Targeting of the hepatitis B virus precore protein to the endoplasmic reticulum membrane: after signal peptide cleavage translocation can be aborted and the product released into the cytoplasm

@article{Garca1988TargetingOT,
  title={Targeting of the hepatitis B virus precore protein to the endoplasmic reticulum membrane: after signal peptide cleavage translocation can be aborted and the product released into the cytoplasm},
  author={Pablo David Garc{\'i}a and Jing-Hsiung James Ou and William J. Rutter and Peter J. Walter},
  journal={The Journal of Cell Biology},
  year={1988},
  volume={106},
  pages={1093 - 1104}
}
The major hepatitis B virus (HBV) core protein is a viral structural protein involved in nucleic acid binding. Its coding sequence contains an extension of 29 codons (the "precore" region) at the amino terminus of the protein which is present in a fraction of the viral transcripts. This region is evolutionarily conserved among mammalian and avian HBVs, suggesting it has functional importance, although at least for duck HBV it has been shown to be nonessential for replication of infectious… CONTINUE READING