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;
2007-08

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.
Mass spectrometry; Nitric oxide; Post-translational modifications; Proteomics; S-nitrosylation; Amino Acid Sequence; Animals; Cerebellum; Female; Male; Molecular Sequence Data; Nerve Tissue Proteins; Nitric Oxide; Nitroso Compounds; Ovalbumin; Rats; Rats, Sprague-Dawley; S-Nitrosoglutathione; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
Settore BIO/09 - Fisiologia
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Utilizza questo identificativo per citare o creare un link a questo documento: http://hdl.handle.net/2434/844895
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