Subcellular localization and topology of the p7 polypeptide of hepatitis C virus.

@article{CarrreKremer2002SubcellularLA,
  title={Subcellular localization and topology of the p7 polypeptide of hepatitis C virus.},
  author={S{\'e}verine Carr{\`e}re-Kremer and Claire Montpellier-Pala and Laurence Cocquerel and Czeslaw Wychowski and François Penin and Jean Dubuisson},
  journal={Journal of virology},
  year={2002},
  volume={76 8},
  pages={3720-30}
}
Although biological and biochemical data have been accumulated on most hepatitis C virus proteins, the structure and function of the 63-amino-acid p7 polypeptide of this virus have never been investigated. In this work, sequence analyses predicted that p7 contains two transmembrane passages connected by a short hydrophilic segment. The C-terminal transmembrane domain of p7 was predicted to function as a signal sequence, which was confirmed experimentally by analyzing the translocation of a… CONTINUE READING
Highly Influential
This paper has highly influenced 13 other papers. REVIEW HIGHLY INFLUENTIAL CITATIONS

Citations

Publications citing this paper.
Showing 1-10 of 78 extracted citations

Viroporins: structure, function and potential as antiviral targets.

The Journal of general virology • 2015
View 8 Excerpts
Highly Influenced

Hepatitis C virus p7: molecular function and importance in hepatitis C virus life cycle and potential antiviral target.

Liver international : official journal of the International Association for the Study of the Liver • 2011
View 12 Excerpts
Highly Influenced

Similar Papers

Loading similar papers…