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Genetically Encoded Copper-Free Click Chemistry

Angewandte Chemie International Edition, 2011-04, Vol.50 (17), p.3878-3881

International ed. in English, 2011

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Molecular basis of host-adaptation interactions between influenza virus polymerase PB2 subunit and ANP32A

Nature communications, 2020-07, Vol.11 (1), p.3656-3656, Article 3656

2020

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Plasticity of an Ultrafast Interaction between Nucleoporins and Nuclear Transport Receptors

Cell, 2015-10, Vol.163 (3), p.734-745

2015

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Die dynamische Funktion intrinsisch ungeordneter Proteine

Biospektrum, 2023-06, Vol.29 (4), p.351-353

Milles, Sigrid

2023

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Single Molecule Study of the Intrinsically Disordered FG-Repeat Nucleoporin 153

Biophysical journal, 2011-10, Vol.101 (7), p.1710-1719

2011

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Deciphering the Dynamic Interaction Profile of an Intrinsically Disordered Protein by NMR Exchange Spectroscopy

Journal of the American Chemical Society, 2018-01, Vol.140 (3), p.1148-1158

2018

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Kirkwood–Buff Approach Rescues Overcollapse of a Disordered Protein in Canonical Protein Force Fields

The journal of physical chemistry. B, 2015-06, Vol.119 (25), p.7975-7984

2015

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An extended interaction site determines binding between AP180 and AP2 in clathrin mediated endocytosis

Nature communications, 2024-07, Vol.15 (1), p.5884-14, Article 5884

2024

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Synergies of Single Molecule Fluorescence and NMR for the Study of Intrinsically Disordered Proteins

Biomolecules (Basel, Switzerland), 2021-12, Vol.12 (1), p.27

2021

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The Nucleoprotein and Phosphoprotein of Measles Virus

Frontiers in microbiology, 2019-08, Vol.10 (1832), p.1832-1832

2019

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Facilitated aggregation of FG nucleoporins under molecular crowding conditions

EMBO reports, 2013-02, Vol.14 (2), p.178-183

2013

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Genetic Encoding of a Bicyclo[6.1.0]nonyne-Charged Amino Acid Enables Fast Cellular Protein Imaging by Metal-Free Ligation

Chembiochem : a European journal of chemical biology, 2012-09, Vol.13 (14), p.2094-2099

2012

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Self-Assembly of Measles Virus Nucleocapsid-like Particles: Kinetics and RNA Sequence Dependence

Angewandte Chemie International Edition, 2016-08, Vol.55 (32), p.9356-9360

International ed. in English, 2016

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Continuous throughput and long-term observation of single-molecule FRET without immobilization

Nature methods, 2014-03, Vol.11 (3), p.297-300

2014

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Die dynamische Funktion intrinsisch ungeordneter Proteine

Biospektrum, 2023-06, Vol.29 (4), p.351-353

Milles, Sigrid

2023

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An ultraweak interaction in the intrinsically disordered replication machinery is essential for measles virus function

Science advances, 2018-08, Vol.4 (8), p.eaat7778-eaat7778

2018

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Organization of fluorescent cholesterol analogs in lipid bilayers — Lessons from cyclodextrin extraction

Biochimica et biophysica acta, 2013-08, Vol.1828 (8), p.1822-1828

2013

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Solubilization of Protein Aggregates by the Acid Stress Chaperones HdeA and HdeB

The Journal of biological chemistry, 2008-05, Vol.283 (20), p.13679-13687

2008

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Nuclear magnetic resonance/single molecule fluorescence combinations to study dynamic protein systems

Current opinion in structural biology, 2023-10, Vol.82, p.102659, Article 102659

2023

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Quantitative Description of Intrinsically Disordered Proteins Using Single-Molecule FRET, NMR, and SAXS

Journal of the American Chemical Society, 2021-12, Vol.143 (48), p.20109-20121

2021

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Investigating the Role of Large-Scale Domain Dynamics in Protein-Protein Interactions

Frontiers in molecular biosciences, 2016-09, Vol.3, p.54-54

2016

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Characterization of intrinsically disordered proteins and their dynamic complexes: From in vitro to cell-like environments

Progress in nuclear magnetic resonance spectroscopy, 2018-12, Vol.109, p.79-100

2018

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The Yeast Plasma Membrane ATP Binding Cassette (ABC) Transporter Aus1

The Journal of biological chemistry, 2011-06, Vol.286 (24), p.21835-21843

2011

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NMR Provides Unique Insight into the Functional Dynamics and Interactions of Intrinsically Disordered Proteins

Chemical reviews, 2022-05, Vol.122 (10), p.9331-9356

2022

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A Unified Description of Intrinsically Disordered Protein Dynamics under Physiological Conditions Using NMR Spectroscopy

Journal of the American Chemical Society, 2019-11, Vol.141 (44), p.17817-17829

2019

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Genetically Encoded Copper-Free Click Chemistry

Molecular basis of host-adaptation interactions between influenza virus polymerase PB2 subunit and ANP32A

Plasticity of an Ultrafast Interaction between Nucleoporins and Nuclear Transport Receptors

Die dynamische Funktion intrinsisch ungeordneter Proteine

Single Molecule Study of the Intrinsically Disordered FG-Repeat Nucleoporin 153

Deciphering the Dynamic Interaction Profile of an Intrinsically Disordered Protein by NMR Exchange Spectroscopy

Kirkwood–Buff Approach Rescues Overcollapse of a Disordered Protein in Canonical Protein Force Fields

An extended interaction site determines binding between AP180 and AP2 in clathrin mediated endocytosis

Synergies of Single Molecule Fluorescence and NMR for the Study of Intrinsically Disordered Proteins

The Nucleoprotein and Phosphoprotein of Measles Virus

Facilitated aggregation of FG nucleoporins under molecular crowding conditions

Genetic Encoding of a Bicyclo[6.1.0]nonyne-Charged Amino Acid Enables Fast Cellular Protein Imaging by Metal-Free Ligation

Self-Assembly of Measles Virus Nucleocapsid-like Particles: Kinetics and RNA Sequence Dependence

Continuous throughput and long-term observation of single-molecule FRET without immobilization

Die dynamische Funktion intrinsisch ungeordneter Proteine

An ultraweak interaction in the intrinsically disordered replication machinery is essential for measles virus function

Organization of fluorescent cholesterol analogs in lipid bilayers — Lessons from cyclodextrin extraction

Solubilization of Protein Aggregates by the Acid Stress Chaperones HdeA and HdeB

Nuclear magnetic resonance/single molecule fluorescence combinations to study dynamic protein systems

Quantitative Description of Intrinsically Disordered Proteins Using Single-Molecule FRET, NMR, and SAXS

Investigating the Role of Large-Scale Domain Dynamics in Protein-Protein Interactions

Characterization of intrinsically disordered proteins and their dynamic complexes: From in vitro to cell-like environments

The Yeast Plasma Membrane ATP Binding Cassette (ABC) Transporter Aus1

NMR Provides Unique Insight into the Functional Dynamics and Interactions of Intrinsically Disordered Proteins

A Unified Description of Intrinsically Disordered Protein Dynamics under Physiological Conditions Using NMR Spectroscopy

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