ArticleChemMedChem2015
Targeting a dynamic protein-protein interaction: fragment screening against the malaria myosin A motor complex.
Article in ChemMedChem, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 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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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
17 citing papers in PubMed, 24 citations in OpenAlex.
- Toward Comprehensive In Vitro Evaluation of Serum Albumin Binding of Per- and Polyfluoroalkyl Substances.Journal of xenobiotics · 2026Review
- ShiftScan: A tool for rapid analysis of high-throughput differential scanning fluorimetry data and compound prioritization.Protein science : a publication of the Protein Society · 2025Article
- Discovery of Novel Inhibitors against ALS-Related SOD1(A4V) Aggregation through the Screening of a Chemical Library Using Differential Scanning Fluorimetry (DSF).Pharmaceuticals (Basel, Switzerland) · 2024Article
- Biochemical and Structural Analysis of the Bacterial Enzyme Succinyl-Diaminopimelate Desuccinylase (DapE) fromACS omega · 2024Article
- Cyclobutanone Inhibitors of Diaminopimelate Desuccinylase (DapE) as Potential New Antibiotics.International journal of molecular sciences · 2024Article
- Plasmodium falciparum GAP40 Plays an Essential Role in Merozoite Invasion and Gametocytogenesis.Microbiology spectrum · 2023Article
- A De novo Peptide from a High Throughput Peptide Library Blocks Myosin A -MTIP Complex Formation inInternational journal of molecular sciences · 2020Article
- Theory and applications of differential scanning fluorimetry in early-stage drug discovery.Biophysical reviews · 2020Review
- Systematic analysis of Plasmodium myosins reveals differential expression, localisation, and function in invasive and proliferative parasite stages.Cellular microbiology · 2019Article
- In vitro interaction between Plasmodium falciparum myosin B (PfMyoB) and myosin A tail interacting protein (MTIP).Parasitology research · 2018Article
- Discovery of Plasmodium (M)TRAP-Aldolase Interaction Stabilizers Interfering with Sporozoite Motility and Invasion.ACS infectious diseases · 2018Article
- Dissecting the molecular assembly of theThe Journal of biological chemistry · 2017Article
- Myosin B of Plasmodium falciparum (PfMyoB): in silico prediction of its three-dimensional structure and its possible interaction with MTIP.Parasitology research · 2017Article
- Drug target identification in protozoan parasites.Expert opinion on drug discovery · 2016Review
- Inhibition by stabilization: targeting the Plasmodium falciparum aldolase-TRAP complex.Malaria journal · 2015Article
- Overcoming Chemical, Biological, and Computational Challenges in the Development of Inhibitors Targeting Protein-Protein Interactions.Chemistry & biology · 2015Review
- The apicomplexan glideosome and adhesins - Structures and function.Journal of structural biology · 2015Review
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Motility is a vital feature of the complex life cycle of Plasmodium falciparum, the apicomplexan parasite that causes human malaria. Processes such as host cell invasion are thought to be powered by a conserved actomyosin motor (containing myosin A or myoA), correct localization of which is dependent on a tight interaction with myosin A tail domain interacting protein (MTIP) at the inner membrane of the parasite. Although disruption of this protein-protein interaction represents an attractive means to investigate the putative roles of myoA-based motility and to inhibit the parasitic life cycle, no small molecules have been identified that bind to MTIP. Furthermore, it has not been possible to obtain a crystal structure of the free protein, which is highly dynamic and unstable in the absence of its natural myoA tail partner. Herein we report the de novo identification of the first molecules that bind to and stabilize MTIP via a fragment-based, integrated biophysical approach and structural investigations to examine the binding modes of hit compounds. The challenges of targeting such a dynamic system with traditional fragment screening workflows are addressed throughout.
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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.