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I've been looking into a lot of papers, and most say that chaperones assisted in the folding of misfolded proteins, or Ubiquitin markers aggregates for degradation by the proteasome. Or it will say something, like... misfolded proteins are implicated in diseases x,y, and z.

What I'm struggling to figure out is what are the proteins these chaperones are assisting in refolding or what are these aggregated proteins implicated in disease?

I'm frustrated by the fact that many times the paper won't tell you the name, and arbitrarily say "protein(s)" which is quite vague and hard for me to do further digging.

Thanks.

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    $\begingroup$ There are non-misfolded proteins that are dependent on chaperone. For e.g. deletion of the GroEL chaperone is lethal. I recommend that you get hold of a better review on this topic (Check out the one by Hartl). There are research papers that try to address the question of which proteins are assisted by chaperones. I'm afraid that as it is written your question is very broad. $\endgroup$ – WYSIWYG Mar 2 at 7:26

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