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Widespread, routine occurrence of pharmaceuticals in sewage effluent, combined sewer overflows and receiving waters

Environmental pollution (1987), 2017-01, Vol.220 (Pt B), p.1447-1455

2017

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Ion Mobility Spectrometry–Mass Spectrometry Defines the Oligomeric Intermediates in Amylin Amyloid Formation and the Mode of Action of Inhibitors

Journal of the American Chemical Society, 2014-01, Vol.136 (2), p.660-670

2014

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Lateral opening in the intact β-barrel assembly machinery captured by cryo-EM

Nature communications, 2016-09, Vol.7 (1), p.12865-12865, Article 12865

2016

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Screening and classifying small-molecule inhibitors of amyloid formation using ion mobility spectrometry-mass spectrometry

Nature chemistry, 2015-01, Vol.7 (1), p.73-81

2015

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Inter-domain dynamics in the chaperone SurA and multi-site binding to its outer membrane protein clients

Nature communications, 2020-05, Vol.11 (1), p.2155-2155, Article 2155

2020

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Long-Range Conformational Changes in Monoclonal Antibodies Revealed Using FPOP-LC-MS/MS

Analytical chemistry (Washington), 2019-12, Vol.91 (23), p.15163-15170

2019

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Effect of Sequence Variation on the Mechanical Response of Amyloid Fibrils Probed by Steered Molecular Dynamics Simulation

Biophysical journal, 2012-02, Vol.102 (3), p.587-596

2012

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Elongated oligomers in β₂-microglobulin amyloid assembly revealed by ion mobility spectrometry-mass spectrometry

Proceedings of the National Academy of Sciences - PNAS, 2010-04, Vol.107 (15), p.6794-6798

2010

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ESI-IMS–MS: A method for rapid analysis of protein aggregation and its inhibition by small molecules

Methods (San Diego, Calif.), 2016-02, Vol.95, p.62-69

2016

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Investigation of D76N β2‑Microglobulin Using Protein Footprinting and Structural Mass Spectrometry

Journal of the American Society for Mass Spectrometry, 2021-07, Vol.32 (7), p.1583-1592

2021

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An in vivo platform to select and evolve aggregation-resistant proteins

Nature communications, 2020-04, Vol.11 (1), p.1816-12, Article 1816

2020

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Understanding co-polymerization in amyloid formation by direct observation of mixed oligomers

Chemical science (Cambridge), 2017-07, Vol.8 (7), p.5030-5040

2017

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Investigating the Structural Compaction of Biomolecules Upon Transition to the Gas-Phase Using ESI-TWIMS-MS

Journal of the American Society for Mass Spectrometry, 2017-09, Vol.28 (9), p.1855-1862

2017

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Role of ADAMs in the Ectodomain Shedding and Conformational Conversion of the Prion Protein

The Journal of biological chemistry, 2009-08, Vol.284 (34), p.22590-22600

2009

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Examination of Ataxin-3 (atx-3) Aggregation by Structural Mass Spectrometry Techniques: A Rationale for Expedited Aggregation upon Polyglutamine (polyQ) Expansion

Molecular & cellular proteomics, 2015-05, Vol.14 (5), p.1241-1253

2015

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Thermodynamic origins of protein folding, allostery, and capsid formation in the human hepatitis B virus core protein

Proceedings of the National Academy of Sciences - PNAS, 2013-07, Vol.110 (30), p.E2782-E2791

2013

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Analysis of Amyloid Nanostructures Using Photo-cross-linking: In Situ Comparison of Three Widely Used Photo-cross-linkers

ACS chemical biology, 2014-03, Vol.9 (3), p.761-768

2014

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Topological Dissection of the Membrane Transport Protein Mhp1 Derived from Cysteine Accessibility and Mass Spectrometry

Analytical chemistry (Washington), 2017-09, Vol.89 (17), p.8844-8852

2017

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Using Ion Mobility Spectrometry–Mass Spectrometry to Decipher the Conformational and Assembly Characteristics of the Hepatitis B Capsid Protein

Biophysical journal, 2013-09, Vol.105 (5), p.1258-1267

2013

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Monitoring Copopulated Conformational States During Protein Folding Events Using Electrospray Ionization-Ion Mobility Spectrometry-Mass Spectrometry

Journal of the American Society for Mass Spectrometry, 2007-12, Vol.18 (12), p.2180-2190

2007

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Assembly Pathway of Hepatitis B Core Virus-like Particles from Genetically Fused Dimers

The Journal of biological chemistry, 2015-06, Vol.290 (26), p.16238-16245

2015

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Cytokine Spätzle binds to the Drosophila immunoreceptor Toll with a neurotrophin-like specificity and couples receptor activation

Proceedings of the National Academy of Sciences - PNAS, 2013-12, Vol.110 (51), p.20461-20466

2013

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Expanding the Repertoire of Amyloid Polymorphs by Co-polymerization of Related Protein Precursors

The Journal of biological chemistry, 2013-03, Vol.288 (10), p.7327-7337

2013

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The role of conformational flexibility in β2-microglobulin amyloid fibril formation at neutral pH

Rapid communications in mass spectrometry, 2012-08, Vol.26 (16), p.1783-1792

2012

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Large-Scale Production and Structural and Biophysical Characterizations of the Human Hepatitis B Virus Polymerase

Journal of Virology, 2014-03, Vol.88 (5), p.2584-2599

2014

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Widespread, routine occurrence of pharmaceuticals in sewage effluent, combined sewer overflows and receiving waters

Ion Mobility Spectrometry–Mass Spectrometry Defines the Oligomeric Intermediates in Amylin Amyloid Formation and the Mode of Action of Inhibitors

Lateral opening in the intact β-barrel assembly machinery captured by cryo-EM

Screening and classifying small-molecule inhibitors of amyloid formation using ion mobility spectrometry-mass spectrometry

Inter-domain dynamics in the chaperone SurA and multi-site binding to its outer membrane protein clients

Long-Range Conformational Changes in Monoclonal Antibodies Revealed Using FPOP-LC-MS/MS

Effect of Sequence Variation on the Mechanical Response of Amyloid Fibrils Probed by Steered Molecular Dynamics Simulation

Elongated oligomers in β₂-microglobulin amyloid assembly revealed by ion mobility spectrometry-mass spectrometry

ESI-IMS–MS: A method for rapid analysis of protein aggregation and its inhibition by small molecules

Investigation of D76N β2‑Microglobulin Using Protein Footprinting and Structural Mass Spectrometry

An in vivo platform to select and evolve aggregation-resistant proteins

Understanding co-polymerization in amyloid formation by direct observation of mixed oligomers

Investigating the Structural Compaction of Biomolecules Upon Transition to the Gas-Phase Using ESI-TWIMS-MS

Role of ADAMs in the Ectodomain Shedding and Conformational Conversion of the Prion Protein

Examination of Ataxin-3 (atx-3) Aggregation by Structural Mass Spectrometry Techniques: A Rationale for Expedited Aggregation upon Polyglutamine (polyQ) Expansion

Thermodynamic origins of protein folding, allostery, and capsid formation in the human hepatitis B virus core protein

Analysis of Amyloid Nanostructures Using Photo-cross-linking: In Situ Comparison of Three Widely Used Photo-cross-linkers

Topological Dissection of the Membrane Transport Protein Mhp1 Derived from Cysteine Accessibility and Mass Spectrometry

Using Ion Mobility Spectrometry–Mass Spectrometry to Decipher the Conformational and Assembly Characteristics of the Hepatitis B Capsid Protein

Monitoring Copopulated Conformational States During Protein Folding Events Using Electrospray Ionization-Ion Mobility Spectrometry-Mass Spectrometry

Assembly Pathway of Hepatitis B Core Virus-like Particles from Genetically Fused Dimers

Cytokine Spätzle binds to the Drosophila immunoreceptor Toll with a neurotrophin-like specificity and couples receptor activation

Expanding the Repertoire of Amyloid Polymorphs by Co-polymerization of Related Protein Precursors

The role of conformational flexibility in β2-microglobulin amyloid fibril formation at neutral pH

Large-Scale Production and Structural and Biophysical Characterizations of the Human Hepatitis B Virus Polymerase

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