Amphipathic alpha-helices and putative cholesterol binding domains of the influenza virus matrix M1 protein are crucial for virion structure organisation.

@article{Tsfasman2015AmphipathicAA,
  title={Amphipathic alpha-helices and putative cholesterol binding domains of the influenza virus matrix M1 protein are crucial for virion structure organisation.},
  author={T. Tsfasman and V. Kost and S. Markushin and V. Lotte and I. Koptiaeva and E. Bogacheva and L. Baratova and V. Radyukhin},
  journal={Virus research},
  year={2015},
  volume={210},
  pages={
          114-8
        }
}
The influenza virus matrix M1 protein is an amphitropic membrane-associated protein, forming the matrix layer immediately beneath the virus raft membrane, thereby ensuring the proper structure of the influenza virion. The objective of this study was to elucidate M1 fine structural characteristics, which determine amphitropic properties and raft membrane activities of the protein, via 3D in silico modelling with subsequent mutational analysis. Computer simulations suggest the amphipathic nature… Expand
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References

SHOWING 1-10 OF 19 REFERENCES
Cholesterol-Binding Viral Proteins in Virus Entry and Morphogenesis
Structural organization of a filamentous influenza A virus
The M1 matrix protein controls the filamentous phenotype of influenza A virus.
Linking new paradigms in protein chemistry to reversible membrane-protein interactions.
Growth restriction of influenza A virus by M2 protein antibody is genetically linked to the M1 protein.
  • S. Zebedee, R. Lamb
  • Biology, Medicine
  • Proceedings of the National Academy of Sciences of the United States of America
  • 1989
...
1
2
...