An Insight to Heat Shock Protein 90: A Remedy for Multiple Problems

dc.contributor.authorYadav, Megha
dc.contributor.authorSingh, Ankit Kumar
dc.contributor.authorKumar, Adarsh
dc.contributor.authorThareja, Suresh
dc.contributor.authorKumar, Pradeep
dc.date.accessioned2024-01-21T10:38:24Z
dc.date.accessioned2024-08-13T12:05:20Z
dc.date.available2024-01-21T10:38:24Z
dc.date.available2024-08-13T12:05:20Z
dc.date.issued2022-08-30T00:00:00
dc.description.abstractHeat shock protein 90 (Hsp90) is a chaperone protein that prevents many other proteins from aggre-gating by folding them in a certain way. Hsp90 consists of three structural domains: N-terminal, middle and C-terminal domains. Hsp90 has many activities in numerous proteins and signaling pathways like chimeric fusion proteins, steroid hormone receptors, tumor suppressor genes, and cell cycle regulatory proteins. The role of Hsp90 is not only in cancer but also in other diseases like COVID-19, leishmaniasis, diabetes, flavi virus, systemic sclerosis, grass carp reovirus, psoriasis, malaria, cardiac fibrosis, and alcohol-related liver diseases. This review is a compilation of the pharmacological profile of Hsp90 inhibitors, problems associated with them, and suggested remedies for the same. � 2022 Bentham Science Publishers.en_US
dc.identifier.doi10.2174/1381612828666220829120630
dc.identifier.issn13816128
dc.identifier.urihttps://kr.cup.edu.in/handle/32116/3557
dc.identifier.urlhttps://www.eurekaselect.com/208152/article
dc.language.isoen_USen_US
dc.publisherBentham Science Publishersen_US
dc.subjectcanceren_US
dc.subjectchaperonesen_US
dc.subjectgeldanamycinen_US
dc.subjectHsp90en_US
dc.subjectproteosomeen_US
dc.subjectradicicolen_US
dc.titleAn Insight to Heat Shock Protein 90: A Remedy for Multiple Problemsen_US
dc.title.journalCurrent Pharmaceutical Designen_US
dc.typeShort surveyen_US
dc.type.accesstypeClosed Accessen_US

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