@article{199336,
  keywords = {Biological Transport, Escherichia coli, Structure-Activity Relationship, Amino Acid Sequence, Cell Membrane, Carrier Proteins, beta-Galactosidase, Cytoplasm, Molecular Weight, Genetic Engineering, Protein Precursors, Galactosidases},
  author = {Moreno and Fowler and Hall and Silhavy and Zabin and Schwartz},
  title = {A signal sequence is not sufficient to lead beta-galactosidase out of the cytoplasm},
  abstract = {<p>Escherichia coli strains have been constructed in which lacZ, the gene for the cytoplasmic enzyme beta-galactosidase, is fused to lamB, the gene for an outer membrane protein. One such strain produces a beta-galactosidase which remains cytoplasmic even though it possesses the complete signal sequence of the lamB protein precursor at the amino-terminal end.</p>
},
  year = {1980},
  journal = {Nature},
  volume = {286},
  pages = {356-9},
  month = {07/1980},
  issn = {0028-0836},
  doi = {10.1038/286356a0},
  language = {eng},
}