Chaperonin-mediated folding of actin and tubulin

@article{Lewis1996ChaperoninmediatedFO,
  title={Chaperonin-mediated folding of actin and tubulin},
  author={Sally A. Lewis and Guoling Tian and Irina E. Vainberg and Nicholas J. Cowan},
  journal={The Journal of Cell Biology},
  year={1996},
  volume={132},
  pages={1 - 4}
}
T HE central dogma of molecular biology holds that proteins contain within their primary amino acid sequence all the information that is required to dictate their three-dimensional structure. In principle, therefore, proteins can fold spontaneously (2). It is now clear, however, that the proper folding of many proteins requires facilitation. The facilitation reaction is accomplished via interaction with chaperonins, a class of multisubunit toroidal complexes which hydrolyzes ATP as part of the… CONTINUE READING

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A yeast TCP-1-like protein is required for actin function in vivo.

Proceedings of the National Academy of Sciences of the United States of America • 1994
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