Data for: Investigating the aggregation and prionogenic properties of human cancer-related proteins

Cancer encompasses a range of severe diseases characterized by uncontrolled cell growth and the potential for metastasis. Understanding the mechanism underlying tumorigenesis has been a central focus of cancer research. Self-propagating protein aggregates, known as prions, are linked to various biological functions and diseases, particularly those related to mammalian neurodegeneration. However, it remains unclear whether prion-like mechanisms contribute to tumorigenesis and cancer. Using a combined approach of algorithmic predictions, alongside genetic and biochemical experimentation, we identified numerous cancer-associated proteins prone to aggregation, many of which contain prion-like domains (PrLDs). These predictions were experimentally validated for both aggregation and prion-formation. We demonstrate that several PrLDs undergo nucleation-limited amyloid formation, which can alter protein activity in a mitotically heritable fashion. These include SSXT, a subunit of the chromatin-..., , , # Data for: Investigating the aggregation and prionogenic properties of human cancer-related proteins [https://doi.org/10.5061/dryad.905qfttw0](https://doi.org/10.5061/dryad.905qfttw0) ## Description of the data and file structure Table S1 shows computational analysis results to rank the aggregation propensity and prionogenicity of 9620 cancer-associated human proteins in this study. In the csv data sheet, FI MaxRun, PASTA Energy, and PASTA Disorder are for folding/free energy/disorder; and PLAAC Score and PAPA Score are used to measure the prionogenicity of a PrLD. Columns D-H are for normalized scores (0-1) and column I is weighted score - average of the normalized scores with distinct weighting factors considering equal importance of folding/free energy/disorder and prionogenicity. Table S2 and S3 include information of plasmids and primers used in this study, respectively. N/A, information unavailable. ## Code/software Microsoft Office Excel or .cvs combatable programs. ,癌症是一类以细胞不受控增殖及潜在转移为特征的重症疾病。解析肿瘤发生的内在机制始终是癌症研究的核心焦点。可自我复制的蛋白质聚集体即朊病毒（prions），与多种生物学功能及疾病密切相关，尤其与哺乳动物神经退行性疾病相关。但目前尚不清楚类朊病毒机制是否参与肿瘤发生与癌症进程。本研究结合算法预测、遗传学与生物化学实验手段，鉴定出大量易于聚集的癌症相关蛋白质，其中多数含有类朊病毒结构域（prion-like domains, PrLDs）。相关预测已通过聚集与朊病毒形成实验得到验证。本研究证实，部分PrLD可经历成核限制型淀粉样蛋白形成过程，并能以有丝分裂可遗传的方式改变蛋白质活性。其中包括染色质亚基SSXT…… # 数据集主题：探究人类癌症相关蛋白质的聚集特性与类朊病毒活性 [https://doi.org/10.5061/dryad.905qfttw0] ## 数据与文件结构说明 表S1展示了本研究中9620个人类癌症相关蛋白质的聚集倾向与类朊病毒活性的计算分析排名结果。在该CSV数据表中，FI MaxRun、PASTA Energy及PASTA Disorder用于反映折叠/自由能/无序性；PLAAC Score与PAPA Score则用于评估类朊病毒结构域（PrLD）的类朊病毒活性。D-H列为归一化得分（范围0-1），I列为加权得分——即综合折叠/自由能/无序性与类朊病毒活性的同等重要性，通过不同权重因子计算得到的归一化得分平均值。表S2与表S3分别收录了本研究中使用的质粒与引物信息。"N/A"表示信息不可用。 ## 代码与软件 可兼容Microsoft Office Excel或CSV格式的程序。