ePrints@IIScePrints@IISc Home | About | Browse | Latest Additions | Advanced Search | Contact | Help

Heat shock protein 90 from neglected protozoan parasites

Roy, Nainita and Nageshan, Rishi Kumar and Ranade, Shatakshi and Tatu, Utpal (2012) Heat shock protein 90 from neglected protozoan parasites. In: Biochimica et Biophysica Acta (BBA) - Molecular Cell Research, 1823 (3, SI). pp. 707-711.

[img] PDF
Heat_shock.pdf - Published Version
Restricted to Registered users only

Download (546kB) | Request a copy
Official URL: http://dx.doi.org/10.1016/j.bbamcr.2011.12.003

Abstract

Significant advances have been made in our understanding of heat shock protein 90 (Hsp90) in terms of its structure, biochemical characteristics, post-translational modifications, interactomes, regulation and functions. In addition to yeast as a model several new systems have now been examined including flies, worms, plants as well as mammalian cells. This review discusses themes emerging out of studies reported on Hsp90 from infectious disease causing protozoa. A common theme of sensing and responding to host cell microenvironment emerges out of analysis of Hsp90 in Malaria, Trypanosmiasis as well as Leishmaniasis. In addition to their functional roles, the potential of Hsp90 from these infectious disease causing organisms to serve as drug targets and the current status of this drug development endeavor are discussed. Finally, a unique and the only known example of a split Hsp90 gene from another disease causing protozoan Giardia lamblia and its evolutionary significance are discussed. Clearly studies on Hsp90 from protozoan parasites promise to reveal important new paradigms in Hsp90 biology while exploring its potential as an anti-infective drug target. This article is part of a Special Issue entitled: Heat Shock Protein 90 (HSP90). (C) 2011 Elsevier B.V. All rights reserved.

Item Type: Journal Article
Publication: Biochimica et Biophysica Acta (BBA) - Molecular Cell Research
Publisher: Elsevier Science
Additional Information: Copyright of this article belongs to Elsevier Science.
Department/Centre: Division of Biological Sciences > Biochemistry
Date Deposited: 18 Apr 2012 05:18
Last Modified: 18 Apr 2012 05:18
URI: http://eprints.iisc.ac.in/id/eprint/44305

Actions (login required)

View Item View Item