Identification of an exported heat shock protein 70 in Plasmodium falciparum
Host cell remodelling is a hallmark of malaria pathogenesis. It involves protein folding, unfolding and trafficking events and thus participation of chaperones such as Hsp70s and Hsp40s is well speculated. Until recently, only Hsp40s were thought to be the sole representative of the parasite chapero...
Main Authors: | Grover Manish, Chaubey Shweta, Ranade Shatakshi, Tatu Utpal |
---|---|
Format: | Article |
Language: | English |
Published: |
EDP Sciences
2013-01-01
|
Series: | Parasite |
Subjects: | |
Online Access: | http://dx.doi.org/10.1051/parasite/2012002 |
Similar Items
-
Supporting data on characterisation of linker switch mutants of Plasmodium falciparum heat shock protein 110 and canonical Hsp70
by: Graham Chakafana, et al.
Published: (2021-08-01) -
Heat Shock Protein 70 Of Plasmodium Falciparum: Proteomic Analysis Of Its Complexes And Cellular Functions
by: Singh, Varsha
Published: (2007) -
Understanding the Heat Shock Response Pathway in Plasmodium Falciparum and Identification of a Novel Exported Heat Shock Protein
by: Grover, Manish
Published: (2018) -
Plasmodial Hsp70s are functionally adapted to the malaria parasite life cycle
by: Jude M Przyborski, et al.
Published: (2015-06-01) -
Mutation of GGMP Repeat Segments of <i>Plasmodium falciparum</i> Hsp70-1 Compromises Chaperone Function and Hop Co-Chaperone Binding
by: Stanley Makumire, et al.
Published: (2021-02-01)