about
Membrane binding and bending in Ebola VP40 assembly and egressBinding of the PX domain of p47(phox) to phosphatidylinositol 3,4-bisphosphate and phosphatidic acid is masked by an intramolecular interactionMembrane insertion of the FYVE domain is modulated by pHEukaryotic virulence determinants utilize phosphoinositides at the ER and host cell surfaceStructural and membrane binding analysis of the Phox homology domain of Bem1p: basis of phosphatidylinositol 4-phosphate specificityMolecular Basis of Phosphatidylinositol 4-Phosphate and ARF1 GTPase Recognition by the FAPP1 Pleckstrin Homology (PH) DomainA molecular mechanism of artemisinin resistance in Plasmodium falciparum malariaMolecular mechanism of membrane docking by the Vam7p PX domain.Contrasting membrane interaction mechanisms of AP180 N-terminal homology (ANTH) and epsin N-terminal homology (ENTH) domainsMembrane-protein interactions in cell signaling and membrane traffickingCeramide kinase uses ceramide provided by ceramide transport protein: localization to organelles of eicosanoid synthesisEmerging methodologies to investigate lipid-protein interactionsCould the Ebola virus matrix protein VP40 be a drug target?Detection of lipid-induced structural changes of the Marburg virus matrix protein VP40 using hydrogen/deuterium exchange-mass spectrometryX-ray reflectivity studies of cPLA2{alpha}-C2 domains adsorbed onto Langmuir monolayers of SOPCMembrane binding assays for peripheral proteins.A loop region in the N-terminal domain of Ebola virus VP40 is important in viral assembly, budding, and egressThe Ebola virus matrix protein VP40 selectively induces vesiculation from phosphatidylserine-enriched membranes.Monitoring peripheral protein oligomerization on biological membranes.Biophysical and computational studies of membrane penetration by the GRP1 pleckstrin homology domain.Genome-wide structural analysis reveals novel membrane binding properties of AP180 N-terminal homology (ANTH) domains.Metabolically stabilized derivatives of phosphatidylinositol 4-phosphate: synthesis and applications.The Ebola Virus: From Basic Research to a Global Health CrisisCellular and molecular interactions of phosphoinositides and peripheral proteinsBinding of the sphingolipid S1P to hTERT stabilizes telomerase at the nuclear periphery by allosterically mimicking protein phosphorylation.Investigation of Ebola VP40 assembly and oligomerization in live cells using number and brightness analysis.pH-dependent binding of the Epsin ENTH domain and the AP180 ANTH domain to PI(4,5)P2-containing bilayers.Single-particle tracking demonstrates that actin coordinates the movement of the Ebola virus matrix protein.Host targeting of virulence determinants and phosphoinositides in blood stage malaria parasitesThe Ebola Virus matrix protein, VP40, requires phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2) for extensive oligomerization at the plasma membrane and viral egress.Crystal Structure of Marburg Virus VP40 Reveals a Broad, Basic Patch for Matrix Assembly and a Requirement of the N-Terminal Domain for Immunosuppression.Membrane binding and subcellular targeting of C2 domains.The Ebola virus matrix protein penetrates into the plasma membrane: a key step in viral protein 40 (VP40) oligomerization and viral egress.Surface plasmon resonance: a useful technique for cell biologists to characterize biomolecular interactions.The molecular basis of ceramide-1-phosphate recognition by C2 domains.The Ebola virus matrix protein deeply penetrates the plasma membrane: an important step in viral egress.A new model of interfacial kinetics for phospholipases.Cellular membranes and lipid-binding domains as attractive targets for drug development.Lipid binding domains: more than simple lipid effectors.Selection of DNA ligands for protein kinase C-delta.
P50
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P50
description
hulumtues
@sq
researcher
@en
wetenschapper
@nl
հետազոտող
@hy
name
Robert V Stahelin
@nl
Robert V Stahelin
@sl
Robert V. Stahelin
@en
Robert V. Stahelin
@es
type
label
Robert V Stahelin
@nl
Robert V Stahelin
@sl
Robert V. Stahelin
@en
Robert V. Stahelin
@es
prefLabel
Robert V Stahelin
@nl
Robert V Stahelin
@sl
Robert V. Stahelin
@en
Robert V. Stahelin
@es
P106
P1153
6602098191
P21
P31
P496
0000-0001-5443-7863