Description
Title: Hsp90 and Related Malaria Parasite Co-Chaperones
Abstract: Through its unique molecular chaperone abilities, heat shock protein 90 (Hsp90) is one of the key defenders of cellular protein homeostasis. In many prokaryotic and higher eukaryotic model organisms, Hsp90 has been thoroughly studied; however, its structural, functional, and biological characteristics in parasitic protozoans are less well understood. Hsp90 works with a variety of co-chaperones to optimize the pathway for folding proteins. Co-chaperones have a variety of functions that affect how Hsp90 is regulated, including the selective targeting of client proteins, control over ATPase activity, modulation of conformational changes, and post-translational modifications. The most dangerous type of human malaria is caused by Plasmodium falciparum. The parasite that causes malaria’s survival inside the The role of molecular chaperones in the host and the vector is crucial. It is well known that the major cytosolic P. falciparum Hsp90 (PfHsp90), in particular during the intra-erythrocytic stage in the human host, is crucial to the development of the parasite. Although PfHsp90 and human Hsp90 share a lot of sequence and structural similarities, there are also a number of significant structural and functional differences. Additionally, it appears that its co-chaperone network differs significantly from the human host, with a possible absence of a significant homolog. In fact, PfHsp90 and the way it interacts with co-chaperones are potential drug targets for the development of antimalarial medications. In this review, we provide a critical overview of the properties of Hsp90, its cofactors, and related the malaria parasite’s escorters.
Keywords: Plasmodium falciparum; heat shock proteins; cytosolic Hsp90; ATPase; co-chaperones;client proteins
Paper Quality: SCOPUS / Web of Science Level Research Paper
Subject: Biomolecules
Writer Experience: 20+ Years
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