Probing Water Accessibility in HET-s(218–289) Amyloid Fibrils by Solid-State NMR-Reference-Cited by-同舟云学术

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Probing Water Accessibility in HET-s(218–289) Amyloid Fibrils by Solid-State NMR

Published:2011-01 Issue:3 Volume:405 Page:765-772
ISSN:0022-2836
Container-title:Journal of Molecular Biology
language:en
Short-container-title:Journal of Molecular Biology

Author:

Van Melckebeke Hélène,Schanda Paul,Gath Julia,Wasmer Christian,Verel René,Lange Adam,Meier Beat H.,Böckmann Anja

Funder

Swiss National Science Foundation

Publisher

Elsevier BV

Subject

Molecular Biology,Structural Biology

Reference40 articles.

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2. Molecular structural basis for polymorphism in Alzheimer's beta-amyloid fibrils;Paravastu;Proc. Natl Acad. Sci. USA,2008

3. Seeded growth of beta-amyloid fibrils from Alzheimer's brain-derived fibrils produces a distinct fibril structure;Paravastu;Proc. Natl Acad. Sci. USA,2009

4. Molecular-level secondary structure, polymorphism, and dynamics of full-length α-synuclein fibrils studied by solid-state NMR;Heise;Proc. Natl Acad. Sci. USA,2005

5. Pre-fibrillar alpha-synuclein variants with impaired beta-structure increase neurotoxicity in Parkinson's disease models;Karpinar;EMBO J.,2009

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1. Mechanistic Studies of Membrane Proteins Using Integrated Solid-state NMR and Computational Approaches;Integrated Structural Biology;2023-12-08

2. Efficient 18.8 T MAS-DNP NMR reveals hidden side chains in amyloid fibrils;Journal of Biomolecular NMR;2023-06

3. The Rigid Core and Flexible Surface of Amyloid Fibrils Probed by Magic‐Angle‐Spinning NMR Spectroscopy of Aromatic Residues;Angewandte Chemie International Edition;2023-03-27

4. Der starre Kern und die flexible Oberfläche von Amyloidfibrillen – Magic‐Angle‐Spinning NMR Spektroskopie von aromatischen Resten;Angewandte Chemie;2023-03-27

5. Side Chain Hydrogen-Bonding Interactions within Amyloid-like Fibrils Formed by the Low-Complexity Domain of FUS: Evidence from Solid State Nuclear Magnetic Resonance Spectroscopy;Biochemistry;2020-01-02

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