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Enhanced Global Post-translational Modification Discovery with MetaMorpheus

Solntsev, Stefan K., Shortreed, Michael R., Frey, Brian L., Smith, Lloyd M.·2018·Journal of Proteome Research

Abstract

Correct identification of protein post-translational modifications (PTMs) is crucial to understanding many aspects of protein function in biological processes. G-PTM-D is a recently developed technique for global identification and localization of PTMs. Spectral file calibration prior to applying G-PTM-D, and algorithmic enhancements in the peptide database search significantly increase the accuracy, speed, and scope of PTM identification. We enhance G-PTM-D by using multinotch searches and demonstrate its effectiveness in identification of numerous types of PTMs including high-mass modifications such as glycosylations. The changes described in this work lead to a 20% increase in the number of identified modifications and an order of magnitude decrease in search time. The complete workflow is implemented in MetaMorpheus, a software tool that integrates the database search procedure, identification of coisolated peptides, spectral calibration, and the enhanced G-PTM-D workflow. Multinotch searches are also shown to be useful in contexts other than G-PTM-D by producing superior results when used instead of standard narrow-window and open database searches.

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Metadata

Authors
Solntsev, S. K., Shortreed, M. R., Frey, B. L., & Smith, L. M.
Venue
Journal of Proteome Research
Published
2018-03-26
Volume
17
Issue
5
Pages
1844-1851
ISSN
  • 1535-3893 (ISSN-L)
  • 1535-3907
OpenAlex
W2789457189
Cited by
262
References
3
FWCI
9.77
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Enhanced Global Post-translational Modification Discovery with MetaMorpheus. https://app.cochat.ai/papers/10.1021/acs.jproteome.7b00873
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Solntsev, S. K., Shortreed, M. R., Frey, B. L., & Smith, L. M. (2018). Enhanced Global Post-translational Modification Discovery with MetaMorpheus. Journal of Proteome Research. https://doi.org/10.1021/acs.jproteome.7b00873

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