Specific glycosaminoglycan chain length and sulfation patterns are required for cell uptake of tau versus α-synuclein and β-amyloid aggregates

Authors

Barbara E. Stopschinski, University of Texas Southwestern Medical Center
Brandon B. Holmes, Washington University School of Medicine in St. Louis
Gregory M. Miller, California Institute of Technology
Victor A. Manon, University of Texas Southwestern Medical Center
Jaime Vaquer-Alicea, University of Texas Southwestern Medical Center
William L. Prueitt, University of Texas Southwestern Medical Center
Linda C. Hsieh-Wilson, California Institute of Technology
Marc I. Diamond, University of Texas Southwestern Medical Center

Journal

Journal of Biological Chemistry

Publication Date

2018

Volume

293

Issue

27

First Page

10826

Last Page

10840

Document Type

Open Access Publication

DOI

10.1074/jbc.RA117.000378

Rights and Permissions

This research was originally published in Journal Biological Chemistry. Stopschinski, B. E., Holmes, B. B., Miller, G. M., Manon, V. A., Vaquer-Alicea, J., Prueitt, W. L., . . . Diamond, M. I. (2018). Specific glycosaminoglycan chain length and sulfation patterns are required for cell uptake of tau versus -synuclein and -amyloid aggregates. Journal of Biological Chemistry, 293(27), 10826-10840. doi:10.1074/jbc.RA117.000378 © the American Society for Biochemistry and Molecular Biology.

Recommended Citation

Stopschinski, Barbara E.; Holmes, Brandon B.; Miller, Gregory M.; Manon, Victor A.; Vaquer-Alicea, Jaime; Prueitt, William L.; Hsieh-Wilson, Linda C.; and Diamond, Marc I., "Specific glycosaminoglycan chain length and sulfation patterns are required for cell uptake of tau versus α-synuclein and β-amyloid aggregates." Journal of Biological Chemistry. 293, 27. 10826 - 10840. (2018).
https://digitalcommons.wustl.edu/open_access_pubs/8436