N-linked glycosylation attenuates H3N2 influenza viruses.
about
Serum amyloid P is a sialylated glycoprotein inhibitor of influenza A virusesConnecting the study of wild influenza with the potential for pandemic diseaseInnate immunity to influenza virus: implications for future therapyRecognition of Mannosylated Ligands and Influenza A Virus by Human Surfactant Protein D: Contributions of an Extended Site and Residue 343 † , ‡Molecular Mechanisms of Inhibition of Influenza by Surfactant Protein D Revealed by Large-Scale Molecular Dynamics SimulationStructure and receptor binding preferences of recombinant human A(H3N2) virus hemagglutininsElucidating the mechanisms of influenza virus recognition by Ncr1Evolution of H3N2 influenza virus in a guinea pig modelPlaying hide and seek: how glycosylation of the influenza virus hemagglutinin can modulate the immune response to infection.Molecular determinants of influenza virus pathogenesis in mice.Influenza A(H1N1)pdm09 resistance and cross-decreased susceptibility to oseltamivir and zanamivir antiviral drugs.Role of viral hemagglutinin glycosylation in anti-influenza activities of recombinant surfactant protein DAcute Lung Injury Results from Innate Sensing of Viruses by an ER Stress PathwayGlycans on influenza hemagglutinin affect receptor binding and immune responseThe effects of influenza A virus PB1-F2 protein on polymerase activity are strain specific and do not impact pathogenesisDoes Glycosylation as a modifier of Original Antigenic Sin explain the case age distribution and unusual toxicity in pandemic novel H1N1 influenza?Neuraminidase Activity and Resistance of 2009 Pandemic H1N1 Influenza Virus to Antiviral Activity in Bronchoalveolar FluidPB1-F2 proteins from H5N1 and 20 century pandemic influenza viruses cause immunopathology.Glycosylation changes in the globular head of H3N2 influenza hemagglutinin modulate receptor binding without affecting virus virulenceGlycan shielding of the influenza virus hemagglutinin contributes to immunopathology in mice.Recent H3N2 Viruses Have Evolved Specificity for Extended, Branched Human-type Receptors, Conferring Potential for Increased Avidity.Pandemic influenza 1918 H1N1 and 1968 H3N2 DNA vaccines induce cross-reactive immunity in ferrets against infection with viruses drifted for decades.The ability of pandemic influenza virus hemagglutinins to induce lower respiratory pathology is associated with decreased surfactant protein D bindingPreventing and treating secondary bacterial infections with antiviral agentsMutagenesis of surfactant protein D informed by evolution and x-ray crystallography enhances defenses against influenza A virus in vivoImpaired wound healing predisposes obese mice to severe influenza virus infection.Molecular and antigenic characterization of reassortant H3N2 viruses from turkeys with a unique constellation of pandemic H1N1 internal genes.A novel pathogenic mechanism of highly pathogenic avian influenza H5N1 viruses involves hemagglutinin mediated resistance to serum innate inhibitors.Immunodominance of antigenic site B over site A of hemagglutinin of recent H3N2 influenza viruses.N-linked glycosylation in the hemagglutinin of influenza A viruses.Glycosylations in the globular head of the hemagglutinin protein modulate the virulence and antigenic properties of the H1N1 influenza virusesFatal cases of influenza A(H3N2) in children: insights from whole genome sequence analysis.Changing selective pressure during antigenic changes in human influenza H3.The Length of N-Glycans of Recombinant H5N1 Hemagglutinin Influences the Oligomerization and Immunogenicity of Vaccine AntigenDynamics of glycoprotein charge in the evolutionary history of human influenzaStrength and tempo of selection revealed in viral gene genealogies.Glycosylation site alteration in the evolution of influenza A (H1N1) viruses.Characterization of Variations in PB2, NS1, M, Neuraminidase and Hemagglutinin of Influenza A (H3N2) Viruses in IranMonoclonal antibody-assisted structure-function analysis of the carbohydrate recognition domain of surfactant protein DMolecular characterization of influenza viruses collected from young children in Uberlandia, Brazil - from 2001 to 2010.
P2860
Q24337745-46CF1A26-5DBB-451D-9139-64A78F8C2C0AQ27027237-E87379D9-338E-4667-9E20-7C217919F22DQ27489605-388EDB85-9CCE-46E9-9967-60FC14E81A73Q27653971-5338525D-7CB8-4F93-8E0E-AC6272691396Q27680598-D681C5C5-63F7-48DA-85E6-3623DD850110Q27697647-55A7F1E5-FDA0-40EA-B0E9-802A4B60CC4BQ28586365-F514EDAC-5F0C-4676-A169-88DD99991843Q28742283-1D50FF83-7D50-4C8A-AC7A-C2438FE3F4E1Q30360290-80916F9E-D3EC-4762-8725-47A855BB3352Q30364868-A4B7885B-94A0-45C1-AA29-67C7AA72EEC4Q30364892-76C7D9D4-0E08-4459-9E70-59A0BD791F1EQ30372223-F5426A6F-FAA5-41ED-AE36-A973CD1148FFQ30375413-BE0375DA-D3C3-4213-AA20-8CF2A3E8C462Q30381577-A1CB8CCD-0D8C-46AD-A05C-2E2D36D9D760Q30381642-6BCFDD65-8540-4526-A5B0-E0700B0863CFQ30384213-29C9D235-85B5-4351-B281-E7DB00018BF1Q30384874-8A3CF3A2-10ED-409D-841E-AEC89E8D7BC7Q30391867-982FE7F5-52A2-4F62-A127-7DC35A51F97AQ30394678-723FFF68-0EA9-4536-BEE3-04B9ABEBF9E6Q30394731-4B10233B-6B69-43D6-93D8-95540049DF7AQ30396804-81FF820F-6E4D-4B2B-9013-4860F46C68E8Q30397107-E0BCC21C-5749-40EA-BE49-A22B83F489D9Q30399889-D1DCEE71-44C8-4401-AC53-AA21BCC35F85Q30401260-419AF81A-A928-45C8-B957-D7F87E8BE009Q30407670-D68594EB-64D7-477F-BB37-5E4FF615E339Q30410362-F68080B3-7EF7-4B05-B0CC-32EF8637530EQ30414913-78CD133E-3FEB-41C6-B79E-292FF195AB44Q30416451-626B3287-EA05-4E13-AAAE-5A2B8C18EA43Q30419865-F928EB4E-8C93-425D-BD22-C7D4065CE084Q30420126-09BF83E6-5AAF-40FC-AC36-5E4BB610805EQ30431220-E678011E-E15E-48DB-BDBB-7BB064B1A35BQ31050886-65397899-0BE6-4B9D-AF97-FDE791E9A9FCQ33331398-0FA3D5D9-6DB5-4A79-A686-E2EC38DEF587Q33580863-274BC26E-2BC0-4679-8E41-A5F20C302C70Q33786867-5BC9E056-0FF0-4322-8FBB-B031E2BADF2FQ33970459-7BED93C5-E0D6-4E88-9612-71957EF3CD7AQ33987971-BBA6CDAD-529F-46DA-AFB1-D43BEB8C09F8Q34068624-564E8A98-7DDC-4669-82DF-4B0A5AA3801DQ34180763-852C79AB-5ECA-4965-B4C9-3D89D42A360FQ35108539-694468A8-7857-45AA-8408-371D6B4A7A27
P2860
N-linked glycosylation attenuates H3N2 influenza viruses.
description
2007 nî lūn-bûn
@nan
2007年の論文
@ja
2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
@zh-mo
2007年論文
@zh-tw
2007年论文
@wuu
2007年论文
@zh
2007年论文
@zh-cn
name
N-linked glycosylation attenuates H3N2 influenza viruses.
@ast
N-linked glycosylation attenuates H3N2 influenza viruses.
@en
type
label
N-linked glycosylation attenuates H3N2 influenza viruses.
@ast
N-linked glycosylation attenuates H3N2 influenza viruses.
@en
prefLabel
N-linked glycosylation attenuates H3N2 influenza viruses.
@ast
N-linked glycosylation attenuates H3N2 influenza viruses.
@en
P2093
P2860
P356
P1433
P1476
N-linked glycosylation attenuates H3N2 influenza viruses.
@en
P2093
David J Vigerust
Jens Madsen
Kelli L Boyd
Kimberly B Ulett
Samuel Hawgood
P2860
P304
P356
10.1128/JVI.00769-07
P407
P577
2007-06-06T00:00:00Z