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DTASelect and Contrast: Tools for Assembling and Comparing Protein Identifications from Shotgun Proteomics
Open accessAbstract
The components of complex peptide mixtures can be separated by liquid chromatography, fragmented by tandem mass spectrometry, and identified by the SEQUEST algorithm. Inferring a mixture's source proteins requires that the identified peptides be reassociated. This process becomes more challenging as the number of peptides increases. DTASelect, a new software package, assembles SEQUEST identifications and highlights the most significant matches. The accompanying Contrast tool compares DTASelect results from multiple experiments. The two programs improve the speed and precision of proteomic data analysis. Keywords: proteomics • protein identification • SEQUEST • data analysis • software • differential analysis • subtractive analysis • MudPIT • assembly
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Citations
Cites
Quantitative analysis of complex protein mixtures using isotope-coded affinity tags
Gygi, S. P., Rist, B., Gerber, S. A., Turecek, F., Gelb, M. H., & Aebersold, R. (1999) · Nature Biotechnology · doi:10.1038/13690 · Cited by 4,683
Cited by
Semi-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
Wnt proteins are lipid-modified and can act as stem cell growth factors
Willert, K., Brown, J. D., Danenberg, E., Duncan, A. W., Weissman, I. L., Reya, T., Yates, J. R., & Nusse, R. (2003) · Nature · doi:10.1038/nature01611 · Cited by 2,257
Self-citationYan, H., Zhong, G., Xu, G., He, W., Jing, Z., Gao, Z., Huang, Y., Qi, Y., Peng, B., Wang, H., et al. (2012) · eLife · doi:10.7554/elife.00049 · Cited by 2,115
Quantitative reactivity profiling predicts functional cysteines in proteomes
Weerapana, E., Wang, C., Simon, G. M., Richter, F., Khare, S., Dillon, M. B. D., Bachovchin, D. A., Mowen, K., Baker, D., & Cravatt, B. F. (2010) · Nature · doi:10.1038/nature09472 · Cited by 1,684
Protein Analysis by Shotgun/Bottom-up Proteomics
Zhang, Y., Fonslow, B. R., Shan, B., Baek, M.-C., & Yates, J. R. (2013) · Chemical Reviews · doi:10.1021/cr3003533 · Cited by 1,491
Self-citationA proteomic view of the Plasmodium falciparum life cycle
Florens, L., Washburn, M. P., Raine, J. D., Anthony, R. M., Grainger, M., Haynes, J. D., Moch, J. K., Muster, N., Sacci, J. B., Tabb, D. L., et al. (2002) · Nature · doi:10.1038/nature01107 · Cited by 1,308
Self-citationProteomics by Mass Spectrometry: Approaches, Advances, and Applications
Yates, J. R., Ruse, C. I., & Nakorchevsky, A. (2009) · Annual Review of Biomedical Engineering · doi:10.1146/annurev-bioeng-061008-124934 · Cited by 1,078
Self-citationInterpretation of Shotgun Proteomic Data
Nesvizhskii, A. I., & Aebersold, R. (2005) · Molecular & Cellular Proteomics · doi:10.1074/mcp.r500012-mcp200 · Cited by 1,025
Monoacylglycerol lipase regulates a fatty acid network that promotes cancer pathogenesis
Nomura, D. K., Long, J. Z., Niessen, S., Hoover, H. S., Ng, S.-W., & Cravatt, B. F. (2010) · Cell · doi:10.1016/j.cell.2009.11.027 · Cited by 1,002
Dieterich, D. C., Link, A. J., Graumann, J., Tirrell, D. A., & Schuman, E. M. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0601637103 · Cited by 874
Identification of long-lived proteins reveals exceptional stability of essential cellular structures
Toyama, B. H., Savas, J. N., Park, S. K., Harris, M. S., Ingolia, N. T., Yates, J. R., & Hetzer, M. W. (2013) · Cell · doi:10.1016/j.cell.2013.07.037 · Cited by 572
Shoulders, M. D., Ryno, L. M., Genereux, J. C., Moresco, J. J., Tu, P. G., Wu, C., Yates, J. R., Su, A. I., Kelly, J. W., & Wiseman, R. L. (2013) · Cell Reports · doi:10.1016/j.celrep.2013.03.024 · Cited by 554
Self-citationPaoletti, A. C., Parmely, T. J., Tomomori-Sato, C., Sato, S., Zhu, D., Conaway, R. C., Conaway, J. W., Florens, L., & Washburn, M. P. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0606379103 · Cited by 538
ProLuCID: An improved SEQUEST-like algorithm with enhanced sensitivity and specificity
Xu, T., Park, S. K., Venable, J. D., Wohlschlegel, J. A., Diedrich, J. K., Cociorva, D., Lu, B., Liao, L., Hewel, J., Han, X., et al. (2015) · Journal of Proteomics · doi:10.1016/j.jprot.2015.07.001 · Cited by 511
Self-citationCytosolic proteostasis through importing of misfolded proteins into mitochondria
Ruan, L., Zhou, C., Jin, E., Kucharavy, A., Zhang, Y., Wen, Z., Florens, L., & Li, R. (2017) · Nature · doi:10.1038/nature21695 · Cited by 474
Macrophage-secreted granulin supports pancreatic cancer metastasis by inducing liver fibrosis
Nielsen, S. R., Quaranta, V., Linford, A., Emeagi, P., Rainer, C., Santos, A., Ireland, L., Sakai, T., Sakai, K., Kim, Y.-S., et al. (2016) · Nature Cell Biology · doi:10.1038/ncb3340 · Cited by 441
Histone Crosstalk between H2B Monoubiquitination and H3 Methylation Mediated by COMPASS
Lee, J.-S., Shukla, A., Schneider, J., Swanson, S. K., Washburn, M. P., Florens, L., Bhaumik, S. R., & Shilatifard, A. (2007) · Cell · doi:10.1016/j.cell.2007.09.046 · Cited by 438
He, M., Chiang, H.-H., Luo, H., Zheng, Z., Qiao, Q., Wang, L., Tan, M., Ohkubo, R., Mu, W.-C., Zhao, S., et al. (2020) · Cell Metabolism · doi:10.1016/j.cmet.2020.01.009 · Cited by 425
Integrated Metagenomics/Metaproteomics Reveals Human Host-Microbiota Signatures of Crohn's Disease
Erickson, A. R., Cantarel, B. L., Lamendella, R., Darzi, Y., Mongodin, E. F., Pan, C., Shah, M., Halfvarson, J., Tysk, C., Henrissat, B., et al. (2012) · PLoS ONE · doi:10.1371/journal.pone.0049138 · Cited by 395
Angers, S., Thorpe, C. J., Biechele, T. L., Goldenberg, S. J., Zheng, N., MacCoss, M. J., & Moon, R. T. (2006) · Nature Cell Biology · doi:10.1038/ncb1381 · Cited by 364
The proteome of the mouse photoreceptor sensory cilium complex
Liu, Q., Tan, G., Levenkova, N., Li, T., Pugh, E. N., Rux, J. J., Speicher, D. W., & Pierce, E. A. (2007) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m700054-mcp200 · Cited by 359
FLORENS, L., CAROZZA, M., SWANSON, S., FOURNIER, M., COLEMAN, M., WORKMAN, J., & WASHBURN, M. (2006) · Methods · doi:10.1016/j.ymeth.2006.07.028 · Cited by 344
Dynamic RNA acetylation revealed by quantitative cross-evolutionary mapping
Sas-Chen, A., Thomas, J. M., Matzov, D., Taoka, M., Nance, K. D., Nir, R., Bryson, K. M., Shachar, R., Liman, G. L. S., Burkhart, B. W., et al. (2020) · Nature · doi:10.1038/s41586-020-2418-2 · Cited by 336
Extremely long-lived nuclear pore proteins in the rat brain
Savas, J. N., Toyama, B. H., Xu, T., Yates, J. R., & Hetzer, M. W. (2012) · Science · doi:10.1126/science.1217421 · Cited by 335
Self-citationImpact of Dietary Resistant Starch on the Human Gut Microbiome, Metaproteome, and Metabolome
Maier, T. V., Lucio, M., Lee, L. H., VerBerkmoes, N. C., Brislawn, C. J., Bernhardt, J., Lamendella, R., McDermott, J. E., Bergeron, N., Heinzmann, S. S., et al. (2017) · mBio · doi:10.1128/mbio.01343-17 · Cited by 316
“9) (44) at 2 peptides per protein and the following widely accepted parameters for all the MS runs: cross correlation (Xcorr) of at least 1.”
Global Analysis of Protein Sumoylation in Saccharomyces cerevisiae
Wohlschlegel, J. A., Johnson, E. S., Reed, S. I., & Yates, J. R. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m409203200 · Cited by 317
Self-citationUBXD7 Binds Multiple Ubiquitin Ligases and Implicates p97 in HIF1α Turnover
Alexandru, G., Graumann, J., Smith, G. T., Kolawa, N. J., Fang, R., & Deshaies, R. J. (2008) · Cell · doi:10.1016/j.cell.2008.06.048 · Cited by 310
Franjic, D., Skarica, M., Ma, S., Arellano, J. I., Tebbenkamp, A. T. N., Choi, J., Xu, C., Li, Q., Morozov, Y. M., Andrijevic, D., et al. (2022) · Neuron · doi:10.1016/j.neuron.2021.10.036 · Cited by 308
Extracting Accurate Precursor Information for Tandem Mass Spectra by RawConverter
He, L., Diedrich, J., Chu, Y.-Y., & Yates, J. R. (2015) · Analytical Chemistry · doi:10.1021/acs.analchem.5b02721 · Cited by 306
Self-citationRuan, H.-B., Han, X., Li, M.-D., Singh, J. P., Qian, K., Azarhoush, S., Zhao, L., Bennett, A. M., Samuel, V. T., Wu, J., et al. (2012) · Cell Metabolism · doi:10.1016/j.cmet.2012.07.006 · Cited by 296
Self-citationMMS19 Assembles Iron-Sulfur Proteins Required for DNA Metabolism and Genomic Integrity
Stehling, O., Vashisht, A. A., Mascarenhas, J., Jonsson, Z. O., Sharma, T., Netz, D. J. A., Pierik, A. J., Wohlschlegel, J. A., & Lill, R. (2012) · Science · doi:10.1126/science.1219723 · Cited by 288
Niche of harmful alga Aureococcus anophagefferens revealed through ecogenomics
Gobler, C. J., Berry, D. L., Dyhrman, S. T., Wilhelm, S. W., Salamov, A., Lobanov, A. V., Zhang, Y., Collier, J. L., Wurch, L. L., Kustka, A. B., et al. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1016106108 · Cited by 285
Nucleolar expansion and elevated protein translation in premature aging
Buchwalter, A., & Hetzer, M. W. (2017) · Nature Communications · doi:10.1038/s41467-017-00322-z · Cited by 263
Bian, C., Xu, C., Ruan, J., Lee, K. K., Burke, T. L., Tempel, W., Barsyte, D., Li, J., Wu, M., Zhou, B. O., et al. (2011) · The EMBO Journal · doi:10.1038/emboj.2011.193 · Cited by 281
Rice, H. C., de Malmazet, D., Schreurs, A., Frere, S., Van Molle, I., Volkov, A. N., Creemers, E., Vertkin, I., Nys, J., Ranaivoson, F. M., et al. (2019) · Science · doi:10.1126/science.aao4827 · Cited by 281
The deubiquitinating enzyme BAP1 regulates cell growth via interaction with HCF-1
Machida, Y. J., Machida, Y., Vashisht, A. A., Wohlschlegel, J. A., & Dutta, A. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.046755 · Cited by 274
Wang, H., Shi, L. Z., Wong, C. C. L., Han, X., Hwang, P. Y.-H., Truong, L. N., Zhu, Q., Shao, Z., Chen, D. J., Berns, M. W., et al. (2013) · PLoS Genetics · doi:10.1371/journal.pgen.1003277 · Cited by 259
Self-citationOptimization of Mass Spectrometry-Compatible Surfactants for Shotgun Proteomics
Chen, E. I., Cociorva, D., Norris, J. L., & Yates, J. R. (2007) · Journal of Proteome Research · doi:10.1021/pr060682a · Cited by 218
Self-citationGlycolytic Enzymes Coalesce in G Bodies under Hypoxic Stress
Jin, M., Fuller, G. G., Han, T., Yao, Y., Alessi, A. F., Freeberg, M. A., Roach, N. P., Moresco, J. J., Karnovsky, A., Baba, M., et al. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.06.082 · Cited by 208
Self-citationSrivastava, S., Swanson, S. K., Manel, N., Florens, L., Washburn, M. P., & Skowronski, J. (2008) · PLoS Pathogens · doi:10.1371/journal.ppat.1000059 · Cited by 209
DAF-16 employs the chromatin remodeller SWI/SNF to promote stress resistance and longevity
Riedel, C. G., Dowen, R. H., Lourenco, G. F., Kirienko, N. V., Heimbucher, T., West, J. A., Bowman, S. K., Kingston, R. E., Dillin, A., Asara, J. M., et al. (2013) · Nature Cell Biology · doi:10.1038/ncb2720 · Cited by 207
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
Costa, K. C., Wong, P. M., Wang, T., Lie, T. J., Dodsworth, J. A., Swanson, I., Burn, J. A., Hackett, M., & Leigh, J. A. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1003653107 · Cited by 203
Mahrour, N., Redwine, W. B., Florens, L., Swanson, S. K., Martin-Brown, S., Bradford, W. D., Staehling-Hampton, K., Washburn, M. P., Conaway, R. C., & Conaway, J. W. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m706987200 · Cited by 196
Chemical proteomic map of dimethyl fumarate–sensitive cysteines in primary human T cells
Blewett, M. M., Xie, J., Zaro, B. W., Backus, K. M., Altman, A., Teijaro, J. R., & Cravatt, B. F. (2016) · Science Signaling · doi:10.1126/scisignal.aaf7694 · Cited by 194
Shanks, N. F., Savas, J. N., Maruo, T., Cais, O., Hirao, A., Oe, S., Ghosh, A., Noda, Y., Greger, I. H., Yates, J. R., et al. (2012) · Cell Reports · doi:10.1016/j.celrep.2012.05.004 · Cited by 194
Self-citationProteomics Analysis Unravels the Functional Repertoire of Coronavirus Nonstructural Protein 3
Neuman, B. W., Joseph, J. S., Saikatendu, K. S., Serrano, P., Chatterjee, A., Johnson, M. A., Liao, L., Klaus, J. P., Yates, J. R., Wüthrich, K., et al. (2008) · Journal of Virology · doi:10.1128/jvi.02631-07 · Cited by 192
Self-citationA Comprehensive Proteomics and Transcriptomics Analysis of Bacillus subtilis Salt Stress Adaptation
Hahne, H., Mäder, U., Otto, A., Bonn, F., Steil, L., Bremer, E., Hecker, M., & Becher, D. (2010) · Journal of Bacteriology · doi:10.1128/jb.01106-09 · Cited by 183
Fournier, M. L., Paulson, A., Pavelka, N., Mosley, A. L., Gaudenz, K., Bradford, W. D., Glynn, E., Li, H., Sardiu, M. E., Fleharty, B., et al. (2010) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m900415-mcp200 · Cited by 161
Quinti, L., Dayalan Naidu, S., Träger, U., Chen, X., Kegel-Gleason, K., Llères, D., Connolly, C., Chopra, V., Low, C., Moniot, S., et al. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1614943114 · Cited by 140
Incorporation of a nucleoside analog maps genome repair sites in postmitotic human neurons
Reid, D. A., Reed, P. J., Schlachetzki, J. C. M., Nitulescu, I. I., Chou, G., Tsui, E. C., Jones, J. R., Chandran, S., Lu, A. T., McClain, C. A., et al. (2021) · Science · doi:10.1126/science.abb9032 · Cited by 121
Degradation of HK2 by chaperone-mediated autophagy promotes metabolic catastrophe and cell death
Xia, H.-G., Najafov, A., Geng, J., Galan-Acosta, L., Han, X., Guo, Y., Shan, B., Zhang, Y., Norberg, E., Zhang, T., et al. (2015) · Journal of Cell Biology · doi:10.1083/jcb.201503044 · Cited by 122
Self-citationBottom-up structural proteomics: cryoEM of protein complexes enriched from the cellular milieu
Ho, C.-M., Li, X., Lai, M., Terwilliger, T. C., Beck, J. R., Wohlschlegel, J., Goldberg, D. E., Fitzpatrick, A. W. P., & Zhou, Z. H. (2020) · Nature Methods · doi:10.1038/s41592-019-0637-y · Cited by 115
Plubell, D. L., Käll, L., Webb-Robertson, B.-J., Bramer, L. M., Ives, A., Kelleher, N. L., Smith, L. M., Montine, T. J., Wu, C. C., & MacCoss, M. J. (2022) · Journal of Proteome Research · doi:10.1021/acs.jproteome.1c00894 · Cited by 85
Krishna, S., Arrojo e Drigo, R., Capitanio, J. S., Ramachandra, R., Ellisman, M., & Hetzer, M. W. (2021) · Developmental Cell · doi:10.1016/j.devcel.2021.10.008 · Cited by 73
Han, X., Wang, Y., Aslanian, A., Fonslow, B., Graczyk, B., Davis, T. N., & Yates, J. R. (2014) · Journal of Proteome Research · doi:10.1021/pr500971h · Cited by 72
Self-citationDimethyl Fumarate Disrupts Human Innate Immune Signaling by Targeting the IRAK4–MyD88 Complex
Zaro, B. W., Vinogradova, E. V., Lazar, D. C., Blewett, M. M., Suciu, R. M., Takaya, J., Studer, S., de la Torre, J. C., Casanova, J.-L., Cravatt, B. F., et al. (2019) · The Journal of Immunology · doi:10.4049/jimmunol.1801627 · Cited by 68
Detecting the Immune System Response of a 500 Year-Old Inca Mummy
Corthals, A., Koller, A., Martin, D. W., Rieger, R., Chen, E. I., Bernaski, M., Recagno, G., & Dávalos, L. M. (2012) · PLoS ONE · doi:10.1371/journal.pone.0041244 · Cited by 65
Choi, J., Lee, K., Ingvarsdottir, K., Bonasio, R., Saraf, A., Florens, L., Washburn, M. P., Tadros, S., Green, M. R., & Busino, L. (2018) · Nature Cell Biology · doi:10.1038/s41556-018-0084-5 · Cited by 50
Frankel, E. B., Shankar, R., Moresco, J. J., Yates, J. R., Volkmann, N., & Audhya, A. (2017) · Nature Communications · doi:10.1038/s41467-017-01636-8 · Cited by 46
Self-citationFiliou, M. D., Teplytska, L., Otte, D. M., Zimmer, A., & Turck, C. W. (2012) · Journal of Psychiatric Research · doi:10.1016/j.jpsychires.2012.07.004 · Cited by 36
Murakami, Y., Hasegawa, Y., Nagano, K., & Yoshimura, F. (2014) · Infection and Immunity · doi:10.1128/iai.02069-14 · Cited by 36
Zinovyeva, A. Y., Veksler-Lublinsky, I., Vashisht, A. A., Wohlschlegel, J. A., & Ambros, V. R. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1506576112 · Cited by 29
An apical protein, Pcr2, is required for persistent movement by the human parasite Toxoplasma gondii
Munera Lopez, J., Tengganu, I. F., Liu, J., Murray, J. M., Arias Padilla, L. F., Zhang, Y., Brown, P. T., Florens, L., & Hu, K. (2022) · PLOS Pathogens · doi:10.1371/journal.ppat.1010776 · Cited by 14
Xu, S., & Onoda, A. (2025) · Journal of Chemical Theory and Computation · doi:10.1021/acs.jctc.4c01288 · Cited by 13
Páez-Moscoso, D. J., Ho, D. V., Pan, L., Hildebrand, K., Jensen, K. L., Levy, M. J., Florens, L., & Baumann, P. (2022) · Nature Communications · doi:10.1038/s41467-022-28545-9 · Cited by 10
Liu, X., Zhang, Y., Wen, Z., Hao, Y., Banks, C. A. S., Cesare, J., Bhattacharya, S., Arvindekar, S., Lange, J. J., Xie, Y., et al. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2318601121 · Cited by 9
Duhay, V., Tian, M., Kosieradzka, K., Ebner, M., Lo, W.-T., Krauss, M., Sprengel, H.-L., Voss, M., Riechmann, M., Savas, J. N., et al. (2026) · Nature Communications · doi:10.1038/s41467-026-70345-y · Cited by 4
Páez-Moscoso, D. J., Ho, D. V., Pan, L., Hildebrand, K., Jensen, K. L., Levy, M. J., Florens, L., & Baumann, P. (2021) · doi:10.1101/2021.12.15.472819 · Cited by 2
Metadata
- Authors
- Tabb, D. L., McDonald, W. H., & Yates, J. R.
- Venue
- Journal of Proteome Research
- Publisher
- American Chemical Society (ACS)
- Published
- 2002-01-07
- Volume
- 1
- Issue
- 1
- Pages
- 21-26
- ISSN
- 1535-3893 (ISSN-L)
- 1535-3907
- OpenAlex
- W1990299806
- Cited by
- 1,367
- References
- 1
- FWCI
- 22.63
- Type
- journal article
- Language
- en
- Open access
- green
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