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NMR Spectroscopic Assignment of Backbone and Side-Chain Protons in Fully Protonated Proteins: Microcrystals, Sedimented Assemblies, and Amyloid Fibrils

Angewandte Chemie (International ed.), 2016-12, Vol.55 (50), p.15504-15509

International ed. in English, 2016

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Membrane-induced tau amyloid fibrils

Communications biology, 2023-04, Vol.6 (1), p.467-467, Article 467

2023

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Structures of AT8 and PHF1 phosphomimetic tau: Insights into the posttranslational modification code of tau aggregation

Proceedings of the National Academy of Sciences - PNAS, 2024-03, Vol.121 (10), p.e2316175121

2024

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Structure of the nonhelical filament of the Alzheimer's disease tau core

Proceedings of the National Academy of Sciences - PNAS, 2023-10, Vol.120 (44), p.e2310067120-e2310067120

2023

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3D structure determination of amyloid fibrils using solid-state NMR spectroscopy

Methods (San Diego, Calif.), 2018-04, Vol.138-139, p.26-38

2018

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Structural and molecular basis of cross-seeding barriers in amyloids

Proceedings of the National Academy of Sciences - PNAS, 2021-01, Vol.118 (1), p.1

2021

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Fluent molecular mixing of Tau isoforms in Alzheimer's disease neurofibrillary tangles

Nature communications, 2022-05, Vol.13 (1), p.2967-2967, Article 2967

2022

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Molecular architecture of bacterial amyloids in Bacillus biofilms

The FASEB journal, 2019-11, Vol.33 (11), p.12146-12163

2019

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Amyloid fibril structures of tau: Conformational plasticity of the second microtubule-binding repeat

Science advances, 2023-07, Vol.9 (28), p.eadh4731-eadh4731

2023

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Structural dissection of amyloid aggregates of TDP‐43 and its C‐terminal fragments TDP‐35 and TDP‐16

The FEBS journal, 2020-06, Vol.287 (12), p.2449-2467

2020

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Structures of Type III Secretion System Needle Filaments

Bacterial Type III Protein Secretion Systems, 2020-01, Vol.427, p.109-131

2020

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Structures of Pathological and Functional Amyloids and Prions, a Solid-State NMR Perspective

Frontiers in molecular neuroscience, 2021-07, Vol.14, p.670513-670513

2021

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Molecular characterization of the N-terminal half of TasA during amyloid-like assembly and its contribution to Bacillus subtilis biofilm formation

NPJ biofilms and microbiomes, 2023-09, Vol.9 (1), p.68-68, Article 68

2023

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Frontispiece: NMR Spectroscopic Assignment of Backbone and Side-Chain Protons in Fully Protonated Proteins: Microcrystals, Sedimented Assemblies, and Amyloid Fibrils

Angewandte Chemie (International ed.), 2016-12, Vol.55 (50), p.n/a

International ed. in English, 2016

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Structural polymorphism of the low-complexity C-terminal domain of TDP-43 amyloid aggregates revealed by solid-state NMR

Frontiers in molecular biosciences, 2023-03, Vol.10, p.1148302-1148302

2023

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Rapid Determination of the Topology of Oligomeric α‑Helical Membrane Proteins by Water- and Lipid-Edited Methyl NMR

The journal of physical chemistry. B, 2023-08, Vol.127 (34), p.7518-7530

2023

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Switchable Lipids: From Conformational Switch to Macroscopic Changes in Lipid Vesicles

Langmuir, 2023-02, Vol.39 (8), p.3072-3082

2023

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Microtubule-binding core of the tau protein

Science advances, 2022-07, Vol.8 (29), p.eabo4459-eabo4459

2022

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Structural dissection of amyloid aggregates of TDP-43 and its C-terminal fragments TDP-35 and TDP-16

The FEBS journal, 2019

2019

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Structural polymorphism of the low-complexity C-terminal domain of TDP-43 amyloid aggregates revealed by solid-state NMR

Frontiers in molecular biosciences, 2023-03, Vol.10

2023

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Backbone and side-chain proton NMR assignment in fully protonated proteins: microcrystals, sedimented assemblies, and amyloid fibrils

Angewandte Chemie (International ed.), 2016-12, Vol.55 (50), p.15504-15509

2016

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NMR Spectroscopic Assignment of Backbone and Side-Chain Protons in Fully Protonated Proteins: Microcrystals, Sedimented Assemblies, and Amyloid Fibrils

Membrane-induced tau amyloid fibrils

Structures of AT8 and PHF1 phosphomimetic tau: Insights into the posttranslational modification code of tau aggregation

Structure of the nonhelical filament of the Alzheimer's disease tau core

3D structure determination of amyloid fibrils using solid-state NMR spectroscopy

Structural and molecular basis of cross-seeding barriers in amyloids

Fluent molecular mixing of Tau isoforms in Alzheimer's disease neurofibrillary tangles

Molecular architecture of bacterial amyloids in Bacillus biofilms

Amyloid fibril structures of tau: Conformational plasticity of the second microtubule-binding repeat

Structural dissection of amyloid aggregates of TDP‐43 and its C‐terminal fragments TDP‐35 and TDP‐16

Structures of Type III Secretion System Needle Filaments

Structures of Pathological and Functional Amyloids and Prions, a Solid-State NMR Perspective

Molecular characterization of the N-terminal half of TasA during amyloid-like assembly and its contribution to Bacillus subtilis biofilm formation

Frontispiece: NMR Spectroscopic Assignment of Backbone and Side-Chain Protons in Fully Protonated Proteins: Microcrystals, Sedimented Assemblies, and Amyloid Fibrils

Structural polymorphism of the low-complexity C-terminal domain of TDP-43 amyloid aggregates revealed by solid-state NMR

Rapid Determination of the Topology of Oligomeric α‑Helical Membrane Proteins by Water- and Lipid-Edited Methyl NMR

Switchable Lipids: From Conformational Switch to Macroscopic Changes in Lipid Vesicles

Microtubule-binding core of the tau protein

Structural dissection of amyloid aggregates of TDP-43 and its C-terminal fragments TDP-35 and TDP-16

Structural polymorphism of the low-complexity C-terminal domain of TDP-43 amyloid aggregates revealed by solid-state NMR

Backbone and side-chain proton NMR assignment in fully protonated proteins: microcrystals, sedimented assemblies, and amyloid fibrils

Zuordnung der Rückgrat- und Seitenketten-Protonen in vollständig protonierten Proteinen durch Festkörper-NMR-Spektroskopie: Mikrokristalle, Sedimente und Amyloidfibrillen

Frontispiz: Zuordnung der Rückgrat- und Seitenketten-Protonen in vollständig protonierten Proteinen durch Festkörper-NMR-Spektroskopie: Mikrokristalle, Sedimente und Amyloidfibrillen

Frontispiz: Zuordnung der Rückgrat‐ und Seitenketten‐Protonen in vollständig protonierten Proteinen durch Festkörper‐NMR‐Spektroskopie: Mikrokristalle, Sedimente und Amyloidfibrillen

Frontispiz: Zuordnung der Rückgrat‐ und Seitenketten‐Protonen in vollständig protonierten Proteinen durch Festkörper‐NMR‐Spektroskopie: Mikrokristalle, Sedimente und Amyloidfibrillen

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