面向飞机PHM的大数据分析与人工智能应用

针对新一代电子产品密集型的飞机,其系统结构和失效机理复杂、失效模式多样,传统的方法难以对其进行有效健康管理的现状,因此提出了基于海量数据挖掘的飞机PHM研究。首先从系统结构、服役环境、数据来源与存储方式等角度分析了新一代飞机对海量数据挖掘的应用需求;其次论述了基于海量数据挖掘的关键技术,包括数据的预处理、集成管理、聚类、分类、关联、预测等;最后提出了一种基于私有云的飞机PHM海量数据挖掘平台,详细阐述了该平台的总体框架和软硬件结构,该平台为飞机PHM提供了验证平台,对促进飞机PHM的集成与工程化实现具有重大的军事应用意义。     

Structural mechanism of WASP activation by the enterohaemorrhagic E. coli effector EspF(U)

During infection, enterohaemorrhagic Escherichia coli (EHEC) takes over the actin cytoskeleton of eukaryotic cells by injecting the EspF(U) protein into the host cytoplasm. EspF(U) controls actin by activating members of the Wiskott-Aldrich syndrome protein (WASP) family. Here we show that EspF(U) binds to the autoinhibitory GTPase binding domain (GBD) in WASP proteins and displaces it from the activity-bearing VCA domain (for verprolin homology, central hydrophobic and acidic regions). This interaction potently activates WASP and neural (N)-WASP in vitro and induces localized actin assembly in cells. In the solution structure of the GBD-EspF(U) complex, EspF(U) forms an amphipathic helix that binds the GBD, mimicking interactions of the VCA domain in autoinhibited WASP. Thus, EspF(U) activates WASP by competing directly for the VCA binding site on the GBD. This mechanism is distinct from that used by the eukaryotic activators Cdc42 and SH2 domains, which globally destabilize the GBD fold to release the VCA. Such diversity of mechanism in WASP proteins is distinct from other multimodular systems, and may result from the intrinsically unstructured nature of the isolated GBD and VCA elements. The structural incompatibility of the GBD complexes with EspF(U) and Cdc42/SH2, plus high-affinity EspF(U) binding, enable EHEC to hijack the eukaryotic cytoskeletal machinery effectively.