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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Animals
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Cerebellum / metabolism*
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Female
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Male
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Molecular Sequence Data
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Nerve Tissue Proteins / analysis*
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Nerve Tissue Proteins / chemistry
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Nitric Oxide / chemistry
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Nitric Oxide / metabolism*
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Nitroso Compounds / chemistry*
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Ovalbumin / analysis
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Ovalbumin / chemistry
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Rats
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Rats, Sprague-Dawley
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S-Nitrosoglutathione / chemistry*
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Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization / methods
Substances
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Nerve Tissue Proteins
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Nitroso Compounds
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Nitric Oxide
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S-Nitrosoglutathione
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Ovalbumin