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Disease‐Associated Tau Phosphorylation Hinders Tubulin Assembly within Tau Condensates

Angewandte Chemie International Edition, 2021-01, Vol.60 (2), p.726-730

International ed. in English, 2021

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Tau stabilizes microtubules by binding at the interface between tubulin heterodimers

Proceedings of the National Academy of Sciences - PNAS, 2015-06, Vol.112 (24), p.7501-7506

2015

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Multivalent cross-linking of actin filaments and microtubules through the microtubule-associated protein Tau

Nature communications, 2017-12, Vol.8 (1), p.1981-12, Article 1981

2017

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Optimization and validation of multi-state NMR protein structures using structural correlations

Journal of biomolecular NMR, 2022-04, Vol.76 (1-2), p.39-47

2022

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Folding of the Tau Protein on Microtubules

Angewandte Chemie (International ed.), 2015-08, Vol.54 (35), p.10347-10351

International ed. in English, 2015

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Die krankheitsassoziierte Tau‐Phosphorylierung behindert die Tubulinpolymerisation in Tau‐Kondensaten

Angewandte Chemie, 2021-01, Vol.133 (2), p.737-741

2021

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Mapping interactions with the chaperone network reveals factors that protect against tau aggregation

Nature structural & molecular biology, 2018-05, Vol.25 (5), p.384-393

2018

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Multi‐Dimensional Structure and Dynamics Landscape of Proteins in Mammalian Cells Revealed by In‐Cell NMR

Angewandte Chemie International Edition, 2023-01, Vol.62 (4), p.e202213976-n/a

International ed. in English, 2023

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Structural Impact of Tau Phosphorylation at Threonine 231

Structure (London), 2015-08, Vol.23 (8), p.1448-1458

2015

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PDBcor: An automated correlation extraction calculator for multi-state protein structures

Structure (London), 2022-04, Vol.30 (4), p.646-652.e2

2022

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The Binding Mode of a Tau Peptide with Tubulin

Angewandte Chemie International Edition, 2018-03, Vol.57 (12), p.3246-3250

International ed. in English, 2018

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Atomic resolution protein allostery from the multi-state structure of a PDZ domain

Nature communications, 2022-10, Vol.13 (1), p.6232-6232, Article 6232

2022

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Protein Allostery at Atomic Resolution

Angewandte Chemie International Edition, 2020-12, Vol.59 (49), p.22132-22139

International ed. in English, 2020

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Phosphorylation of Human Tau Protein by Microtubule Affinity-Regulating Kinase 2

Biochemistry (Easton), 2013-12, Vol.52 (50), p.9068-9079

2013

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Multi‐Dimensional Structure and Dynamics Landscape of Proteins in Mammalian Cells Revealed by In‐Cell NMR

Angewandte Chemie, 2023-01, Vol.135 (4), p.n/a

2023

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Der Bindungsmodus eines Tau‐Peptids mit Tubulin

Angewandte Chemie, 2018-03, Vol.130 (12), p.3301-3305

2018

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An improved, time-efficient approach to extract accurate distance restraints for NMR2 structure calculation

Magnetic Resonance : (Göttingen), 2022-08, Vol.3 (2), p.137-144

2022

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Evaluation of the methoxy-X04 derivative BSC4090 for diagnosis of prodromal and early Alzheimer’s disease from bioptic olfactory mucosa

European archives of psychiatry and clinical neuroscience, 2019-12, Vol.269 (8), p.973-984

2019

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The 100-protein NMR spectra dataset: A resource for biomolecular NMR data analysis

Scientific data, 2024-01, Vol.11 (1), p.30-30, Article 30

2024

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Protein structure determination in human cells by in-cell NMR and a reporter system to optimize protein delivery or transexpression

Communications biology, 2022-12, Vol.5 (1), p.1322-1322, Article 1322

2022

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Protein Allostery at Atomic Resolution

Angewandte Chemie, 2020-12, Vol.132 (49), p.22316-22323

2020

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NMR tools to detect protein allostery

Current opinion in structural biology, 2024-06, Vol.86, p.102792-102792, Article 102792

2024

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Rapid Protein–Ligand Affinity Determination by Photoinduced Hyperpolarized NMR

Journal of the American Chemical Society, 2024-07, Vol.146 (26), p.17974-17985

2024

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Ultrafast Fragment Screening Using Photo-Hyperpolarized (CIDNP) NMR

Journal of the American Chemical Society, 2023-06, Vol.145 (22), p.12066-12080

2023

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A structural rationale for reversible vs irreversible amyloid fibril formation from a single protein

Nature communications, 2024-09, Vol.15 (1), p.8448, Article 8448

2024

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Disease‐Associated Tau Phosphorylation Hinders Tubulin Assembly within Tau Condensates

Tau stabilizes microtubules by binding at the interface between tubulin heterodimers

Multivalent cross-linking of actin filaments and microtubules through the microtubule-associated protein Tau

Optimization and validation of multi-state NMR protein structures using structural correlations

Folding of the Tau Protein on Microtubules

Die krankheitsassoziierte Tau‐Phosphorylierung behindert die Tubulinpolymerisation in Tau‐Kondensaten

Mapping interactions with the chaperone network reveals factors that protect against tau aggregation

Multi‐Dimensional Structure and Dynamics Landscape of Proteins in Mammalian Cells Revealed by In‐Cell NMR

Structural Impact of Tau Phosphorylation at Threonine 231

PDBcor: An automated correlation extraction calculator for multi-state protein structures

The Binding Mode of a Tau Peptide with Tubulin

Atomic resolution protein allostery from the multi-state structure of a PDZ domain

Protein Allostery at Atomic Resolution

Phosphorylation of Human Tau Protein by Microtubule Affinity-Regulating Kinase 2

Multi‐Dimensional Structure and Dynamics Landscape of Proteins in Mammalian Cells Revealed by In‐Cell NMR

Der Bindungsmodus eines Tau‐Peptids mit Tubulin

An improved, time-efficient approach to extract accurate distance restraints for NMR2 structure calculation

Evaluation of the methoxy-X04 derivative BSC4090 for diagnosis of prodromal and early Alzheimer’s disease from bioptic olfactory mucosa

The 100-protein NMR spectra dataset: A resource for biomolecular NMR data analysis

Protein structure determination in human cells by in-cell NMR and a reporter system to optimize protein delivery or transexpression

Protein Allostery at Atomic Resolution

NMR tools to detect protein allostery

Rapid Protein–Ligand Affinity Determination by Photoinduced Hyperpolarized NMR

Ultrafast Fragment Screening Using Photo-Hyperpolarized (CIDNP) NMR

A structural rationale for reversible vs irreversible amyloid fibril formation from a single protein

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