Article Information
History
- December 7, 2022.
Copyright
The copyright holder for this preprint is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under a CC-BY-ND 4.0 International license.
Author Information
- Maria D. Flores*,1,
- Michael R. Sawaya2,
- David R. Boyer2,
- Samantha Zink1,
- Susanna Tovmasyan1,
- Adrian Saucedo1,
- Chih-Te Zee1,
- Jorge Cardenas1,
- Luana Fioriti*,3,4 and
- Jose A. Rodriguez*,1
- 1Department of Chemistry and Biochemistry; UCLA-DOE Institute for Genomics and Proteomics; STROBE, NSF Science and Technology Center; University of California, Los Angeles (UCLA); Los Angeles, CA 90095, USA
- 2Department of Biological Chemistry and Department of Chemistry and Biochemistry, University of California Los Angeles (UCLA), Howard Hughes Medical Institute (HHMI), UCLA-DOE Institute for Genomics and Proteomics, Los Angeles, CA 90095, USA
- 3Department of Neuroscience, Istituto di Ricerche Farmacologiche Mario Negri, Milano MI, 20156, Italy
- 4Department of Neuroscience, Columbia University, New York, NY 10027, USA
- ↵* Correspondence to: Jose A. Rodriguez (jrodriguez{at}mbi.ucla.edu), Luana Fioriti (luana.fioriti{at}marionegri.it), Maria D. Flores (mflores{at}mbi.ucla.edu).
Posted December 07, 2022.
Structure of a reversible amyloid fibril formed by the CPEB3 prion-like domain reveals a core sequence involved in translational regulation
