The Path of Least Resistance: Mechanisms to Reduce Influenza's Sensitivity to Oseltamivir

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The Path of Least Resistance: Mechanisms to Reduce Influenza's Sensitivity to Oseltamivir

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2015 nî lūn-bûn

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2015年の論文

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2015年論文

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2015年論文

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2015年論文

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2015年論文

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2015年論文

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2015年论文

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2015年论文

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2015年论文

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The Path of Least Resistance: Mechanisms to Reduce Influenza's Sensitivity to Oseltamivir

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The Path of Least Resistance: Mechanisms to Reduce Influenza's Sensitivity to Oseltamivir

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The Path of Least Resistance: Mechanisms to Reduce Influenza's Sensitivity to Oseltamivir

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P1476

The Path of Least Resistance: Mechanisms to Reduce Influenza's Sensitivity to Oseltamivir

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P2093

Angela M Phillips

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Matthew D Shoulders

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P2860

Experimental illumination of a fitness landscape

The structure of the complex between influenza virus neuraminidase and sialic acid, the viral receptor

Crystal structures of oseltamivir-resistant influenza virus neuraminidase mutants

H1N1 2009 Pandemic Influenza Virus: Resistance of the I223R Neuraminidase Mutant Explained by Kinetic and Structural Analysis

Discovery and development of GS 4104 (oseltamivir): an orally active influenza neuraminidase inhibitor

Estimating the fitness advantage conferred by permissive neuraminidase mutations in recent oseltamivir-resistant A(H1N1)pdm09 influenza viruses

Rational design of potent sialidase-based inhibitors of influenza virus replication

Influenza: lessons from past pandemics, warnings from current incidents.

A conformational restriction in the influenza A virus neuraminidase binding site by R152 results in a combinational effect of I222T and H274Y on oseltamivir resistance.

High-throughput profiling of influenza A virus hemagglutinin gene at single-nucleotide resolution

P304

533-537

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P31

scholarly article

P356

10.1016/J.JMB.2015.12.019

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P407

English

P433

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P478

428

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P577

2015-12-31T00:00:00Z

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P698

26748011

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P932

4886345

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