Characterisation of complexes formed by parasite proteins exported into the host cell compartment of Plasmodium falciparum infected red blood cells-Reference-Cited by-同舟云学术

Characterisation of complexes formed by parasite proteins exported into the host cell compartment of Plasmodium falciparum infected red blood cells

Published:2021-05-03 Issue:8 Volume:23 Page:
ISSN:1462-5814
Container-title:Cellular Microbiology
language:en
Short-container-title:Cellular Microbiology

Author:

Jonsdottir Thorey K.¹²^ORCID,Counihan Natalie A.³,Modak Joyanta K.³,Kouskousis Betty¹⁴,Sanders Paul R.¹,Gabriela Mikha¹³,Bullen Hayley E.¹,Crabb Brendan S.¹²⁵,Koning‐Ward Tania F.³,Gilson Paul R.¹

Affiliation:

1. Burnet Institute Melbourne Australia

2. Department of Microbiology and Immunology University of Melbourne Melbourne Australia

3. School of Medicine Deakin University Waurn Ponds Australia

4. Monash Micro‐imaging Monash University Melbourne Australia

5. Department of Microbiology Monash University Melbourne Australia

Funder

Deakin University

University of Melbourne

National Health and Medical Research Council

Publisher

Hindawi Limited

Subject

Virology,Immunology,Microbiology

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1111/cmi.13332

Reference58 articles.

1. Live-Cell FRET Reveals that Malaria Nutrient Channel Proteins CLAG3 and RhopH2 Remain Associated throughout Their Tortuous Trafficking

2. Plasmodium falciparum Transfected with Ultra Bright NanoLuc Luciferase Offers High Sensitivity Detection for the Screening of Growth and Cellular Trafficking Inhibitors

3. Lamellar membranes associated with rhoptries in erythrocytic merozoites of Plasmodium knowlesi: a clue to the mechanism of invasion

4. PTEX component HSP101 mediates export of diverse malaria effectors into host erythrocytes

5. Cholesterol bound Plasmodium falciparum co-chaperone ‘PFA0660w’ complexes with major virulence factor ‘PfEMP1’ via chaperone ‘PfHsp70-x’

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