about
Antisense morpholino-oligomers directed against the 5' end of the genome inhibit coronavirus proliferation and growthCrystal Structure of a Monomeric Form of Severe Acute Respiratory Syndrome Coronavirus Endonuclease nsp15 Suggests a Role for Hexamerization as an Allosteric SwitchNuclear Magnetic Resonance Structure of the N-Terminal Domain of Nonstructural Protein 3 from the Severe Acute Respiratory Syndrome CoronavirusNuclear Magnetic Resonance Structure Shows that the Severe Acute Respiratory Syndrome Coronavirus-Unique Domain Contains a Macrodomain FoldNuclear Magnetic Resonance Structure of the Nucleic Acid-Binding Domain of Severe Acute Respiratory Syndrome Coronavirus Nonstructural Protein 3SARS Coronavirus Unique Domain: Three-Domain Molecular Architecture in Solution and RNA BindingAtlas of coronavirus replicase structure.Complementarity in the supramolecular design of arenaviruses and retroviruses revealed by electron cryomicroscopy and image analysis.A structural analysis of M protein in coronavirus assembly and morphology.Structural genomics of the severe acute respiratory syndrome coronavirus: nuclear magnetic resonance structure of the protein nsP7Direct observation of membrane insertion by enveloped virus matrix proteins by phosphate displacementCrystal structure of nonstructural protein 10 from the severe acute respiratory syndrome coronavirus reveals a novel fold with two zinc-binding motifs.Supramolecular architecture of severe acute respiratory syndrome coronavirus revealed by electron cryomicroscopy.How the double spherules of infectious bronchitis virus impact our understanding of RNA virus replicative organelles.Synthesis and antiviral properties of spirocyclic [1,2,3]-triazolooxazine nucleosides.Ribose 2'-O-methylation provides a molecular signature for the distinction of self and non-self mRNA dependent on the RNA sensor Mda5.Development of peptide-conjugated morpholino oligomers as pan-arenavirus inhibitors.Inhibition and escape of SARS-CoV treated with antisense morpholino oligomers.Proteomics analysis unravels the functional repertoire of coronavirus nonstructural protein 3.Severe acute respiratory syndrome coronavirus nonstructural proteins 3, 4, and 6 induce double-membrane vesiclesUntangling membrane rearrangement in the nidovirales.Competitive fitness in coronaviruses is not correlated with size or number of double-membrane vesicles under reduced-temperature growth conditions.Does form meet function in the coronavirus replicative organelle?Inhibition, escape, and attenuated growth of severe acute respiratory syndrome coronavirus treated with antisense morpholino oligomersArenavirus budding resulting from viral-protein-associated cell membrane curvature.Extensive coronavirus-induced membrane rearrangements are not a determinant of pathogenicity.Mapping the landscape of the lymphocytic choriomeningitis virus stable signal peptide reveals novel functional domains.The proteome of the infectious bronchitis virus Beau-R virion.Identification and Characterization of a Ribose 2'-O-Methyltransferase Encoded by the Ronivirus Branch of Nidovirales.New insights on the role of paired membrane structures in coronavirus replication.Purification and electron cryomicroscopy of coronavirus particles.Purification of coronavirus virions for Cryo-EM and proteomic analysis.Structural basis of severe acute respiratory syndrome coronavirus ADP-ribose-1''-phosphate dephosphorylation by a conserved domain of nsP3.The species Severe acute respiratory syndrome-related coronavirus: classifying 2019-nCoV and naming it SARS-CoV-2
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P50
description
hulumtues
@sq
onderzoeker
@nl
researcher
@en
հետազոտող
@hy
name
Benjamin Neuman
@fr
Benjamin W Neuman
@nl
Benjamin W Neuman
@sl
Benjamin W. Neuman
@en
Benjamin W. Neuman
@es
type
label
Benjamin Neuman
@fr
Benjamin W Neuman
@nl
Benjamin W Neuman
@sl
Benjamin W. Neuman
@en
Benjamin W. Neuman
@es
prefLabel
Benjamin Neuman
@fr
Benjamin W Neuman
@nl
Benjamin W Neuman
@sl
Benjamin W. Neuman
@en
Benjamin W. Neuman
@es
P108
P106
P1153
8263558000
P21
P31
P496
0000-0003-1240-8954