Methodologies for the characterization, identification and quantification of S-nitrosylated proteins.
Methodologies for the characterization, identification and quantification of S-nitrosylated proteins.
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DOI：
10.1016/j.bbagen.2011.03.013
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发表时间：
2012-06
影响因子：
3
通讯作者：
Foster, Matthew W.
中科院分区：
文献类型：
--
作者：
Foster, Matthew W.
蛋白质S-亚硝基化在一氧化氮（NO）信号转导中起着核心作用，特定蛋白质的异常S-亚硝基化越来越多地与疾病有关。由于S-亚硝基化蛋白（SNO-蛋白）的低丰度和相对不稳定性，其在生物系统中一直难以检测和定量。然而，在过去的10年中，生物素开关技术（BST）和相关的基于巯基的测定已经允许从复杂的生物混合物中富集和鉴定特定的SNO蛋白，以及蛋白质S-亚硝基化位点（SNO位点）的简便鉴定和定量，从而导致了大量重要的新发现。通过X射线晶体学对SNO-蛋白质的结构表征也越来越多地用于理解蛋白质结构和Cys巯基反应性之间的关系以及S-亚硝基化对蛋白质结构和功能的影响。在这里，我们回顾这些和其他方法的表征，鉴定和定量的SNO蛋白。
Protein S-nitrosylation plays a central role in signal transduction by nitric oxide (NO), and aberrant S-nitrosylation of specific proteins is increasingly implicated in disease. Due to their low-abundance and relative instability, S-nitrosylated proteins (SNO-proteins) have been difficult to detect and quantify in biological systems. However, over the last 10 years, the biotin switch technique (BST) and related thiol-based assays have allowed enrichment and identification of specific SNO-proteins from complex biological mixtures as well as the facile identification and quantification of sites of protein S-nitrosylation (SNO-sites), leading to scores of important new discoveries. Structural characterization of SNO-proteins by X-ray crystallography is also increasingly being utilized to understand both the relationships between protein structure and Cys thiol reactivity as well as the consequences of S-nitrosylation on protein structure and function. Here, we review these and other methodologies for the characterization, identification and quantification of SNO-proteins.
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DOI：
10.1006/bbrc.1998.9688
发表时间：
1998-11-27
影响因子：
3.1
作者：
Fang, KZ;Ragsdale, NV;Gaston, B
通讯作者：
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DOI：
10.1073/pnas.1008036107
发表时间：
2010-09-28
影响因子：
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作者：
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通讯作者：
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影响因子：
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作者：
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影响因子：
2.9
作者：
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通讯作者：
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影响因子：
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作者：
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