Cell-cell membrane fusion induced by p15 Fusion-associated Small Transmembrane (FAST) protein requires a novel fusion peptide motif containing a myristoylated polyproline type II helix

Journal of Biological Chemistry

Volumn 287, Issue 5, 2012, Pages 3403-3414

  Top, Deniz ^a   Read, Jolene A ^a   Dawe, Sandra J ^a   Syvitski, Raymond T ^c   Duncan, Roy ^a,b  

^a DALHOUSIE UNIVERSITY   (Canada)

^b DALHOUSIE UNIVERSITY   (Canada)

^c NATIONAL RESEARCH COUNCIL CANADA   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE SUBSTITUTION; BIPHASIC; CD SPECTROSCOPY; CELL-CELL FUSION; ECTODOMAIN; FUSION MODULES; FUSION PEPTIDES; FUSION PROTEINS; FUSION-ASSOCIATED SMALL TRANSMEMBRANE; HYDROPHOBIC AMINO ACIDS; LAG PHASE; LIPID MIXING; MECHANISM OF ACTION; MEMBRANE BINDING; MEMBRANE FUSION; MULTIPLE SUBSTITUTIONS; N-TERMINALS; PEPTIDE-MEMBRANE INTERACTIONS; POLYPROLINE; PROLINE-RICH MOTIF; RATE LIMITING; SIDE-CHAINS; SOLVENT EXPOSURE; TYPE II; VIRAL PROTEINS;

AMINO ACIDS; CELL MEMBRANES; CIRCULAR DICHROISM SPECTROSCOPY; CYTOLOGY; FUSION REACTORS; LIPOSOMES; PEPTIDES; PHOSPHOLIPIDS;

MEMBRANES;

FUSION ASSOCIATED SMALL TRANSMEMBRANE PROTEIN; LIPOSOME; MEMBRANE PROTEIN; POLYPROLINE TYPE II HELIX; PROTEIN P15; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; ANIMAL CELL; ARTICLE; CARBOXY TERMINAL SEQUENCE; CELL MEMBRANE; CIRCULAR DICHROISM; CONTROLLED STUDY; HYDROPHOBICITY; MEMBRANE STRUCTURE; MYRISTYLATION; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN LOCALIZATION; PROTEIN MOTIF; PROTEIN PROTEIN INTERACTION; STRUCTURE ANALYSIS;

AMINO ACID MOTIFS; ANIMALS; CERCOPITHECUS AETHIOPS; LIPOSOMES; LIPOYLATION; MODELS, CHEMICAL; MYRISTIC ACID; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PEPTIDES; PROTEIN STRUCTURE, TERTIARY; REOVIRIDAE; VERO CELLS; VIRAL FUSION PROTEINS;

EID: 84856289583     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.305268     Document Type: Article

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