Heat Shock Proteins; An Overview

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dc.contributor.authorTutar, Lutfi
dc.contributor.authorTutar, Yusuf
dc.date.accessioned2019-07-27T12:10:23Z
dc.date.accessioned2019-07-28T10:13:47Z
dc.date.available2019-07-27T12:10:23Z
dc.date.available2019-07-28T10:13:47Z
dc.date.issued2010
dc.department[Tutar, Yusuf] Cumhuriyet Univ, Dept Biochem, Fac Med, TR-58140 Sivas, Turkey -- [Tutar, Lutfi] Selcuk Univ, Fac Sci, Dept Biol, TR-42075 Konya, Turkeyen_US
dc.description.abstractHeat shock proteins (Hsps) protect protein substrates against conformational damage to promote the function of the proteins, prevent aggregation and prevent formation of toxic inclusion bodies. Protein aggregates and fibrils have been associated with neurodegenerative diseases and with inclusion bodies. High-level expression of recombinant protein for biotechnological purposes often leads to insoluble inclusion bodies. Therefore, misfolded proteins must be properly folded or must be degraded through heat shock protein action. This function protects cells against cytotoxic outcomes. In addition to their cytoprotective roles, Hsps are involved in other functions since Hsps exist in all types of cells and tissues. Therefore, several diseases are associated with alterations of these biochemical functions. This first review of the theme issue will discuss general properties of Hsps concisely along with their potential use in pharmaceutical and biotechnological applications.en_US
dc.description.sponsorshipTurkish Planning Organization [DPT-K.120220-2006]; Turkish National Academy of Sciences (TUBA-GEBIP)en_US
dc.description.sponsorshipThere are several important articles in this broad research field therefore, the authors would like to apologies for not citing these papers. We thank Dr. Daniel C. Masison for critically reading the manuscript. This work was funded partly by the Turkish Planning Organization (DPT-K.120220-2006) and through a seed grant from the Turkish National Academy of Sciences (TUBA-GEBIP).en_US
dc.identifier.doi10.2174/138920110790909632en_US
dc.identifier.endpage222en_US
dc.identifier.issn1389-2010
dc.identifier.issn1873-4316
dc.identifier.issue2en_US
dc.identifier.pmid20170474en_US
dc.identifier.scopus2-s2.0-77949890661en_US
dc.identifier.scopusqualityQ2
dc.identifier.startpage216en_US
dc.identifier.urihttps://dx.doi.org/10.2174/138920110790909632
dc.identifier.urihttps://hdl.handle.net/20.500.12418/9932
dc.identifier.volume11en_US
dc.identifier.wosWOS:000275517100010en_US
dc.identifier.wosqualityQ1
dc.indekslendigikaynakWeb of Scienceen_US
dc.indekslendigikaynakScopusen_US
dc.indekslendigikaynakPubMeden_US
dc.language.isoenen_US
dc.publisherBENTHAM SCIENCE PUBL LTDen_US
dc.relation.ispartofCURRENT PHARMACEUTICAL BIOTECHNOLOGYen_US
dc.relation.publicationcategoryDiğeren_US
dc.rightsinfo:eu-repo/semantics/closedAccessen_US
dc.subjectHeat shock proteinen_US
dc.subjectbiotechnologyen_US
dc.subjectpharmacologyen_US
dc.titleHeat Shock Proteins; An Overviewen_US
dc.typeReviewen_US

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