Molecular characterization of a novel, developmentally regulated small embryonic chaperone from Caenorhabditis elegans.

@article{Linder1996MolecularCO,
  title={Molecular characterization of a novel, developmentally regulated small embryonic chaperone from Caenorhabditis elegans.},
  author={Bengt Linder and Zhaohui Jin and Jonathan H. Freedman and Charles S. Rubin},
  journal={The Journal of biological chemistry},
  year={1996},
  volume={271 47},
  pages={30158-66}
}
Low molecular weight chaperones inhibit protein aggregation and facilitate refolding of partially denatured polypeptides in cells subjected to physical and chemical stresses. The nematode Caenorhabditis elegans provides a system amenable for investigations on roles for chaperone proteins in normal homeostasis and development. We characterized a C. elegans gene and cDNAs that encode a novel, small embryonic chaperone-like protein (SEC-1) that is composed of 159 amino acids. The central core of… CONTINUE READING

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The nematode Caenorhabditis elegans provides a system amenable for investigations on roles for chaperone proteins in normal homeostasis and development .
The nematode Caenorhabditis elegans provides a system amenable for investigations on roles for chaperone proteins in normal homeostasis and development .
The nematode Caenorhabditis elegans provides a system amenable for investigations on roles for chaperone proteins in normal homeostasis and development .
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