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采用质谱法鉴定和表征唾液组蛋白 1 复合物。

Identification and characterization of histatin 1 salivary complexes by using mass spectrometry.

机构信息

Department of Biochemistry, School of Dentistry, Schulich School of Medicine & Dentistry, Western University, London, ON, Canada.

出版信息

Proteomics. 2012 Nov;12(22):3426-35. doi: 10.1002/pmic.201100665.

Abstract

With recent progress in the analysis of the salivary proteome, the number of salivary proteins identified has increased dramatically. However, the physiological functions of many of the newly discovered proteins remain unclear. Closely related to the study of a protein's function is the identification of its interaction partners. We investigated interactions among and functions of histatin 1 and the other proteins that are present in saliva by using high-throughput mass spectrometric techniques. This led to the identification of 43 proteins able to interact with histatin 1. In addition, we found that these protein-protein interactions protect complex partners from proteolysis and modulate their antifungal activity. Our data contribute significantly to characterization of the salivary interactome and to understanding the biology of salivary protein complexes.

摘要

随着唾液蛋白质组分析的最新进展,已鉴定出的唾液蛋白质数量显著增加。然而,许多新发现的蛋白质的生理功能仍然不清楚。与研究蛋白质的功能密切相关的是鉴定其相互作用伙伴。我们使用高通量质谱技术研究了组织蛋白酶 1 及其它存在于唾液中的蛋白质之间的相互作用及其功能。这导致鉴定出 43 种能够与组织蛋白酶 1 相互作用的蛋白质。此外,我们发现这些蛋白质-蛋白质相互作用保护复合物伙伴免受蛋白水解,并调节它们的抗真菌活性。我们的数据为唾液相互作用组的特征描述和理解唾液蛋白复合物的生物学提供了重要贡献。

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