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Proteomics

Proteomics

A proteome is the entire set of proteins that a cell type produces. We can study proteomes using the knowledge of genomes because genes code for mRNAs, and the mRNAs encode proteins. Although mRNA analysis is a step in the right direction, not all mRNAs are translated into proteins.
Proteomics is the study of proteomes' function. It involves the large-scale systematic study of the proteome to denote the protein complement expressed by a genome. Scientist Mark Wilkins coined the term proteomics...

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Updated: May 31, 2026

Phosphoproteomic Strategy for Profiling Osmotic Stress Signaling in Arabidopsis

Phosphoproteomic Strategy for Profiling Osmotic Stress Signaling in Arabidopsis

Published on: June 25, 2020

PROTAC-Based Proteomics Strategy Uncovers Arsenic-Binding Proteomes.

Jiahui Liu¹, Ling Fang², Shijun Wen³

¹State Key Laboratory of Biocontrol, School of Life Sciences, Sun Yat-Sen University, Guangzhou 510275, China.

Analytical Chemistry

|May 29, 2026

Summary

This summary is machine-generated.

Researchers developed novel arsenic-targeting proteolysis-targeting chimeras (PROTACs) to identify proteins that bind arsenic. This method revealed 135 downregulated proteins in lung cancer cells, offering new insights into arsenical toxicity and drug discovery.

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Last Updated: May 31, 2026

Phosphoproteomic Strategy for Profiling Osmotic Stress Signaling in Arabidopsis

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2 in 1: One-step Affinity Purification for the Parallel Analysis of Protein-Protein and Protein-Metabolite Complexes

2 in 1: One-step Affinity Purification for the Parallel Analysis of Protein-Protein and Protein-Metabolite Complexes

Published on: August 6, 2018

Area of Science:

Biochemistry
Proteomics
Chemical Biology

Background:

Intracellular protein degradation systems are crucial for drug discovery.
Proteolysis-targeting chimeras (PROTACs) are a powerful tool for targeted protein degradation.

Purpose of the Study:

To develop an in situ proteolysis strategy using trivalent arsenical-PROTAC (As(III)-PROTAC) probes to uncover arsenic-binding proteomes.
To identify novel arsenic-binding proteins and understand their biological roles.

Main Methods:

Development and application of As(III)-PROTAC probes for in situ proteolysis.
Proteomic analysis to identify downregulated proteins.
Bioinformatics analysis to determine involved pathways.
Western blotting and Cellular Thermal Shift Assay (CETSA) to validate protein binding and downregulation.

Main Results:

Identified 135 downregulated proteins in A549 human lung carcinoma cells.
Discovered that identified proteins are involved in pathways including the tricarboxylic acid cycle, DNA replication, and DNA repair.
Confirmed downregulation of EED and PLAA proteins and demonstrated intracellular binding of iAs(III) to EED and PLAA.

Conclusions:

The study successfully developed and applied PROTAC probes for screening arsenic-binding proteomes.
Established a methodological foundation for understanding the biological effects of arsenicals.
Provided a candidate list of As-binding proteins for further investigation in drug discovery and toxicology.