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Synthesis and characterization of high affinity fluorogenic α-synuclein probes

Chemical communications (Cambridge, England), 2020-03, Vol.56 (24), p.3567-3570

2020

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Multiply labeling proteins for studies of folding and stability

Current opinion in chemical biology, 2015-10, Vol.28, p.123-130

2015

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Receptor-templated stapling of intrinsically disordered peptide ligands

Organic & biomolecular chemistry, 2015-04, Vol.13 (14), p.4183-4189

2015

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Selective imaging of internalized proteopathic α-synuclein seeds in primary neurons reveals mechanistic insight into transmission of synucleinopathies

The Journal of biological chemistry, 2017-08, Vol.292 (32), p.13482-13497

2017

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Fluorescence spectroscopy reveals N-terminal order in fibrillar forms of α-synuclein

Chemical communications (Cambridge, England), 2018-01, Vol.54 (7), p.833-836

2018

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A “Clickable” Photoconvertible Small Fluorescent Molecule as a Minimalist Probe for Tracking Individual Biomolecule Complexes

Journal of the American Chemical Society, 2019-02, Vol.141 (5), p.1893-1897

2019

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Promoting peptide α-helix formation with dynamic covalent oxime side-chain cross-links

Chemical communications (Cambridge, England), 2011-10, Vol.47 (39), p.10915-10917

2011

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Oxime Side-Chain Cross-Links in an [alpha]-Helical Coiled-Coil Protein: Structure, Thermodynamics, and Folding-Templated Synthesis of Bicyclic Species

Chemistry : a European journal, 2013-08, Vol.19 (34), p.11342-11351

2013

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Using a FRET Library with Multiple Probe Pairs To Drive Monte Carlo Simulations of α-Synuclein

Biophysical journal, 2018-01, Vol.114 (1), p.53-64

2018

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Oxime Side-Chain Cross-Links in an α-Helical Coiled-Coil Protein: Structure, Thermodynamics, and Folding-Templated Synthesis of Bicyclic Species

Chemistry : a European journal, 2013-08, Vol.19 (34), p.11342-11351

2013

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Multicolor protein FRET with tryptophan, selective coumarin-cysteine labeling, and genetic acridonylalanine encoding

Chemical communications (Cambridge, England), 2017-10, Vol.53 (80), p.11072-11075

2017

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Cyclized NDGA modifies dynamic α-synuclein monomers preventing aggregation and toxicity

Scientific reports, 2019-02, Vol.9 (1), p.2937-2937, Article 2937

2019

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Dynamic covalent side-chain cross-links via intermolecular oxime or hydrazone formation from bifunctional peptides and simple organic linkers

Journal of peptide science, 2014-02, Vol.20 (2), p.108-114

2014

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Site-Specific Fluorescence Polarization for Studying the Disaggregation of α‑Synuclein Fibrils by Small Molecules

Biochemistry (Easton), 2017-02, Vol.56 (5), p.683-691

2017

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Comparison of strategies for non-perturbing labeling of α-synuclein to study amyloidogenesis

Organic & biomolecular chemistry, 2016-02, Vol.14 (5), p.1584-1592

2016

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Thermodynamic origin of α-helix stabilization by side-chain cross-links in a small protein

Organic & biomolecular chemistry, 2016-01, Vol.14 (24), p.5768-5773

2016

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Correction: Comparison of strategies for non-perturbing labeling of α-synuclein to study amyloidogenesis

Organic & biomolecular chemistry, 2016-06, Vol.14 (21), p.4957-4957

2016

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Identification of Hsp70 modulators through modeling of the substrate binding domain

Bioorganic & medicinal chemistry letters, 2009-07, Vol.19 (14), p.3828-3831

2009

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Fluorescence spectroscopy reveals N-terminal order in fibrillar forms of α-synucleinElectronic supplementary information (ESI) available. See DOI: 10.1039/c7cc08601f

2018-01

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Receptor-templated stapling of intrinsically disordered peptide ligandsElectronic supplementary information (ESI) available: Fig. S1-S4, Table S1. See DOI: 10.1039/c5ob00269a

2015-03

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Selective imaging of internalized proteopathic α‐synuclein seeds in primary neurons reveals mechanistic insight into transmission of synucleinopathies

The FASEB journal, 2018-04, Vol.32 (S1), p.118.3-118.3

2018

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Studying α-Synuclein Misfolding through Förster Resonance Energy Transfer

Biophysical journal, 2015-01, Vol.108 (2), p.64a-64a

2015

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Utilzing Forster Resonance Energy Transfer (FRET) and Photocrosslinking to Visualize Conformational Changes of Alpha-Synuclein

Biophysical journal, 2018-02, Vol.114 (3), p.586a-587a

2018

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Multicolor protein FRET with tryptophan, selective coumarin-cysteine labeling, and genetic acridonylalanine encodingElectronic supplementary information (ESI) available: Descriptions of the synthesis of methoxycoumarin maleimide (Mcm-Mal), protein expression and labelling, and FRET experiments. See DOI: 10.1039/c7cc05492k

2017-10

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Thermodynamic origin of α-helix stabilization by side-chain cross-links in a small proteinElectronic supplementary information (ESI) available: Fig. S1-S3, Table S1. See DOI: 10.1039/c6ob00475j

2016-06

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Synthesis and characterization of high affinity fluorogenic α-synuclein probes

Multiply labeling proteins for studies of folding and stability

Receptor-templated stapling of intrinsically disordered peptide ligands

Selective imaging of internalized proteopathic α-synuclein seeds in primary neurons reveals mechanistic insight into transmission of synucleinopathies

Fluorescence spectroscopy reveals N-terminal order in fibrillar forms of α-synuclein

A “Clickable” Photoconvertible Small Fluorescent Molecule as a Minimalist Probe for Tracking Individual Biomolecule Complexes

Promoting peptide α-helix formation with dynamic covalent oxime side-chain cross-links

Oxime Side-Chain Cross-Links in an [alpha]-Helical Coiled-Coil Protein: Structure, Thermodynamics, and Folding-Templated Synthesis of Bicyclic Species

Using a FRET Library with Multiple Probe Pairs To Drive Monte Carlo Simulations of α-Synuclein

Oxime Side-Chain Cross-Links in an α-Helical Coiled-Coil Protein: Structure, Thermodynamics, and Folding-Templated Synthesis of Bicyclic Species

Multicolor protein FRET with tryptophan, selective coumarin-cysteine labeling, and genetic acridonylalanine encoding

Cyclized NDGA modifies dynamic α-synuclein monomers preventing aggregation and toxicity

Dynamic covalent side-chain cross-links via intermolecular oxime or hydrazone formation from bifunctional peptides and simple organic linkers

Site-Specific Fluorescence Polarization for Studying the Disaggregation of α‑Synuclein Fibrils by Small Molecules

Comparison of strategies for non-perturbing labeling of α-synuclein to study amyloidogenesis

Thermodynamic origin of α-helix stabilization by side-chain cross-links in a small protein

Correction: Comparison of strategies for non-perturbing labeling of α-synuclein to study amyloidogenesis

Identification of Hsp70 modulators through modeling of the substrate binding domain

Fluorescence spectroscopy reveals N-terminal order in fibrillar forms of α-synucleinElectronic supplementary information (ESI) available. See DOI: 10.1039/c7cc08601f

Receptor-templated stapling of intrinsically disordered peptide ligandsElectronic supplementary information (ESI) available: Fig. S1-S4, Table S1. See DOI: 10.1039/c5ob00269a

Selective imaging of internalized proteopathic α‐synuclein seeds in primary neurons reveals mechanistic insight into transmission of synucleinopathies

Studying α-Synuclein Misfolding through Förster Resonance Energy Transfer

Utilzing Forster Resonance Energy Transfer (FRET) and Photocrosslinking to Visualize Conformational Changes of Alpha-Synuclein

Thermodynamic origin of α-helix stabilization by side-chain cross-links in a small proteinElectronic supplementary information (ESI) available: Fig. S1-S3, Table S1. See DOI: 10.1039/c6ob00475j

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