ArticleAnalytical chemistry2008
Characterization of strategies for obtaining confident identifications in bottom-up proteomics measurements using hybrid FTMS instruments.
Article in Analytical chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- Mining the Wheat Grain Proteome.International journal of molecular sciences · 2022Article
- Assessment of the Utility of the Oral Fluid and Plasma Proteomes for Hydrocodone Exposure.Journal of medical toxicology : official journal of the American College of Medical Toxicology · 2020Article
- Enzyme immobilization: an update.Journal of chemical biology · 2013Review
- Quantitative analysis of global phosphorylation changes with high-resolution tandem mass spectrometry and stable isotopic labeling.Methods (San Diego, Calif.) · 2013Review
- Aging enhances the production of reactive oxygen species and bactericidal activity in peritoneal macrophages by upregulating classical activation pathways.Biochemistry · 2011Article
- UNiquant, a program for quantitative proteomics analysis using stable isotope labeling.Journal of proteome research · 2011Article
- Proteomic profiling of a layered tissue reveals unique glycolytic specializations of photoreceptor cells.Molecular & cellular proteomics : MCP · 2011Article
- Microproteomics: quantitative proteomic profiling of small numbers of laser-captured cells.Cold Spring Harbor protocols · 2011Article
- Liquid Chromatography Mass Spectrometry-Based Proteomics: Biological and Technological Aspects.The annals of applied statistics · 2010Article
- CE-MALDI interface based on inkjet technology.Electrophoresis · 2009Article
- Characterization of strategies for obtaining confident identifications in bottom-up proteomics measurements using hybrid FTMS instruments.Analytical chemistry · 2008Article
Corrections and comments
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Authors and funding
8 authors.
Funding
Abstract
Hybrid FTMS instruments, such as the LTQ-FT and LTQ-Orbitrap, are capable of generating high duty cycle linear ion trap MS/MS data along with high resolution information without compromising the overall throughput of measurements. Combined with online LC separations, these instruments provide powerful capabilities for proteomics research. In the present work, we explore three alternative strategies for high throughput proteomics measurements using hybrid FTMS instruments. Our accurate mass and time tag (AMT tag) strategy enables identification of thousands of peptides in a single LC-FTMS analysis by comparing accurate molecular mass and LC elution time information from the analysis to a reference database. An alternative strategy considered here, termed accurate precursor mass filter (APMF), employs linear ion trap (low resolution) MS/MS identifications generated by an appropriate search engine, such as SEQUEST, refined with high resolution precursor ion data obtained from FTMS mass spectra. The APMF results can be additionally filtered using the LC elution time information from the AMT tag database, which constitutes a precursor mass and time filter (PMTF), the third approach implemented in this study. Both the APMF and the PMTF approaches are evaluated for coverage and confidence of peptide identifications and contrasted with the AMT tag strategy. The commonly used decoy database method and an alternative method based on mass accuracy histograms were used to reliably quantify identification confidence, revealing that both methods yielded similar results. Comparison of the AMT, APMF and PMTF approaches indicates that the AMT tag approach is preferential for studies desiring a highest achievable number of identified peptides. In contrast, the APMF approach does not require an AMT tag database and provides a moderate level of peptide coverage combined with acceptable confidence values of approximately 99%. The PMTF approach yielded a significantly better peptide identification confidence, >99.9%, that essentially excluded any false peptide identifications. Since AMT tag databases that exclude incorrect identifications are desirable, this study points to the value of a multipass APMF approach to generate AMT tag databases, which are then validated using the PMTF approach. The resulting compact, high quality databases can then be used for subsequent high-throughput, high peptide coverage AMT tag studies.
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