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Additionally, celastrol reorganizes the expression pattern of chaperone genes. Specifically, celastrol up-regulates genes coding for Heat-shock protein 70 (Hsp70), DnaJ homolog subfamily B members 1 and 9 (DNAJB1\/9), and BAG family chaperone regulator 3 (BAG3). Celastrol stabilizes mutant GCase by specifically targeting BAG3. These findings provide insight into the molecular mechanisms underlying human disorders that result from abnormalities of protein stability.<\/jats:p>","DOI":"10.1073\/pnas.1321341111","type":"journal-article","created":{"date-parts":[[2013,12,19]],"date-time":"2013-12-19T02:39:18Z","timestamp":1387420758000},"page":"249-254","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":41,"title":["Celastrol increases glucocerebrosidase activity in Gaucher disease by modulating molecular chaperones"],"prefix":"10.1073","volume":"111","author":[{"given":"Chunzhang","family":"Yang","sequence":"first","affiliation":[{"name":"Surgical Neurology Branch, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, MD 20892-1260; and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Cody L.","family":"Swallows","sequence":"additional","affiliation":[{"name":"Surgical Neurology Branch, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, MD 20892-1260; 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