Liquid–liquid phase separation of the prion protein is regulated by the octarepeat domain independently of histidines and copper-Reference-Cited by-同舟云学术

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Liquid–liquid phase separation of the prion protein is regulated by the octarepeat domain independently of histidines and copper

Published:2024-06 Issue:6 Volume:300 Page:107310
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Kamps Janine,Bader Verian,Winklhofer Konstanze F.,Tatzelt Jörg^ORCID

Funder

Deutsche Forschungsgemeinschaft

Publisher

Elsevier BV

Reference60 articles.

1. Structure of the recombinant full-length hamster prion protein PrP(29-231): the N terminus is highly flexible;Donne;Proc. Natl. Acad. Sci. U. S. A.,1997

2. NMR structure of the mouse prion protein domain PrP(121-321);Riek;Nature,1996

3. NMR characterization of the full-length recombinant murine prion protein, mPrP(23-231);Riek;FEBS Lett.,1997

4. Prion protein NMR structures of chickens, turtles, and frogs;Calzolai;Proc. Natl. Acad. Sci. U. S. A.,2005

5. Evolutionary rate heterogeneity in proteins with long disordered regions;Brown;J. Mol. Evol.,2002

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