Statistical control of peptide and protein error rates in large-scale targeted data-independent acquisition analyses
Open accessAbstract
Liquid chromatography coupled to tandem mass spectrometry (LC-MS/MS) is the main method for high-throughput identification and quantification of peptides and inferred proteins. Within this field, data-independent acquisition (DIA) combined with peptide-centric scoring, as exemplified by the technique SWATH-MS, has emerged as a scalable method to achieve deep and consistent proteome coverage across large-scale data sets. We demonstrate that statistical concepts developed for discovery proteomics based on spectrum-centric scoring can be adapted to large-scale DIA experiments that have been analyzed with peptide-centric scoring strategies, and we provide guidance on their application. We show that optimal tradeoffs between sensitivity and specificity require careful considerations of the relationship between proteins in the samples and proteins represented in the spectral library. We propose the application of a global analyte constraint to prevent the accumulation of false positives across large-scale data sets. Furthermore, to increase the quality and reproducibility of published proteomic results, well-established confidence criteria should be reported for the detected peptide queries, peptides and inferred proteins.
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When FDR was controlled only at peptide query level and not protein level, and only sample-by-sample and not in the global context, the accumulation of new peak groups steadily increased, indicating likely accumulation of false positives.
“The accumulation of new peak groups steadily increased across the data set, indicating a likely accumulation of false positives and, highlighting the importance of appropriate global FDR control55, 56.”
From Multi-laboratory assessment of reproducibility, qualitative and quantitative performance of SWATH-mass spectrometry (2017) · cites this paper as [55]
The result of this study, focused on assessing variation in data acquisition, is paralleled by concurrent improvements in robustness of data analysis tools, methods for error rate control, and sample preparation techniques.
“The result of our study, focused on assessing variation in data acquisition, is paralleled by concurrent improvements in the robustness of data analysis tools39, methods for error rate control55, and sample preparation techniques43.”
From Multi-laboratory assessment of reproducibility, qualitative and quantitative performance of SWATH-mass spectrometry (2017) · cites this paper as [55]
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Cites
Controlling the False Discovery Rate: A Practical and Powerful Approach to Multiple Testing
Benjamini, Y., & Hochberg, Y. (1995) · Journal of the Royal Statistical Society Series B: Statistical Methodology · doi:10.1111/j.2517-6161.1995.tb02031.x · Cited by 109,482 · see citing works
Statistical significance for genomewide studies
Storey, J. D., & Tibshirani, R. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1530509100 · Cited by 9,692 · see citing works
Keller, A., Nesvizhskii, A., Kolker, E., & Aebersold, R. (2002) · Analytical Chemistry · doi:10.1021/ac025747h · Cited by 4,970 · see citing works
Self-citationSkyline: an open source document editor for creating and analyzing targeted proteomics experiments
MacLean, B., Tomazela, D. M., Shulman, N., Chambers, M., Finney, G. L., Frewen, B., Kern, R., Tabb, D. L., Liebler, D. C., & MacCoss, M. J. (2010) · Bioinformatics · doi:10.1093/bioinformatics/btq054 · Cited by 4,697 · see citing works
Self-citationGillet, L. C., Navarro, P., Tate, S., Röst, H., Selevsek, N., Reiter, L., Bonner, R., & Aebersold, R. (2012) · Molecular & Cellular Proteomics · doi:10.1074/mcp.o111.016717 · Cited by 2,877 · see citing works
Self-citationSemi-supervised learning for peptide identification from shotgun proteomics datasets
Käll, L., Canterbury, J. D., Weston, J., Noble, W. S., & MacCoss, M. J. (2007) · Nature Methods · doi:10.1038/nmeth1113 · Cited by 2,424 · see citing works
Self-citationThe positive false discovery rate: a Bayesian interpretation and the q-value
Storey, J. D. (2003) · The Annals of Statistics · doi:10.1214/aos/1074290335 · Cited by 2,204 · see citing works
The Proteomics Identifications (PRIDE) database and associated tools: status in 2013
Vizcaíno, J. A., Côté, R. G., Csordas, A., Dianes, J. A., Fabregat, A., Foster, J. M., Griss, J., Alpi, E., Birim, M., Contell, J., et al. (2012) · Nucleic Acids Research · doi:10.1093/nar/gks1262 · Cited by 1,918 · see citing works
Bruderer, R., Bernhardt, O. M., Gandhi, T., Miladinović, S. M., Cheng, L.-Y., Messner, S., Ehrenberger, T., Zanotelli, V., Butscheid, Y., Escher, C., et al. (2015) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m114.044305 · Cited by 1,238 · see citing works
Self-citationOpenSWATH enables automated, targeted analysis of data-independent acquisition MS data
Röst, H. L., Rosenberger, G., Navarro, P., Gillet, L. C. J., Miladinović, S. M., Schubert, O. T., Wolski, W., Collins, B. C., Malmström, J. A., Malmström, L., et al. (2014) · Nature Biotechnology · doi:10.1038/nbt.2841 · Cited by 741 · see citing works
Self-citationQuantitative Proteomic Analysis by Accurate Mass Retention Time Pairs
Silva, J. C., Denny, R., Dorschel, C. A., Gorenstein, M., Kass, I. J., Li, G., McKenna, T., Nold, M. J., Richardson, K., Young, P., et al. (2005) · Analytical Chemistry · doi:10.1021/ac048455k · Cited by 641 · see citing works
DIA-Umpire: comprehensive computational framework for data-independent acquisition proteomics
Tsou, C., Avtonomov, D. M., Larsen, B. G., Tucholska, M., Choi, H., Gingras, A., & Nesvizhskii, A. I. (2015) · Nature Methods · doi:10.1038/nmeth.3255 · Cited by 622 · see citing works
Self-citationOptions and considerations when selecting a quantitative proteomics strategy
Domon, B., & Aebersold, R. H. (2010) · Nature Biotechnology · doi:10.1038/nbt.1661 · Cited by 601 · see citing works
Self-citationCollins, B. C., Hunter, C. L., Liu, Y., Schilling, B., Rosenberger, G., Bader, S. L., Chan, D. W., Gibson, B. W., Gingras, A.-C., Held, J. M., et al. (2017) · Nature Communications · doi:10.1038/s41467-017-00249-5 · Cited by 576 · see citing works
Self-citationCarr, S. A., Abbatiello, S. E., Ackermann, B. L., Borchers, C., Domon, B., Deutsch, E. W., Grant, R. P., Hoofnagle, A. N., Hüttenhain, R., Koomen, J. M., et al. (2014) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m113.036095 · Cited by 561 · see citing works
Self-citationShteynberg, D. D., Deutsch, E. W., Lam, H., Eng, J. K., Sun, Z., Tasman, N., Mendoza, L., Moritz, R. L., Aebersold, R. H., & Nesvizhskii, A. I. (2011) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m111.007690 · Cited by 548 · see citing works
Self-citationOperating Characteristics and Extensions of the False Discovery Rate Procedure
Genovese, C. R., & Wasserman, L. (2002) · Journal of the Royal Statistical Society Series B (Statistical Methodology) · doi:10.1111/1467-9868.00347 · Cited by 545 · see citing works
Nesvizhskii, A. I. (2010) · Journal of Proteomics · doi:10.1016/j.jprot.2010.08.009 · Cited by 535 · see citing works
Self-citationmProphet: automated data processing and statistical validation for large-scale SRM experiments
Reiter, L., Rinner, O., Picotti, P., Hüttenhain, R., Beck, M., Brusniak, M.-Y., Hengartner, M. O., & Aebersold, R. (2011) · Nature Methods · doi:10.1038/nmeth.1584 · Cited by 532 · see citing works
Self-citationThe, M., MacCoss, M. J., Noble, W. S., & Käll, L. (2016) · Journal of the American Society for Mass Spectrometry · doi:10.1007/s13361-016-1460-7 · Cited by 454 · see citing works
Self-citationA Scalable Approach for Protein False Discovery Rate Estimation in Large Proteomic Data Sets
Savitski, M. M., Wilhelm, M., Hahne, H., Küster, B., & Bantscheff, M. (2015) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m114.046995 · Cited by 436 · see citing works
A repository of assays to quantify 10,000 human proteins by SWATH-MS
Rosenberger, G., Koh, C. C., Guo, T., Röst, H. L., Kouvonen, P., Collins, B. C., Heusel, M., Liu, Y., Caron, E., Vichalkovski, A., et al. (2014) · Scientific Data · doi:10.1038/sdata.2014.31 · Cited by 413 · see citing works
Self-citationGuo, T., Kouvonen, P., Koh, C. C., Gillet, L. C., Wolski, W. E., Röst, H. L., Rosenberger, G., Collins, B. C., Blum, L. C., Gillessen, S., et al. (2015) · Nature Medicine · doi:10.1038/nm.3807 · Cited by 376 · see citing works
Self-citationQuantitative variability of 342 plasma proteins in a human twin population
Liu, Y., Buil, A., Collins, B. C., Gillet, L. C., Blum, L. C., Cheng, L., Vitek, O., Mouritsen, J., Lachance, G., Spector, T. D., et al. (2015) · Molecular Systems Biology · doi:10.15252/msb.20145728 · Cited by 328 · see citing works
Self-citationGillet, L. C., Leitner, A., & Aebersold, R. (2016) · Annual Review of Analytical Chemistry · doi:10.1146/annurev-anchem-071015-041535 · Cited by 323 · see citing works
Self-citationA complete mass-spectrometric map of the yeast proteome applied to quantitative trait analysis
Picotti, P., Clément-Ziza, M., Lam, H., Campbell, D. S., Schmidt, A., Deutsch, E. W., Röst, H., Sun, Z., Rinner, O., Reiter, L., et al. (2013) · Nature · doi:10.1038/nature11835 · Cited by 318 · see citing works
Self-citationReiter, L., Claassen, M., Schrimpf, S. P., Jovanovic, M., Schmidt, A., Buhmann, J. M., Hengartner, M. O., & Aebersold, R. (2009) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m900317-mcp200 · Cited by 312 · see citing works
Self-citationBuilding high-quality assay libraries for targeted analysis of SWATH MS data
Schubert, O. T., Gillet, L. C. J., Collins, B. C., Navarro, P., Rosenberger, G., Wolski, W., Lam, H., Amodei, D., Mallick, P., MacLean, B., et al. (2015) · Nature Protocols · doi:10.1038/nprot.2015.015 · Cited by 309 · see citing works
Self-citationPosterior Error Probabilities and False Discovery Rates: Two Sides of the Same Coin
Käll, L., Storey, J. D., MacCoss, M. J., & Noble, W. S. (2007) · Journal of Proteome Research · doi:10.1021/pr700739d · Cited by 293 · see citing works
Self-citationMultiplexed and data‐independent tandem mass spectrometry for global proteome profiling
Chapman, J. D., Goodlett, D. R., & Masselon, C. (2013) · Mass Spectrometry Reviews · doi:10.1002/mas.21400 · Cited by 258 · see citing works
Schubert, O. T., Ludwig, C., Kogadeeva, M., Zimmermann, M., Rosenberger, G., Gengenbacher, M., Gillet, L. C., Collins, B. C., Röst, H. L., Kaufmann, S. H. E., et al. (2015) · Cell Host & Microbe · doi:10.1016/j.chom.2015.06.001 · Cited by 211 · see citing works
Self-citationFalse Discovery Rates of Protein Identifications: A Strike against the Two-Peptide Rule
Gupta, N., & Pevzner, P. A. (2009) · Journal of Proteome Research · doi:10.1021/pr9004794 · Cited by 188 · see citing works
Ting, Y. S., Egertson, J. D., Payne, S. H., Kim, S., MacLean, B., Käll, L., Aebersold, R., Smith, R. D., Noble, W. S., & MacCoss, M. J. (2015) · Molecular & Cellular Proteomics · doi:10.1074/mcp.o114.047035 · Cited by 175 · see citing works
Self-citationSelevsek, N., Chang, C.-Y., Gillet, L. C. J., Navarro, P., Bernhardt, O. M., Reiter, L., Cheng, L., Vitek, O., & Aebersold, R. H. (2015) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m113.035550 · Cited by 174 · see citing works
Self-citationSchubert, O. T., Mouritsen, J., Ludwig, C., Röst, H. L., Rosenberger, G., Arthur, P. K., Claassen, M., Campbell, D. S., Sun, Z., Farrah, T., et al. (2013) · Cell Host & Microbe · doi:10.1016/j.chom.2013.04.008 · Cited by 173 · see citing works
Self-citationGenerating and navigating proteome maps using mass spectrometry
Ahrens, C. H., Brunner, E., Qeli, E., Basler, K., & Aebersold, R. H. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2973 · Cited by 167 · see citing works
Self-citationChoi, H., & Nesvizhskii, A. I. (2007) · Journal of Proteome Research · doi:10.1021/pr070542g · Cited by 148 · see citing works
Self-citationMuntel, J., Xuan, Y., Berger, S. T., Reiter, L., Bachur, R. G., Kentsis, A., & Steen, H. (2015) · Journal of Proteome Research · doi:10.1021/acs.jproteome.5b00826 · Cited by 134 · see citing works
Self-citationChoi, H., Ghosh, D., & Nesvizhskii, A. I. (2007) · Journal of Proteome Research · doi:10.1021/pr7006818 · Cited by 122 · see citing works
Self-citationMSPLIT-DIA: sensitive peptide identification for data-independent acquisition
Wang, J., Tucholska, M., Knight, J. D. R., Lambert, J., Tate, S. A., Larsen, B. G., Gingras, A., & Bandeira, N. (2015) · Nature Methods · doi:10.1038/nmeth.3655 · Cited by 119 · see citing works
Self-citationGroup-DIA: analyzing multiple data-independent acquisition mass spectrometry data files
Li, Y., Zhong, C., Xu, X., Cai, S., Wu, X., Zhang, Y., Chen, J., Shi, J., Lin, S., & Han, J. (2015) · Nature Methods · doi:10.1038/nmeth.3593 · Cited by 101 · see citing works
DIANA—algorithmic improvements for analysis of data-independent acquisition MS data
Teleman, J., Röst, H. L., Rosenberger, G., Schmitt, U., Malmström, L., Malmström, J. A., & Levander, F. (2014) · Bioinformatics · doi:10.1093/bioinformatics/btu686 · Cited by 100 · see citing works
Self-citationTsou, C., Tsai, C., Teo, G. C., Chen, Y., & Nesvizhskii, A. I. (2016) · PROTEOMICS · doi:10.1002/pmic.201500526 · Cited by 72 · see citing works
Self-citationA review of statistical methods for protein identification using tandem mass spectrometry
Noble, W. S., & Serang, O. (2012) · Statistics and Its Interface · doi:10.4310/sii.2012.v5.n1.a2 · Cited by 67 · see citing works
Proteome-wide selected reaction monitoring assays for the human pathogen Streptococcus pyogenes
Karlsson, C. A. Q., Malmström, L., Aebersold, R. H., & Malmström, J. A. (2012) · Nature Communications · doi:10.1038/ncomms2297 · Cited by 66 · see citing works
Self-citationSolution to Statistical Challenges in Proteomics Is More Statistics, Not Less
Serang, O., & Käll, L. (2015) · Journal of Proteome Research · doi:10.1021/acs.jproteome.5b00568 · Cited by 50 · see citing works
Blattmann, P., Heusel, M., & Aebersold, R. H. (2016) · PLoS ONE · doi:10.1371/journal.pone.0153160 · Cited by 48 · see citing works
Self-citationHow to talk about protein‐level false discovery rates in shotgun proteomics
The, M., Tasnim, A., & Käll, L. (2016) · PROTEOMICS · doi:10.1002/pmic.201500431 · Cited by 47 · see citing works
Keller, A., Bader, S. L., Shteynberg, D. D., Hood, L., & Moritz, R. L. (2015) · Molecular & Cellular Proteomics · doi:10.1074/mcp.o114.044917 · Cited by 35 · see citing works
An Adaptive Single‐step FDR Procedure with Applications to DNA Microarray Analysis
Iyer, V. R., & Sarkar, S. K. (2007) · Biometrical Journal · doi:10.1002/bimj.200610316 · Cited by 5 · see citing works
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Meier, F., Brunner, A., Frank, M., Ha, A., Bludau, I., Voytik, E., Kaspar‐Schoenefeld, S., Lubeck, M., Raether, O., Bache, N., et al. (2020) · Nature Methods · doi:10.1038/s41592-020-00998-0 · Cited by 902 · see citing works
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Self-citationSearle, B. C., Pino, L. K., Egertson, J. D., Ting, Y. S., Lawrence, R., MacLean, B., Villén, J., & MacCoss, M. J. (2018) · Nature Communications · doi:10.1038/s41467-018-07454-w · Cited by 508 · see citing works
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Zhang, B., Vogelzang, A., Miyajima, M., Sugiura, Y., Wu, Y., Chamoto, K., Nakano, R., Hatae, R., Menzies, R. J., Sonomura, K., et al. (2021) · Nature · doi:10.1038/s41586-021-04082-1 · Cited by 455 · see citing works
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Self-citationXuan, Y., Bateman, N. W., Gallien, S., Götze, S., Zhou, Y., Navarro, P., Hu, M., Parikh, N., Hood, B. L., Conrads, K. A., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-18904-9 · Cited by 91 · see citing works
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Ye, Z., Mao, Y., Clausen, H., & Vakhrushev, S. Y. (2019) · Nature Methods · doi:10.1038/s41592-019-0504-x · Cited by 90 · see citing works
Systematic detection of functional proteoform groups from bottom-up proteomic datasets
Bludau, I., Frank, M., Dörig, C., Cai, Y., Heusel, M., Rosenberger, G., Picotti, P., Collins, B. C., Röst, H., & Aebersold, R. (2021) · Nature Communications · doi:10.1038/s41467-021-24030-x · Cited by 88 · see citing works
Self-citationChen, Z., Amro, E. M., Becker, F. R., Hölzer, M., Rasa, S. M. M., Njeru, S. N., Han, B., Sanzo, S. D., Chen, Y.-L., Tang, D., et al. (2018) · The Journal of Experimental Medicine · doi:10.1084/jem.20181505 · Cited by 87 · see citing works
SPIN enables high throughput species identification of archaeological bone by proteomics
Rüther, P. L., Husic, I., Bangsgaard, P., Gregersen, K. M., Pantmann, P., Carvalho, M. M., Godinho, R. M., Friedl, L., Cascalheira, J., Taurozzi, A. J., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-30097-x · Cited by 79 · see citing works
A Comparative Analysis of Data Analysis Tools for Data-Independent Acquisition Mass Spectrometry
Zhang, F., Ge, W., Huang, L., Li, D., Liu, L., Dong, Z., Xu, L., Ding, X., Zhang, C., Sun, Y., et al. (2023) · Molecular & Cellular Proteomics · doi:10.1016/j.mcpro.2023.100623 · Cited by 75 · see citing works
AlphaPept: a modern and open framework for MS-based proteomics
Strauss, M. T., Bludau, I., Zeng, W., Voytik, E., Ammar, C., Schessner, J. P., Ilango, R., Gill, M. L., Meier, F., Willems, S., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-46485-4 · Cited by 72 · see citing works
Self-citationA Global Screen for Assembly State Changes of the Mitotic Proteome by SEC-SWATH-MS
Heusel, M., Frank, M., Köhler, M., Amon, S., Frommelt, F., Rosenberger, G., Bludau, I., Aulakh, S. K., Linder, M. I., Liu, Y., et al. (2020) · Cell Systems · doi:10.1016/j.cels.2020.01.001 · Cited by 72 · see citing works
Self-citationŠalovská, B., Zhu, H.-W., Gandhi, T., Frank, M., Li, W.-X., Rosenberger, G. A., Wu, C.-D., Germain, P., Zhou, H., Hodny, Z., et al. (2020) · Molecular Systems Biology · doi:10.15252/msb.20199170 · Cited by 62 · see citing works
Self-citationTo the proteome and beyond: advances in single-cell omics profiling for plant systems
Clark, N. M., Elmore, J. M., & Walley, J. W. (2021) · PLANT PHYSIOLOGY · doi:10.1093/plphys/kiab429 · Cited by 66 · see citing works
Bludau, I., Heusel, M., Frank, M., Rosenberger, G. A., Hafen, R., Banaei‐Esfahani, A., van Drogen, A., Collins, B. C., Gstaiger, M., & Aebersold, R. (2019) · Nature Protocols · doi:10.1038/s41596-020-0332-6 · Cited by 65 · see citing works
Self-citationGerner, C., Costigliola, V., & Golubnitschaja, O. (2019) · Mass Spectrometry Reviews · doi:10.1002/mas.21612 · Cited by 63 · see citing works
Multilayered omics Reveal Sex- and Depot-Dependent Adipose Progenitor Cell Heterogeneity
Bo, S., Barker, C., Shao, M.-L., Zhang, Q.-B., Gupta, R. K., & Wu, Y. (2022) · Cell Metabolism · doi:10.1016/j.cmet.2022.03.012 · Cited by 48 · see citing works
Zhao, J., Yang, Y., Xu, H., Zheng, J., Shen, C., Tian, C., Wang, T., Wang, B., Yi, J., Zhao, D., et al. (2023) · npj Biofilms and Microbiomes · doi:10.1038/s41522-023-00373-9 · Cited by 62 · see citing works
Genetic loci and metabolic states associated with murine epigenetic aging
Mozhui, K., Lu, A. T., Li, C. Z., Haghani, A., Sandoval-Sierra, J. V., Wu, Y., Williams, R. W., & Horvath, S. (2022) · eLife · doi:10.7554/elife.75244 · Cited by 55 · see citing works
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Dowell, J. A., Wright, L. J., Armstrong, E. A., & Denu, J. M. (2021) · ACS Omega · doi:10.1021/acsomega.0c04030 · Cited by 57 · see citing works
Baker, C. P., Bruderer, R., Abbott, J., Arthur, J. S. C., & Brenes, A. J. (2024) · Journal of Proteome Research · doi:10.1021/acs.jproteome.3c00671 · Cited by 55 · see citing works
Guo, J., Kufer, R., Li, D., Wohlrab, S., Greenwood‐Goodwin, M., & Yang, F. (2023) · mAbs · doi:10.1080/19420862.2023.2213365 · Cited by 57 · see citing works
Data-independent Acquisition Improves Quantitative Cross-linking Mass Spectrometry
Müller, F., Kolbowski, L., Bernhardt, O. M., Reiter, L., & Rappsilber, J. (2019) · Molecular & Cellular Proteomics · doi:10.1074/mcp.tir118.001276 · Cited by 54 · see citing works
Self-citationProteomics, Glycomics, and Glycoproteomics of Matrisome Molecules
Raghunathan, R., Sethi, M. K., Klein, J., & Zaia, J. (2019) · Molecular & Cellular Proteomics · doi:10.1074/mcp.r119.001543 · Cited by 53 · see citing works
Pena, A. B., Munoz, N. M., Kim, J., Orton, D., Gao, Y., Poorey, K., Pomraning, K., Weitz, K., Burnet, M., Nicora, C., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-37031-9 · Cited by 52 · see citing works
Unifying the analysis of bottom-up proteomics data with CHIMERYS
Frejno, M., Berger, M. T., Tüshaus, J., Hogrebe, A., Seefried, F., Graber, M., Samaras, P., Fredj, S. B., Sukumar, V., Eljagh, L., et al. (2025) · Nature Methods · doi:10.1038/s41592-025-02663-w · Cited by 46 · see citing works
GproDIA enables data-independent acquisition glycoproteomics with comprehensive statistical control
Yang, Y., Yan, G., Kong, S., Wu, M., Yang, P., Cao, W., & Qiao, L. (2021) · Nature Communications · doi:10.1038/s41467-021-26246-3 · Cited by 47 · see citing works
Mehnert, M., Li, W., Wu, C., Šalovská, B., & Liu, Y. (2019) · PROTEOMICS · doi:10.1002/pmic.201800438 · Cited by 38 · see citing works
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Puyvelde, B. V., Willems, S., Gabriels, R., Daled, S., Clerck, L. D., Casteele, S. V., Staes, A., Impens, F., Deforce, D. L. D., Martens, L., et al. (2020) · PROTEOMICS · doi:10.1002/pmic.201900306 · Cited by 44 · see citing works
Rosenberger, G., Heusel, M., Bludau, I., Collins, B. C., Martelli, C., Williams, E. G., Xue, P., Liu, Y., Aebersold, R. H., & Califano, A. (2020) · Cell Systems · doi:10.1016/j.cels.2020.11.006 · Cited by 40 · see citing works
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Blattmann, P., Stutz, V., Lizzo, G., Richard, J., Gut, P., & Aebersold, R. H. (2019) · Scientific Data · doi:10.1038/sdata.2019.11 · Cited by 45 · see citing works
Self-citationPrediction of glycopeptide fragment mass spectra by deep learning
Yang, Y., & Fang, Q. (2024) · Nature Communications · doi:10.1038/s41467-024-46771-1 · Cited by 44 · see citing works
Characterization of Cerebrospinal Fluid via Data-Independent Acquisition Mass Spectrometry
Barkovits, K., Linden, A., Galozzi, S., Schilde, L. M., Pacharra, S., Mollenhauer, B., Stoepel, N., Steinbach, S., May, C., Uszkoreit, J., et al. (2018) · Journal of Proteome Research · doi:10.1021/acs.jproteome.8b00308 · Cited by 43 · see citing works
Li, W., Chi, H., Šalovská, B., Wu, C., Sun, L., Rosenberger, G., & Liu, Y. (2019) · Journal of the American Society for Mass Spectrometry · doi:10.1007/s13361-019-02243-1 · Cited by 43 · see citing works
Self-citationHülsmann, J., Kravić, B., Weith, M., Gstaiger, M., Aebersold, R. H., Collins, B. C., & Meyer, H. H. (2018) · Molecular & Cellular Proteomics · doi:10.1074/mcp.ra117.000471 · Cited by 39 · see citing works
Self-citationSystematic Comparison of Strategies for the Enrichment of Lysosomes by Data Independent Acquisition
Singh, J., Kaade, E., Muntel, J., Bruderer, R., Reiter, L., Thelen, M., & Winter, D. (2019) · Journal of Proteome Research · doi:10.1021/acs.jproteome.9b00580 · Cited by 39 · see citing works
Self-citationLou, R., Tang, P., Ding, K., Li, S., Tian, C., Li, Y., Zhao, S., Zhang, Y., & Shui, W. (2020) · iScience · doi:10.1016/j.isci.2020.100903 · Cited by 38 · see citing works
Integrated Identification and Quantification Error Probabilities for Shotgun Proteomics
The, M., & Käll, L. (2019) · Molecular & Cellular Proteomics · doi:10.1074/mcp.ra118.001018 · Cited by 37 · see citing works
Olaya‐Abril, A., Biełło, K. A., Rodríguez-Caballero, G., Cabello, P., Sáez, L. P., Moreno‐Vivián, C., Luque‐Almagro, V. M., & Roldán, M. D. (2024) · Microbial Biotechnology · doi:10.1111/1751-7915.14399 · Cited by 37 · see citing works
Quantitative Proteomics of Xenopus Embryos I, Sample Preparation
Gupta, M., Sonnett, M., Ryazanova, L. V., Presler, M., & Wühr, M. (2018) · Methods in molecular biology · doi:10.1007/978-1-4939-8784-9_13 · Cited by 39 · see citing works
The Art of Validating Quantitative Proteomics Data
Handler, D. C. L., Pascovici, D., Mirzaei, M., Gupta, V., Salekdeh, G. H., & Haynes, P. A. (2018) · PROTEOMICS · doi:10.1002/pmic.201800222 · Cited by 37 · see citing works
Jevtić, Ž., Stoll, B., Pfeiffer, F., Sharma, K., Urlaub, H., Marchfelder, A., & Lenz, C. (2019) · PROTEOMICS · doi:10.1002/pmic.201800491 · Cited by 37 · see citing works
Thomas, S. N., Friedrich, B., Schnaubelt, M., Chan, D. W., Zhang, H., & Aebersold, R. H. (2020) · iScience · doi:10.1016/j.isci.2020.101079 · Cited by 34 · see citing works
Self-citationSiyal, A. A., Chen, E. S.-W., Chan, H., Kitata, R. B., Yang, J., Tu, H., & Chen, Y. (2021) · Analytical Chemistry · doi:10.1021/acs.analchem.1c03477 · Cited by 35 · see citing works
Data‐independent acquisition proteomics methods for analyzing post‐translational modifications
Yang, Y., & Qiao, L. (2022) · PROTEOMICS · doi:10.1002/pmic.202200046 · Cited by 34 · see citing works
Banaei‐Esfahani, A., Nicod, C., Aebersold, R. H., & Collins, B. C. (2017) · Current Opinion in Microbiology · doi:10.1016/j.mib.2017.09.013 · Cited by 34 · see citing works
Self-citationKim, Y. J., Chambers, A. G., Cecchi, F., & Hembrough, T. (2018) · Journal of Proteomics · doi:10.1016/j.jprot.2018.04.022 · Cited by 34 · see citing works
Gupta, S., Ahadi, S., Zhou, W., & Röst, H. L. (2019) · Molecular & Cellular Proteomics · doi:10.1074/mcp.tir118.001132 · Cited by 32 · see citing works
Self-citationEshghi, S. T., Auger, P., & Mathews, W. R. (2018) · Clinical Proteomics · doi:10.1186/s12014-018-9209-x · Cited by 30 · see citing works
Avant-garde: an automated data-driven DIA data curation tool
Jácome, A. S. V., Peckner, R., Shulman, N., Krug, K., DeRuff, K. C., Officer, A., Christianson, K. E., MacLean, B., MacCoss, M. J., Carr, S. A., et al. (2020) · Nature Methods · doi:10.1038/s41592-020-00986-4 · Cited by 30 · see citing works
Self-citationWillems, P., Fels, U., Staes, A., Gevaert, K., & Damme, P. V. (2021) · Journal of Proteome Research · doi:10.1021/acs.jproteome.0c00350 · Cited by 30 · see citing works
Alka, O., Shanthamoorthy, P., Witting, M. A., Kleigrewe, K., Kohlbacher, O., & Röst, H. L. (2022) · Nature Communications · doi:10.1038/s41467-022-29006-z · Cited by 30 · see citing works
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Bludau, I., Nicod, C., Martelli, C., Xue, P., Heusel, M., Fossati, A., Uliana, F., Frommelt, F., Aebersold, R., & Collins, B. C. (2021) · bioRxiv · doi:10.1021/acs.jproteome.3c00125 · Cited by 26 · see citing works
Self-citationPonnaiyan, S., Akter, F., Singh, J., & Winter, D. (2020) · Scientific Data · doi:10.1038/s41597-020-0399-5 · Cited by 29 · see citing works
Walzer, M., García‐Seisdedos, D., Prakash, A., Brack, P., Crowther, P., Graham, R. L., George, N., Mohammed, S., Moreno, P. A., Papatheodorou, I., et al. (2022) · Scientific Data · doi:10.1038/s41597-022-01380-9 · Cited by 30 · see citing works
Bichmann, L., Gupta, S., Rosenberger, G., Kuchenbecker, L., Sachsenberg, T. T., Ewels, P., Alka, O., Pfeuffer, J., Kohlbacher, O., & Röst, H. L. (2021) · Journal of Proteome Research · doi:10.1021/acs.jproteome.1c00123 · Cited by 29 · see citing works
Self-citationvan Wijk, K. J., Leppert, T., Sun, Z., Kearly, A., Li, M., Mendoza, L., Guzchenko, I., Debley, E. L., Sauermann, G., Routray, P., et al. (2023) · Journal of Proteome Research · doi:10.1021/acs.jproteome.3c00536 · Cited by 30 · see citing works
Kim, Y. J., Sweet, S. M. M., Egertson, J. D., Sedgewick, A. J., Woo, S., Liao, W., Merrihew, G. E., Searle, B. C., Vaske, C. J., Heaton, R. K., et al. (2018) · Journal of Proteome Research · doi:10.1021/acs.jproteome.8b00699 · Cited by 29 · see citing works
Self-citationGao, M., Yang, W., Li, C., Chang, Y., Liu, Y., Wang, S., He, Q., Zhong, C., Shuai, J., Yu, R., et al. (2021) · Communications Biology · doi:10.1038/s42003-021-02726-6 · Cited by 28 · see citing works
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Gan, G., Xu, X., Chen, X., Zhang, X., Wang, J., & Zhong, C. (2021) · Molecular & Cellular Proteomics · doi:10.1016/j.mcpro.2021.100051 · Cited by 27 · see citing works
Fossati, A., Frommelt, F., Uliana, F., Martelli, C., Vizovišek, M., Gillet, L. C. J., Collins, B. C., Gstaiger, M., & Aebersold, R. H. (2021) · Methods in molecular biology · doi:10.1007/978-1-0716-1178-4_18 · Cited by 27 · see citing works
Self-citationSchacke, S., Kirkpatrick, J. M., Stocksdale, A., Bauer, R., Hagel, C., Riecken, L. B., & Morrison, H. (2022) · Glia · doi:10.1002/glia.24253 · Cited by 27 · see citing works
Biological mass spectrometry enables spatiotemporal ‘omics: From tissues to cells to organelles
Pade, L. R., Stepler, K. E., Portero, E. P., DeLaney, K., & Nemes, P. (2023) · Mass Spectrometry Reviews · doi:10.1002/mas.21824 · Cited by 28 · see citing works
Meier, F., Brunner, A., Frank, M., Ha, A., Bludau, I., Voytik, E., Kaspar‐Schoenefeld, S., Lubeck, M., Raether, O., Aebersold, R. H., et al. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/656207 · Cited by 27 · see citing works
Self-citationValo, I., Raro, P., Boissard, A., Maarouf, A., Jézéquel, P., Verrièle, V., Campone, M., Coqueret, O., & Guette, C. (2019) · PROTEOMICS · doi:10.1002/pmic.201800446 · Cited by 26 · see citing works
Targeted Quantification of the Lysosomal Proteome in Complex Samples
Mosen, P., Sanner, A., Singh, J., & Winter, D. (2021) · Proteomes · doi:10.3390/proteomes9010004 · Cited by 26 · see citing works
Ge, W., Liang, X., Zhang, F., Hu, Y., Xu, L., Xiang, N., Sun, R., Liu, W., Xue, Z., Yi, X., et al. (2021) · Journal of Proteome Research · doi:10.1021/acs.jproteome.1c00640 · Cited by 26 · see citing works
Li, W., Liu, C., Huang, Z., Shi, L., Zhong, C., Zhou, W., Meng, P., Li, Z., Wang, S., Luo, F., et al. (2021) · Journal of Cell Science · doi:10.1242/jcs.255273 · Cited by 25 · see citing works
Deep learning approaches for data-independent acquisition proteomics
Yang, Y., Lin, L., & Qiao, L. (2021) · Expert Review of Proteomics · doi:10.1080/14789450.2021.2020654 · Cited by 25 · see citing works
Qian, P., Wang, X., Zhong, C., Wang, J., Cai, M., Nguitragool, W., Li, J., Cui, H., & Yuan, J. (2022) · eLife · doi:10.7554/elife.77447 · Cited by 24 · see citing works
Merrihew, G. E., Park, J., Plubell, D. L., Searle, B. C., Keene, C. D., Larson, E. B., Bateman, R. J., Perrin, R. J., Chhatwal, J. P., Farlow, M. R., et al. (2023) · Scientific Data · doi:10.1038/s41597-023-02057-7 · Cited by 24 · see citing works
Self-citation
- Authors
- Rosenberger, G., Bludau, I., Schmitt, U., Heusel, M., Hunter, C. L., Liu, Y., MacCoss, M. J., MacLean, B. X., Nesvizhskii, A. I., Pedrioli, P. G. A., Reiter, L., Röst, H. L., Tate, S., Ting, Y. S., Collins, B. C., & Aebersold, R.
- Affiliations
- University of Zurich (CH)
- ETH Zurich (CH)
- University of Washington (US)
- University of Michigan (US)
- Biognosys (Switzerland) (CH)
- Sciex (Canada) (CA)
- Corresponding author
- Collins, Ben C
- Aebersold, Ruedi
- ORCID
- Venue
- Nature Methods
- Published
- 2017-08-21
- Volume
- 14
- Issue
- 9
- Pages
- 921-927
- ISSN
- 1548-7091 (ISSN-L)
- 1548-7105
- PMC
- PMC5581544
- OpenAlex
- W2745376284
- Cited by
- 203
- References
- 50
- Citations by year
- 2026: 15 · 2025: 11 · 2024: 19 · 2023: 19 · 2022: 27 · 2021: 27 · 2020: 36 · 2019: 25 · 2018: 20 · 2017: 4
- FWCI
- 11.46
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature Methods (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Research Portal (Queen's University Belfast) (submittedVersion, other-oa)
- Funders
- National Science Foundation
- Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung (P2EZP3, 31003A, 130530, 162268, 161435)
- Eidgenössische Technische Hochschule Zürich
- Institut Mérieux (PZ00P3_161435)
- National Institutes of Health
- National Institute of General Medical Sciences (P41GM103533, R01GM094231)
- FP7 Ideas: European Research Council (233226)
- Topics
- Physical Sciences › Chemistry › Spectroscopy › Advanced Proteomics Techniques and Applications
- Physical Sciences › Chemistry › Spectroscopy › Mass Spectrometry Techniques and Applications
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolomics and Mass Spectrometry Studies
- Keywords
- data-independent acquisition, false discovery rate, SWATH-MS, spectral library, large-scale proteomics, targeted proteomics
- MeSH terms
- Computer Simulation, Data Interpretation, Statistical, Peptide Mapping, Proteins, Sensitivity and Specificity, Mass Spectrometry, Reproducibility of Results, Models, Statistical, Sequence Analysis, Protein, High-Throughput Screening Assays
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