Profilin reduces aggregation and phase separation of huntingtin N-terminal fragments by preferentially binding to soluble monomers and oligomers

Authors

Ammon E. Posey, Washington University School of Medicine in St. Louis
Kiersten M. Ruff, Washington University School of Medicine in St. Louis
Tyler S. Harmon, Washington University School of Medicine in St. Louis
Scott L. Crick, Washington University School of Medicine in St. Louis
Aimin Li, Washington University School of Medicine in St. Louis
Marc I. Diamond, University of Texas Southwestern Medical Center

Journal

Journal of Biological Chemistry

Publication Date

2018

Volume

293

Issue

10

Inclusive Pages

3734-3746

Document Type

Open Access Publication

DOI

10.1074/jbc.RA117.000357

Rights and Permissions

This research was originally published in the Journal of Biological Chemistry. Posey AE, Ruff KM, Harmon TS, Crick SL, Li A, Diamond MI, Pappu RV. Profilin reduces aggregation and phase separation of huntingtin N-terminal fragments by preferentially binding to soluble monomers and oligomers. J Biol Chem. 2018 Mar 9;293(10):3734-3746. doi: 10.1074/jbc.RA117.000357. © 2018 by The American Society for Biochemistry and Molecular Biology, Inc.

Recommended Citation

Posey, Ammon E.; Ruff, Kiersten M.; Harmon, Tyler S.; Crick, Scott L.; Li, Aimin; and Diamond, Marc I., "Profilin reduces aggregation and phase separation of huntingtin N-terminal fragments by preferentially binding to soluble monomers and oligomers." Journal of Biological Chemistry. 293, 10. 3734-3746. (2018).
https://digitalcommons.wustl.edu/open_access_pubs/6663