Nipah virus outbreak(s) in Bangladesh, January-April 2004
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Ephrin-B2 ligand is a functional receptor for Hendra virus and Nipah virusNipah virus-associated encephalitis outbreak, Siliguri, IndiaNipah virus in Lyle's flying foxes, CambodiaInhibition of Henipavirus fusion and infection by heptad-derived peptides of the Nipah virus fusion glycoprotein.Potent neutralization of Hendra and Nipah viruses by human monoclonal antibodies.Vaccine potential of Nipah virus-like particlesCombined chloroquine and ribavirin treatment does not prevent death in a hamster model of Nipah and Hendra virus infection.Novel innate immune functions for galectin-1: galectin-1 inhibits cell fusion by Nipah virus envelope glycoproteins and augments dendritic cell secretion of proinflammatory cytokinesEmerging paramyxoviruses: molecular mechanisms and antiviral strategiesGenomic characterization of Nipah virus, West Bengal, IndiaGenetic characterization of Nipah virus, Bangladesh, 2004.Neuroepidemiology and the epidemiology of viral infections of the nervous systemIndividual N-glycans added at intervals along the stalk of the Nipah virus G protein prevent fusion but do not block the interaction with the homologous F protein.Risk factors for Nipah virus encephalitis in Bangladesh.The YPLGVG sequence of the Nipah virus matrix protein is required for buddingNipah virus infection: current scenario.Serodiagnosis using recombinant nipah virus nucleocapsid protein expressed in Escherichia coli.Determination of a phosphorylation site in Nipah virus nucleoprotein and its involvement in virus transcriptionA quantitative and kinetic fusion protein-triggering assay can discern distinct steps in the nipah virus membrane fusion cascadeEstablishment and characterization of plasmid-driven minigenome rescue systems for Nipah virus: RNA polymerase I- and T7-catalyzed generation of functional paramyxoviral RNA.Surface density of the Hendra G protein modulates Hendra F protein-promoted membrane fusion: role for Hendra G protein trafficking and degradation.N-glycans on Nipah virus fusion protein protect against neutralization but reduce membrane fusion and viral entry.Receptor binding, fusion inhibition, and induction of cross-reactive neutralizing antibodies by a soluble G glycoprotein of Hendra virus.Quantitative estimation of Nipah virus replication kinetics in vitro.Polybasic KKR motif in the cytoplasmic tail of Nipah virus fusion protein modulates membrane fusion by inside-out signaling.A VLP-based vaccine provides complete protection against Nipah virus challenge following multiple-dose or single-dose vaccination schedules in a hamster model.
P2860
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P2860
Nipah virus outbreak(s) in Bangladesh, January-April 2004
description
scientific article published on 01 April 2004
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wetenschappelijk artikel
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наукова стаття, опублікована у квітні 2004
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name
Nipah virus outbreak(s) in Bangladesh, January-April 2004
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Nipah virus outbreak(s) in Bangladesh, January-April 2004
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type
label
Nipah virus outbreak(s) in Bangladesh, January-April 2004
@en
Nipah virus outbreak(s) in Bangladesh, January-April 2004
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prefLabel
Nipah virus outbreak(s) in Bangladesh, January-April 2004
@en
Nipah virus outbreak(s) in Bangladesh, January-April 2004
@nl
P1476
Nipah virus outbreak(s) in Bangladesh, January-April 2004
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P407
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2004-04-01T00:00:00Z