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Monitoring Early-Stage Protein Aggregation by an Aggregation-Induced Emission Fluorogen

Analytical chemistry (Washington), 2017-09, Vol.89 (17), p.9322-9329

2017

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β-Synuclein: An Enigmatic Protein with Diverse Functionality

Biomolecules (Basel, Switzerland), 2022-01, Vol.12 (1), p.142

2022

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The structured core domain of αB-crystallin can prevent amyloid fibrillation and associated toxicity

Proceedings of the National Academy of Sciences - PNAS, 2014-04, Vol.111 (16), p.5771-5771

2014

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Binding of the Molecular Chaperone αB-Crystallin to Aβ Amyloid Fibrils Inhibits Fibril Elongation

Biophysical journal, 2011-10, Vol.101 (7), p.1681-1689

2011

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A multi-pathway perspective on protein aggregation: Implications for control of the rate and extent of amyloid formation

FEBS letters, 2015-03, Vol.589 (6), p.672-679

2015

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Protein aggregate turbidity: Simulation of turbidity profiles for mixed-aggregation reactions

Analytical biochemistry, 2016-04, Vol.498, p.78-94

2016

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The Amyloid Fibril-Forming β-Sheet Regions of Amyloid β and α-Synuclein Preferentially Interact with the Molecular Chaperone 14-3-3ζ

Molecules (Basel, Switzerland), 2021-10, Vol.26 (20), p.6120

2021

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Terminal Regions Confer Plasticity to the Tetrameric Assembly of Human HspB2 and HspB3

Journal of molecular biology, 2018-09, Vol.430 (18), p.3297-3310

2018

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The Effect of Oxidized Dopamine on the Structure and Molecular Chaperone Function of the Small Heat-Shock Proteins, αB-Crystallin and Hsp27

International journal of molecular sciences, 2021-04, Vol.22 (7), p.3700

2021

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Hardware Validation of the Advanced Plant Habitat on ISS: Canopy Photosynthesis in Reduced Gravity

Frontiers in plant science, 2020-06, Vol.11, p.673-673

2020

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Small heat-shock proteins: important players in regulating cellular proteostasis

Cellular and molecular life sciences : CMLS, 2015-02, Vol.72 (3), p.429-451

2015

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The multifaceted nature of αB-crystallin

Cell stress & chaperones, 2020-07, Vol.25 (4), p.639-654

2020

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Recognizing and analyzing variability in amyloid formation kinetics: Simulation and statistical methods

Analytical biochemistry, 2016-10, Vol.510, p.56-71

2016

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Small heat-shock proteins interact with a flanking domain to suppress polyglutamine aggregation

Proceedings of the National Academy of Sciences - PNAS, 2010-06, Vol.107 (23), p.10424-10429

2010

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Measurement of amyloid formation by turbidity assay—seeing through the cloud

Biophysical reviews, 2016, Vol.8 (4), p.445-471

2016

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The dissociated form of kappa-casein is the precursor to its amyloid fibril formation

Biochemical journal, 2010-07, Vol.429 (2), p.251-260

2010

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The Extracellular Molecular Chaperone Clusterin Inhibits Amyloid Fibril Formation and Suppresses Cytotoxicity Associated with Semen-Derived Enhancer of Virus Infection (SEVI)

Cells (Basel, Switzerland), 2022-10, Vol.11 (20), p.3259

2022

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Quantitative multivalent binding model of the structure, size distribution and composition of the casein micelles of cow milk

International dairy journal, 2022-03, Vol.126, p.105292, Article 105292

2022

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Structure of biomimetic casein micelles: Critical tests of the hydrophobic colloid and multivalent-binding models using recombinant deuterated and phosphorylated β-casein

Journal of structural biology. X, 2024-06, Vol.9, p.100096-100096, Article 100096

2024

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Preventing α-synuclein aggregation: The role of the small heat-shock molecular chaperone proteins

Biochimica et biophysica acta, 2014-09, Vol.1842 (9), p.1830-1843

2014

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thioflavin T fluorescence assay for amyloid fibril detection can be biased by the presence of exogenous compounds

The FEBS journal, 2009-10, Vol.276 (20), p.5960-5972

2009

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Functional Amyloid Protection in the Eye Lens: Retention of α-Crystallin Molecular Chaperone Activity after Modification into Amyloid Fibrils

Biomolecules (Basel, Switzerland), 2017-09, Vol.7 (3), p.67

2017

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Amyloid Fibril Formation by Lens Crystallin Proteins and Its Implications for Cataract Formation

The Journal of biological chemistry, 2004-01, Vol.279 (5), p.3413-3419

2004

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A Spectroscopic Marker for Structural Transitions Associated with Amyloid‑β Aggregation

Biochemistry (Easton), 2020-05, Vol.59 (19), p.1813-1822

2020

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Are casein micelles extracellular condensates formed by liquid‐liquid phase separation?

FEBS letters, 2022-08, Vol.596 (16), p.2072-2085

2022

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Monitoring Early-Stage Protein Aggregation by an Aggregation-Induced Emission Fluorogen

β-Synuclein: An Enigmatic Protein with Diverse Functionality

The structured core domain of αB-crystallin can prevent amyloid fibrillation and associated toxicity

Binding of the Molecular Chaperone αB-Crystallin to Aβ Amyloid Fibrils Inhibits Fibril Elongation

A multi-pathway perspective on protein aggregation: Implications for control of the rate and extent of amyloid formation

Protein aggregate turbidity: Simulation of turbidity profiles for mixed-aggregation reactions

The Amyloid Fibril-Forming β-Sheet Regions of Amyloid β and α-Synuclein Preferentially Interact with the Molecular Chaperone 14-3-3ζ

Terminal Regions Confer Plasticity to the Tetrameric Assembly of Human HspB2 and HspB3

The Effect of Oxidized Dopamine on the Structure and Molecular Chaperone Function of the Small Heat-Shock Proteins, αB-Crystallin and Hsp27

Hardware Validation of the Advanced Plant Habitat on ISS: Canopy Photosynthesis in Reduced Gravity

Small heat-shock proteins: important players in regulating cellular proteostasis

The multifaceted nature of αB-crystallin

Recognizing and analyzing variability in amyloid formation kinetics: Simulation and statistical methods

Small heat-shock proteins interact with a flanking domain to suppress polyglutamine aggregation

Measurement of amyloid formation by turbidity assay—seeing through the cloud

The dissociated form of kappa-casein is the precursor to its amyloid fibril formation

The Extracellular Molecular Chaperone Clusterin Inhibits Amyloid Fibril Formation and Suppresses Cytotoxicity Associated with Semen-Derived Enhancer of Virus Infection (SEVI)

Quantitative multivalent binding model of the structure, size distribution and composition of the casein micelles of cow milk

Structure of biomimetic casein micelles: Critical tests of the hydrophobic colloid and multivalent-binding models using recombinant deuterated and phosphorylated β-casein

Preventing α-synuclein aggregation: The role of the small heat-shock molecular chaperone proteins

thioflavin T fluorescence assay for amyloid fibril detection can be biased by the presence of exogenous compounds

Functional Amyloid Protection in the Eye Lens: Retention of α-Crystallin Molecular Chaperone Activity after Modification into Amyloid Fibrils

Amyloid Fibril Formation by Lens Crystallin Proteins and Its Implications for Cataract Formation

A Spectroscopic Marker for Structural Transitions Associated with Amyloid‑β Aggregation

Are casein micelles extracellular condensates formed by liquid‐liquid phase separation?

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