ArticleJournal of proteome research2025
Unveiling the Potential Binding Targets of Celastrol in Colorectal Cancer: A Proteomic Profiling Approach Integrating Cellular Thermal Shift Assay and Pulse Proteolysis.
Article in Journal of proteome research, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
2 citing papers in PubMed.
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Celastrol, a natural compound classified as a pentacyclic triterpenoid, has demonstrated efficacy in inhibiting human colorectal cancer cells' growth, adhesion, and metastasis through various signaling pathways. However, the specific protein target responsible for the effects of celastrol remains unclear, limiting its potential for further applications in colon cancer treatment and drug development. In this study, we propose a novel approach by combining a cellular thermal shift assay and pulse proteolysis techniques to identify the potential binding proteins of celastrol. Utilizing proteomic profiling on 2-dimensional electrophoresis, we successfully identified eight potential binding targets. MALDI-TOF mass spectrometry was conducted to verify these proteins as EEF2, STIP1, GAPDH, FLNA, SETSIP, GANAB, TXNDC17, and PRDX2. Our results provide valuable insights into the protein targets through which celastrol exerts its pharmacological effects, opening up new avenues for targeted therapies and drug development in colorectal cancer.
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