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Cryo-EM structure of disease-related prion fibrils provides insights into seeding barriers

A cryo-EM structure of disease-related human Y145Stop prion protein amyloid fibrils explains species-dependent seeding barriers in prion protein amyloid propagation.

Qiuye Li
Christopher P. Jaroniec
Witold K. Surewicz
Research12 Sept 2022
Nature Structural & Molecular Biology

Volume: 29, P: 962-965
Protein fold determined by paramagnetic magic-angle spinning solid-state NMR spectroscopy

Despite recent progress, solving protein structures using solid-state NMR spectroscopy is not routine. Now, a method for the rapid determination of global protein fold is reported, based on measurements of ¹⁵N longitudinal paramagnetic relaxation enhancements in several protein variants modified with covalently attached cysteine–EDTA–Cu²⁺ tags.

Ishita Sengupta
Philippe S. Nadaud
Christopher P. Jaroniec
Research18 Mar 2012
Nature Chemistry

Volume: 4, P: 410-417
Species-dependent structural polymorphism of Y145Stop prion protein amyloid revealed by solid-state NMR spectroscopy

Prion diseases can be transmitted across species. Here the authors use solid-state NMR to study prion protein (PrP) amyloids from human, mouse and Syrian hamster and show that their structural differences are mainly governed by two residues, which helps to understand interspecies PrP propagation on a molecular level.

Theint Theint
Philippe S. Nadaud
Christopher P. Jaroniec
ResearchOpen Access29 Sept 2017
Nature Communications

Volume: 8, P: 1-10
Targeted production of reactive oxygen species in mitochondria to overcome cancer drug resistance

Multidrug resistance is a major challenge in cancer therapy. Here, the authors develop a mitochondria-targeting nanoparticle system that inhibits adenosine triphosphate transporter activity via reactive oxygen species generation and can thus be used to target multidrug-resistant cancer.

Hai Wang
Zan Gao
Xiaoming He
ResearchOpen Access08 Feb 2018
Nature Communications

Volume: 9, P: 1-16
Effect of amino acid mutations on the conformational dynamics of amyloidogenic immunoglobulin light-chains: A combined NMR and in silico study

Sujoy Mukherjee
Simon P. Pondaven
Christopher P. Jaroniec
ResearchOpen Access04 Sept 2017
Scientific Reports

Volume: 7, P: 1-13

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Cryo-EM structure of disease-related prion fibrils provides insights into seeding barriers

Protein fold determined by paramagnetic magic-angle spinning solid-state NMR spectroscopy

Species-dependent structural polymorphism of Y145Stop prion protein amyloid revealed by solid-state NMR spectroscopy

Targeted production of reactive oxygen species in mitochondria to overcome cancer drug resistance

Effect of amino acid mutations on the conformational dynamics of amyloidogenic immunoglobulin light-chains: A combined NMR and in silico study

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