Heat Shock Protein 90 Inhibitors repurposed against Entamoeba histolytica

Heat Shock Protein 90 Inhibitors repurposed against Entamoeba histolytica

Hsp90 is an essential chaperone responsible for trafficking a vast array of client proteins, which are substrates that Hsp90 regulates in eukaryotic cells under stress conditions. The ATP-binding N-terminal domain of Hsp90 (also known as a GHKL type ATPase domain) can serve as a specific drug target...

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Bibliographic Details
Main Authors: Dea eShahinas, Anjan eDebnath, Christan eBenedict, James H McKerrow, Dylan R Pillai
Format: Article
Language:English
Published: Frontiers Media S.A. 2015-04-01
Series:Frontiers in Microbiology
Subjects:
Gentian Violet
Rifabutin
cetylpyridinium chloride
EhHsp90 inhibitors
rutilantin
pararosaniline pamoate
Online Access:http://journal.frontiersin.org/Journal/10.3389/fmicb.2015.00368/full

Internet

http://journal.frontiersin.org/Journal/10.3389/fmicb.2015.00368/full

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