ArticleStructure (London, England : 1993)2018
Structural Basis of Phosphatidic Acid Sensing by APH in Apicomplexan Parasites.
Article in Structure (London, England : 1993), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
11 citing papers in PubMed, 24 citations in OpenAlex.
- HOPS/CORVET tethering complexes are critical for endocytosis and protein trafficking to invasion related organelles in malaria parasites.PLoS pathogens · 2025Article
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- Marine gregarine genomes reveal the breadth of apicomplexan diversity with a partially conserved glideosome machinery.BMC genomics · 2022Article
- Toxoplasma gondii phosphatidylserine flippase complex ATP2B-CDC50.4 critically participates in microneme exocytosis.PLoS pathogens · 2022Article
- Dominique Soldati-Favre: BringingFrontiers in cellular and infection microbiology · 2022Article
- A pan-apicomplexan phosphoinositide-binding protein acts in malarial microneme exocytosis.EMBO reports · 2019Article
- Computational Modeling of Realistic Cell Membranes.Chemical reviews · 2019Review
- The triumvirate of signaling molecules controlling Toxoplasma microneme exocytosis: Cyclic GMP, calcium, and phosphatidic acid.PLoS pathogens · 2019Article
- Structural determinants of lipid specificity within Ups/PRELI lipid transfer proteins.Nature communications · 2019Article
- Three F-actin assembly centers regulate organelle inheritance, cell-cell communication and motility ineLife · 2019Article
Corrections and comments
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Authors and funding
9 authors at 2 institutions in 3 countries.
Funding
Abstract
Plasmodium falciparum and Toxoplasma gondii are obligate intracellular parasites that belong to the phylum of Apicomplexa and cause major human diseases. Their access to an intracellular lifestyle is reliant on the coordinated release of proteins from the specialized apical organelles called micronemes and rhoptries. A specific phosphatidic acid effector, the acylated pleckstrin homology domain-containing protein (APH) plays a central role in microneme exocytosis and thus is essential for motility, cell entry, and egress. TgAPH is acylated on the surface of the micronemes and recruited to phosphatidic acid (PA)-enriched membranes. Here, we dissect the atomic details of APH PA-sensing hub and its functional interaction with phospholipid membranes. We unravel the key determinant of PA recognition for the first time and show that APH inserts into and clusters multiple phosphate head-groups at the bilayer binding surface.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.