Related Experiment Video

Updated: Aug 11, 2026

A Method to Study α-Synuclein Toxicity and Aggregation Using a Humanized Yeast Model
08:24

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

Published on: November 25, 2022

Cysteine misincorporation in bacterially expressed human alpha-synuclein

Masami Masuda1, Naoshi Dohmae, Takashi Nonaka

  • 1Department of Molecular Neurobiology, Tokyo Institute of Psychiatry, 2-1-8 Kamikitazawa, Setagaya-ku 156-8585, Tokyo, Japan.

FEBS Letters
|March 4, 2006
PubMed
Summary

Bacterial expression of human alpha-synuclein (alpha-syn) can lead to mistranslation, incorporating cysteine instead of tyrosine at position 136. Using a modified Y136-TAT construct minimizes these errors for accurate research.

More Related Videos

Detection of Disease-associated α-synuclein by Enhanced ELISA in the Brain of Transgenic Mice Overexpressing Human A53T Mutated α-synuclein12:01

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

Exogenous Administration of Microsomes-associated Alpha-synuclein Aggregates to Primary Neurons As a Powerful Cell Model of Fibrils Formation09:16

Exogenous Administration of Microsomes-associated Alpha-synuclein Aggregates to Primary Neurons As a Powerful Cell Model of Fibrils Formation

Published on: June 26, 2018

Related Concept Videos

Amyloid Fibrils03:03

Amyloid Fibrils

Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
Amyloid deposits were observed as early as 1639 in the liver and the spleen.   In 1854, Rudolph Virchow performed iodine staining, normally used to...