Inhibition of neuraminidase activity by derivatives of 2-deoxy-2,3-dehydro-N-acetylneuraminic acid.
about
Existing antivirals are effective against influenza viruses with genes from the 1918 pandemic virus.Infectivities of human and other primate lentiviruses are activated by desialylation of the virion surfaceParainfluenza virusesPeramivir (BCX-1812, RWJ-270201): potential new therapy for influenzaRWJ-270201 (BCX-1812): a novel neuraminidase inhibitor for influenzaThe anti-influenza virus agent 4-GU-DANA (zanamivir) inhibits cell fusion mediated by human parainfluenza virus and influenza virus HA.Novel alpha- and beta-amino acid inhibitors of influenza virus neuraminidase4-Guanidino-2,4-dideoxy-2,3-dehydro-N-acetylneuraminic acid is a highly effective inhibitor both of the sialidase (neuraminidase) and of growth of a wide range of influenza A and B viruses in vitroParallel screening of wild-type and drug-resistant targets for anti-resistance neuraminidase inhibitorsExploring the chemical space of influenza neuraminidase inhibitorsDrug resistance in influenza A virus: the epidemiology and management.Progress of small molecular inhibitors in the development of anti-influenza virus agents.Impact of neuraminidase inhibitors on influenza A(H1N1)pdm09-related pneumonia: an individual participant data meta-analysis.ANTIVIRAL COMPOUNDS IN THE PIPELINE TO TACKLE H1N1 INFLUENZA INFECTION.Progress in structure-based drug design against influenza A virus.Neuraminidase inhibitors for influenza: a review and public health perspective in the aftermath of the 2009 pandemic.Recent progress and challenges in the discovery of new neuraminidase inhibitors.Approaches and strategies for the treatment of influenza virus infections.A strategy for neuraminidase inhibitors using mechanism-based labeling information.Mutation of neuraminidase cysteine residues yields temperature-sensitive influenza viruses.A single amino acid alteration in the human parainfluenza virus type 3 hemagglutinin-neuraminidase glycoprotein confers resistance to the inhibitory effects of zanamivir on receptor binding and neuraminidase activity.Emerging antiviral resistant strains of influenza A and the potential therapeutic targets within the viral ribonucleoprotein (vRNP) complex.Influenza virus neuraminidase: structure, antibodies, and inhibitors.Specific inhibition of Trypanosoma cruzi neuraminidase by the human plasma glycoprotein "cruzin".Neuraminidase-Dependent Degradation of Polysialic Acid Is Required for the Lamination of Newly Generated Neurons.Development of antivirals against influenza.Studies on cell adhesion and recognition. II. The kinetics of cell adhesion and cell spreading on surfaces coated with carbohydrate-reactive proteins (glycosidases and lectins) and fibronectin.Studies on cell adhesion and recognition. I. Extent and specificity of cell adhesion triggered by carbohydrate-reactive proteins (glycosidases and lectins) and by fibronectin.Molecular forms of N-CAM and its RNA in developing and denervated skeletal muscle.A cell-free assay for the insertion of a viral glycoprotein into the plasma membrane.Lectin receptors as markers for Trypanosoma cruzi. Developmental stages and a study of the interaction of wheat germ agglutinin with sialic acid residues on epimastigote cellsBiological consequences of neuraminidase deficiency in Newcastle disease virus.Molecular aspects of immunoglobulin A1 degradation by oral streptococciVirulence factors of influenza A viruses: WSN virus neuraminidase required for plaque production in MDBK cells.Inhibition of parainfluenza virus type 3 and Newcastle disease virus hemagglutinin-neuraminidase receptor binding: effect of receptor avidity and steric hindrance at the inhibitor binding sites.Influenza neuraminidase: a druggable target for natural products.Trypanosoma cruzi trans-sialidase as a drug target against Chagas disease (American trypanosomiasis).Application of virus-like particles (VLP) to NMR characterization of viral membrane protein interactions.Biological roles of glycans.Relationship between hemagglutinin and sialidase from Clostridium perfringens CN3870: chromatographic characterization of the biologically active proteins.
P2860
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P2860
Inhibition of neuraminidase activity by derivatives of 2-deoxy-2,3-dehydro-N-acetylneuraminic acid.
description
1974 nî lūn-bûn
@nan
1974 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
1974 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
1974年の論文
@ja
1974年論文
@yue
1974年論文
@zh-hant
1974年論文
@zh-hk
1974年論文
@zh-mo
1974年論文
@zh-tw
1974年论文
@wuu
name
Inhibition of neuraminidase ac ...... hydro-N-acetylneuraminic acid.
@ast
Inhibition of neuraminidase ac ...... hydro-N-acetylneuraminic acid.
@en
Inhibition of neuraminidase ac ...... hydro-N-acetylneuraminic acid.
@nl
type
label
Inhibition of neuraminidase ac ...... hydro-N-acetylneuraminic acid.
@ast
Inhibition of neuraminidase ac ...... hydro-N-acetylneuraminic acid.
@en
Inhibition of neuraminidase ac ...... hydro-N-acetylneuraminic acid.
@nl
prefLabel
Inhibition of neuraminidase ac ...... hydro-N-acetylneuraminic acid.
@ast
Inhibition of neuraminidase ac ...... hydro-N-acetylneuraminic acid.
@en
Inhibition of neuraminidase ac ...... hydro-N-acetylneuraminic acid.
@nl
P2093
P1433
P1476
Inhibition of neuraminidase ac ...... hydro-N-acetylneuraminic acid.
@en
P2093
P304
P356
10.1016/0042-6822(74)90080-4
P407
P50
P577
1974-04-01T00:00:00Z