about
A mechanistic paradigm for broad-spectrum antivirals that target virus-cell fusionFlaviviruses: braking the enteringFormation and characterization of the trimeric form of the fusion protein of Semliki Forest VirusMolecular dissection of the Semliki Forest virus homotrimer reveals two functionally distinct regions of the fusion protein.The fusion peptide of Semliki Forest virus associates with sterol-rich membrane domains.Effects of membrane potential and sphingolipid structures on fusion of Semliki Forest virus.Novel mutations that control the sphingolipid and cholesterol dependence of the Semliki Forest virus fusion proteinSecond-Site Revertants of a Semliki Forest Virus Fusion-Block Mutation Reveal the Dynamics of a Class II Membrane Fusion ProteinFurin Processing and Proteolytic Activation of Semliki Forest VirusSite-Directed Antibodies against the Stem Region Reveal Low pH-Induced Conformational Changes of the Semliki Forest Virus Fusion ProteinFunctions of the Stem Region of the Semliki Forest Virus Fusion Protein during Virus Fusion and AssemblyCholesterol is required in the exit pathway of Semliki Forest virusUbiquitin Depletion and Dominant-Negative VPS4 Inhibit Rhabdovirus Budding without Affecting Alphavirus BuddingDomain III from class II fusion proteins functions as a dominant-negative inhibitor of virus membrane fusionCholesterol is required for infection by Semliki Forest virusRole of spike protein conformational changes in fusion of Semliki Forest virusDifferential Cholesterol Binding by Class II Fusion Proteins Determines Membrane Fusion PropertiesRole of Conserved Histidine Residues in the Low-pH Dependence of the Semliki Forest Virus Fusion ProteinE1 Mutants Identify a Critical Region in the Trimer Interface of the Semliki Forest Virus Fusion ProteinDealing with low pH: entry and exit of alphaviruses and flavivirusesA Stable Prefusion Intermediate of the Alphavirus Fusion Protein Reveals Critical Features of Class II Membrane FusionConformational change and protein-protein interactions of the fusion protein of Semliki Forest virusVirus membrane-fusion proteins: more than one way to make a hairpinImaging the alphavirus exit pathway.The cholesterol requirement for sindbis virus entry and exit and characterization of a spike protein region involved in cholesterol dependenceIn vitro and in vivo studies identify important features of dengue virus pr-E protein interactionsA toggle switch controls the low pH-triggered rearrangement and maturation of the dengue virus envelope proteins.In vitro reconstitution reveals key intermediate states of trimer formation by the dengue virus membrane fusion proteinSpecific roles for lipids in virus fusion and exit. Examples from the alphaviruses.Pseudorevertants of a Semliki forest virus fusion-blocking mutation reveal a critical interchain interaction in the core trimerRubella virus: first calcium-requiring viral fusion protein.Alphavirus Entry and Membrane Fusion.Genome-wide RNAi screen identifies novel host proteins required for alphavirus entry.The domain I-domain III linker plays an important role in the fusogenic conformational change of the alphavirus membrane fusion proteinAlphavirus entry: NRAMP leads the way.The interaction of alphavirus E1 protein with exogenous domain III defines stages in virus-membrane fusionBST2/tetherin inhibition of alphavirus exit.Comprehensive mapping of functional epitopes on dengue virus glycoprotein E DIII for binding to broadly neutralizing antibodies 4E11 and 4E5A by phage display.Haploid Genetic Screen Reveals a Profound and Direct Dependence on Cholesterol for Hantavirus Membrane FusionIdentification of a specific region in the e1 fusion protein involved in zinc inhibition of semliki forest virus fusion.
P50
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P50
description
hulumtuese
@sq
onderzoeker
@nl
researcher
@en
հետազոտող
@hy
name
Margaret Kielian
@ast
Margaret Kielian
@en
Margaret Kielian
@es
Margaret Kielian
@nl
Margaret Kielian
@sl
type
label
Margaret Kielian
@ast
Margaret Kielian
@en
Margaret Kielian
@es
Margaret Kielian
@nl
Margaret Kielian
@sl
prefLabel
Margaret Kielian
@ast
Margaret Kielian
@en
Margaret Kielian
@es
Margaret Kielian
@nl
Margaret Kielian
@sl
P106
P21
P31
P496
0000-0002-7395-4791