| Literature DB >> 17629318 |
Serena Camerini1, Maria L Polci, Umberto Restuccia, Vera Usuelli, Antonio Malgaroli, Angela Bachi.
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.Entities:
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Year: 2007 PMID: 17629318 DOI: 10.1021/pr0701456
Source DB: PubMed Journal: J Proteome Res ISSN: 1535-3893 Impact factor: 4.466