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Single molecule secondary structure determination of proteins through infrared absorption nanospectroscopy

Nature communications, 2020-06, Vol.11 (1), p.2945-2945, Article 2945

2020

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Molecular mechanisms of protein aggregation from global fitting of kinetic models

Nature protocols, 2016-02, Vol.11 (2), p.252-272

2016

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From Protein Building Blocks to Functional Materials

ACS nano, 2021-04, Vol.15 (4), p.5819-5837

2021

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Nucleation and Growth of Amino Acid and Peptide Supramolecular Polymers through Liquid–Liquid Phase Separation

Angewandte Chemie International Edition, 2019-12, Vol.58 (50), p.18116-18123

International ed. in English, 2019

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Learning the molecular grammar of protein condensates from sequence determinants and embeddings

Proceedings of the National Academy of Sciences - PNAS, 2021-04, Vol.118 (15), p.1-11

2021

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The role of fibril structure and surface hydrophobicity in secondary nucleation of amyloid fibrils

Proceedings of the National Academy of Sciences - PNAS, 2020-10, Vol.117 (41), p.25272-25283

2020

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Physical determinants of the self-replication of protein fibrils

Nature physics, 2016-09, Vol.12 (9), p.874-880

2016

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Determination of Polypeptide Conformation with Nanoscale Resolution in Water

ACS nano, 2018-07, Vol.12 (7), p.6612-6619

2018

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Controlled self-assembly of plant proteins into high-performance multifunctional nanostructured films

Nature communications, 2021-06, Vol.12 (1), p.3529-10, Article 3529

2021

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Expanding the Solvent Chemical Space for Self-Assembly of Dipeptide Nanostructures

ACS nano, 2014-02, Vol.8 (2), p.1243-1253

2014

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Crucial role of nonspecific interactions in amyloid nucleation

Proceedings of the National Academy of Sciences - PNAS, 2014-12, Vol.111 (50), p.17869-17874

2014

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Biomolecular condensates undergo a generic shear-mediated liquid-to-solid transition

Nature nanotechnology, 2020-10, Vol.15 (10), p.841-847

2020

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Shear-mediated sol-gel transition of regenerated silk allows the formation of Janus-like microgels

Scientific reports, 2021-03, Vol.11 (1), p.6673-10, Article 6673

2021

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Small soluble α-synuclein aggregates are the toxic species in Parkinson’s disease

Nature communications, 2022-09, Vol.13 (1), p.5512-5512, Article 5512

2022

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Different soluble aggregates of Aβ42 can give rise to cellular toxicity through different mechanisms

Nature communications, 2019-04, Vol.10 (1), p.1541-11, Article 1541

2019

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Analytical Solution to the Kinetics of Breakable Filament Assembly

Science (American Association for the Advancement of Science), 2009-12, Vol.326 (5959), p.1533-1537

2009

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Bioprinting microporous functional living materials from protein-based core-shell microgels

Nature communications, 2023-01, Vol.14 (1), p.322-322, Article 322

2023

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Flow photochemistry: Old light through new windows

Beilstein journal of organic chemistry, 2012-11, Vol.8 (1), p.2025-2052

2012

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Label-Free Analysis of Protein Aggregation and Phase Behavior

ACS nano, 2019-12, Vol.13 (12), p.13940-13948

2019

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Identification of on- and off-pathway oligomers in amyloid fibril formation

Chemical science (Cambridge), 2020-06, Vol.11 (24), p.6236-6247

2020

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Phase-separating RNA-binding proteins form heterogeneous distributions of clusters in subsaturated solutions

Proceedings of the National Academy of Sciences - PNAS, 2022-07, Vol.119 (28), p.e2202222119-e2202222119

2022

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Kinetic model of the aggregation of alpha-synuclein provides insights into prion-like spreading

Proceedings of the National Academy of Sciences - PNAS, 2016-03, Vol.113 (9), p.E1206-E1215

2016

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Surface Electrostatics Govern the Emulsion Stability of Biomolecular Condensates

Nano letters, 2022-01, Vol.22 (2), p.612-621

2022

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Kinetic diversity of amyloid oligomers

Proceedings of the National Academy of Sciences - PNAS, 2020-06, Vol.117 (22), p.12087-12094

2020

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Transthyretin Inhibits Primary and Secondary Nucleations of Amyloid‑β Peptide Aggregation and Reduces the Toxicity of Its Oligomers

Biomacromolecules, 2020-03, Vol.21 (3), p.1112-1125

2020

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Single molecule secondary structure determination of proteins through infrared absorption nanospectroscopy

Molecular mechanisms of protein aggregation from global fitting of kinetic models

From Protein Building Blocks to Functional Materials

Nucleation and Growth of Amino Acid and Peptide Supramolecular Polymers through Liquid–Liquid Phase Separation

Learning the molecular grammar of protein condensates from sequence determinants and embeddings

The role of fibril structure and surface hydrophobicity in secondary nucleation of amyloid fibrils

Physical determinants of the self-replication of protein fibrils

Determination of Polypeptide Conformation with Nanoscale Resolution in Water

Controlled self-assembly of plant proteins into high-performance multifunctional nanostructured films

Expanding the Solvent Chemical Space for Self-Assembly of Dipeptide Nanostructures

Crucial role of nonspecific interactions in amyloid nucleation

Biomolecular condensates undergo a generic shear-mediated liquid-to-solid transition

Shear-mediated sol-gel transition of regenerated silk allows the formation of Janus-like microgels

Small soluble α-synuclein aggregates are the toxic species in Parkinson’s disease

Different soluble aggregates of Aβ42 can give rise to cellular toxicity through different mechanisms

Analytical Solution to the Kinetics of Breakable Filament Assembly

Bioprinting microporous functional living materials from protein-based core-shell microgels

Flow photochemistry: Old light through new windows

Label-Free Analysis of Protein Aggregation and Phase Behavior

Identification of on- and off-pathway oligomers in amyloid fibril formation

Phase-separating RNA-binding proteins form heterogeneous distributions of clusters in subsaturated solutions

Kinetic model of the aggregation of alpha-synuclein provides insights into prion-like spreading

Surface Electrostatics Govern the Emulsion Stability of Biomolecular Condensates

Kinetic diversity of amyloid oligomers

Transthyretin Inhibits Primary and Secondary Nucleations of Amyloid‑β Peptide Aggregation and Reduces the Toxicity of Its Oligomers

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