Ontology highlight
ABSTRACT:
SUBMITTER: Kumpula EP
PROVIDER: S-EPMC5610305 | biostudies-literature | 2017 Sep
REPOSITORIES: biostudies-literature
Kumpula Esa-Pekka EP Pires Isa I Lasiwa Devaki D Piirainen Henni H Bergmann Ulrich U Vahokoski Juha J Kursula Inari I
Scientific reports 20170922 1
Filamentous actin is critical for apicomplexan motility and host cell invasion. Yet, parasite actin filaments are short and unstable. Their kinetic characterization has been hampered by the lack of robust quantitative methods. Using a modified labeling method, we carried out thorough biochemical characterization of malaria parasite actin. In contrast to the isodesmic polymerization mechanism suggested for Toxoplasma gondii actin, Plasmodium falciparum actin I polymerizes via the classical nuclea ...[more]