Projects per year
Abstract / Description of output
Accurate quantification and enumeration of peptide motifs is hampered by redundancy in peptide identification. A single phosphorylation motif may be split across charge states, alternative modifications (e.g. acetylation and oxidation), and multiple miss-cleavage sites which render the biological interpretation of MS data a challenge. In addition motif redundancy can affect quantitative and statistical analysis and prevent a realistic comparison of peptide numbers between datasets. In this study, we present a merging tool set developed for the Galaxy workflow environment to achieve a non-redundant set of quantifications for phospho-motifs. We present a Galaxy workflow to merge three exemplar dataset, and observe reduced phospho-motif redundancy and decreased replicate variation. The qpMerge tools provide a straightforward and reusable approach to facilitating phospho-motif analysis. The source-code and wiki documentation is publically available at http://sourceforge.net/projects/ppmerge. The galaxy pipeline used in the exemplar analysis can be found at http://www.myexperiment.org/workflows/4186.
Original language | English |
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Publisher | bioRxiv, at Cold Spring Harbor Laboratory |
Number of pages | 9 |
DOIs | |
Publication status | Published - 5 Apr 2016 |
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Dive into the research topics of 'qpMerge: Merging different peptide isoforms using a motif centric strategy'. Together they form a unique fingerprint.Projects
- 1 Finished
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Does an Ancient Circadian Clock control transcriptional rhythms using a non transcriptional oscillator
Millar, A. & Le Bihan, T.
1/10/12 → 31/01/16
Project: Research
Research output
- 2 Working paper
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Circadian protein regulation in the green lineage II. The clock gene circuit controls a phospho-dawn in Arabidopsis thaliana
Krahmer, J., Hindle, M., Perby, L. K., Nielsen, T. H., Van Ooijen, G., Halliday, K. J., Bihan, T. L. & Millar, A. J., 8 Sept 2019, bioRxiv, at Cold Spring Harbor Laboratory.Research output: Working paper
Open Access -
Time-resolved Interaction Proteomics of the Putative Scaffold Protein GIGANTEA in Arabidopsis thaliana
Krahmer, J., Goralogia, G., Kubota, A., Johnson, R. S., Song, Y. H., Halliday, K., MacCoss, M. J., LeBihan, T., Imaizumi, T. & Millar, A., 28 Aug 2017, bioRxiv, at Cold Spring Harbor Laboratory, 58 p.Research output: Working paper