Factors contributing to the fusogenic potency of foamy virus

Biochemical and Biophysical Research Communications

Volumn 284, Issue 4, 2001, Pages 870-874

  Epand, Richard M ^a   Epand, Raquel F ^a  

^a MCMASTER UNIVERSITY   (Canada)

Author keywords

Foamy virus; Membrane curvature; Spumavirus; Viral fusion peptide; Viral membrane fusion

Indexed keywords

HYBRID PROTEIN; LIPID; TRIFLUOROETHANOL; VIRUS FUSION PROTEIN;

ALPHA HELIX; AMINO TERMINAL SEQUENCE; ARTICLE; CIRCULAR DICHROISM; CONTROLLED STUDY; GENETIC POLYMORPHISM; MEMBRANE FUSION; NONHUMAN; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN STRUCTURE; SPUMA VIRUS;

EID: 0034810729     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1006/bbrc.2001.5060     Document Type: Article

References (14)

1. Common properties of fusion peptides from diverse systems
2. Viral fusion peptides: A tool set to disrupt and connect biological membranes
3. Hydrophobic-at-interface regions in viral fusion protein ectodomains
4. Foamy viruses are unconventional retroviruses
5. The foamy viruses
6. Nucleotide sequence analysis of a cloned DNA fragment from human cells reveals homology to retrotransposons
7. An evolutionarily conserved positively charged amino acid in the putative membrane-spanning domain of the foamy virus envelope protein controls fusion activity
8. Experimentally determined hydrophobicity scale for proteins at membrane interfaces
9. A simple method for displaying the hydropathic character of a protein
10. Estimation of the number of alpha-helical and beta-strand segments in proteins using circular dichroism spectroscopy
11. Use of resonance energy transfer to monitor membrane fusion
12. Relationship between the infectivity of influenza virus and the ability of its fusion peptide to perturb bilayers
13. Role of the N-terminal peptides of viral envelope proteins in membrane fusion
14. The polar region consecutive to the HIV fusion peptide participates in membrane fusion