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Rational Structure‐Based Design of Fluorescent Probes for Amyloid Folds

Chembiochem : a European journal of chemical biology, 2019-05, Vol.20 (9), p.1161-1166

2019

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NMR-Based Determination of the 3D Structure of the Ligand–Protein Interaction Site without Protein Resonance Assignment

Journal of the American Chemical Society, 2016-04, Vol.138 (13), p.4393-4400

2016

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Contribution of specific residues of the β-solenoid fold to HET-s prion function, amyloid structure and stability

PLoS pathogens, 2014-06, Vol.10 (6), p.e1004158

2014

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The NMR2 Method to Determine Rapidly the Structure of the Binding Pocket of a Protein–Ligand Complex with High Accuracy

Magnetochemistry, 2018-03, Vol.4 (1), p.12

2018

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Quenched hydrogen-deuterium exchange NMR of a disease-relevant A[beta](1-42) amyloid polymorph.(Research Article)(Nuclear magnetic resonance)

PloS one, 2017-03, Vol.12 (3), p.e0172862

2017

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Quenched hydrogen-deuterium exchange NMR of a disease-relevant Aβ(1-42) amyloid polymorph

PloS one, 2017-03, Vol.12 (3), p.e0172862-e0172862

2017

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Atomic-resolution structure of a disease-relevant Aβ(1–42) amyloid fibril

Proceedings of the National Academy of Sciences - PNAS, 2016-08, Vol.113 (34), p.E4976-E4984

2016

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Towards a true protein movie: A perspective on the potential impact of the ensemble-based structure determination using exact NOEs

Journal of magnetic resonance (1997), 2014-04, Vol.241, p.53-59

2014

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Elucidation of a nutlin-derivative—HDM2 complex structure at the interaction site by NMR molecular replacement: A straightforward derivation

Journal of Magnetic Resonance Open, 2022-06, Vol.10-11, p.100032, Article 100032

2022

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Solid-state NMR sequential assignment of an Amyloid-β(1–42) fibril polymorph

Biomolecular NMR assignments, 2016-10, Vol.10 (2), p.269-276

2016

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The three-dimensional structure of human β-endorphin amyloid fibrils

Nature structural & molecular biology, 2020-12, Vol.27 (12), p.1178

2020

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Solution NMR Studies of Recombinant Aβ(1-42): From the Presence of a Micellar Entity to Residual β-Sheet Structure in the Soluble Species

Chembiochem : a European journal of chemical biology, 2015-03, Vol.16 (4), p.659-669

2015

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Atomic-resolution structure of a disease-relevant A[Beta](1-42) amyloid fibril

Proceedings of the National Academy of Sciences - PNAS, 2016-08, Vol.113 (34), p.E4976

2016

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Quenched hydrogen-deuterium exchange NMR of a disease-relevant A[beta](Nuclear magnetic resonance)

PloS one, 2017-03, Vol.12 (3), p.e0172862

2017

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Contribution of Specific Residues of the [beta]-Solenoid Fold to HET-s Prion Function, Amyloid Structure and Stability: e1004158

PLoS pathogens, 2014-06, Vol.10 (6)

2014

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Solution NMR Studies of Recombinant A[beta](1-42): From the Presence of a Micellar Entity to Residual [beta]-Sheet Structure in the Soluble Species

Chembiochem : a European journal of chemical biology, 2015-03, Vol.16 (4), p.659

2015

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Contribution of specific residues of the [beta]-solenoid fold to HET-s prion function, amyloid structure and stability

PLoS pathogens, 2014-06, Vol.10 (6)

2014

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Amyloid-β Can Form Fractal Antenna-Like Networks Responsive to Electromagnetic Beating and Wireless Signaling

Proceedings of Trends in Electronics and Health Informatics, p.323-344

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Rational Structure‐Based Design of Fluorescent Probes for Amyloid Folds

NMR-Based Determination of the 3D Structure of the Ligand–Protein Interaction Site without Protein Resonance Assignment

Contribution of specific residues of the β-solenoid fold to HET-s prion function, amyloid structure and stability

The NMR2 Method to Determine Rapidly the Structure of the Binding Pocket of a Protein–Ligand Complex with High Accuracy

Quenched hydrogen-deuterium exchange NMR of a disease-relevant A[beta](1-42) amyloid polymorph.(Research Article)(Nuclear magnetic resonance)

Quenched hydrogen-deuterium exchange NMR of a disease-relevant Aβ(1-42) amyloid polymorph

Atomic-resolution structure of a disease-relevant Aβ(1–42) amyloid fibril

Towards a true protein movie: A perspective on the potential impact of the ensemble-based structure determination using exact NOEs

Elucidation of a nutlin-derivative—HDM2 complex structure at the interaction site by NMR molecular replacement: A straightforward derivation

Solid-state NMR sequential assignment of an Amyloid-β(1–42) fibril polymorph

The three-dimensional structure of human β-endorphin amyloid fibrils

Solution NMR Studies of Recombinant Aβ(1-42): From the Presence of a Micellar Entity to Residual β-Sheet Structure in the Soluble Species

Atomic-resolution structure of a disease-relevant A[Beta](1-42) amyloid fibril

Quenched hydrogen-deuterium exchange NMR of a disease-relevant A[beta](Nuclear magnetic resonance)

Contribution of Specific Residues of the [beta]-Solenoid Fold to HET-s Prion Function, Amyloid Structure and Stability: e1004158

Solution NMR Studies of Recombinant A[beta](1-42): From the Presence of a Micellar Entity to Residual [beta]-Sheet Structure in the Soluble Species

Contribution of specific residues of the [beta]-solenoid fold to HET-s prion function, amyloid structure and stability

Amyloid-β Can Form Fractal Antenna-Like Networks Responsive to Electromagnetic Beating and Wireless Signaling

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