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Identification of proteins interacting with human SP110 during the process of viral infections.

机译:鉴定病毒感染过程中与人SP110相互作用的蛋白质。

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Human SP110 plays an important role in resisting intracellular pathogens, and hence has become an important drug target for preventing intracellular pathogen diseases, such as tuberculosis, hepatic veno-occlusive disease, and intracellular cancers. Unfortunately, so far little is known about the interactions of SP110 with the other proteins in a cell, which is considered to be the key for revealing its action mechanism and mediated pathway. Using both the genetic and structural analyses as well as the segment-docking approach, we have identified two proteins: the human remodeling and spacing factor 1 (RSF1) and the activating transcription factor 7 interacting protein (ATF7IP). They are very likely interacting with human SP110 during the process of viral infections. Owing to the close relationship of RSF1 with the chromatin remodeling and ATF7IP with the chromatin formation, it is logical to infer that human SP110 may be involved in the chromatin remodeling and formation as well. These findings may provide useful insights into the development of new drugs for treating and preventing intracellular pathogen diseases.
机译:人SP110在抵抗细胞内病原体中起着重要的作用,因此已经成为预防细胞内病原体疾病如结核,肝静脉闭塞性疾病和细胞内癌症的重要药物靶标。不幸的是,到目前为止,关于SP110与细胞中其他蛋白质相互作用的信息知之甚少,这被认为是揭示其作用机理和介导途径的关键。使用遗传和结构分析以及片段对接方法,我们确定了两种蛋白质:人类重塑和间隔因子1(RSF1)和激活转录因子7相互作用蛋白(ATF7IP)。它们很可能在病毒感染过程中与人SP110相互作用。由于RSF1与染色质重塑密切相关,而ATF7IP与染色质重塑密切相关,因此逻辑推断人类SP110也可能参与染色质重塑和形成。这些发现可能为开发用于治疗和预防细胞内病原体疾病的新药物提供有用的见识。

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