoses are outstanding models for the many common human amyloid-based diseases that are increasingly found to have some infectious characteristics.","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":"29698650","pmcid":null,"openalex_id":"https://openalex.org/W2802046579","authors":[],"funders":[{"funder_name":"Intramural Program of the National Institute of Diabetes and Digestive and Kidney Diseases of the National Institutes of Health","grant_id":"DK024950","title":null}],"total_grants":1,"fwci":1.9774,"citation_percentile":0.87127516,"influential_citations":0,"citation_trend":[{"year":2018,"count":2},{"year":2019,"count":8},{"year":2020,"count":7},{"year":2021,"count":7},{"year":2022,"count":1},{"year":2023,"count":4},{"year":2024,"count":4},{"year":2025,"count":4},{"year":2026,"count":2}],"oa_status":"closed","license":"https://www.elsevier.com/tdm/userlicense/1.0/","oa_locations":[{"url":"https://api.elsevier.com/content/article/PII:S0022283618302754?httpAccept=text/xml","host_type":"publisher"},{"url":"https://api.elsevier.com/content/article/PII:S0022283618302754?httpAccept=text/plain","host_type":"publisher"},{"url":"https://doi.org/10.1016/j.jmb.2018.04.022","host_type":"journal"},{"url":"https://pubmed.ncbi.nlm.nih.gov/29698650","host_type":"repository"}],"fields_of_study":["Prion Diseases and Protein Misfolding","Neurological diseases and metabolism","Trace Elements in Health","Amyloid","Amyloidogenic Proteins","Biological Evolution","Fungal Proteins","Humans","Prions","Protein Binding","Protein Interaction Domains and Motifs","Structure-Activity Relationship"],"mesh_terms":["Amyloid","Biological Evolution","Fungal Proteins","Humans","Prions","Protein Binding","Structure-Activity Relationship","Protein Interaction Domains and Motifs","Amyloidogenic Proteins"],"keywords":["Fungal prion","Yeast","Amyloid (mycology)","Saccharomyces cerevisiae","Podospora anserina","Biology","Protein subunit","Prion protein","Protein aggregation","Protein structure","Biochemistry","Cell biology","Mutant","Gene","Inositol Polyphosphates","Upf, Btn2p, Cur1p, Hsp104, Ssb1, Siw14","Amyloid Of Sup35 Or Ure2","Anti-prion Systems","Folded In-register Parallel Beta Sheets"],"sdg_mappings":[{"sdg_number":0,"sdg_label":"Life in Land"}],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[],"source":"live","citation_network_status":"fetched"},"created_at":"2026-08-18T21:01:42.670354Z","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":[]}