The active oligomeric state of the minimalistic influenza virus M2 ion channel is a tetramer

Proceedings of the National Academy of Sciences of the United States of America

Volumn 94, Issue 10, 1997, Pages 5000-5005

  Sakaguchi, Takemasa ^a   Tu, Qiang ^a   Pinto, Lawrence H ^a   Lamb, Robert A ^a  

^a NORTHWESTERN UNIVERSITY   (United States)

Author keywords

amantadine; channel oligomeric form; influenza A virus; M2 protein

Indexed keywords

AMANTADINE; ION CHANNEL; MUTANT PROTEIN; OLIGOMER; TETRAMER; VIRUS PROTEIN;

ANIMAL CELL; ARTICLE; CONTROLLED STUDY; ENDOSOME; GOLGI COMPLEX; HUMAN; HUMAN CELL; INFLUENZA VIRUS; NONHUMAN; PRIORITY JOURNAL; PROTON TRANSPORT; VIRUS PARTICLE; XENOPUS LAEVIS;

AMANTADINE; ANIMALS; ENDOSOMES; HELA CELLS; HUMANS; INFLUENZA A VIRUS; ION CHANNELS; KINETICS; MACROMOLECULAR SUBSTANCES; MAMMALS; MEMBRANE POTENTIALS; OOCYTES; VIRION;

EID: 0030973121     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.94.10.5000     Document Type: Article

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