HSPB7 is the most potent polyQ aggregation suppressor within the HSPB family of molecular chaperones.

@article{Vos2010HSPB7IT,
  title={HSPB7 is the most potent polyQ aggregation suppressor within the HSPB family of molecular chaperones.},
  author={Michel J Vos and Marianne P Zijlstra and Bart Kanon and Maria A W H van Waarde-Verhagen and Ewout R. P. Brunt and Hendrika M J Oosterveld-Hut and Serena Carra and Ody C. M. Sibon and Harm H. Kampinga},
  journal={Human molecular genetics},
  year={2010},
  volume={19 23},
  pages={4677-93}
}
A small number of heat-shock proteins have previously been shown to act protectively on aggregation of several proteins containing an extended polyglutamine (polyQ) stretch, which are linked to a variety of neurodegenerative diseases. A specific subfamily of heat-shock proteins is formed by the HSPB family of molecular chaperones, which comprises 10 members (HSPB1-10, also called small HSP). Several of them are known to act as anti-aggregation proteins in vitro. Whether they also act… CONTINUE READING
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