Mutational analysis of the human HSP70 protein: distinct domains for nucleolar localization and adenosine triphosphate binding

@article{Milarski1989MutationalAO,
  title={Mutational analysis of the human HSP70 protein: distinct domains for nucleolar localization and adenosine triphosphate binding},
  author={K L Milarski and Richard I. Morimoto},
  journal={The Journal of Cell Biology},
  year={1989},
  volume={109},
  pages={1947 - 1962}
}
The human HSP70 gene was modified in vitro using oligonucleotide-directed mutagenesis to add sequences encoding a peptide from the testis-specific form of human lactate dehydrogenase (LDH) to the carboxy terminus of HSP70. The peptide-tagged HSP70 can be distinguished from the endogenous HSP70 protein using an LDH peptide-specific antiserum in indirect immunofluorescence assays of cells transiently transfected with an expression vector containing the tagged HSP70 gene regulated by the human… CONTINUE READING

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