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Membrane association induces a conformational change in the Ebola virus matrix protein
The matrix protein VP40 from Ebola virus is targeted to the plasma membrane, where it is thought to induce assembly and budding of virions through its association with the lipid bilayer. Ebola virusExpand
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Ebola virus matrix protein VP40 interaction with human cellular factors Tsg101 and Nedd4.
The Ebola virus matrix protein VP40 is a major viral structural protein and plays a central role in virus assembly and budding at the plasma membrane of infected cells. For efficient budding, a fullExpand
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Vesicular release of ebola virus matrix protein VP40.
We have analysed the expression and cellular localisation of the matrix protein VP40 from Ebola virus. Full-length VP40 and an N-terminal truncated construct missing the first 31 residuesExpand
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Characterization of the receptor and translocator domains of colicin N.
Intact colicin N and various colicin derivatives, including a natural fragment lacking the first 36 amino-acid residues, a chymotryptic fragment lacking the first 66 amino acids and a thermolyticExpand
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Structure of the membrane-bound form of the pore-forming domain of colicin A: a partial proteolysis and mass spectrometry study.
The ion-channel-forming thermolytic fragment (thA) of colicin A binds to negatively charged vesicles and provides an example of the insertion of a soluble protein into a lipid bilayer. The solubleExpand
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Puncturing cell membranes : comparison of colicin A and Aerolysin
Colicin A from Citrobacter freundii and aerolysin from Aeromonas hydrophila are representatives of two classes of pore-forming toxins. Colicin A, an alpha-helical protein, contains a hydrophobicExpand