Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by

Same author

Establishing an RNA Sensor with High Sensitivity and Dynamic Range Utilizing a Signal Amplifier Platform.

ACS synthetic biology·2026

Same author

Pyroglutamate PTMs as Bioorthogonal Reactive Handles: Ru/Ni Photoredox Coupling.

Angewandte Chemie (International ed. in English)·2025

Same author

Generating tolerance through in situ recruitment of regulatory T cells for allogeneic cell transplantation in a bioengineered lymphoid platform.

Materials today. Bio·2025

Same author

Establishing an RNA sensor with high sensitivity and dynamic range utilizing a signal amplifier platform.

bioRxiv : the preprint server for biology·2025

Same author

Novel Approaches to Label the Surface of <i>S. aureus</i> with DBCO for Click Chemistry-Mediated Deposition of Sensitive Cargo.

Bioconjugate chemistry·2025

Same author

Feedback-responsive cell factories for dynamic modulation of the unfolded protein response.

Nature communications·2025

Search research articles

Related Experiment Video

Updated: May 19, 2026

A Method to Study α-Synuclein Toxicity and Aggregation Using a Humanized Yeast Model

A Method to Study α-Synuclein Toxicity and Aggregation Using a Humanized Yeast Model

Published on: November 25, 2022

Quantitative analysis of α-synuclein solubility in living cells using split GFP complementation.

Ahmed Kothawala¹, Kiri Kilpatrick, Jose Andres Novoa

¹Department of Chemical and Biomolecular Engineering, Rice University, Houston, Texas, United States of America.

|August 29, 2012

Summary

This study introduces a split GFP assay to measure alpha-synuclein (αsyn) solubility in living cells, crucial for understanding Parkinson's disease (PD) mechanisms and developing treatments.

More Related Videos

Studying Pre-formed Fibril Induced α-Synuclein Accumulation in Primary Embryonic Mouse Midbrain Dopamine Neurons

Studying Pre-formed Fibril Induced α-Synuclein Accumulation in Primary Embryonic Mouse Midbrain Dopamine Neurons

Published on: August 16, 2020

Detection of Disease-associated α-synuclein by Enhanced ELISA in the Brain of Transgenic Mice Overexpressing Human A53T Mutated α-synuclein

Detection of Disease-associated α-synuclein by Enhanced ELISA in the Brain of Transgenic Mice Overexpressing Human A53T Mutated α-synuclein

Published on: May 30, 2015

Related Experiment Videos

Last Updated: May 19, 2026

A Method to Study α-Synuclein Toxicity and Aggregation Using a Humanized Yeast Model

A Method to Study α-Synuclein Toxicity and Aggregation Using a Humanized Yeast Model

Published on: November 25, 2022

Studying Pre-formed Fibril Induced α-Synuclein Accumulation in Primary Embryonic Mouse Midbrain Dopamine Neurons

Studying Pre-formed Fibril Induced α-Synuclein Accumulation in Primary Embryonic Mouse Midbrain Dopamine Neurons

Published on: August 16, 2020

Detection of Disease-associated α-synuclein by Enhanced ELISA in the Brain of Transgenic Mice Overexpressing Human A53T Mutated α-synuclein

Detection of Disease-associated α-synuclein by Enhanced ELISA in the Brain of Transgenic Mice Overexpressing Human A53T Mutated α-synuclein

Published on: May 30, 2015

Area of Science:

Neuroscience
Molecular Biology
Biochemistry

Background:

Parkinson's disease (PD) is a common neurodegenerative disorder affecting motor function.
PD pathogenesis involves dopaminergic neuron loss and alpha-synuclein (αsyn) aggregation into Lewy bodies.
Understanding αsyn solubility is key to elucidating PD cytotoxicity and therapeutic strategies.

Purpose of the Study:

To develop and validate a split GFP complementation assay for quantifying soluble αsyn in living cells.
To investigate how αsyn sequence variations influence its solubility.
To explore the impact of the cellular folding network on αsyn solubility.

Main Methods:

Utilized a split GFP complementation assay to monitor αsyn solubility.
Examined naturally occurring and designed αsyn variants.
Assessed the influence of cellular folding machinery on αsyn solubility.

Main Results:

The split GFP assay effectively quantifies αsyn solubility in living cells.
Demonstrated that αsyn sequence specificity impacts its solubility.
Showcased the assay's utility in studying the cellular folding network's effect on αsyn.

Conclusions:

The split GFP assay is a valuable tool for measuring αsyn solubility.
Provides insights into factors governing αsyn aggregation relevant to PD.
Facilitates research into therapeutic interventions targeting αsyn misfolding.