Novel sialic acid derivatives lock open the 150-loop of an influenza A virus group-1 sialidase. - Wikidata - wikimedia - TriplyDB

Novel sialic acid derivatives lock open the 150-loop of an influenza A virus group-1 sialidase.

Novel sialic acid derivatives lock open the 150-loop of an influenza A virus group-1 sialidase.

http://www.wikidata.org/entity/Q27665921

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Recent progress in structure-based anti-influenza drug design Influenza A Virus N5 Neuraminidase Has an Extended 150-Cavity Structural and functional characterization of neuraminidase-like molecule N10 derived from bat influenza A virus Crystal structures of two subtype N10 neuraminidase-like proteins from bat influenza A viruses reveal a diverged putative active site H1N1 2009 Pandemic Influenza Virus: Resistance of the I223R Neuraminidase Mutant Explained by Kinetic and Structural Analysis Structural and Functional Analysis of Laninamivir and its Octanoate Prodrug Reveals Group Specific Mechanisms for Influenza NA Inhibition Induced opening of influenza virus neuraminidase N2 150-loop suggests an important role in inhibitor binding Structural basis for a class of nanomolar influenza A neuraminidase inhibitors Flavin-Dependent Thymidylate Synthase as a Drug Target for Deadly Microbes: Mutational Study and a Strategy for Inhibitor Design Synthesis and evaluation of novel 3-C-alkylated-Neu5Ac2en derivatives as probes of influenza virus sialidase 150-loop flexibility Structure of Influenza Virus N7: the Last Piece of the Neuraminidase"Jigsaw"Puzzle Serendipitous discovery of a potent influenza virus a neuraminidase inhibitor Synthesis, structure and inhibitory activity of a stereoisomer of oseltamivir carboxylate New small-molecule drug design strategies for fighting resistant influenza A Plasticity of 150-loop in influenza neuraminidase explored by Hamiltonian replica exchange molecular dynamics simulations The influence of 150-cavity binders on the dynamics of influenza A neuraminidases as revealed by molecular dynamics simulations and combined clustering Locking the 150-cavity open: in silico design and verification of influenza neuraminidase inhibitors Interface dynamics explain assembly dependency of influenza neuraminidase catalytic activity.From neuraminidase inhibitors to conjugates: a step towards better anti-influenza drugs?Mechanism of 150-cavity formation in influenza neuraminidase.Molecular-level simulation of pandemic influenza glycoproteins.Recent advances in neuraminidase inhibitor development as anti-influenza drugs.Variable ligand- and receptor-binding hot spots in key strains of influenza neuraminidase.Combinatorial effect of two framework mutations (E119V and I222L) in the neuraminidase active site of H3N2 influenza virus on resistance to oseltamivir Discovery and Characterization of Diazenylaryl Sulfonic Acids as Inhibitors of Viral and Bacterial Neuraminidases.Influenza neuraminidase: a druggable target for natural products.Learning from structure-based drug design and new antivirals targeting the ribonucleoprotein complex for the treatment of influenza.Zwitterionic structures: from physicochemical properties toward computer-aided drug designs.Synthesis and evaluation of influenza A viral neuraminidase candidate inhibitors based on a bicyclo[3.1.0]hexane scaffold.Identification of neuraminidase inhibitors against dual H274Y/I222R mutant strains.Mutation effects of neuraminidases and their docking with ligands: a molecular dynamics and free energy calculation study.Atypical group 1 neuraminidase pH1N1-N1 bound to a group 1 inhibitor.[The flexibility of the protein neuraminidase opens new possibilities for drug development].Synthesis of acylguanidine zanamivir derivatives as neuraminidase inhibitors and the evaluation of their bio-activities.Influenza glycoproteins: Hemagglutinin and neuraminidase A Critical Prospect of Structural Designing of Avian Influenza A/H5N1 Neuraminidase Inhibitors That Evade Tamiflu Resistance

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Novel sialic acid derivatives lock open the 150-loop of an influenza A virus group-1 sialidase.

http://www.wikidata.org/entity/Q27665921

description

2010 nî lūn-bûn

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2010 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

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2010 թվականի նոյեմբերին հրատարակված գիտական հոդված

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2010年の論文

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2010年論文

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2010年論文

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2010年論文

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2010年論文

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2010年論文

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2010年论文

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name

Novel sialic acid derivatives ...... enza A virus group-1 sialidase

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Novel sialic acid derivatives ...... nza A virus group-1 sialidase.

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Novel sialic acid derivatives ...... nza A virus group-1 sialidase.

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Novel sialic acid derivatives ...... enza A virus group-1 sialidase

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Novel sialic acid derivatives ...... nza A virus group-1 sialidase.

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Novel sialic acid derivatives ...... enza A virus group-1 sialidase

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Novel sialic acid derivatives ...... nza A virus group-1 sialidase.

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Novel sialic acid derivatives ...... nza A virus group-1 sialidase.

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Nature Communications

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Novel sialic acid derivatives ...... nza A virus group-1 sialidase.

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P2093

Faith J Rose

http://www.w3.org/2001/XMLSchema#string

Jeffrey C Dyason

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Mark von Itzstein

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Philip S Kerry

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Rupert J M Russell

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Santosh Rudrawar

http://www.w3.org/2001/XMLSchema#string

P2860

New low-viscosity overlay medium for viral plaque assays

Improved methods for building protein models in electron density maps and the location of errors in these models

The 2009 pandemic H1N1 neuraminidase N1 lacks the 150-cavity in its active site

Coot: model-building tools for molecular graphics

SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling

The finer things in X-ray diffraction data collection

PHENIX: building new software for automated crystallographic structure determination

The CCP4 suite: programs for protein crystallography

The war against influenza: discovery and development of sialidase inhibitors

Automated docking of flexible ligands: applications of AutoDock

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113

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scholarly article

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10.1038/NCOMMS1114

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P433

8

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1

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Marie-Anne Rameix-Welti

Sylvie van der Werf

Robin J. Thomson

Sylvie van der Werf

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2010-11-16T00:00:00Z

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47809402

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1006947378

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21081911

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3060605

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