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Molecular mechanisms of membrane-shaping proteins on the endoplasmic reticulum

Biophysical journal, 2024-02, Vol.123 (3), p.478a-478a

Pan, Buyan

2024

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Small fluorescence-activating and absorption-shifting tag for tunable protein imaging in vivo

Proceedings of the National Academy of Sciences - PNAS, 2016-01, Vol.113 (3), p.497-502

2016

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Molecular basis for N-terminal alpha-synuclein acetylation by human NatB

eLife, 2020-09, Vol.9

2020

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The membrane curvature-inducing REEP1-4 proteins generate an ER-derived vesicular compartment

Nature communications, 2024-10, Vol.15 (1), p.8655-16, Article 8655

2024

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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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α-Synuclein arginylation in the human brain

Translational neurodegeneration, 2022-04, Vol.11 (1), p.20-20, Article 20

2022

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Chemoenzymatic Semisynthesis of Phosphorylated α‑Synuclein Enables Identification of a Bidirectional Effect on Fibril Formation

ACS chemical biology, 2020-03, Vol.15 (3), p.640-645

2020

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Investigating the Effect of Alpha-Synuclein Post-Translational Modifications on Synaptic Vesicle Trafficking

Biophysical journal, 2019-02, Vol.116 (3), p.64

2019

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Chemoenzymatic Semi-Synthesis of Phosphorylated α-Synuclein Enables Identification of a Bidirectional Effect on Fibril Formation

ACS chemical biology, 2020-02, Vol.15 (3), p.640-645

2020

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Cysteine-Based Mimic of Arginylation Reproduces Neuroprotective Effects of the Authentic Post-Translational Modification on α‑Synuclein

Journal of the American Chemical Society, 2022-05, Vol.144 (17), p.7911-7918

2022

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Investigating the Effect of Alpha-Synuclein Post-translational Modifications on Synaptic Vesicle Trafficking

Biophysical journal, 2018-02, Vol.114 (3), p.583a-583a

2018

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A PARP‑1 Feed-Forward Mechanism To Accelerate α‑Synuclein Toxicity in Parkinson’s Disease

Biochemistry (Easton), 2019-02, Vol.58 (7), p.859-860

2019

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Structure and Mechanism of Acetylation by the N-Terminal Dual Enzyme NatA/Naa50 Complex

Structure (London), 2019-07, Vol.27 (7), p.1057-1070.e4

2019

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Effects of Glutamate Arginylation on α‑Synuclein: Studying an Unusual Post-Translational Modification through Semisynthesis

Journal of the American Chemical Society, 2020-12, Vol.142 (52), p.21786-21798

2020

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Synthesis of Peptides and Proteins with Site-Specific Glutamate Arginylation

Methods in molecular biology (Clifton, N.J.), 2023, Vol.2620, p.177

2023

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Molecular role of NAA38 in thermostability and catalytic activity of the human NatC N-terminal acetyltransferase

Structure (London), 2023-02, Vol.31 (2), p.166-173.e4

2023

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Molecular mechanism of N-terminal acetylation by the ternary NatC complex

Structure (London), 2021-10, Vol.29 (10), p.1094-1104.e4

2021

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Combining non-canonical amino acid mutagenesis and native chemical ligation for multiply modifying proteins: A case study of α-synuclein post-translational modifications

Methods (San Diego, Calif.), 2023-10, Vol.218, p.101-109

2023

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The Effects of Glutamate Arginylation on α-Synuclein: Studying an Unusual Post-translational Modification Through Semi-Synthesis

Journal of the American Chemical Society, 2020-12, Vol.142 (52), p.21786-21798

2020

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Chemoenzymatic Semi‐synthesis Enables Efficient Production of Isotopically Labeled α‐Synuclein with Site‐Specific Tyrosine Phosphorylation

Chembiochem : a European journal of chemical biology, 2021-04, Vol.22 (8), p.1440-1447

2021

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Examining Post-Translational Modifications in Alpha-Synuclein through Semi-Synthesis and Single Molecule Spectroscopy

Pan, Buyan

2021

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Post-translational modifications of soluble α-synuclein regulate the amplification of pathological α-synuclein

Nature neuroscience, 2023-02, Vol.26 (2), p.213-225

2023

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Semi-Synthetic CoA-α-Synuclein Constructs Trap N‑Terminal Acetyltransferase NatB for Binding Mechanism Studies

Journal of the American Chemical Society, 2023-06, Vol.145 (25), p.14019-14030

2023

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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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Author Correction: Post-translational modifications of soluble α-synuclein regulate the amplification of pathological α-synuclein

Nature neuroscience, 2023-12, Vol.26 (12), p.2250-2250

2023

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Molecular mechanisms of membrane-shaping proteins on the endoplasmic reticulum

Small fluorescence-activating and absorption-shifting tag for tunable protein imaging in vivo

Molecular basis for N-terminal alpha-synuclein acetylation by human NatB

The membrane curvature-inducing REEP1-4 proteins generate an ER-derived vesicular compartment

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

α-Synuclein arginylation in the human brain

Chemoenzymatic Semisynthesis of Phosphorylated α‑Synuclein Enables Identification of a Bidirectional Effect on Fibril Formation

Investigating the Effect of Alpha-Synuclein Post-Translational Modifications on Synaptic Vesicle Trafficking

Chemoenzymatic Semi-Synthesis of Phosphorylated α-Synuclein Enables Identification of a Bidirectional Effect on Fibril Formation

Cysteine-Based Mimic of Arginylation Reproduces Neuroprotective Effects of the Authentic Post-Translational Modification on α‑Synuclein

Investigating the Effect of Alpha-Synuclein Post-translational Modifications on Synaptic Vesicle Trafficking

A PARP‑1 Feed-Forward Mechanism To Accelerate α‑Synuclein Toxicity in Parkinson’s Disease

Structure and Mechanism of Acetylation by the N-Terminal Dual Enzyme NatA/Naa50 Complex

Effects of Glutamate Arginylation on α‑Synuclein: Studying an Unusual Post-Translational Modification through Semisynthesis

Synthesis of Peptides and Proteins with Site-Specific Glutamate Arginylation

Molecular role of NAA38 in thermostability and catalytic activity of the human NatC N-terminal acetyltransferase

Molecular mechanism of N-terminal acetylation by the ternary NatC complex

Combining non-canonical amino acid mutagenesis and native chemical ligation for multiply modifying proteins: A case study of α-synuclein post-translational modifications

The Effects of Glutamate Arginylation on α-Synuclein: Studying an Unusual Post-translational Modification Through Semi-Synthesis

Chemoenzymatic Semi‐synthesis Enables Efficient Production of Isotopically Labeled α‐Synuclein with Site‐Specific Tyrosine Phosphorylation

Examining Post-Translational Modifications in Alpha-Synuclein through Semi-Synthesis and Single Molecule Spectroscopy

Post-translational modifications of soluble α-synuclein regulate the amplification of pathological α-synuclein

Semi-Synthetic CoA-α-Synuclein Constructs Trap N‑Terminal Acetyltransferase NatB for Binding Mechanism Studies

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

Author Correction: Post-translational modifications of soluble α-synuclein regulate the amplification of pathological α-synuclein

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