One domain fits all: Using disordered regions to sequester misfolded proteins
2018 ◽
Vol 217
(4)
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pp. 1173-1175
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Keyword(s):
Small heat shock proteins (sHsps) are adenosine triphosphate–independent chaperones that protect cells from misfolded proteins. In this issue, Grousl et al. (2018. J. Cell Biol. https://doi.org/10.1083/jcb.201708116) show that the yeast sHsp Hsp42 uses a prion-like intrinsically disordered domain to bind and sequester misfolded proteins in protein deposition sites.
2012 ◽
Vol 13
(1)
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pp. 76-85
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Keyword(s):
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2009 ◽
Vol 1793
(11)
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pp. 1738-1748
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Keyword(s):
2015 ◽
Vol 21
(1)
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pp. 167-178
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Keyword(s):
2012 ◽
Vol 44
(10)
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pp. 1632-1645
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Keyword(s):