Initial Steps of Amyloidogenic Peptide Assembly Revealed by Cold-Ion Spectroscopy

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Initial Steps of Amyloidogenic Peptide Assembly Revealed by Cold-Ion Spectroscopy

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im Dezember 2017 veröffentlichter wissenschaftlicher Artikel

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wetenschappelijk artikel

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наукова стаття, опублікована в грудні 2017

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Initial Steps of Amyloidogenic Peptide Assembly Revealed by Cold-Ion Spectroscopy

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Initial Steps of Amyloidogenic Peptide Assembly Revealed by Cold-Ion Spectroscopy

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Initial Steps of Amyloidogenic Peptide Assembly Revealed by Cold-Ion Spectroscopy

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Initial Steps of Amyloidogenic Peptide Assembly Revealed by Cold-Ion Spectroscopy

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Initial Steps of Amyloidogenic Peptide Assembly Revealed by Cold-Ion Spectroscopy

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Initial Steps of Amyloidogenic Peptide Assembly Revealed by Cold-Ion Spectroscopy

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P1476

Initial Steps of Amyloidogenic Peptide Assembly Revealed by Cold-Ion Spectroscopy

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P2093

Cait MacPhee

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Ewan W. Blanch

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Jakub Ujma

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Lukasz G. Migas

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Maria Giovanna Lizio

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Natalia S. Nagornova

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Oleg V. Boyarkin

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Perdita E. Barran

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Vladimir Kopysov

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P2860

High-resolution molecular structure of a peptide in an amyloid fibril determined by magic angle spinning NMR spectroscopy

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Protein misfolding, functional amyloid, and human disease

ATR-FTIR: a "rejuvenated" tool to investigate amyloid proteins.

Photoredox activation of carbon dioxide for amino acid synthesis in continuous flow

Amyloid-β protein oligomerization and the importance of tetramers and dodecamers in the aetiology of Alzheimer's disease.

Interplay of intra- and intermolecular H-bonding in a progressively solvated macrocyclic peptide.

Molecular conformation of a peptide fragment of transthyretin in an amyloid fibril.

Alzheimer's disease beta-amyloid peptides are released in association with exosomes.

Resonance Energy Transfer Relates the Gas-Phase Structure and Pharmacological Activity of Opioid Peptides.

P304

219-223

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P31

scholarly article

P356

10.1002/ANGE.201710188

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P433

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P478

130

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P577

2017-12-07T00:00:00Z

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