The Hemagglutinin-Neuraminidase (HN) Head Domain and the Fusion (F) Protein Stalk Domain of the Parainfluenza Viruses Affect the Specificity of the HN-F Interaction.

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The Hemagglutinin-Neuraminidase (HN) Head Domain and the Fusion (F) Protein Stalk Domain of the Parainfluenza Viruses Affect the Specificity of the HN-F Interaction.

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http://www.wikidata.org/entity/Q54246479

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2018 nî lūn-bûn

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2018年の論文

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2018年学术文章

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2018年学术文章

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2018年学术文章

@zh-hans

2018年学术文章

@zh-my

2018年学术文章

@zh-sg

2018年學術文章

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2018年學術文章

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2018年學術文章

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name

The Hemagglutinin-Neuraminidas ...... icity of the HN-F Interaction.

@en

The Hemagglutinin-Neuraminidase

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type

Item

label

The Hemagglutinin-Neuraminidas ...... icity of the HN-F Interaction.

@en

The Hemagglutinin-Neuraminidase

@nl

prefLabel

The Hemagglutinin-Neuraminidas ...... icity of the HN-F Interaction.

@en

The Hemagglutinin-Neuraminidase

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P1476

The Hemagglutinin-Neuraminidas ...... icity of the HN-F Interaction.

@en

P2093

Junpei Ohtsuka

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

Machiko Nishio

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Masato Tsurudome

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Morihiro Ito

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Tetsuya Nosaka

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P2860

Structural basis of viral invasion: lessons from paramyxovirus F

Hemagglutinin-neuraminidase-independent fusion activity of simian virus 5 fusion (F) protein: difference in conformation between fusogenic and nonfusogenic F proteins on the cell surface.

Structural studies of the parainfluenza virus 5 hemagglutinin-neuraminidase tetramer in complex with its receptor, sialyllactose.

Timing is everything: Fine-tuned molecular machines orchestrate paramyxovirus entry.

Functional interaction of paramyxovirus glycoproteins: identification of a domain in Sendai virus HN which promotes cell fusion

Paramyxovirus fusion and entry: multiple paths to a common end

Fusion activation by a headless parainfluenza virus 5 hemagglutinin-neuraminidase stalk suggests a modular mechanism for triggering.

Mutagenesis of Paramyxovirus Hemagglutinin-Neuraminidase Membrane-Proximal Stalk Region Influences Stability, Receptor Binding, and Neuraminidase Activity.

Mutations in the parainfluenza virus 5 fusion protein reveal domains important for fusion triggering and metastability.

Fusion activation through attachment protein stalk domains indicates a conserved core mechanism of paramyxovirus entry into cells

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391

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P31

scholarly article

P356

10.3389/FMICB.2018.00391

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P478

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

P577

2018-03-13T00:00:00Z

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P698

29593671

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P921

membrane fusion involved in viral entry into host cell

P932

5859044

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