(Q39458024)

English

Analyses of mutations selected by passaging a chimeric flavivirus identify mutations that alter infectivity and reveal an interaction between the structural proteins and the nonstructural glycoprotein NS1.

scientific article published on 13 October 2011

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scholarly article

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Europe PubMed Central

PubMed publication ID

12 September 2017

Analyses of mutations selected by passaging a chimeric flavivirus identify mutations that alter infectivity and reveal an interaction between the structural proteins and the nonstructural glycoprotein NS1. (English)

1 reference

Europe PubMed Central

PubMed publication ID

12 September 2017

1 reference

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author name string

Evandro R Winkelmann

1

1 reference

Europe PubMed Central

PubMed publication ID

12 September 2017

Douglas G Widman

2

1 reference

Europe PubMed Central

PubMed publication ID

12 September 2017

Ryosuke Suzuki

3

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Europe PubMed Central

PubMed publication ID

12 September 2017

Peter W Mason

4

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Europe PubMed Central

PubMed publication ID

12 September 2017

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publication date

13 October 2011

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12 September 2017

number of pages

9

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Europe PubMed Central

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12 September 2017

421

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Europe PubMed Central

PubMed publication ID

12 September 2017

2

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Europe PubMed Central

PubMed publication ID

12 September 2017

96-104

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Europe PubMed Central

PubMed publication ID

12 September 2017

Enzyme-linked immunosorbent assay specific to Dengue virus type 1 nonstructural protein NS1 reveals circulation of the antigen in the blood during the acute phase of disease in patients experiencing primary or secondary infections

1 reference

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Membrane association and secretion of the Japanese encephalitis virus NS1 protein from cells expressing NS1 cDNA.

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A conserved predicted pseudoknot in the NS2A-encoding sequence of West Nile and Japanese encephalitis flaviviruses suggests NS1' may derive from ribosomal frameshifting

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Role of heparan sulfate for attachment and entry of tick-borne encephalitis virus

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Substitutions at the putative receptor-binding site of an encephalitic flavivirus alter virulence and host cell tropism and reveal a role for glycosaminoglycans in entry

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Common E protein determinants for attenuation of glycosaminoglycan-binding variants of Japanese encephalitis and West Nile viruses

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Virulence attenuation of Dengue virus due to augmented glycosaminoglycan-binding affinity and restriction in extraneural dissemination

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The flavivirus precursor membrane-envelope protein complex: structure and maturation

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High circulating levels of the dengue virus nonstructural protein NS1 early in dengue illness correlate with the development of dengue hemorrhagic fever

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Attenuation of tick-borne encephalitis virus by structure-based site-specific mutagenesis of a putative flavivirus receptor binding site

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Maturation of Japanese encephalitis virus glycoproteins produced by infected mammalian and mosquito cells

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Production and characterization of vaccines based on flaviviruses defective in replication

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NS1' of Flaviviruses in the Japanese Encephalitis Virus Serogroup Is a Product of Ribosomal Frameshifting and Plays a Role in Viral Neuroinvasiveness

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Mutagenesis of the N-linked glycosylation sites of the yellow fever virus NS1 protein: effects on virus replication and mouse neurovirulence

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Yellow Fever Virus NS3 Plays an Essential Role in Virus Assembly Independent of Its Known Enzymatic Functions

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Construction and Characterization of a Single-Cycle Chimeric Flavivirus Vaccine Candidate That Protects Mice against Lethal Challenge with Dengue Virus Type 2

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A short N-terminal peptide motif on flavivirus nonstructural protein NS1 modulates cellular targeting and immune recognition

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Structure of the immature dengue virus at low pH primes proteolytic maturation

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based on heuristic

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Genetic analysis of the yellow fever virus NS1 protein: identification of a temperature-sensitive mutation which blocks RNA accumulation

1 reference

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Identifiers

10.1016/J.VIROL.2011.09.007

1 reference

Europe PubMed Central

PubMed publication ID

12 September 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

12 September 2017

ResearchGate publication ID

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