Genetically destined potentials for N-linked glycosylation of influenza virus hemagglutinin.
about
Predicting the antigenic structure of the pandemic (H1N1) 2009 influenza virus hemagglutininShort linear motifs - ex nihilo evolution of protein regulationAntigenically intact hemagglutinin in circulating avian and swine influenza viruses and potential for H3N2 pandemic.Playing hide and seek: how glycosylation of the influenza virus hemagglutinin can modulate the immune response to infection.Genetic analysis of post-pandemic 2010-2011 influenza A(H1N1)pdm09 hemagglutinin virus variants that caused mild, severe, and fatal infections in Northern Greece.Genomic reassortants of pandemic A (H1N1) 2009 virus and endemic porcine H1 and H3 viruses in swine in Japan.Isolation and complete genomic characterization of H1N1 subtype swine influenza viruses in southern China through the 2009 pandemic.Genetic characterization of swine influenza viruses (H3N2) isolated from Minnesota in 2006-2007.Molecular and antigenic characterization of reassortant H3N2 viruses from turkeys with a unique constellation of pandemic H1N1 internal genes.Glycosylation on hemagglutinin affects the virulence and pathogenicity of pandemic H1N1/2009 influenza A virus in miceGenetic diversity of HA1 domain of heammaglutinin gene of influenza A(H1N1)pdm09 in Tunisia.Glycosylations in the globular head of the hemagglutinin protein modulate the virulence and antigenic properties of the H1N1 influenza virusesGlycosylation focuses sequence variation in the influenza A virus H1 hemagglutinin globular domain.Glycosylation site alteration in the evolution of influenza A (H1N1) viruses.Prediction of biological functions on glycosylation site migrations in human influenza H1N1 virusesProtein clustering and RNA phylogenetic reconstruction of the influenza A [corrected] virus NS1 protein allow an update in classification and identification of motif conservation.Immune escape mutants of Highly Pathogenic Avian Influenza H5N1 selected using polyclonal sera: identification of key amino acids in the HA proteinGlycosylation at Asn91 of H1N1 haemagglutinin affects binding to glycan receptors.Complete Genome Sequences of Six Avian-Like H1N1 Swine Influenza Viruses from Northwestern China.Correlating novel variable and conserved motifs in the Hemagglutinin protein with significant biological functions.Cell-surface receptors on macrophages and dendritic cells for attachment and entry of influenza virus.Structural insights into key sites of vulnerability on HIV-1 Env and influenza HA.A Perspective on the Structural and Functional Constraints for Immune Evasion: Insights from Influenza Virus.Highly pathogenic avian influenza (H5N1) in Nigeria in 2015: evidence of widespread circulation of WA2 clade 2.3.2.1c.Genetic characterization and evolution of H1N1pdm09 after circulation in a swine farm.Evidence for N-glycan shielding of antigenic sites during evolution of human influenza A virus hemagglutininUse of host-like peptide motifs in viral proteins is a prevalent strategy in host-virus interactions.Molecular analysis of influenza A H1N1pdm09 virus circulating in Madhya Pradesh, India in the year 2017
P2860
Q21562628-458CCC3B-B1DF-40B5-A94E-BF8CAA5274D5Q26863643-1196062B-DC98-4CC1-AF68-D433BD17E82AQ30223015-CCA1C4E5-889D-4CFE-8F5D-6149D6847135Q30360290-92CA1C59-A743-4E35-B6E4-7CDBB5A9E1AEQ30363285-BC028F71-9A59-44DF-9C27-AE034DE3070FQ30365051-D04FB0E1-D69F-43C8-9495-3534269A2466Q30400921-FCFB2C8A-1E76-4D02-B011-C5887CCF60B1Q30403039-5EC51DDF-90CB-4878-B0A4-8A0C04B5952FQ30414913-35E1183C-CAC2-4DA8-8AC9-79EDB5D9BA3FQ30430049-4B4889DD-DA4F-4446-8A12-92D2DD98F1CCQ30430619-E3DDC4F1-AE3A-49E8-8657-C50E4DFFE600Q30431220-CEDEB7CC-A81A-4702-B748-48705C905EB1Q33760809-50609795-59F1-40AC-9AA0-A41105166963Q33987971-7EF1EE8B-3FC6-4191-B4E9-ABA39ADE7485Q34166548-C7D2E44A-B867-4EA3-A596-229E301862F6Q34718021-EA2B80C6-5439-4F7D-A4D1-7659FDC8C636Q35105831-1E347940-7F20-4979-9A4B-307EC421950AQ36029870-95879586-1CB3-4432-AF60-0AEEEF301F70Q36601132-DFB80384-A1D7-47E7-B7B2-72CF17EB8199Q36908267-8EB230DD-5DEC-434C-BCCE-5382AEFD021EQ37962296-B3860BBC-A1BB-4D6E-87D6-26EF91F1690AQ38050485-16AD189A-4772-4ED7-8E3A-544935D7C2DAQ39397313-02F828B8-1A4B-4298-BF0E-BE613A39AF34Q40462918-7DCA8CCE-16E9-46C7-9383-A290B94A1D9EQ42038402-AD2D9B8B-D715-4D4A-8FD8-B5C92B1B68C1Q42145923-42F06699-54E6-45F3-A58C-5E9ABC6A7D03Q42215545-CAE801BE-A19D-424E-89B5-BD66155D1EF3Q56556483-E478584D-5295-454B-9361-AE27201D7FE0
P2860
Genetically destined potentials for N-linked glycosylation of influenza virus hemagglutinin.
description
2008 nî lūn-bûn
@nan
2008 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2008 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
name
Genetically destined potential ...... influenza virus hemagglutinin.
@ast
Genetically destined potential ...... influenza virus hemagglutinin.
@en
type
label
Genetically destined potential ...... influenza virus hemagglutinin.
@ast
Genetically destined potential ...... influenza virus hemagglutinin.
@en
prefLabel
Genetically destined potential ...... influenza virus hemagglutinin.
@ast
Genetically destined potential ...... influenza virus hemagglutinin.
@en
P2093
P1433
P1476
Genetically destined potential ...... influenza virus hemagglutinin.
@en
P2093
Ayato Takada
Hiroshi Kida
Kimihito Ito
Manabu Igarashi
P304
P356
10.1016/J.VIROL.2008.03.036
P407
P577
2008-05-05T00:00:00Z