塔皮奥卡:在动态环境中预测新的蛋白质-蛋白质相互作用的平台
Tavis J Reed1,2,3, Matthew D Tyl3, Alicja Tadych1,2
1Lewis-Sigler Institute for Integrative Genomics, Princeton University, Carl Icahn Laboratory, Princeton, NJ, USA.
Nature methods
|February 16, 2024
概括
新的机器学习框架Tapioca可以预测动态细胞状态中的蛋白质与蛋白质相互作用 (PPI). 它确定了NUCKS作为卡波西的肉瘤相关的疹病毒重新激活中的关键蛋白质.
科学领域:
- 蛋白质组学是指蛋白质组学.
- 系统生物学 系统生物学
- 生物信息学是一种生物信息学.
背景情况:
- 蛋白与蛋白相互作用 (PPI) 对细胞功能和反应至关重要.
- 了解动态PPI对于破译细胞状态和疾病机制至关重要.
研究的目的:
- 开发Tapioca,一个整体机器学习框架,用于在动态细胞环境中预测全球PPI.
- 改进PPI研究的实验工作流程,特别是热近距离聚合.
- 通过描述时间PPI来研究病毒感染动态.
主要方法:
- 质谱互原子数据 (热/离子去化,共分化) 与蛋白质特性和功能网络的整合.
- 优化热变性化以提高吞吐量和细胞溶解以提高蛋白质检测.
- 在卡波西的肉瘤相关的疹病毒重新激活期间,应用塔皮奥卡工作流程来研究PPI.
主要成果:
- 塔皮奥卡通过整合各种数据类型,成功地预测了新的PPI.
- 实验工作流的改进导致了更高的吞吐量和更好地检测来自各种亚细胞区的蛋白质.
- 鉴定NUCKS作为病毒再激活期间的前病毒枢纽蛋白.
- 通过整合不同疹病毒家族的PPI网络,发现了NUCKS的更广泛的作用.
结论:
- 塔皮奥卡为研究PPI在动态生物环境中提供了一种新的计算方法.
- 优化的实验工作流提高了互动原子研究的效率和范围.
- 这些发现提供了对病毒感染机制的洞察,并确定了潜在的治疗点.
更多相关视频
08:38Genome-wide Protein-protein Interaction Screening by Protein-fragment Complementation Assay PCA in Living Cells
Published on: March 3, 2015
13.4K
07:08Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues
Published on: July 14, 2015
7.3K
相关概念视频
Protein-protein Interfaces
12.5K
Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...
12.5K
Protein Networks
4.0K
An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...
4.0K
Protein-Protein Interfaces
3.8K
3.8K
Protein Complexes with Interchangeable Parts
2.5K
Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order...
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order...
2.5K
Conserved Binding Sites
4.2K
Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally...
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally...
4.2K
Protein Dynamics in Living Cells
2.1K
Different fluorescence-based techniques are used to study the protein dynamics in living cells. These techniques include FRAP, FRET, and PET.
Fluorescent recovery after photobleaching (FRAP) is a fluorescent-protein-based detection technique used to quantify protein movement rates within the cell. This method exposes a small portion of the cell to an intense laser beam. The laser beam causes permanent photobleaching of the fluorophore-tagged proteins in the exposed region. As the bleached...
Fluorescent recovery after photobleaching (FRAP) is a fluorescent-protein-based detection technique used to quantify protein movement rates within the cell. This method exposes a small portion of the cell to an intense laser beam. The laser beam causes permanent photobleaching of the fluorophore-tagged proteins in the exposed region. As the bleached...
2.1K
