The chaperone αB-crystallin uses different interfaces to capture an amorphous and an amyloid client
Author:
Publisher
Springer Science and Business Media LLC
Subject
Molecular Biology,Structural Biology
Link
http://www.nature.com/articles/nsmb.3108.pdf
Reference69 articles.
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3. Horwitz, J. Alpha crystallin: the quest for a homogeneous quaternary structure. Exp. Eye Res. 88, 190–194 (2009).
4. Aquilina, J.A., Benesch, J.L.P., Bateman, O.A., Slingsby, C. & Robinson, C.V. Polydispersity of a mammalian chaperone: mass spectrometry reveals the population of oligomers in αB-crystallin. Proc. Natl. Acad. Sci. USA 100, 10611–10616 (2003).
5. Jehle, S. et al. Solid-state NMR and SAXS studies provide a structural basis for the activation of αB-crystallin oligomers. Nat. Struct. Mol. Biol. 17, 1037–1042 (2010).
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