Protein-solvent interfaces in human Y145Stop prion protein amyloid fibrils probed by paramagnetic solid-state NMR spectroscopy-Reference-Cited by-同舟云学术

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Protein-solvent interfaces in human Y145Stop prion protein amyloid fibrils probed by paramagnetic solid-state NMR spectroscopy

Published:2019-04 Issue:1 Volume:206 Page:36-42
ISSN:1047-8477
Container-title:Journal of Structural Biology
language:en
Short-container-title:Journal of Structural Biology

Author:

Aucoin Darryl,Xia Yongjie,Theint Theint,Nadaud Philippe S.,Surewicz Krystyna,Surewicz Witold K.,Jaroniec Christopher P.

Funder

National Science Foundation

National Institutes of Health

Camille & Henry Dreyfus Foundation

Publisher

Elsevier BV

Subject

Structural Biology

Reference49 articles.

1. Molecular mechanisms of prion pathogenesis;Aguzzi;Annu. Rev. Pathol.,2008

2. Primary structure effects on peptide group hydrogen exchange;Bai;Proteins,1993

3. Biochemical properties of highly neuroinvasive prion strains;Bett;PLoS Pathog.,2012

4. Strain-dependent differences in β-sheet conformations of abnormal prion protein;Caughey;J. Biol. Chem.,1998

5. Measurement of backbone hydrogen-deuterium exchange in the type III secretion system needle protein PrgI by solid-state NMR;Chevelkov;J. Magn. Reson.,2017

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