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Influenza A Virus N5 Neuraminidase Has an Extended 150-Cavity

Influenza A Virus N5 Neuraminidase Has an Extended 150-Cavity

http://www.wikidata.org/entity/Q27666275

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New world bats harbor diverse influenza A viruses 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 Structural and Functional Analysis of Laninamivir and its Octanoate Prodrug Reveals Group Specific Mechanisms for Influenza NA Inhibition Binding of herpes simplex virus glycoprotein D to nectin-1 exploits host cell adhesion Induced opening of influenza virus neuraminidase N2 150-loop suggests an important role in inhibitor binding Functional and Structural Analysis of Influenza Virus Neuraminidase N3 Offers Further Insight into the Mechanisms of Oseltamivir Resistance 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 Synthesis, structure and inhibitory activity of a stereoisomer of oseltamivir carboxylate Plasticity of 150-loop in influenza neuraminidase explored by Hamiltonian replica exchange molecular dynamics simulations Locking the 150-cavity open: in silico design and verification of influenza neuraminidase inhibitors Resistance to Mutant Group 2 Influenza Virus Neuraminidases of an Oseltamivir-Zanamivir Hybrid Inhibitor.Targeting a cluster of arginine residues of neuraminidase to avoid oseltamivir resistance in influenza A (H1N1): a theoretical study.Molecular Characterizations of Surface Proteins Hemagglutinin and Neuraminidase from Recent H5Nx Avian Influenza Viruses.Structural and functional analysis of surface proteins from an A(H3N8) influenza virus isolated from New England harbor seals.Structural basis of nectin-1 recognition by pseudorabies virus glycoprotein D The neuraminidase of bat influenza viruses is not a neuraminidase.Reduced susceptibility to all neuraminidase inhibitors of influenza H1N1 viruses with haemagglutinin mutations and mutations in non-conserved residues of the neuraminidase.The significance of naturally occurring neuraminidase quasispecies of H5N1 avian influenza virus on resistance to oseltamivir: a point of concern Adventures and lessons of an American biochemist in China.Drug Susceptibility Evaluation of an Influenza A(H7N9) Virus by Analyzing Recombinant Neuraminidase Proteins.Assessment of Molecular, Antigenic, and Pathological Features of Canine Influenza A(H3N2) Viruses That Emerged in the United States.Screening for Neuraminidase Inhibitor Resistance Markers among Avian Influenza Viruses of the N4, N5, N6, and N8 Neuraminidase Subtypes.

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P2860

Influenza A Virus N5 Neuraminidase Has an Extended 150-Cavity

http://www.wikidata.org/entity/Q27666275

description

2011 nî lūn-bûn

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2011 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

@hyw

2011 թվականի օգոստոսին հրատարակված գիտական հոդված

@hy

2011年の論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年论文

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Influenza A Virus N5 Neuraminidase Has an Extended 150-Cavity

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Influenza A Virus N5 Neuraminidase Has an Extended 150-Cavity

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Journal of Virology

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Influenza A Virus N5 Neuraminidase Has an Extended 150-Cavity

@en

P2093

Christopher J Vavricka

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

Jianxun Qi

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

Mingyang Wang

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

Qing Li

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

Yan Wu

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

Yue Liu

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

P2860

PHENIX: a comprehensive Python-based system for macromolecular structure solution

CS-8958, a prodrug of the new neuraminidase inhibitor R-125489, shows long-acting anti-influenza virus activity

Structural Characterization of the 1918 Influenza Virus H1N1 Neuraminidase

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

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

Crystal structure of the swine-origin A (H1N1)-2009 influenza A virus hemagglutinin (HA) reveals similar antigenicity to that of the 1918 pandemic virus

Coot: model-building tools for molecular graphics

Pushing the boundaries of molecular replacement with maximum likelihood

Refinement of macromolecular structures by the maximum-likelihood method

The CCP4 suite: programs for protein crystallography

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8431-5

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10.1128/JVI.00638-11

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16

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