RGG Repeats of PrP-like Shadoo Protein Bind Nucleic Acids
Author:
Affiliation:
1. Centre for Prions and Protein Folding Diseases, ‡Division of Neurology, and §Department of Biochemistry, Faculty of Medicine and Dentistry, University of Alberta, Edmonton, Alberta T6G 2M8, Canada
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi301395w
Reference26 articles.
1. Shadoo, a new protein highly conserved from fish to mammals and with similarity to prion protein
2. Biological properties of the PrP-like Shadoo protein
3. Wild-type Shadoo proteins convert to amyloid-like forms under native conditions
4. The CNS glycoprotein Shadoo has PrPC-like protective properties and displays reduced levels in prion infections
5. Identification of the RGG Box Motif in Shadoo: RNA-Binding and Signaling Roles?
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1. Prion protein with a mutant N-terminal octarepeat region undergoes cobalamin-dependent assembly into high–molecular weight complexes;Journal of Biological Chemistry;2022-04
2. Membrane Domain Localization and Interaction of the Prion-Family Proteins, Prion and Shadoo with Calnexin;Membranes;2021-12-13
3. Intrinsic disorder and phase transitions: Pieces in the puzzling role of the prion protein in health and disease;Progress in Molecular Biology and Translational Science;2021
4. Prion protein PrP nucleic acid binding and mobilization implicates retroelements as the replicative component of transmissible spongiform encephalopathy;Archives of Virology;2020-02-05
5. Proteasomal Inhibition Redirects the PrP-Like Shadoo Protein to the Nucleus;Molecular Neurobiology;2019-05-25
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