Solution structure of a 142-residue recombinant prion protein corresponding to the infectious fragment of the scrapie isoform-Reference-Cited by-同舟云学术

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Solution structure of a 142-residue recombinant prion protein corresponding to the infectious fragment of the scrapie isoform

Published:1997-09-16 Issue:19 Volume:94 Page:10086-10091
ISSN:0027-8424
Container-title:Proceedings of the National Academy of Sciences
language:en
Short-container-title:Proceedings of the National Academy of Sciences

Author:

James T. L.,Liu H.,Ulyanov N. B.,Farr-Jones S.,Zhang H.,Donne D. G.,Kaneko K.,Groth D.,Mehlhorn I.,Prusiner S. B.,Cohen F. E.

Publisher

Proceedings of the National Academy of Sciences

Subject

Multidisciplinary

Reference55 articles.

1. Unconventional Viruses and the Origin and Disappearance of Kuru

2. CREUTZFELDT-JAKOB DISEASE VIRUS ISOLATIONS FROM THE GERSTMANN-STRÄUSSLER SYNDROME

3. Fatal Familial Insomnia, a Prion Disease with a Mutation at Codon 178 of the Prion Protein Gene

4. Transmission dynamics and epidemiology of BSE in British cattle

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1. Different folding mechanisms in prion proteins from mammals with different disease susceptibility observed at the single-molecule level;2024-08-10

2. N-glycosylation is a potent regulator of prion protein neurotoxicity;Journal of Biological Chemistry;2023-09

3. Intrinsic determinants of prion protein neurotoxicity in Drosophila: from sequence to (dys)function;Frontiers in Molecular Neuroscience;2023-08-14

4. Y225A induces long-range conformational changes in human prion protein that are protective in Drosophila;Journal of Biological Chemistry;2023-07

5. N-Glycosylation is a Potent Regulator of Prion Protein Neurotoxicity;2023-02-26

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