Exported plasmodial J domain protein, PFE0055c, and PfHsp70-x form a specific co-chaperone-chaperone partnership
Author:
Funder
The University of Notre Dame Australia
Publisher
Springer Science and Business Media LLC
Subject
Cell Biology,Biochemistry
Link
http://link.springer.com/content/pdf/10.1007/s12192-020-01181-2.pdf
Reference59 articles.
1. Ahmad A, Bhattacharya A, McDonald RA et al (2011) Heat shock protein 70 kDa chaperone/DnaJ cochaperone complex employs an unusual dynamic interface. PNAS 108:18966–18971
2. Akide-Ndunge OB, Tambini E, Giribaldi G, McMillan PJ, Müller S, Arese P, Turrini F (2009) Co-ordinated stage-dependent enhancement of Plasmodium falciparum antioxidant enzymes and heat shock protein expression in parasites growing in oxidatively stressed or G6PD-deficient red blood cells. Malar J 8:113
3. Anas M, Shukla A, Tripathi A, Kumari V, Prakash C, Nag P, Kumar LS, Sharma SK, Ramachandran R, Kumar N (2020) Structural–functional diversity of malaria parasite’s PfHSP70-1 and PfHSP40 chaperone pair gives an edge over human orthologs in chaperone-assisted protein folding. Biochem J 477:3625–3643
4. Behl A, Kumar V, Bisht A, Panda JJ, Hora R, Mishra PC (2019) Cholesterol bound Plasmodium falciparum co-chaperone ‘PFA0660w’complexes with major virulence factor ‘PfEMP1’via chaperone ‘PfHsp70-x’. Sci Rep 9:1–7
5. Bondos SE, Bicknell A (2003) Detection and prevention of protein aggregation before, during, and after purification. Anal Biochem 316:223–231
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