Qingfei Zheng

The paper identifies TG3 as a new histone monoaminylation writer capable of catalyzing H3Q5 histaminylation.

The paper develops a chemoselective bioconjugation method to detect and analyze NEylation, revealing it as a widespread PTM affecting protein function in cells.

This study identifies new TGM2-catalyzed histaminylation marks on core histones in cancer cells and reveals their crosstalk with γH2AX formation in DNA damage responses.

This study identifies QR2 as a reader of H3Q5ser, showing its role in human neuron development through transcriptional and electrophysiological effects.

This study introduces a pH-controlled regioselective rapid ene-type reaction (RRER) for selectively modifying histone H3Q5 serotonylation and measuring its levels in cells and tissues.

The paper develops a chemical proteomic method to globally profile serotonylation in cancer cells, identifying over 1,000 serotonylated proteins and their modification sites.

This study develops chemical probes to label and enrich histone monoaminylation, revealing its enrichment in cancer tissues and its role in chromatin architecture regulation.

The paper identifies 425 dopaminylated proteins in colorectal cancer cells using a chemical probe, revealing their involvement in nucleic acid metabolism and transcription, and suggests targeting protein dopaminylation as a potential anti-cancer strategy.

A single enzyme, TGM2, bidirectionally controls H3 monoaminylation dynamics, which, in turn, facilitate neural rhythmicity.