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.
A novel approach to identify proteins modified by nitric oxide : The HIS-TAG switch method / S. Camerini, M.L. Polci, U. Restuccia, V. Usuelli, A. Malgaroli, A. Bachi. - In: JOURNAL OF PROTEOME RESEARCH. - ISSN 1535-3893. - 6:8(2007 Aug), pp. 3224-3231.
A novel approach to identify proteins modified by nitric oxide : The HIS-TAG switch method
V. Usuelli;
2007
Abstract
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.
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