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. 2017 Sep 27;8:1673. doi: 10.3389/fpls.2017.01673

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Copyright © 2017 Wu, Xi, Pertl-Obermeyer, Li, Chu and Schulze.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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High specificity and reproducibility of phosphopeptide enrichment in ShortPhos phosphoproteomics workflow. (A) High percentage of phosphopeptides (84%) and low percentage of non-phosphopeptides identified in ShortPhos workflow. (B) Distribution of phosphorylated residues in the phosphopeptides: 1998 phosphopeptides with single phosphorylation site (87%), 278 with double phosphorylation sites (12%) and 10 (1%) with multiple phosphorylation sites. (C) Distribution of identified phosphorylation sites to serine (S), threonine (T) and tyrosine (Y). (D) Phosphopeptide intensity (log₂ LFQ) comparison for LC-MS/MS replicates displayed a high label-free quantitative reproducibility between three biological replicates (R1, R2, and R3).