3 results match your criteria: "Peking University Beijing China chuwang@pku.edu.cn.[Affiliation]"

A simplified and efficient extracellular vesicle-based proteomics strategy for early diagnosis of colorectal cancer.

Chem Sci

October 2024

Beijing National Laboratory for Molecular Sciences, Key Laboratory of Bioorganic Chemistry and Molecular Engineering of Ministry of Education, College of Chemistry and Molecular Engineering, Peking University Beijing China

Colorectal cancer (CRC) is a major cause of cancer-related death worldwide and an effective screening strategy for diagnosis of early-stage CRC is highly desired. Although extracellular vesicles (EVs) are expected to become some of the most promising tools for liquid biopsy of early disease diagnosis, the existing EV-based proteomics methods for practical application in clinical samples are limited by technical challenges in high-throughput isolation and detection of EVs. In the current study, we have developed a simplified and efficient EV-based proteomics strategy for early diagnosis of CRC.

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Discovery of cisplatin-binding proteins by competitive cysteinome profiling.

RSC Chem Biol

August 2023

Synthetic and Functional Biomolecules Center, Beijing National Laboratory for Molecular Sciences, Key Laboratory of Bioorganic Chemistry and Molecular Engineering of Ministry of Education, College of Chemistry and Molecular Engineering, Peking University Beijing China

Cisplatin is a widely used cancer metallodrug that induces cytotoxicity by targeting DNA and chelating cysteines in proteins. Here we applied a competitive activity-based protein profiling strategy to identify cisplatin-binding cysteines in cancer proteomes. A novel cisplatin target, MetAP1, was identified and functionally validated to contribute to cisplatin's cytotoxicity.

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Post-translational modifications (PTMs) play important roles in modulating the biological functions of proteins. Stoichiometry, which quantifies the modification percentage, is a critical factor for any given PTM. In this work, we developed a chemoproteomic strategy called "STO-MS" to systematically quantify the PTM stoichiometry in complex biological samples.

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