Global Identification of Protein Post-translational Modifications in a Single-Pass Database Search

[Image: see text] Bottom-up proteomics database search algorithms used for peptide identification cannot comprehensively identify post-translational modifications (PTMs) in a single-pass because of high false discovery rates (FDRs). A new approach to database searching enables global PTM (G-PTM) ide...

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Autores principales: Shortreed, Michael R., Wenger, Craig D., Frey, Brian L., Sheynkman, Gloria M., Scalf, Mark, Keller, Mark P., Attie, Alan D., Smith, Lloyd M.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Chemical Society 2015
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4642219/
https://www.ncbi.nlm.nih.gov/pubmed/26418581
http://dx.doi.org/10.1021/acs.jproteome.5b00599
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author Shortreed, Michael R.
Wenger, Craig D.
Frey, Brian L.
Sheynkman, Gloria M.
Scalf, Mark
Keller, Mark P.
Attie, Alan D.
Smith, Lloyd M.
author_facet Shortreed, Michael R.
Wenger, Craig D.
Frey, Brian L.
Sheynkman, Gloria M.
Scalf, Mark
Keller, Mark P.
Attie, Alan D.
Smith, Lloyd M.
author_sort Shortreed, Michael R.
collection PubMed
description [Image: see text] Bottom-up proteomics database search algorithms used for peptide identification cannot comprehensively identify post-translational modifications (PTMs) in a single-pass because of high false discovery rates (FDRs). A new approach to database searching enables global PTM (G-PTM) identification by exclusively looking for curated PTMs, thereby avoiding the FDR penalty experienced during conventional variable modification searches. We identified over 2200 unique, high-confidence modified peptides comprising 26 different PTM types in a single-pass database search.
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spelling pubmed-46422192015-11-27 Global Identification of Protein Post-translational Modifications in a Single-Pass Database Search Shortreed, Michael R. Wenger, Craig D. Frey, Brian L. Sheynkman, Gloria M. Scalf, Mark Keller, Mark P. Attie, Alan D. Smith, Lloyd M. J Proteome Res [Image: see text] Bottom-up proteomics database search algorithms used for peptide identification cannot comprehensively identify post-translational modifications (PTMs) in a single-pass because of high false discovery rates (FDRs). A new approach to database searching enables global PTM (G-PTM) identification by exclusively looking for curated PTMs, thereby avoiding the FDR penalty experienced during conventional variable modification searches. We identified over 2200 unique, high-confidence modified peptides comprising 26 different PTM types in a single-pass database search. American Chemical Society 2015-09-07 2015-11-06 /pmc/articles/PMC4642219/ /pubmed/26418581 http://dx.doi.org/10.1021/acs.jproteome.5b00599 Text en Copyright © 2015 American Chemical Society This is an open access article published under an ACS AuthorChoice License (http://pubs.acs.org/page/policy/authorchoice_termsofuse.html) , which permits copying and redistribution of the article or any adaptations for non-commercial purposes.
spellingShingle Shortreed, Michael R.
Wenger, Craig D.
Frey, Brian L.
Sheynkman, Gloria M.
Scalf, Mark
Keller, Mark P.
Attie, Alan D.
Smith, Lloyd M.
Global Identification of Protein Post-translational Modifications in a Single-Pass Database Search
title Global Identification of Protein Post-translational Modifications in a Single-Pass Database Search
title_full Global Identification of Protein Post-translational Modifications in a Single-Pass Database Search
title_fullStr Global Identification of Protein Post-translational Modifications in a Single-Pass Database Search
title_full_unstemmed Global Identification of Protein Post-translational Modifications in a Single-Pass Database Search
title_short Global Identification of Protein Post-translational Modifications in a Single-Pass Database Search
title_sort global identification of protein post-translational modifications in a single-pass database search
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4642219/
https://www.ncbi.nlm.nih.gov/pubmed/26418581
http://dx.doi.org/10.1021/acs.jproteome.5b00599
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