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Red blood cell invasion by Plasmodium vivax: structural basis for DBP engagement of DARCThe crystal structure of the Argonaute2 PAZ domain reveals an RNA binding motif in RNAi effector complexesDimerization of Plasmodium vivax DBP is induced upon receptor binding and drives recognition of DARCCrystal and Solution Structures of Plasmodium falciparum Erythrocyte-binding Antigen 140 Reveal Determinants of Receptor Specificity during Erythrocyte InvasionMolecular Basis for Sialic Acid-dependent Receptor Recognition by the Plasmodium falciparum Invasion Protein Erythrocyte-binding Antigen-140/BAEBLStructural and Functional Basis for Inhibition of Erythrocyte Invasion by Antibodies that Target Plasmodium falciparum EBA-175A sugar phosphatase regulates the methylerythritol phosphate (MEP) pathway in malaria parasitesPurified Argonaute2 and an siRNA form recombinant human RISCArgonaute slicing is required for heterochromatic silencing and spreadingStructural analysis of the synthetic Duffy Binding Protein (DBP) antigen DEKnull relevant for Plasmodium vivax malaria vaccine designData publication with the structural biology data grid supports live analysisAllosteric activation of ADAMTS13 by von Willebrand factor.Plasmodium falciparum ligand binding to erythrocytes induce alterations in deformability essential for invasionPlasmodium falciparum erythrocyte-binding antigen 175 triggers a biophysical change in the red blood cell that facilitates invasionEvolutionary fine-tuning of conformational ensembles in FimH during host-pathogen interactions.Critical glycosylated residues in exon three of erythrocyte glycophorin A engage Plasmodium falciparum EBA-175 and define receptor specificity.Analysis of the C. elegans Argonaute family reveals that distinct Argonautes act sequentially during RNAi.Multimeric assembly of host-pathogen adhesion complexes involved in apicomplexan invasion.Rhoptry Proteins ROP5 and ROP18 Are Major Murine Virulence Factors in Genetically Divergent South American Strains of Toxoplasma gondii.Slicer and the argonautes.Broadly neutralizing epitopes in the Plasmodium vivax vaccine candidate Duffy Binding Protein.Inhibitory humoral responses to the Plasmodium falciparum vaccine candidate EBA-175 are independent of the erythrocyte invasion pathway.Molecular Mechanism of Action of Antimalarial Benzoisothiazolones: Species-Selective Inhibitors of the Plasmodium spp. MEP Pathway enzyme, IspDMalaria parasite CelTOS targets the inner leaflet of cell membranes for pore-dependent disruption.A quantitative assay for binding and inhibition of Plasmodium falciparum Erythrocyte Binding Antigen 175 reveals high affinity binding depends on both DBL domains.Malaria adhesins: structure and function.DARC extracellular domain remodeling in maturating reticulocytes explains Plasmodium vivax tropism.Red cell receptors as access points for malaria infection.Comparison of Type 1 D-3-phosphoglycerate dehydrogenases reveals unique regulation in pathogenic Mycobacteria.Cap-domain closure enables diverse substrate recognition by the C2-type haloacid dehalogenase-like sugar phosphatase Plasmodium falciparum HAD1Plasticity, dynamics, and inhibition of emerging tetracycline resistance enzymes.Defining the interaction of the protease CpaA with its type II secretion chaperone CpaB and its contribution to virulence in Acinetobacter species.Strategies for protein coexpression in Escherichia coli.Prediction of New Stabilizing Mutations Based on Mechanistic Insights from Markov State Models.An engineered vaccine of the Plasmodium vivax Duffy binding protein enhances induction of broadly neutralizing antibodies.Plasmepsins IX and X are essential and druggable mediators of malaria parasite egress and invasion.Native Mass Spectrometry, Ion mobility, and Collision-Induced Unfolding Categorize Malaria Antigen/Antibody Binding.Structural basis for the EBA-175 erythrocyte invasion pathway of the malaria parasite Plasmodium falciparum.Structural Basis for the EBA-175 Erythrocyte Invasion Pathway of the Malaria Parasite Plasmodium falciparumShed EBA-175 mediates red blood cell clustering that enhances malaria parasite growth and enables immune evasion
P50
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P50
description
researcher
@en
wetenschapper
@nl
հետազոտող
@hy
name
Niraj H Tolia
@ast
Niraj H Tolia
@en
Niraj H Tolia
@es
Niraj H Tolia
@nl
Niraj H Tolia
@sl
type
label
Niraj H Tolia
@ast
Niraj H Tolia
@en
Niraj H Tolia
@es
Niraj H Tolia
@nl
Niraj H Tolia
@sl
prefLabel
Niraj H Tolia
@ast
Niraj H Tolia
@en
Niraj H Tolia
@es
Niraj H Tolia
@nl
Niraj H Tolia
@sl
P1053
D-2332-2014
P106
P31
P4012
P496
0000-0002-2689-1337