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Hsp10 a chaperone by itself?
Canonically, Hsp10 has been known to be a helper for its much more studied partner, Hsp60. Our research shows that Hsp10 can not only prevent fibrilization of toxic amyloid species, but promote the folding of larger substrates (MDH1 and MnSOD). Using cryoEM and NMR, we have structurally characterized this binding and show that Hsp10 is a much larger player than previously thought.
Hsp10 inhibits Ab aggregation
The Alzheimer's peptide aggregates over time and forms amyloid fibrils. Hsp10 inhibits this toxic event and may play a role in Alzheimer's disease.
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Hsp10 supports folding of MDH
Malate dehydrogenase is an obligate substrate of Hsp60. Hsp10 in absence of Hsp60 can also support the folding of MDH.
Cryo-EM structure of Single- and Double- ring Hsp10
The structure of both apo forms of Hsp10 was solved using cryoEM
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