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Article

Aldolase provides an unusual binding site for thrombospondin-related anonymous protein in the invasion machinery of the malaria parasite.

Proceedings of the National Academy of Sciences of the United States of America - 24 Apr 2007

Bosch Jürgen, Buscaglia Carlos A, Krumm Brian, Ingason Bjarni P, Lucas Robert, Roach Claudia, Cardozo Timothy, Nussenzweig Victor, Hol Wim G J

Abstract excerpt

An actomyosin motor located underneath the plasma membrane drives motility and host-cell invasion of apicomplexan parasites such as Plasmodium falciparum and Plasmodium vivax, the causative agents of malaria. Aldolase connects the motor actin filaments to transmembrane adhesive proteins of the th...

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Identifiers

PMID: 17426153
DOI: 10.1073/pnas.0605301104
PMCID: PMC1855406

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026. Prepared record publication-17426153-2026-09-04.2. Manifest publication-graph-cohort-2026-09-04.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 4 Sept 2026.

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Aldolase provides an unusual binding site for thrombospondin-related anonymous protein in the invasion machinery of the malaria parasite.PMID 17426153Read ↗

Modeling the interaction between aldolase and the thrombospondin-related anonymous protein, a key connection of the malaria parasite invasion machinery.Semantic proximity Read ↗

Aldolase forms a bridge between cell surface adhesins and the actin cytoskeleton in apicomplexan parasites.Semantic proximity Read ↗

Characterization of an aldolase-binding site in the Wiskott-Aldrich syndrome protein.Semantic proximity Read ↗

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Towards a molecular understanding of the apicomplexan actin motor: on a road to novel targets for malaria remedies?Semantic proximity Read ↗

Aldolase is essential for energy production and bridging adhesin-actin cytoskeletal interactions during parasite invasion of host cells.Semantic proximity Read ↗

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