{"doi":"10.3390/ijms20204976","title":"Hsp90 and Its Co-Chaperones in Neurodegenerative Diseases","abstract":"<jats:p>Proper folding is crucial for proteins to achieve functional activity in the cell. However, it often occurs that proteins are improperly folded (misfolded) and form aggregates, which are the main hallmark of many diseases including cancers, neurodegenerative diseases and many others. Proteins that assist other proteins in proper folding into three-dimensional structures are chaperones and co-chaperones. The key role of chaperones/co-chaperones is to prevent protein aggregation, especially under stress. An imbalance between chaperone/co-chaperone levels has been documented in neurons, and suggested to contribute to protein misfolding. An essential protein and a major regulator of protein folding in all eukaryotic cells is the heat shock protein 90 (Hsp90). The function of Hsp90 is tightly regulated by many factors, including co-chaperones. In this review we summarize results regarding the role of Hsp90 and its co-chaperones in neurodegenerative disorders such as Alzheimer’s disease (AD), Parkinson’s disease (PD), Huntington’s disease (HD), and prionopathies.</jats:p>","journal":"International Journal of Molecular Sciences","year":2019,"id":24995,"datarank":3.0487472627336665,"base_score":4.804021044733257,"endowment":4.804021044733257,"self_citation_contribution":0.7206031567099886,"citation_network_contribution":2.328144106023678,"self_endowment_contribution":0.7206031567099886,"citer_contribution":2.328144106023678,"corpus_percentile":null,"corpus_rank":null,"citation_count":121,"citer_count":117,"citers_with_citation_signal":90,"citers_with_endowment":90,"datacite_reuse_total":2,"is_dataset":false,"is_dataset_confidence":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":148331,"name":"Paweł Bieganowski","orcid":"0000-0002-1169-4517","position":1,"is_corresponding":false},{"id":148332,"name":"Anna Filipek","orcid":"0000-0001-9484-9555","position":2,"is_corresponding":false},{"id":148330,"name":"Anastasiia Bohush","orcid":null,"position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"base_score":4.804021044733257,"endowment":4.804021044733257,"datacite_reuse_total":2,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"31600883","pmcid":"PMC6834326","openalex_id":"https://openalex.org/W2980049403","authors":[],"funders":[{"funder_name":"Narodowe Centrum Nauki","grant_id":"2018/29/B/NZ4/01384; 2016/23/B/NZ6/02536","title":null},{"funder_name":"Marie Sklodowska-Curie and Polish Ministry of Science and Higher Education","grant_id":"665735 (Bio4Med), 3548/H2020/COFUND/2016/2","title":null},{"funder_name":"European Commission","grant_id":"665735","title":"International Doctoral Programme in Biological Bases of Human Diseases"}],"total_grants":3,"fwci":3.8466,"citation_percentile":0.94553601,"influential_citations":3,"citation_trend":[{"year":2019,"count":2},{"year":2020,"count":11},{"year":2021,"count":23},{"year":2022,"count":9},{"year":2023,"count":21},{"year":2024,"count":25},{"year":2025,"count":20},{"year":2026,"count":10}],"oa_status":"gold","license":"cc-by","oa_locations":[{"url":"https://www.mdpi.com/1422-0067/20/20/4976/pdf","host_type":"journal"},{"url":"https://www.mdpi.com/1422-0067/20/20/4976/pdf","host_type":"GOLD"},{"url":"https://www.mdpi.com/1422-0067/20/20/4976/pdf","host_type":"publisher"},{"url":"https://doi.org/10.3390/ijms20204976","host_type":"journal"},{"url":"https://pubmed.ncbi.nlm.nih.gov/31600883","host_type":"repository"},{"url":"https://doaj.org/article/5bc355f339c14ea9a143dc1e80032405","host_type":"repository"},{"url":"https://www.ncbi.nlm.nih.gov/pmc/articles/6834326","host_type":"repository"},{"url":"http://dx.doi.org/10.3390/ijms20204976","host_type":"repository"},{"url":"https://pure.au.dk/portal/en/publications/29a69960-2d30-487e-a0a7-68f643f5d97e","host_type":""},{"url":"https://europepmc.org/articles/PMC6834326","host_type":"Europe_PMC"},{"url":"https://europepmc.org/articles/PMC6834326?pdf=render","host_type":"Europe_PMC"},{"url":"https://dx.doi.org/10.3390/ijms20204976","host_type":""}],"fields_of_study":["Heat shock proteins research","Protein Structure and Dynamics","Enzyme Structure and Function","Medicine","Biology","0301 basic medicine","0303 health sciences","03 medical and health sciences","Animals","Biomarkers","Disease Susceptibility","Gene Expression Regulation","HSP90 Heat-Shock Proteins","Humans","Molecular Chaperones","Neurodegenerative Diseases","Signal Transduction"],"mesh_terms":["Animals","Disease Susceptibility","Gene Expression Regulation","Humans","Signal Transduction","Biomarkers","Molecular Chaperones","HSP90 Heat-Shock Proteins","Neurodegenerative Diseases"],"keywords":["Co-chaperone","Protein folding","Chaperone (clinical)","Hsp90","Heat shock protein","Protein aggregation","Neurodegeneration","Cell biology","Biology","Chemical chaperone","Disease","Regulator","Chemistry","Computational biology","Biochemistry","Unfolded protein response","Medicine","Endoplasmic reticulum","Gene","Alzheimer’s disease","Parkinson’s Disease","Huntington’s Disease","Hsp90 Inhibitors","Co-chaperones","Prionopathy","Neurodegenerative Diseases","Molecular Chaperones/genetics","Neurodegenerative Diseases/diagnosis","Review","Gene Expression Regulation","HSP90 Heat-Shock Proteins/genetics","Animals","Humans","Disease Susceptibility","HSP90 Heat-Shock Proteins","Biomarkers","Molecular Chaperones","Signal Transduction"],"sdg_mappings":[{"sdg_number":3,"sdg_label":"3. 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