Year-end Sale % OFF 
Abstract
Studies in mammalian and yeast chaperone systems have significantly advanced our understanding of the biochemistry of heat shock protein 90 (Hsp90), particularly as it pertains to structural details, interaction regulation, and function. Harnessing this body of knowledge, parasitologists have made tremendous steps in understanding the role of the Hsp90 chaperone machine in protozoal parasites, especially in malaria. Heat shock proteins are a crucial part of the signaling events involved in malaria parasite acclimatization in the host. Even though studies of the role of Hsp90 in malaria have been thorough and discovered some of the most intricate details of the utility of the Hsp90 interactome for pathogen-host interactions, the full and elaborate extent of the role of Hsp90 homologs in malaria remains to be uncovered. This chapter discusses the current knowledge about the biochemistry and cellular role of Hsp90 in Plasmodium falciparum malaria. In addition, the involvement of both parasitic and host Hsp90s by the parasite in the infected cell is discussed.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
