Conformational changes of Newcastle disease virus envelope glycoproteins triggered by gangliosides.

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description

2004 nî lūn-bûn

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2004年の論文

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2004年論文

@yue

2004年論文

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2004年論文

@zh-hk

2004年論文

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2004年論文

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2004年论文

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2004年论文

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2004年论文

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name

Conformational changes of Newc ...... ins triggered by gangliosides.

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type

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label

Conformational changes of Newc ...... ins triggered by gangliosides.

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Conformational changes of Newc ...... ins triggered by gangliosides.

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P1476

Conformational changes of Newc ...... ins triggered by gangliosides.

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P2093

Enrique Villar

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Isabel Muñoz-Barroso

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Laura Ferreira

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P2860

Role of the hemagglutinin-neuraminidase protein in the mechanism of paramyxovirus-cell membrane fusion.

Crystal structure of the multifunctional paramyxovirus hemagglutinin-neuraminidase

Low pH-induced conformational changes in vesicular stomatitis virus glycoprotein involve dramatic structure reorganization.

A single amino acid change in the Newcastle disease virus fusion protein alters the requirement for HN protein in fusion

Structural and functional relationship between the receptor recognition and neuraminidase activities of the Newcastle disease virus hemagglutinin-neuraminidase protein: receptor recognition is dependent on neuraminidase activity.

Activation of fusion by the SER virus F protein: a low-pH-dependent paramyxovirus entry process.

Conformational changes in cell surface HIV-1 envelope glycoproteins are triggered by cooperation between cell surface CD4 and co-receptors.

Acidic pH enhancement of the fusion of Newcastle disease virus with cultured cells.

The attachment function of the Newcastle disease virus hemagglutinin-neuraminidase protein can be separated from fusion promotion by mutation.

Proteins of newcastle disease virus envelope: interaction between the outer hemagglutinin-neuraminidase glycoprotein and the inner non-glycosylated matrix protein

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581-588

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scholarly article

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10.1111/J.1432-1033.2003.03960.X

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English

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P478

271

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P577

2004-02-01T00:00:00Z

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P5875

8914733

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P698

14728685

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