MN Aminake, HD Arndt, G Pradel - International Journal for Parasitology …, 2012 - Elsevier
The ubiquitin/proteasome system serves as a regulated protein degradation pathway in eukaryotes, and is involved in many cellular processes featuring high protein turnover rates …
Artemisinin (ART)-based combination therapies are the most efficacious treatment of uncomplicated Plasmodium falciparum malaria. Alarmingly, P. falciparum strains have …
Quite aside from its immense importance as a human pathogen, studies in recent years have brought to light the fact that the malaria parasite Plasmodium falciparum is an …
KM Krishnan, KC Williamson - Translational Research, 2018 - Elsevier
The proteasome plays a vital role throughout the life cycle as Plasmodium parasites quickly adapt to a new host and undergo a series of morphologic changes during asexual …
EM Pasini, D Van den Ierssel, HJ Vial, CHM Kocken - Malaria journal, 2013 - Springer
Background Malaria is a major health and socio-economical problem in tropical and sub- tropical areas of the world. Several methodologies have been used to assess parasite …
M Mishra, V Singh, S Singh - Frontiers in Microbiology, 2019 - frontiersin.org
Malaria, caused by protozoan of genus Plasmodium, remains one of the highest mortality infectious diseases. Malaria parasites have a complex life cycle, easily adapt to their host's …
G Lehmann, T Ziv, O Braten, A Admon… - Biochemical and …, 2016 - Elsevier
Several protein quality control systems in bacteria and/or mitochondrial matrix from lower eukaryotes are absent in higher eukaryotes. These are transfer-messenger RNA (tmRNA) …
The ATP-dependent ClpQY protease system in Plasmodium falciparum is a prokaryotic machinery in the parasite. In the present study, we have identified the complete ClpQY …
S Jain, S Rathore, M Asad, ME Hossain… - Cellular …, 2013 - Wiley Online Library
The ATP‐dependent ClpQY system is a prokaryotic proteasome‐like multi‐subunit machinery localized in the mitochondrion of malaria parasite. The ClpQY machinery consists …