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PfHop

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https://www.readbyqxmd.com/read/29206141/-epigallocatechin-3-gallate-inhibits-the-chaperone-activity-of-plasmodium-falciparum-hsp70-chaperones-and-abrogates-their-association-with-functional-partners
#1
Tawanda Zininga, Lebogang Ramatsui, Pertunia Bveledzani Makhado, Stanley Makumire, Ikechukwu Achilinou, Heinrich Hoppe, Heini Dirr, Addmore Shonhai
Heat shock proteins (Hsps), amongst them, Hsp70 and Hsp90 families, serve mainly as facilitators of protein folding (molecular chaperones) of the cell. The Hsp70 family of proteins represents one of the most important molecular chaperones in the cell. Plasmodium falciparum , the main agent of malaria, expresses six Hsp70 isoforms. Two (PfHsp70-1 and PfHsp70-z) of these localize to the parasite cytosol. PHsp70-1 is known to occur in a functional complex with another chaperone, PfHsp90 via a co-chaperone, P. falciparum Hsp70-Hsp90 organising protein (PfHop)...
December 5, 2017: Molecules: a Journal of Synthetic Chemistry and Natural Product Chemistry
https://www.readbyqxmd.com/read/26684582/synthesis-of-platinum-complexes-with-2-5-perfluoroalkyl-1-2-4-oxadiazol-3yl-pyridine-and-2-3-perfluoroalkyl-1-methyl-1-2-4-triazole-5yl-pyridine-ligands-and-their-in-vitro-antitumor-activity
#2
Simona Rubino, Ivana Pibiri, Cristina Costantino, Silvestre Buscemi, Maria Assunta Girasolo, Alessandro Attanzio, Luisa Tesoriere
Five new mononuclear Pt(II) complexes with 5-perfluoroalkyl-1,2,4-oxadiazolyl-pyridine and 3-perfluoroalkyl-1,2,4-triazolyl-pyridine ligands are reported. The ligands 2-(5-perfluoroheptyl-1,2,4-oxadiazole-3yl)-pyridine (pfhop), 2-(5-perfluoropropyl)-1,2,4-oxadiazole-3yl)-pyridine (pfpop), 2-(3-perfluoroheptyl-1-methyl-1,2,4-triazole-5yl)-pyridine (pfhtp), 2-(3-perfluoropropyl-1-methyl-1,2,4-triazole-5yl)-pyridine (pfptp) and their complexes [PtCl2(pfhop)2]·1.5 DMSO (2a), [PtCl2(pfpop)2]·1.5 DMSO (3a), [PtCl2(pfhtp)2]·1...
February 2016: Journal of Inorganic Biochemistry
https://www.readbyqxmd.com/read/26267894/plasmodium-falciparum-hop-pfhop-interacts-with-the-hsp70-chaperone-in-a-nucleotide-dependent-fashion-and-exhibits-ligand-selectivity
#3
Tawanda Zininga, Stanely Makumire, Grace Wairimu Gitau, James M Njunge, Ofentse Jacob Pooe, Hanna Klimek, Robina Scheurr, Hartmann Raifer, Earl Prinsloo, Jude M Przyborski, Heinrich Hoppe, Addmore Shonhai
Heat shock proteins (Hsps) play an important role in the development and pathogenicity of malaria parasites. One of the most prominent functions of Hsps is to facilitate the folding of other proteins. Hsps are thought to play a crucial role when malaria parasites invade their host cells and during their subsequent development in hepatocytes and red blood cells. It is thought that Hsps maintain proteostasis under the unfavourable conditions that malaria parasites encounter in the host environment. Although heat shock protein 70 (Hsp70) is capable of independent folding of some proteins, its functional cooperation with heat shock protein 90 (Hsp90) facilitates folding of some proteins such as kinases and steroid hormone receptors into their fully functional forms...
2015: PloS One
https://www.readbyqxmd.com/read/25482441/plasmodium-falciparum-hop-detailed-analysis-on-complex-formation-with-hsp70-and-hsp90
#4
Rowan Hatherley, Crystal-Leigh Clitheroe, Ngonidzashe Faya, Özlem Tastan Bishop
The heat shock organizing protein (Hop) is important in modulating the activity and co-interaction of two chaperones: heat shock protein 70 and 90 (Hsp70 and Hsp90). Recent research suggested that Plasmodium falciparum Hop (PfHop), PfHsp70 and PfHsp90 form a complex in the trophozoite infective stage. However, there has been little computational research on the malarial Hop protein in complex with other malarial Hsps. Using in silico characterization of the protein, this work showed that individual domains of Hop are evolving at different rates within the protein...
January 2, 2015: Biochemical and Biophysical Research Communications
https://www.readbyqxmd.com/read/24560171/co-chaperones-of-hsp90-in-plasmodium-falciparum-and-their-concerted-roles-in-cellular-regulation
#5
REVIEW
Chun-Song Chua, Huiyu Low, Tiow-Suan Sim
Co-chaperones are well-known regulators of heat shock protein 90 (Hsp90). Hsp90 is a molecular chaperone that is essential in the eukaryotes for the folding and activation of numerous proteins involved in important cellular processes such as signal transduction, growth and developmental regulation. Co-chaperones assist Hsp90 in the protein folding process by modulating conformational changes to promote client protein interaction and functional maturation. With the recognition of Plasmodium falciparum Hsp90 (PfHsp90) as a potential antimalarial drug target, there is obvious interest in the study of its co-chaperones in their partnership in regulating cellular processes in malaria parasite...
August 2014: Parasitology
https://www.readbyqxmd.com/read/22005844/characterisation-of-the-plasmodium-falciparum-hsp70-hsp90-organising-protein-pfhop
#6
Grace W Gitau, Pradipta Mandal, Gregory L Blatch, Jude Przyborski, Addmore Shonhai
Malaria is caused by Plasmodium species, whose transmission to vertebrate hosts is facilitated by mosquito vectors. The transition from the cold blooded mosquito vector to the host represents physiological stress to the parasite, and additionally malaria blood stage infection is characterised by intense fever periods. In recent years, it has become clear that heat shock proteins play an essential role during the parasite's life cycle. Plasmodium falciparum expresses two prominent heat shock proteins: heat shock protein 70 (PfHsp70) and heat shock protein 90 (PfHsp90)...
March 2012: Cell Stress & Chaperones
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