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Structural basis for mutation-induced destabilization of profilin 1 in ALS

Proceedings of the National Academy of Sciences - PNAS, 2015-06, Vol.112 (26), p.7984-7989

2015

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Folding of the RNA Recognition Motif (RRM) Domains of the Amyotrophic Lateral Sclerosis (ALS)-linked Protein TDP-43 Reveals an Intermediate State

The Journal of biological chemistry, 2014-03, Vol.289 (12), p.8264-8276

2014

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Disulfide-Reduced ALS Variants of Cu, Zn Superoxide Dismutase Exhibit Increased Populations of Unfolded Species

Journal of molecular biology, 2010-04, Vol.398 (2), p.320-331

2010

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Characterization of TDP-43 RRM2 Partially Folded States and Their Significance to ALS Pathogenesis

Biophysical journal, 2018-11, Vol.115 (9), p.1673-1680

2018

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Metal-free ALS variants of dimeric human Cu,Zn-superoxide dismutase have enhanced populations of monomeric species

PloS one, 2010-04, Vol.5 (4), p.e10064-e10064

2010

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Mapping the Folding Free Energy Surface for Metal-free Human Cu,Zn Superoxide Dismutase

Journal of molecular biology, 2006-12, Vol.364 (5), p.1084-1102

2006

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Mapping the Structure of Folding Cores in TIM Barrel Proteins by Hydrogen Exchange Mass Spectrometry: The Roles of Motif and Sequence for the Indole-3-glycerol Phosphate Synthase from Sulfolobus solfataricus

Journal of molecular biology, 2007-04, Vol.368 (2), p.582-594

2007

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Structural Rearrangement upon Fragmentation of the Stability Core of the ALS-Linked Protein TDP-43

Biophysical journal, 2017-08, Vol.113 (3), p.540-549

2017

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Nonnative structure in a peptide model of the unfolded state of superoxide dismutase 1 (SOD1): Implications for ALS-linked aggregation

The Journal of biological chemistry, 2019-09, Vol.294 (37), p.13708-13717

2019

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Trifluoroethanol Partially Unfolds G93A SOD1 Leading to Protein Aggregation: A Study by Native Mass Spectrometry and FPOP Protein Footprinting

Biochemistry (Easton), 2020-10, Vol.59 (39), p.3650-3659

2020

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Friction-Limited Folding of Disulfide-Reduced Monomeric SOD1

Biophysical journal, 2020-04, Vol.118 (8), p.1992-2000

2020

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Incorporation of a Reporter Peptide in FPOP Compensates for Adventitious Scavengers and Permits Time-Dependent Measurements

Journal of the American Society for Mass Spectrometry, 2017-02, Vol.28 (2), p.389-392

2017

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Preformed secondary structure drives the association reaction of GCN4-p1, a model coiled-coil system

Journal of molecular biology, 2000-03, Vol.296 (4), p.1105-1116

2000

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Zinc Binding Modulates the Entire Folding Free Energy Surface of Human Cu,Zn Superoxide Dismutase

Journal of molecular biology, 2008-12, Vol.384 (2), p.540-555

2008

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The relationship between chain connectivity and domain stability in the equilibrium and kinetic folding mechanisms of dihydrofolate reductase from E.coli

Protein engineering, design and selection, 2006-04, Vol.19 (4), p.175-185

2006

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The Folding Free-Energy Surface of HIV-1 Protease: Insights into the Thermodynamic Basis for Resistance to Inhibitors

Journal of molecular biology, 2009-04, Vol.387 (4), p.1002-1016

2009

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Salt-bridges can Stabilize but do not Accelerate the Folding of the Homodimeric Coiled-coil Peptide GCN4-p1

Journal of molecular biology, 2004-03, Vol.336 (5), p.989-996

2004

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Folding Mechanism of the α-Subunit of Tryptophan Synthase, an α/β Barrel Protein: Global Analysis Highlights the Interconversion of Multiple Native, Intermediate, and Unfolded Forms through Parallel Channels

Biochemistry (Easton), 1999-01, Vol.38 (3), p.1018-1029

1999

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Probing the Folding Mechanism of a Leucine Zipper Peptide by Stopped-Flow Circular Dichroism Spectroscopy

Biochemistry (Easton), 1995-10, Vol.34 (39), p.12812-12819

1995

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Molecular Dissection of the Folding Mechanism of the α Subunit of Tryptophan Synthase: An Amino-Terminal Autonomous Folding Unit Controls Several Rate-Limiting Steps in the Folding of a Single Domain Protein

Biochemistry (Easton), 1999-08, Vol.38 (31), p.10205-10214

1999

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A Buried Polar Residue in the Hydrophobic Interface of the Coiled-coil Peptide, GCN4-p1, Plays a Thermodynamic, not a Kinetic Role in Folding

Journal of molecular biology, 2002-08, Vol.321 (1), p.1-6

2002

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Examination of the Oligomerization Mechanism of SOD1 In Vitro and in Live Cells

Biophysical journal, 2017-02, Vol.112 (3), p.316a-316a

2017

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Apparent Radii of the Native, Stable Intermediates and Unfolded Conformers of the α-Subunit of Tryptophan Synthase from E. coli, a TIM Barrel Protein

Biochemistry (Easton), 1999-10, Vol.38 (40), p.13367-13378

1999

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Time-Resolved Fluorescence Anisotropy Study of the Refolding Reaction of the α-Subunit of Tryptophan Synthase Reveals Nonmonotonic Behavior of the Rotational Correlation Time

Biochemistry (Easton), 1999-03, Vol.38 (13), p.4177-4187

1999

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Structural basis for mutation-induced destabilization of profilin 1 in ALS

Folding of the RNA Recognition Motif (RRM) Domains of the Amyotrophic Lateral Sclerosis (ALS)-linked Protein TDP-43 Reveals an Intermediate State

Disulfide-Reduced ALS Variants of Cu, Zn Superoxide Dismutase Exhibit Increased Populations of Unfolded Species

Characterization of TDP-43 RRM2 Partially Folded States and Their Significance to ALS Pathogenesis

Metal-free ALS variants of dimeric human Cu,Zn-superoxide dismutase have enhanced populations of monomeric species

Mapping the Folding Free Energy Surface for Metal-free Human Cu,Zn Superoxide Dismutase

Mapping the Structure of Folding Cores in TIM Barrel Proteins by Hydrogen Exchange Mass Spectrometry: The Roles of Motif and Sequence for the Indole-3-glycerol Phosphate Synthase from Sulfolobus solfataricus

Structural Rearrangement upon Fragmentation of the Stability Core of the ALS-Linked Protein TDP-43

Nonnative structure in a peptide model of the unfolded state of superoxide dismutase 1 (SOD1): Implications for ALS-linked aggregation

Trifluoroethanol Partially Unfolds G93A SOD1 Leading to Protein Aggregation: A Study by Native Mass Spectrometry and FPOP Protein Footprinting

Friction-Limited Folding of Disulfide-Reduced Monomeric SOD1

Incorporation of a Reporter Peptide in FPOP Compensates for Adventitious Scavengers and Permits Time-Dependent Measurements

Preformed secondary structure drives the association reaction of GCN4-p1, a model coiled-coil system

Zinc Binding Modulates the Entire Folding Free Energy Surface of Human Cu,Zn Superoxide Dismutase

The relationship between chain connectivity and domain stability in the equilibrium and kinetic folding mechanisms of dihydrofolate reductase from E.coli

The Folding Free-Energy Surface of HIV-1 Protease: Insights into the Thermodynamic Basis for Resistance to Inhibitors

Salt-bridges can Stabilize but do not Accelerate the Folding of the Homodimeric Coiled-coil Peptide GCN4-p1

Folding Mechanism of the α-Subunit of Tryptophan Synthase, an α/β Barrel Protein: Global Analysis Highlights the Interconversion of Multiple Native, Intermediate, and Unfolded Forms through Parallel Channels

Probing the Folding Mechanism of a Leucine Zipper Peptide by Stopped-Flow Circular Dichroism Spectroscopy

Molecular Dissection of the Folding Mechanism of the α Subunit of Tryptophan Synthase: An Amino-Terminal Autonomous Folding Unit Controls Several Rate-Limiting Steps in the Folding of a Single Domain Protein

Mutations in the profilin 1 gene cause familial amyotrophic lateral sclerosis

A Buried Polar Residue in the Hydrophobic Interface of the Coiled-coil Peptide, GCN4-p1, Plays a Thermodynamic, not a Kinetic Role in Folding

Examination of the Oligomerization Mechanism of SOD1 In Vitro and in Live Cells

Apparent Radii of the Native, Stable Intermediates and Unfolded Conformers of the α-Subunit of Tryptophan Synthase from E. coli, a TIM Barrel Protein

Time-Resolved Fluorescence Anisotropy Study of the Refolding Reaction of the α-Subunit of Tryptophan Synthase Reveals Nonmonotonic Behavior of the Rotational Correlation Time

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