ArticleScience advances2020
Membrane surface recognition by the ASAP1 PH domain and consequences for interactions with the small GTPase Arf1.
Article in Science advances, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed.
- Article
- Probing Solution Dynamics of Tissue Factor Using Molecular Dynamics Simulations Guided by NMR Chemical Shifts.The journal of physical chemistry. B · 2026Article
- Binding orientation of weakly associating membrane peripheral proteins via membrane paramagnetic relaxation enhancement NMR.Communications chemistry · 2026Article
- Complex Structural Examination of Protein-Lipid Interactions with Neutron Scattering Techniques.Methods in molecular biology (Clifton, N.J.) · 2026Review
- An active allosteric mechanism in ASAP1-mediated Arf1 GTP hydrolysis redefines PH domain function.Nature communications · 2025Article
- Cholesterol-targeting Wnt-β-catenin signaling inhibitors for colorectal cancer.Nature chemical biology · 2025Article
- Regulation of Rho guanine nucleotide exchange factor 3 by phosphorylation in the PH domain.iScience · 2025Article
- The Influence of Phosphoinositide Lipids in the Molecular Biology of Membrane Proteins: Recent Insights from Simulations.Journal of molecular biology · 2025Review
- The PH domain in the ArfGAP ASAP1 drives catalytic activation through an unprecedented allosteric mechanism.bioRxiv : the preprint server for biology · 2024Article
- Atomistic characterization of β2-glycoprotein I domain V interaction with anionic membranes.Journal of thrombosis and haemostasis : JTH · 2024Article
- Myr-Arf1 conformational flexibility at the membrane surface sheds light on the interactions with ArfGAP ASAP1.Nature communications · 2023Article
- Exploring Sulfur Sites in Proteins via Triple-ResonanceJournal of the American Chemical Society · 2023Article
- Structural Insights Uncover the Specific Phosphoinositide Recognition by the PH1 Domain of Arap3.International journal of molecular sciences · 2023Article
- Assessment of a host-guest interaction in a bilayer membrane model.RSC advances · 2022Article
- Structural and biophysical properties of farnesylated KRas interacting with the chaperone SmgGDS-558.Biophysical journal · 2022Article
- Systematic simulation of the interactions of pleckstrin homology domains with membranes.Science advances · 2022Article
- Simulations of Kindlin-2 PIP binding domains reveal protonation-dependent membrane binding modes.Biophysical journal · 2021Article
- PIPCommunications biology · 2021Article
- Structural basis for the association of PLEKHA7 with membrane-embedded phosphatidylinositol lipids.Structure (London, England : 1993) · 2021Article
- Flexible pivoting of dynamin pleckstrin homology domain catalyzes fission: insights into molecular degrees of freedom.Molecular biology of the cell · 2021Article
Corrections and comments
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Authors and funding
12 authors.
Funding
Abstract
Adenosine diphosphate-ribosylation factor (Arf) guanosine triphosphatase-activating proteins (GAPs) are enzymes that need to bind to membranes to catalyze the hydrolysis of guanosine triphosphate (GTP) bound to the small GTP-binding protein Arf. Binding of the pleckstrin homology (PH) domain of the ArfGAP With SH3 domain, ankyrin repeat and PH domain 1 (ASAP1) to membranes containing phosphatidylinositol 4,5-bisphosphate [PI(4,5)P
Identifiers
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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.