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A."},{"key":"10.1016\/j.mcpro.2025.101072_bib92","doi-asserted-by":"crossref","first-page":"1285","DOI":"10.1038\/nbt1240","article-title":"A probability-based approach for high-throughput protein phosphorylation analysis and site localization","volume":"24","author":"Beausoleil","year":"2006","journal-title":"Nat. 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