Neuraminidase is important for the initiation of influenza virus infection in human airway epithelium. - Wikidata - awgldk - TriplyDB

Neuraminidase is important for the initiation of influenza virus infection in human airway epithelium.

Neuraminidase is important for the initiation of influenza virus infection in human airway epithelium.

http://www.wikidata.org/entity/Q37596932

about

Neuraminidase inhibitors for the treatment of influenza infection in people with cystic fibrosis Neuraminidase inhibitors for the treatment of influenza infection in people with cystic fibrosis Neuraminidase inhibitors for preventing and treating influenza in healthy adults and children Neuraminidase inhibitors for preventing and treating influenza in healthy adults and children - a review of clinical study reports Neuraminidase inhibitors for the treatment of influenza infection in people with cystic fibrosis Neuraminidase inhibitors for the treatment of influenza infection in people with cystic fibrosis Entry of parainfluenza virus into cells as a target for interrupting childhood respiratory disease The biology of influenza viruses Influenza A virus neuraminidase limits viral superinfection Current and future antiviral therapy of severe seasonal and avian influenza Safety, efficacy, and immunogenicity of Flublok in the prevention of seasonal influenza in adults Optimal Use of Vaccines for Control of Influenza A Virus in Swine Glycotherapy: new advances inspire a reemergence of glycans in medicine Broad-Spectrum Drugs Against Viral Agents Structural Characterization of the 1918 Influenza Virus H1N1 Neuraminidase Influenza Virus Neuraminidases with Reduced Enzymatic Activity That Avidly Bind Sialic Acid Receptors Inﬂuenza and Memory T Cells: How to Awake the Force New small-molecule drug design strategies for fighting resistant influenza A The M segment of the 2009 pandemic influenza virus confers increased neuraminidase activity, filamentous morphology, and efficient contact transmissibility to A/Puerto Rico/8/1934-based reassortant viruses Molecular basis for broad neuraminidase immunity: conserved epitopes in seasonal and pandemic H1N1 as well as H5N1 influenza viruses The short stalk length of highly pathogenic avian influenza H5N1 virus neuraminidase limits transmission of pandemic H1N1 virus in ferrets Pandemic Swine H1N1 Influenza Viruses with Almost Undetectable Neuraminidase Activity Are Not Transmitted via Aerosols in Ferrets and Are Inhibited by Human Mucus but Not Swine Mucus Bacterial neuraminidase rescues influenza virus replication from inhibition by a neuraminidase inhibitor Comparison of mutation patterns in full-genome A/H3N2 influenza sequences obtained directly from clinical samples and the same samples after a single MDCK passage Identification of traditional medicinal plant extracts with novel anti-influenza activity Expression and Characterization of Recombinant, Tetrameric and Enzymatically Active Influenza Neuraminidase for the Setup of an Enzyme-Linked Lectin-Based Assay Exploring cell tropism as a possible contributor to influenza infection severity A miniaturized assay for influenza neuraminidase-inhibiting antibodies utilizing reverse genetics-derived antigens Oseltamivir (Tamiflu(®)) in the environment, resistance development in influenza A viruses of dabbling ducks and the risk of transmission of an oseltamivir-resistant virus to humans - a review Influenza virus neuraminidase (NA): a target for antivirals and vaccines.Sialidase activity of influenza A virus in an endocytic pathway enhances viral replication.Tracking oseltamivir-resistance in New Zealand influenza viruses during a medicine reclassification in 2007, a resistant-virus importation in 2008 and the 2009 pandemic.Restricted infectivity of a human-Lineage H3N2 influenza A virus in pigs is hemagglutinin and neuraminidase gene dependent.Molecular epidemiology of influenza A virus infection in Cyprus in four consecutive seasons (2009 pandemic-2013).In vitro activity of favipiravir and neuraminidase inhibitor combinations against oseltamivir-sensitive and oseltamivir-resistant pandemic influenza A (H1N1) virus.New vaccines against influenza virus.Upconversion luminescence resonance energy transfer (LRET)-based biosensor for rapid and ultrasensitive detection of avian influenza virus H7 subtype.One-way trip: influenza virus' adaptation to gallinaceous poultry may limit its pandemic potential.Influenza viruses with receptor-binding N1 neuraminidases occur sporadically in several lineages and show no attenuation in cell culture or mice.Oseltamivir-resistant influenza A viruses are transmitted efficiently among guinea pigs by direct contact but not by aerosol.

P2860

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P2860

Neuraminidase is important for the initiation of influenza virus infection in human airway epithelium.

http://www.wikidata.org/entity/Q37596932

description

2004 nî lūn-bûn

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2004年の論文

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2004年学术文章

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2004年学术文章

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2004年学术文章

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2004年學術文章

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2004年學術文章

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2004年學術文章

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name

Neuraminidase is important for ...... on in human airway epithelium.

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Neuraminidase is important for ...... on in human airway epithelium.

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Neuraminidase is important for ...... on in human airway epithelium.

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Neuraminidase is important for ...... on in human airway epithelium.

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Neuraminidase is important for ...... on in human airway epithelium.

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Neuraminidase is important for ...... on in human airway epithelium.

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P1433

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P356

JVI.78.22.12665-12667.2004

P1433

Journal of Virology

P1476

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P2093

Mikhail N Matrosovich

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Noel A Roberts

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Tatyana Y Matrosovich

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Thomas Gray

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P2860

Avian influenza A virus (H7N7) associated with human conjunctivitis and a fatal case of acute respiratory distress syndrome

Are we ready for pandemic influenza?

Human and avian influenza viruses target different cell types in cultures of human airway epithelium.

Anti-influenza drugs and neuraminidase inhibitors.

Position statement: global neuraminidase inhibitor susceptibility network.

The neuraminidase of influenza virus.

Influenza virus carrying neuraminidase with reduced sensitivity to oseltamivir carboxylate has altered properties in vitro and is compromised for infectivity and replicative ability in vivo.

P304

12665-12667

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scholarly article

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10.1128/JVI.78.22.12665-12667.2004

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22

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78

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Hans-Dieter Klenk

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2004-11-01T00:00:00Z

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15507653

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525087

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