{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,24]],"date-time":"2026-10-24T00:27:42Z","timestamp":1792801662989,"version":"4.5.0"},"reference-count":333,"publisher":"MDPI AG","issue":"1","license":[{"start":{"date-parts":[[2018,1,22]],"date-time":"2018-01-22T00:00:00Z","timestamp":1516579200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["IJMS"],"abstract":"<jats:p>Neurodegenerative diseases (NDDs) such as Alzheimer\u2019s disease, Parkinson\u2019s disease and Huntington\u2019s disease (HD), amyotrophic lateral sclerosis, and prion diseases are all characterized by the accumulation of protein aggregates (amyloids) into inclusions and\/or plaques. The ubiquitous presence of amyloids in NDDs suggests the involvement of disturbed protein homeostasis (proteostasis) in the underlying pathomechanisms. This review summarizes specific mechanisms that maintain proteostasis, including molecular chaperons, the ubiquitin-proteasome system (UPS), endoplasmic reticulum associated degradation (ERAD), and different autophagic pathways (chaperon mediated-, micro-, and macro-autophagy). The role of heat shock proteins (Hsps) in cellular quality control and degradation of pathogenic proteins is reviewed. Finally, putative therapeutic strategies for efficient removal of cytotoxic proteins from neurons and design of new therapeutic targets against the progression of NDDs are discussed.<\/jats:p>","DOI":"10.3390\/ijms19010325","type":"journal-article","created":{"date-parts":[[2018,1,22]],"date-time":"2018-01-22T13:40:39Z","timestamp":1516628439000},"page":"325","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":98,"title":["Heat Shock Proteins and Autophagy Pathways in Neuroprotection: From Molecular Bases to Pharmacological Interventions"],"prefix":"10.3390","volume":"19","author":[{"given":"Botond","family":"Penke","sequence":"first","affiliation":[{"name":"Department of Medical Chemistry, University of Szeged, H-6720 Szeged, D\u00f3m Square 8, Hungary"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-0611-1452","authenticated-orcid":false,"given":"Ferenc","family":"Bog\u00e1r","sequence":"additional","affiliation":[{"name":"Department of Medical Chemistry, University of Szeged, H-6720 Szeged, D\u00f3m Square 8, Hungary"},{"name":"MTA-SZTE Biomimetic Systems Research Group, University of Szeged, H-6720 Szeged, D\u00f3m Square 8, Hungary"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-6053-7016","authenticated-orcid":false,"given":"Tim","family":"Crul","sequence":"additional","affiliation":[{"name":"Institute of Biochemistry, Biological Research Centre, Hungarian Academy of Sciences, H-6726 Szeged, Temesv\u00e1ri krt. 62, Hungary"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mikl\u00f3s","family":"S\u00e1ntha","sequence":"additional","affiliation":[{"name":"Institute of Biochemistry, Biological Research Centre, Hungarian Academy of Sciences, H-6726 Szeged, Temesv\u00e1ri krt. 62, Hungary"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Melinda E.","family":"T\u00f3th","sequence":"additional","affiliation":[{"name":"Institute of Biochemistry, Biological Research Centre, Hungarian Academy of Sciences, H-6726 Szeged, Temesv\u00e1ri krt. 62, Hungary"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"L\u00e1szl\u00f3","family":"V\u00edgh","sequence":"additional","affiliation":[{"name":"Institute of Biochemistry, Biological Research Centre, Hungarian Academy of Sciences, H-6726 Szeged, Temesv\u00e1ri krt. 62, Hungary"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2018,1,22]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"524","DOI":"10.1016\/S0962-8924(00)01852-3","article-title":"Aggresomes, inclusion bodies and protein aggregation","volume":"10","author":"Kopito","year":"2000","journal-title":"Trends Cell Biol."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"916","DOI":"10.1126\/science.1141448","article-title":"Adapting proteostasis for disease intervention","volume":"319","author":"Balch","year":"2008","journal-title":"Science"},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"491","DOI":"10.1016\/j.devcel.2015.02.002","article-title":"Neuronal aggregates: Formation, clearance, and spreading","volume":"32","author":"Lim","year":"2015","journal-title":"Dev. 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