alexa Heat Shock Proteins, microRNAs, and Drug Design Studies
ISSN: 2168-9431

Single Cell Biology
Open Access

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Heat Shock Proteins, microRNAs, and Drug Design Studies in Medicinal Chemistry

Yusuf Tutar*
Basic Pharmaceutical Sciences, Faculty of Pharmacy, Division of Biochemistry, Cumhuriyet University, Sivas, 58140, Turkey
Corresponding Author : Yusuf TUTAR
Cumhuriyet University
Faculty of Pharmacy
Basic Pharmaceutical Sciences
Division of Biochemistry, Sivas
58140, Turkey
Tel: 90346 2191010
E-mail: [email protected]
Received May 01, 2015; Accepted May 27, 2015; Published May 29, 2015
Citation: Tutar Y (2015) Heat Shock Proteins, microRNAs, and Drug Design Studies in Medicinal Chemistry. Single Cell Biol 4:112. doi: 10.4172/2168-9431.1000112
Copyright: © 2015 Tutar Y. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.


Heat shock proteins (Hsps) are highly conserved chaperone protein family which is responsible for proper folding of newly synthesized and misfolded proteins, cellular signaling, and prevention of protein aggregation. Hsps consist of six major members: small Hsps (<30 kDa), Hsp40 (40 kDa), Hsp60 (60 kDa), Hsp70 (70 kDa), Hsp90 (90 kDa), and Hsp100 (100 kDa). Hsps are found at different parts of the cell (mitochondria, endoplasmic reticulum, cytosol) and their expression level is increased under cellular stress conditions (i.e. malignancy, infection, heavy metals, heat, hypoxia, and oxidative stress). Therefore, expression of high levels of Hsps is related with disease’s pathogenesis.

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