A novel approach to identify proteins modified by nitric oxide: the HIS-TAG switch method

被引：67

作者：

Camerini, Serena

Polci, Maria L.

Restuccia, Umberto

Usuelli, Vera

Malgaroli, Antonio

Bachi, Angela

机构：

[1] Ist Sci San Raffaele, DIBIT, Mass Spectrometry Unit, I-20132 Milan, Italy

[2] Univ Vita Salute San Raffaele, I-20132 Milan, Italy

来源：

JOURNAL OF PROTEOME RESEARCH | 2007年 / 6卷 / 08期

关键词：

S-nitrosylation; proteomics; mass spectrometry; post-translational modifications; nitric oxide;

D O I：

10.1021/pr0701456

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

S-nitrosylation is emerging as an important signaling mechanism that regulates a broad range of cellular functions. The recognition of Cysteine residues that undergo S-nitrosylation is crucial to elucidate how this modification modulates protein activity. We report here a novel strategy, defined His-tag switch, which allows the purification and identification of S-nitrosylated proteins and the unambiguous localization of the modified cysteine residues by mass spectrometry analysis.

引用

页码：3224 / 3231

页数：8

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