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Journal ArticleDOI

Influenza virus M2 protein is an integral membrane protein expressed on the infected-cell surface

Robert A. Lamb, +2 more
- 01 Mar 1985 - 
- Vol. 40, Iss: 3, pp 627-633
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TLDR
The influenza A virus M 2 protein is expressed abundantly at the cell surface, and in addition to the hemagglutinin (HA) and neuraminidase (NA), is a third virus-specific membrane protein this paper.
About
This article is published in Cell.The article was published on 1985-03-01. It has received 557 citations till now. The article focuses on the topics: Neuraminidase & Hemagglutinin (influenza).

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Citations
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Journal ArticleDOI

Influenza virus M2 protein has ion channel activity.

TL;DR: Analysis of the currents of altered M2 proteins suggests that the channel pore is formed by the transmembrane domain of the M2 protein, which is proposed to have a pivotal role in the biology of influenza virus infection.
Journal ArticleDOI

A universal influenza A vaccine based on the extracellular domain of the M2 protein.

TL;DR: The enhanced immunogenicity of the M2 extracellular domain exposed on HBc particles allows broad-spectrum, long-lasting protection against influenza A infections.
Journal ArticleDOI

The molecular basis of the specific anti-influenza action of amantadine.

TL;DR: The data reported here demonstrate that the basis of these actions is similar and resides in the virus‐coded M2 membrane protein, the product of a spliced transcript of RNA segment 7.
Journal ArticleDOI

Topogenic signals in integral membrane proteins.

TL;DR: A positive-inside rule seems to apply universally to all integral membrane proteins, with apolar regions targeting for membrane integration and charged residues providing the topological information.
Journal ArticleDOI

Influenza virus assembly and budding.

TL;DR: This review investigates the latest research on influenza virus budding in an attempt to provide a step-by-step analysis of the assembly and budding processes for influenza viruses.
References
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Journal ArticleDOI

A simple method for displaying the hydropathic character of a protein

TL;DR: A computer program that progressively evaluates the hydrophilicity and hydrophobicity of a protein along its amino acid sequence has been devised and its simplicity and its graphic nature make it a very useful tool for the evaluation of protein structures.
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Solubilization of membranes by detergents

TL;DR: This review focuses on work that deals with the mechanisms of detergent action in membrane solubilization including properties of detergents model lipid systems and detergent-protein interactions; in addition a possible sequence of events when deterGents interact with biological membranes receives attention.
Journal ArticleDOI

Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 A resolution.

TL;DR: The haemagglutinin glycoprotein of influenza virus is a trimer comprising two structurally distinct regions: a triple-stranded coiled-coil of α-helices extends 76 Å from the membrane and a globular region of antiparallel β-sheet is positioned on top of this stem.
Journal ArticleDOI

Intracellular protein topogenesis.

TL;DR: A cell contains millions of protein molecules, which are continually being synthesized and degraded, and at homeostasis, a given species of protein is represented by a characteristic number of molecules that is kept constant within a narrow range.
Journal ArticleDOI

Structure of the influenza virus glycoprotein antigen neuraminidase at 2.9 Å resolution

TL;DR: The tetrameric enzyme has circular 4-fold symmetry stabilized in part by metal ions bound on the symmetry axis, and sugar residues are attached to four of the five potential glycosylation sequences, and in one case contribute to the interaction between subunits in the tetramer.
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