ArticleOmics : a journal of integrative biology2012
MRMaid 2.0: mining PRIDE for evidence-based SRM transitions.
Article in Omics : a journal of integrative biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Application of targeted mass spectrometry in bottom-up proteomics for systems biology research.Journal of proteomics · 2018Review
- 2016 update of the PRIDE database and its related tools.Nucleic acids research · 2016Article
- Exploring the potential of public proteomics data.Proteomics · 2016Review
- Making proteomics data accessible and reusable: current state of proteomics databases and repositories.Proteomics · 2015Review
- Open source libraries and frameworks for mass spectrometry based proteomics: a developer's perspective.Biochimica et biophysica acta · 2014Review
- Pride-asap: automatic fragment ion annotation of identified PRIDE spectra.Journal of proteomics · 2013Article
- Review of software tools for design and analysis of large scale MRM proteomic datasets.Methods (San Diego, Calif.) · 2013Review
- Bioinformatics challenges and solutions in proteomics as quantitative methods mature.Omics : a journal of integrative biology · 2012Article
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5 authors.
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Abstract
Selected reaction monitoring (SRM) is becoming the tool of choice for targeted quantitative proteomics. The fundamental principle of proteomic SRM is that, for a given protein of interest, there is a set of peptides that are unique to that protein. The characteristic retention time (RT), and intact peptide m/z of these so-called proteotypic peptides are then programmed into the mass spectrometer, along with the m/z of high-intensity product ions for targeted quantitation. The particular combination of RT, peptide m/z, and product m/z for a given peptide is referred to as a transition. Selection of the most appropriate set of transitions for a given set of proteins is crucial to any SRM experiment. We previously developed the web-based MRMaid tool, which suggested the optimal transitions for a given human protein by mining spectral evidence from a small in-house database. In this article we present a completely new implementation of MRMaid, which offers substantial improvements over the original. The new version, MRMaid 2.0, uses spectra from the EBI's PRIDE database, which massively increases the coverage and quality of transitions. Transition lists can now be generated for multiple proteins simultaneously, edited within the web browser, and exported for laboratory use.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.