Neuraminidase stalk length and additional glycosylation of the hemagglutinin influence the virulence of influenza H5N1 viruses for mice
about
A generic system for the expression and purification of soluble and stable influenza neuraminidaseHuman H7N9 avian influenza virus infection: a review and pandemic risk assessmentAssessment of the internal genes of influenza A (H7N9) virus contributing to high pathogenicity in miceThe short stalk length of highly pathogenic avian influenza H5N1 virus neuraminidase limits transmission of pandemic H1N1 virus in ferretsHost adaptation and transmission of influenza A viruses in mammalsInfluenza A virus infections in swine: pathogenesis and diagnosis.Protective immunity to H7N9 influenza viruses elicited by synthetic DNA vaccine.H7N9: A killer in the making or a false alarm?Molecular determinants of influenza virus pathogenesis in mice.Mutations associated with severity of the pandemic influenza A(H1N1)pdm09 in humans: a systematic review and meta-analysis of epidemiological evidence.One-way trip: influenza virus' adaptation to gallinaceous poultry may limit its pandemic potential.Detection and Characterization of Clade 1 Reassortant H5N1 Viruses Isolated from Human Cases in Vietnam during 2013The Neuraminidase Stalk Deletion Serves as Major Virulence Determinant of H5N1 Highly Pathogenic Avian Influenza Viruses in Chicken.Introduction of virulence markers in PB2 of pandemic swine-origin influenza virus does not result in enhanced virulence or transmission.Novel Highly Pathogenic Avian H5 Influenza A Viruses in Live Poultry Markets, Wuxi City, China, 2013-2014.Virulence-associated substitution D222G in the hemagglutinin of 2009 pandemic influenza A(H1N1) virus affects receptor binding.Transforming growth factor-β: activation by neuraminidase and role in highly pathogenic H5N1 influenza pathogenesis.Characterization of neuraminidases from the highly pathogenic avian H5N1 and 2009 pandemic H1N1 influenza A viruses.Genetic evolution of low pathogenecity H9N2 avian influenza viruses in Tunisia: acquisition of new mutations.The 2009 pandemic H1N1 virus induces anti-neuraminidase (NA) antibodies that cross-react with the NA of H5N1 viruses in ferretsH5N1 pathogenesis studies in mammalian models.Highly pathogenic H5N1 influenza viruses carry virulence determinants beyond the polybasic hemagglutinin cleavage site.A genetically engineered waterfowl influenza virus with a deletion in the stalk of the neuraminidase has increased virulence for chickens.Glycosylation site alteration in the evolution of influenza A (H1N1) viruses.Single-domain antibodies targeting neuraminidase protect against an H5N1 influenza virus challenge.Avian influenza H7N9/13 and H7N7/13: a comparative virulence study in chickens, pigeons, and ferrets.Prediction of biological functions on glycosylation site migrations in human influenza H1N1 virusesPB2 and hemagglutinin mutations are major determinants of host range and virulence in mouse-adapted influenza A virusHuman infection with highly pathogenic A(H7N7) avian influenza virus, Italy, 2013.The evolutionary pattern of glycosylation sites in influenza virus (H5N1) hemagglutinin and neuraminidase.Feasibility of reconstructed ancestral H5N1 influenza viruses for cross-clade protective vaccine development.Identification of critical residues of influenza neuraminidase in viral particle release.Influenza A virus nucleoprotein selectively decreases neuraminidase gene-segment packaging while enhancing viral fitness and transmissibility.Characterization of a novel reassortant influenza A virus (H2N2) from a domestic duck in Eastern China.Epidemiological and viral genome characteristics of the first human H7N9 influenza infection in Guangdong Province, ChinaCould a deletion in neuraminidase stalk strengthen human tropism of the novel avian influenza virus H7N9 in China, 2013?Structural analysis of the novel influenza A (H7N9) viral Neuraminidase interactions with current approved neuraminidase inhibitors Oseltamivir, Zanamivir, and Peramivir in the presence of mutation R289KA 20-amino-acid deletion in the neuraminidase stalk and a five-amino-acid deletion in the NS1 protein both contribute to the pathogenicity of H5N1 avian influenza viruses in mallard ducksLipidWrapper: an algorithm for generating large-scale membrane models of arbitrary geometryGalectin-1 binds to influenza virus and ameliorates influenza virus pathogenesis.
P2860
Q21091069-45C7E6AF-B9A7-4E53-822D-131F440FF55DQ27025880-11496D01-D744-4A42-8C10-1C3DFE921747Q28386118-B1920126-29F4-48E4-AD00-2792E98B921CQ28390168-68CE2C1C-3BB7-4CF6-BEEA-8907EFDAEFA2Q28397046-3817025A-C559-43EA-8E3D-35750B51C348Q30357141-30D0CFD3-C687-4A87-9748-DEF362F0677DQ30360232-EED8CBFB-8E7B-4BB3-81CB-E2C74D88D261Q30363225-798DF55B-F1ED-462A-9F4C-FFD8DA067DA7Q30364868-817908DA-469D-41E1-85D0-4AC0CBAD95F2Q30365296-94062E08-A292-4709-BB57-A0920ECD3C81Q30370246-F7BC320B-CD31-4C6D-92A4-E433D07B464EQ30377552-45CDA61E-3E2C-4C86-9C26-86742F76CFD9Q30378364-56CA5FAD-457F-4A3C-9050-0FD4FB3BCADCQ30385332-82F0770D-F523-4574-B1CC-9E1067C6C33CQ30388133-4AD9E038-46FF-4E09-9848-0051632784F9Q30393671-02C7F710-95D7-4467-930A-06B79189EF4CQ30394903-617B4D00-B898-4B0F-96A4-ECD975D3F332Q30398292-1908CCF7-CE2E-40C2-9A38-4106C50D6285Q30408051-D89E1F12-4951-4CF6-8092-DD7ADCB8AFFBQ30413023-2B37C464-8DED-4E0F-BF45-57B382C3BB3DQ30427806-6D9FCD58-7A73-4350-9ED5-55E296FF005AQ30986632-B637636B-3F3B-49E0-9790-CDB2D634BB41Q33558443-4902815F-42FB-44CB-B337-3DEE29A8BBC3Q33987971-7D442EBF-384F-4FE5-AE8A-5108EEE95BE6Q34057785-50D9C91A-A4B7-470D-AA38-97A98BA1F0FBQ34059130-D794D67B-5D8D-4ED3-BF9D-C86172D54221Q34166548-7E0B331A-5128-454B-A69B-EF6E47B5D0CDQ34178176-D0AE8209-010D-4549-8FF7-E4CCC14665BAQ34320476-A5943472-F868-4237-9789-65A6CFCB3356Q34469957-30AE5ACA-21F9-42EF-B956-4EB6872B2ECDQ34472018-18CAEEC1-EAE4-4E2F-9DCC-3CE5EE735FF6Q34552726-3ADBDE19-135F-4586-AEDB-F727B33CCF0DQ34601394-FE17DE85-9D35-4237-9EF5-A9BC4F4CBD7EQ34760846-40A931FA-F7FA-49CB-B3A6-C380576F23C4Q34814431-A99EE76F-A41B-4114-9EBD-BE8C5512F39DQ35015239-D2D4F2DB-177B-4273-9168-6169D719565FQ35101694-2110AF64-BA7E-4D90-BBF4-6F6533FF9FABQ35151564-6ED48258-E571-4904-AC27-1EC09426FA6AQ35208080-B2C2586A-5D10-4E39-91CE-77D2CC19B775Q35383245-01F1E9F8-C365-48B5-9E5F-BAEA23EC4B0A
P2860
Neuraminidase stalk length and additional glycosylation of the hemagglutinin influence the virulence of influenza H5N1 viruses for mice
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on 18 February 2009
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Neuraminidase stalk length and ...... nfluenza H5N1 viruses for mice
@en
Neuraminidase stalk length and ...... fluenza H5N1 viruses for mice.
@nl
type
label
Neuraminidase stalk length and ...... nfluenza H5N1 viruses for mice
@en
Neuraminidase stalk length and ...... fluenza H5N1 viruses for mice.
@nl
prefLabel
Neuraminidase stalk length and ...... nfluenza H5N1 viruses for mice
@en
Neuraminidase stalk length and ...... fluenza H5N1 viruses for mice.
@nl
P2093
P2860
P50
P356
P1433
P1476
Neuraminidase stalk length and ...... nfluenza H5N1 viruses for mice
@en
P2093
Christine Warnes
Colleen Thomas
Melanie Altholtz
Yumiko Matsuoka
P2860
P304
P356
10.1128/JVI.01987-08
P407
P577
2009-02-18T00:00:00Z