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Novel Lipofuscin Bisretinoids Prominent in Human Retina and in a Model of Recessive Stargardt Disease

The Journal of biological chemistry, 2009-07, Vol.284 (30), p.20155-20166

2009

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Cataract-associated mutant E107A of human γD-crystallin shows increased attraction to α-crystallin and enhanced light scattering

Proceedings of the National Academy of Sciences - PNAS, 2011-01, Vol.108 (2), p.574-579

2011

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Altered phase diagram due to a single point mutation in human γD-crystallin

Proceedings of the National Academy of Sciences - PNAS, 2007-10, Vol.104 (43), p.16856-16861

2007

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Crystal Cataracts: Human Genetic Cataract Caused by Protein Crystallization

Proceedings of the National Academy of Sciences - PNAS, 2001-05, Vol.98 (11), p.6116-6120

2001

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Oxidation of active cysteines mediates protein aggregation of S10R, the cataract‐associated mutant of mouse GammaB‐crystallin

Proteins, structure, function, and bioinformatics, 2022-11, Vol.90 (11), p.1987-2000

2022

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Effect of Polyethylene Glycol on the Liquid-Liquid Phase Transition in Aqueous Protein Solutions

Proceedings of the National Academy of Sciences - PNAS, 2002-10, Vol.99 (22), p.14165-14170

2002

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Deamidation of Human γS-Crystallin Increases Attractive Protein Interactions: Implications for Cataract

Biochemistry (Easton), 2015-08, Vol.54 (31), p.4890-4899

2015

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Nuclear Magnetic Resonance-Based Structural Characterization and Backbone Dynamics of Recombinant Bee Venom Melittin

Biochemistry (Easton), 2018-05, Vol.57 (19), p.2775-2785

2018

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Helical Structure of Recombinant Melittin

The journal of physical chemistry. B, 2019-01, Vol.123 (2), p.356-368

2019

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Single-Walled Carbon Nanotubes Probing the Denaturation of Lysozyme

Journal of physical chemistry. C, 2010-05, Vol.114 (17), p.7717-7720

2010

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Molecular Basis of a Progressive Juvenile-Onset Hereditary Cataract

Proceedings of the National Academy of Sciences - PNAS, 2000-02, Vol.97 (5), p.1993-1998

2000

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High Resolution NMR Structure and Backbone Dynamics of Recombinant Bee Venom Melittin

Biochemistry (Easton), 2018-04, Vol.57 (19), p.2775-2785

2018

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Hydrophobic residues of melittin mediate its binding to αA−crystallin

Protein science, 2020-02, Vol.29 (2), p.572-588

2020

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Self-Assembly of Helical Ribbons

Proceedings of the National Academy of Sciences - PNAS, 1999-07, Vol.96 (14), p.7883-7887

1999

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The cataract-associated V41M mutant of human γS-crystallin shows specific structural changes that directly enhance local surface hydrophobicity

Biochemical and biophysical research communications, 2014-01, Vol.443 (1), p.110-114

2014

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RNA aptamers targeted for human αA-crystallin do not bind αB-crystallin, and spare the α−crystallin domain

Biochemical and biophysical research communications, 2017-09, Vol.491 (2), p.423-428

2017

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Molecular Mechanism of the Chaperone Function of Mini-α-Crystallin, a 19-Residue Peptide of Human α‑Crystallin

Biochemistry (Easton), 2015-01, Vol.54 (2), p.505-515

2015

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The Cataract-Associated R14C Mutant of Human γD-Crystallin Shows a Variety of Intermolecular Disulfide Cross-Links: A Raman Spectroscopic Study

Biochemistry (Easton), 2009-06, Vol.48 (22), p.4937-4945

2009

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Nuclear Magnetic Resonance Structure of a Major Lens Protein, Human γC-Crystallin: Role of the Dipole Moment in Protein Solubility

Biochemistry (Easton), 2016-06, Vol.55 (22), p.3136-3149

2016

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Binding of γ-Crystallin Substrate Prevents the Binding of Copper and Zinc Ions to the Molecular Chaperone α-Crystallin

Biochemistry (Easton), 2011-04, Vol.50 (16), p.3279-3281

2011

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The Cataract-associated V41M1 mutant of human γS-crystallin shows specific structural changes that directly enhance local surface hydrophobicity2

Biochemical and biophysical research communications, 2013-11, Vol.443 (1), p.110-114

2013

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Increase in Surface Hydrophobicity of the Cataract-Associated P23T Mutant of Human γD-Crystallin Is Responsible for Its Dramatically Lower, Retrograde Solubility

Biochemistry (Easton), 2010-07, Vol.49 (29), p.6122-6129

2010

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High-resolution X-ray Crystal Structures of Human γD Crystallin (1.25 Å) and the R58H Mutant (1.15 Å) Associated with Aculeiform Cataract

Journal of molecular biology, 2003-05, Vol.328 (5), p.1137-1147

2003

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NMR study of the cataract-linked P23T mutant of human γD-crystallin shows minor changes in hydrophobic patches that reflect its retrograde solubility

Biochemical and biophysical research communications, 2009-04, Vol.382 (1), p.196-199

2009

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Increased Hydrophobicity and Decreased Backbone Flexibility Explain the Lower Solubility of a Cataract-Linked Mutant of γD-Crystallin

Journal of molecular biology, 2011-09, Vol.412 (4), p.647-659

2011

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Novel Lipofuscin Bisretinoids Prominent in Human Retina and in a Model of Recessive Stargardt Disease

Cataract-associated mutant E107A of human γD-crystallin shows increased attraction to α-crystallin and enhanced light scattering

Altered phase diagram due to a single point mutation in human γD-crystallin

Crystal Cataracts: Human Genetic Cataract Caused by Protein Crystallization

Oxidation of active cysteines mediates protein aggregation of S10R, the cataract‐associated mutant of mouse GammaB‐crystallin

Effect of Polyethylene Glycol on the Liquid-Liquid Phase Transition in Aqueous Protein Solutions

Deamidation of Human γS-Crystallin Increases Attractive Protein Interactions: Implications for Cataract

Nuclear Magnetic Resonance-Based Structural Characterization and Backbone Dynamics of Recombinant Bee Venom Melittin

Helical Structure of Recombinant Melittin

Single-Walled Carbon Nanotubes Probing the Denaturation of Lysozyme

Molecular Basis of a Progressive Juvenile-Onset Hereditary Cataract

High Resolution NMR Structure and Backbone Dynamics of Recombinant Bee Venom Melittin

Hydrophobic residues of melittin mediate its binding to αA−crystallin

Self-Assembly of Helical Ribbons

The cataract-associated V41M mutant of human γS-crystallin shows specific structural changes that directly enhance local surface hydrophobicity

RNA aptamers targeted for human αA-crystallin do not bind αB-crystallin, and spare the α−crystallin domain

Molecular Mechanism of the Chaperone Function of Mini-α-Crystallin, a 19-Residue Peptide of Human α‑Crystallin

The Cataract-Associated R14C Mutant of Human γD-Crystallin Shows a Variety of Intermolecular Disulfide Cross-Links: A Raman Spectroscopic Study

Nuclear Magnetic Resonance Structure of a Major Lens Protein, Human γC-Crystallin: Role of the Dipole Moment in Protein Solubility

Binding of γ-Crystallin Substrate Prevents the Binding of Copper and Zinc Ions to the Molecular Chaperone α-Crystallin

The Cataract-associated V41M1 mutant of human γS-crystallin shows specific structural changes that directly enhance local surface hydrophobicity2

Increase in Surface Hydrophobicity of the Cataract-Associated P23T Mutant of Human γD-Crystallin Is Responsible for Its Dramatically Lower, Retrograde Solubility

High-resolution X-ray Crystal Structures of Human γD Crystallin (1.25 Å) and the R58H Mutant (1.15 Å) Associated with Aculeiform Cataract

NMR study of the cataract-linked P23T mutant of human γD-crystallin shows minor changes in hydrophobic patches that reflect its retrograde solubility

Increased Hydrophobicity and Decreased Backbone Flexibility Explain the Lower Solubility of a Cataract-Linked Mutant of γD-Crystallin

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