钟传奇 Chuanqi Zhong

研究领域：
1.蛋白组学方法的开发：蛋白组学是研究生物样品中所有蛋白的功能状态的学科，它分为样品前处理，质谱数据采集和质谱数据生物信息学分析三个部分。其中，我们开发了数据不依赖质谱（Data-independent acquisition mass spectrometry, DIA-MS）数据的算法（Nature Methods, 2015）,此算法可以不依赖于数据依赖质谱（Data-dependent acquisition mass spectrometry, DDA-MS）而可直接分析DIA-MS数据。此外我们开发了基于SDS的蛋白组学样品制备方法SCASP (MCP, 2021)以及无需脱盐方法的翻译后修饰富集方法SCASP-PTM (Cell Reports, 2025).
2.先天免疫和肿瘤免疫信号通路分子机制研究：我们整合自主研发的蛋白组学技术与高通量CRISPR/Cas9筛选工具，系统解析信号通路中关键的调控机制。利用SCASP-PTM方法分析了RNA类似物poly(I:C)刺激HeLa-S3细胞的蛋白、泛素化修饰、磷酸化修饰和糖基化修饰的变化，发现poly(I:C)诱导GSK3B介导的p62蛋白28位磷酸化，进而诱发TNFAIP1介导的420位赖氨酸泛素化，最终导致p62降解并减弱细胞自噬 (Cell Reports, 2025)。此外，利用SCASP-PTM方法分析了临床肺癌和癌旁组织的总蛋白、泛素化修饰、乙酰化修饰、磷酸化修饰和糖基化修饰的变化，揭示了ALDOA的K330的乙酰化修饰和泛素化修饰促进了肿瘤的发展 (Cell Reports, 2025)。

Research Areas:
1. Development of proteomics methods: Proteomics is the discipline that studies the functional states of all proteins in biological samples. It consists of three parts: sample preprocessing, mass spectrometry data acquisition, and mass spectrometry data bioinformatics analysis. We developed an algorithm for data-independent acquisition mass spectrometry (DIA-MS) data (Nature Methods, 2015), which can directly analyze DIA-MS data without relying on data-dependent acquisition mass spectrometry (DDA-MS). Additionally, we developed the SDS-based proteomics sample preparation method SCASP (MCP, 2021) and the desalting-free post-translational modification enrichment method SCASP-PTM (Cell Reports, 2025).
2. Molecular mechanism research on innate immunity and tumor immunity signaling pathways: We integrate self-developed proteomics technologies with high-throughput CRISPR/Cas9 screening tools to systematically analyze key regulatory mechanisms in signaling pathways. Using the SCASP-PTM method, we analyzed changes in proteins, ubiquitination, phosphorylation, and glycosylation in HeLa-S3 cells stimulated by RNA analog poly(I:C), discovering that poly(I:C) induces GSK3B-mediated phosphorylation at position 28 of p62 protein, which triggers TNFAIP1-mediated ubiquitination at lysine 420, ultimately leading to p62 degradation and weakened autophagy (Cell Reports, 2025). Furthermore, using the SCASP-PTM method to analyze total proteins, ubiquitination, acetylation, phosphorylation, and glycosylation in clinical lung cancer and adjacent tissues, we revealed that acetylation and ubiquitination of ALDOA at K330 promotes tumor development (Cell Reports, 2025).

代表论文：
1. Lin ZP, Gan G, Xu X, Wen C, Ding X, Chen XY, Zhang K, Guo WY, Lin M, Wang YY, Chen X, Xie C, Wang J*, Li M*, Zhong CQ*. Comprehensive PTM profiling with SCASP-PTM uncovers mechnisms of p62 degradation and ALDOA-mediated tumor progression. Cell Rep. 2025 Apr 3;44(4):115500. Doi: 10.1016/j.celrep.2025.115500. (IF=7.5)
2. Wen C, Wu X*, Lin G, Yan W, Gan G, Xu X, Chen XY, Chen X, Liu X, Fu G*, Zhong CQ*. Evaluation of DDA Library-Free Strategies for Phosphoproteomics and Ubiquitinomics Data-Independent Acquisition Data. J Proteome Res. 22, 2232-2245 (2023). (IF=5.3)