Solid-state NMR structural studies of the fibril form of a mutant mouse prion peptide PrP89–143(P101L)-Reference-Cited by-同舟云学术

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Solid-state NMR structural studies of the fibril form of a mutant mouse prion peptide PrP89–143(P101L)

Published:2006-02 Issue:1-3 Volume:29 Page:183-190
ISSN:0926-2040
Container-title:Solid State Nuclear Magnetic Resonance
language:en
Short-container-title:Solid State Nuclear Magnetic Resonance

Author:

Hun Lim Kwang,Nguyen Tuan N.,Damo Steven M.,Mazur Tanya,Ball Haydn L.,Prusiner Stanley B.,Pines Alexander,Wemmer David E.

Publisher

Elsevier BV

Subject

Instrumentation,Nuclear and High Energy Physics,General Chemistry,Radiation

Reference34 articles.

1. The structural basis of protein folding and its links with human disease

2. Protein aggregation and aggregate toxicity: new insights into protein folding, misfolding diseases and biological evolution

3. From the globular to the fibrous state: protein structure and structural conversion in amyloid formation

4. Amyloid fibrillogenesis: themes and variations

5. Common core structure of amyloid fibrils by synchrotron X-ray diffraction 1 1Edited by F. E. Cohen

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1. Early Stages of RNA-Mediated Conversion of Human Prions;The Journal of Physical Chemistry B;2022-08-16

2. Structural Mechanism of Barriers to Interspecies Seeding Transmissibility of Full‐Length Prion Protein Amyloid;ChemBioChem;2019-10-15

3. Mutations in Prion Protein Gene: Pathogenic Mechanisms in C-Terminal vs. N-Terminal Domain, a Review;International Journal of Molecular Sciences;2019-07-23

4. Protein-solvent interfaces in human Y145Stop prion protein amyloid fibrils probed by paramagnetic solid-state NMR spectroscopy;Journal of Structural Biology;2019-04

5. The G126V Mutation in the Mouse Prion Protein Hinders Nucleation-Dependent Fibril Formation by Slowing Initial Fibril Growth and by Increasing the Critical Concentration;Biochemistry;2017-10-26

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