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Andromeda: A Peptide Search Engine Integrated into the MaxQuant Environment
Open accessAbstract
A key step in mass spectrometry (MS)-based proteomics is the identification of peptides in sequence databases by their fragmentation spectra. Here we describe Andromeda, a novel peptide search engine using a probabilistic scoring model. On proteome data, Andromeda performs as well as Mascot, a widely used commercial search engine, as judged by sensitivity and specificity analysis based on target decoy searches. Furthermore, it can handle data with arbitrarily high fragment mass accuracy, is able to assign and score complex patterns of post-translational modifications, such as highly phosphorylated peptides, and accommodates extremely large databases. The algorithms of Andromeda are provided. Andromeda can function independently or as an integrated search engine of the widely used MaxQuant computational proteomics platform and both are freely available at www.maxquant.org. The combination enables analysis of large data sets in a simple analysis workflow on a desktop computer. For searching individual spectra Andromeda is also accessible via a web server. We demonstrate the flexibility of the system by implementing the capability to identify cofragmented peptides, significantly improving the total number of identified peptides.
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Cites
Cox, J., & Mann, M. (2008) · Nature Biotechnology · doi:10.1038/nbt.1511 · Cited by 14,855
Self-citationMass spectrometry-based proteomics
Aebersold, R., & Mann, M. (2003) · Nature · doi:10.1038/nature01511 · Cited by 6,955
Self-citationOng, S.-E., Blagoev, B., Kratchmarova, I., Kristensen, D. B., Steen, H., Pandey, A., & Mann, M. (2002) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m200025-mcp200 · Cited by 5,574
Self-citationFunctional and quantitative proteomics using SILAC
Mann, M. (2006) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2067 · Cited by 931
Self-citationQuantitative proteomics reveals subset-specific viral recognition in dendritic cells
Luber, C. A., Cox, J., Lauterbach, H., Fancke, B., Selbach, M., Tschopp, J., Akira, S., Wiegand, M., Hochrein, H., O'Keeffe, M., et al. (2010) · Immunity · doi:10.1016/j.immuni.2010.01.013 · Cited by 576
Self-citationSenko, M. W., Beu, S. C., & McLaffertycor, F. W. (1995) · Journal of the American Society for Mass Spectrometry · doi:10.1016/1044-0305(95)00017-8 · Cited by 451
Precision proteomics: The case for high resolution and high mass accuracy
Mann, M., & Kelleher, N. L. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0800788105 · Cited by 450
Self-citation
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Tyanova, S., Temu, T., Sinitcyn, P., Carlson, A., Hein, M. Y., Geiger, T., Mann, M., & Cox, J. (2016) · Nature Methods · doi:10.1038/nmeth.3901 · Cited by 8,803
Self-citationCox, J., Hein, M. Y., Luber, C. A., Paron, I., Nagaraj, N., & Mann, M. (2014) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m113.031591 · Cited by 5,180
Self-citationCyclic GMP-AMP Synthase Is a Cytosolic DNA Sensor That Activates the Type I Interferon Pathway
Sun, L., Wu, J., Du, F., Chen, X., & Chen, Z. J. (2013) · Science · doi:10.1126/science.1232458 · Cited by 4,996
L-Arginine Modulates T Cell Metabolism and Enhances Survival and Anti-tumor Activity
Geiger, R., Rieckmann, J. C., Wolf, T., Basso, C., Feng, Y., Fuhrer, T., Kogadeeva, M., Picotti, P., Meissner, F., Mann, M., et al. (2016) · Cell · doi:10.1016/j.cell.2016.09.031 · Cited by 1,775
Self-citationKulak, N. A., Pichler, G., Paron, I., Nagaraj, N., & Mann, M. (2014) · Nature Methods · doi:10.1038/nmeth.2834 · Cited by 1,719
Self-citationProtein 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
Lysosome-targeting chimaeras for degradation of extracellular proteins
Banik, S. M., Pedram, K., Wisnovsky, S., Ahn, G., Riley, N. M., & Bertozzi, C. R. (2020) · Nature · doi:10.1038/s41586-020-2545-9 · Cited by 1,199
MS-GF+ makes progress towards a universal database search tool for proteomics
Kim, S., & Pevzner, P. A. (2014) · Nature Communications · doi:10.1038/ncomms6277 · Cited by 1,098
Phosphoproteomics reveals that Parkinson's disease kinase LRRK2 regulates a subset of Rab GTPases
Steger, M., Tonelli, F., Ito, G., Davies, P., Trost, M., Vetter, M., Wachter, S., Lorentzen, E., Duddy, G., Wilson, S., et al. (2016) · eLife · doi:10.7554/elife.12813 · Cited by 1,042
Self-citationJohnson, E. C. B., Dammer, E. B., Duong, D. M., Ping, L., Zhou, M., Yin, L., Higginbotham, L. A., Guajardo, A., White, B., Troncoso, J. C., et al. (2020) · Nature Medicine · doi:10.1038/s41591-020-0815-6 · Cited by 1,001
SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways
Park, J., Chen, Y., Tishkoff, D. X., Peng, C., Tan, M., Dai, L., Xie, Z., Zhang, Y., Zwaans, B. M. M., Skinner, M. E., et al. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.06.001 · Cited by 1,000
Deep proteome and transcriptome mapping of a human cancer cell line
Nagaraj, N., Wisniewski, J. R., Geiger, T., Cox, J., Kircher, M., Kelso, J., Pääbo, S., & Mann, M. (2011) · Molecular Systems Biology · doi:10.1038/msb.2011.81 · Cited by 979
Self-citationBudnik, B., Levy, E., Harmange, G., & Slavov, N. (2018) · Genome Biology · doi:10.1186/s13059-018-1547-5 · Cited by 832
Cell type- and brain region-resolved mouse brain proteome
Sharma, K., Schmitt, S., Bergner, C. G., Tyanova, S., Kannaiyan, N., Manrique-Hoyos, N., Kongi, K., Cantuti, L., Hanisch, U.-K., Philips, M.-A., et al. (2015) · Nature Neuroscience · doi:10.1038/nn.4160 · Cited by 785
Self-citationThe target landscape of clinical kinase drugs
Klaeger, S., Heinzlmeir, S., Wilhelm, M., Polzer, H., Vick, B., Koenig, P.-A., Reinecke, M., Ruprecht, B., Petzoldt, S., Meng, C., et al. (2017) · Science · doi:10.1126/science.aan4368 · Cited by 854
Recalibrating equus evolution using the genome sequence of an early middle pleistocene horse
Orlando, L., Ginolhac, A., Zhang, G., Froese, D., Albrechtsen, A., Stiller, M., Schubert, M., Cappellini, E., Petersen, B., Moltke, I., et al. (2013) · Nature · doi:10.1038/nature12323 · Cited by 841
Self-citationMichalski, A., Damoc, E., Hauschild, J.-P., Lange, O., Wieghaus, A., Makarov, A., Nagaraj, N., Cox, J., Mann, M., & Horning, S. (2011) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m111.011015 · Cited by 832
Self-citationGeiger, T., Wehner, A., Schaab, C., Cox, J., & Mann, M. (2012) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m111.014050 · Cited by 797
Self-citationRichter, B., Sliter, D. A., Herhaus, L., Stolz, A., Wang, C., Beli, P., Zaffagnini, G., Wild, P., Martens, S., Wagner, S. A., et al. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1523926113 · Cited by 755
Composition of isolated synaptic boutons reveals the amounts of vesicle trafficking proteins
Wilhelm, B. G., Mandad, S., Truckenbrodt, S., Kröhnert, K., Schäfer, C., Rammner, B., Koo, S. J., Claßen, G. A., Krauss, M., Haucke, V., et al. (2014) · Science · doi:10.1126/science.1252884 · Cited by 770
Dowdle, W. E., Nyfeler, B., Nagel, J., Elling, R. A., Liu, S., Triantafellow, E., Menon, S., Wang, Z., Honda, A., Pardee, G., et al. (2014) · Nature Cell Biology · doi:10.1038/ncb3053 · Cited by 759
Tau PTM Profiles Identify Patient Heterogeneity and Stages of Alzheimer’s Disease
Wesseling, H., Mair, W., Kumar, M., Schlaffner, C. N., Tang, S., Beerepoot, P., Fatou, B., Guise, A. J., Cheng, L., Takeda, S., et al. (2020) · Cell · doi:10.1016/j.cell.2020.10.029 · Cited by 688
“10 (Cox and Mann, 2008) and peptide list searched against the Homo sapiens Uniprot protein sequence database (December 2017, only reviewed entries appended with common laboratory contaminants [cRAP database, 247 entries]) using the Andromeda search engine (Cox et al., 2011).”
MethodPlasma Proteome Profiling to Assess Human Health and Disease
Geyer, P. E., Kulak, N. A., Pichler, G., Holdt, L. M., Teupser, D., & Mann, M. (2016) · Cell Systems · doi:10.1016/j.cels.2016.02.015 · Cited by 734
Self-citationAn atlas of the aging lung mapped by single cell transcriptomics and deep tissue proteomics
Angelidis, I., Simon, L. M., Fernandez, I. E., Strunz, M., Mayr, C. H., Greiffo, F. R., Tsitsiridis, G., Ansari, M., Graf, E., Strom, T.-M., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-08831-9 · Cited by 637
Self-citationBassani-Sternberg, M., Bräunlein, E., Klar, R., Engleitner, T., Sinitcyn, P., Audehm, S., Straub, M., Weber, J., Slotta-Huspenina, J., Specht, K., et al. (2016) · Nature Communications · doi:10.1038/ncomms13404 · Cited by 693
Self-citationA “Proteomic Ruler” for Protein Copy Number and Concentration Estimation without Spike-in Standards
Wiśniewski, J. R., Hein, M. Y., Cox, J., & Mann, M. (2014) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m113.037309 · Cited by 690
Self-citationMetabolic modulation of tumours with engineered bacteria for immunotherapy
Canale, F. P., Basso, C., Antonini, G., Perotti, M., Li, N., Sokolovska, A., Neumann, J., James, M. J., Geiger, S., Jin, W., et al. (2021) · Nature · doi:10.1038/s41586-021-04003-2 · Cited by 619
Yoon, H. S., Cho, C. H., Yun, M. S., Jang, S. J., You, H. J., Kim, J.-H., Han, D., Cha, K. H., Moon, S. H., Lee, K., et al. (2021) · Nature Microbiology · doi:10.1038/s41564-021-00880-5 · Cited by 602
Genetic diagnosis of Mendelian disorders via RNA sequencing
Kremer, L. S., Bader, D. M., Mertes, C., Kopajtich, R., Pichler, G., Iuso, A., Haack, T. B., Graf, E., Schwarzmayr, T., Terrile, C., et al. (2017) · Nature Communications · doi:10.1038/ncomms15824 · Cited by 590
Decoding Human Cytomegalovirus
Stern-Ginossar, N., Weisburd, B., Michalski, A., Le, V. T. K., Hein, M. Y., Huang, S.-X., Ma, M., Shen, B., Qian, S.-B., Hengel, H., et al. (2012) · Science · doi:10.1126/science.1227919 · Cited by 589
Self-citationNrf2 Activation Promotes Lung Cancer Metastasis by Inhibiting the Degradation of Bach1
Lignitto, L., LeBoeuf, S. E., Homer, H., Jiang, S., Askenazi, M., Karakousi, T. R., Pass, H. I., Bhutkar, A. J., Tsirigos, A., Ueberheide, B., et al. (2019) · Cell · doi:10.1016/j.cell.2019.06.003 · Cited by 573
Widespread Proteome Remodeling and Aggregation in Aging C. elegans
Walther, D. M., Kasturi, P., Zheng, M., Pinkert, S., Vecchi, G., Ciryam, P., Morimoto, R. I., Dobson, C. M., Vendruscolo, M., Mann, M., et al. (2015) · Cell · doi:10.1016/j.cell.2015.03.032 · Cited by 569
Self-citationSeyfried, N. T., Dammer, E. B., Swarup, V., Nandakumar, D., Duong, D. M., Yin, L., Deng, Q., Nguyen, T., Hales, C. M., Wingo, T., et al. (2017) · Cell Systems · doi:10.1016/j.cels.2016.11.006 · Cited by 477
BAF complex vulnerabilities in cancer demonstrated via structure-based PROTAC design
Farnaby, W., Koegl, M., Roy, M. J., Whitworth, C., Diers, E., Trainor, N., Zollman, D., Steurer, S., Karolyi-Oezguer, J., Riedmueller, C., et al. (2019) · Nature Chemical Biology · doi:10.1038/s41589-019-0294-6 · Cited by 562
Structure of a RING E3 ligase and ubiquitin-loaded E2 primed for catalysis
Plechanovová, A., Jaffray, E. G., Tatham, M. H., Naismith, J. H., & Hay, R. T. (2012) · Nature · doi:10.1038/nature11376 · Cited by 521
A comprehensive compilation of SUMO proteomics
Hendriks, I. A., & Vertegaal, A. C. O. (2016) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2016.81 · Cited by 514
Wang, M., Beckmann, N. D., Roussos, P., Wang, E., Zhou, X., Wang, Q., Ming, C., Neff, R., Ma, W., Fullard, J. F., et al. (2018) · Scientific Data · doi:10.1038/sdata.2018.185 · Cited by 502
Single-cell proteomic and transcriptomic analysis of macrophage heterogeneity using SCoPE2
Specht, H., Emmott, E., Petelski, A. A., Huffman, R. G., Perlman, D. H., Serra, M., Kharchenko, P., Koller, A., & Slavov, N. (2021) · Genome Biology · doi:10.1186/s13059-021-02267-5 · Cited by 493
The functional landscape of the human phosphoproteome
Ochoa, D., Jarnuczak, A. F., Viéitez, C., Gehre, M., Soucheray, M., Mateus, A., Kleefeldt, A. A., Hill, A., Garcia-Alonso, L., Stein, F., et al. (2020) · Nature Biotechnology · doi:10.1038/s41587-019-0344-3 · Cited by 491
Mills, R. J., Titmarsh, D. M., Koenig, X., Parker, B. L., Ryall, J. G., Quaife-Ryan, G. A., Voges, H. K., Hodson, M. P., Ferguson, C., Drowley, L., et al. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1707316114 · Cited by 478
Psychedelics promote plasticity by directly binding to BDNF receptor TrkB
Moliner, R., Girych, M., Brunello, C. A., Kovaleva, V., Biojone, C., Enkavi, G., Antenucci, L., Kot, E. F., Goncharuk, S. A., Kaurinkoski, K., et al. (2023) · Nature Neuroscience · doi:10.1038/s41593-023-01316-5 · Cited by 478
Steger, M., Diez, F., Dhekne, H. S., Lis, P., Nirujogi, R. S., Karayel, O., Tonelli, F., Martinez, T. N., Lorentzen, E., Pfeffer, S. R., et al. (2017) · eLife · doi:10.7554/elife.31012 · Cited by 482
Self-citationStructure of activated transcription complex Pol II–DSIF–PAF–SPT6
Vos, S. M., Farnung, L., Boehning, M., Wigge, C., Linden, A., Urlaub, H., & Cramer, P. (2018) · Nature · doi:10.1038/s41586-018-0440-4 · Cited by 432
Nagaraj, N., Alexander Kulak, N., Cox, J., Neuhauser, N., Mayr, K., Hoerning, O., Vorm, O., & Mann, M. (2012) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m111.013722 · Cited by 392
Self-citationη-Secretase processing of APP inhibits neuronal activity in the hippocampus
Willem, M., Tahirovic, S., Busche, M. A., Ovsepian, S. V., Chafai, M., Kootar, S., Hornburg, D., Evans, L. D. B., Moore, S., Daria, A., et al. (2015) · Nature · doi:10.1038/nature14864 · Cited by 398
Robles, M. S., Cox, J., & Mann, M. (2014) · PLoS Genetics · doi:10.1371/journal.pgen.1004047 · Cited by 383
Self-citationSerine ADP-ribosylation depends on HPF1
Bonfiglio, J. J., Fontana, P., Zhang, Q., Colby, T., Gibbs-Seymour, I., Atanassov, I., Bartlett, E., Zaja, R., Ahel, I., & Matic, I. (2017) · Molecular Cell · doi:10.1016/j.molcel.2017.01.003 · Cited by 352
Kim, S., Min, S., Choi, Y. S., Jo, S.-H., Jung, J. H., Han, K., Kim, J., An, S., Ji, Y. W., Kim, Y.-G., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-29279-4 · Cited by 375
Michalski, A., Damoc, E., Lange, O., Denisov, E., Nolting, D., Müller, M., Viner, R., Schwartz, J., Remes, P., Belford, M., et al. (2012) · Molecular & Cellular Proteomics · doi:10.1074/mcp.o111.013698 · Cited by 373
Self-citationPolyamines control eIF5A hypusination, TFEB translation, and autophagy to reverse B cell senescence
Zhang, H., Alsaleh, G., Feltham, J., Sun, Y., Napolitano, G., Riffelmacher, T., Charles, P., Frau, L., Hublitz, P., Yu, Z., et al. (2019) · Molecular Cell · doi:10.1016/j.molcel.2019.08.005 · Cited by 341
Phosphorylated tau interactome in the human Alzheimer's disease brain
Drummond, E., Pires, G., MacMurray, C., Askenazi, M., Nayak, S., Bourdon, M., Safar, J., Ueberheide, B., & Wisniewski, T. (2020) · Brain · doi:10.1093/brain/awaa223 · Cited by 357
Plasma Proteome Profiling to detect and avoid sample‐related biases in biomarker studies
Geyer, P. E., Voytik, E., Treit, P. V., Doll, S., Kleinhempel, A., Niu, L., Müller, J. B., Buchholtz, M., Bader, J. M., Teupser, D., et al. (2019) · EMBO Molecular Medicine · doi:10.15252/emmm.201910427 · Cited by 348
Self-citationQuantitative maps of protein phosphorylation sites across 14 different rat organs and tissues
Lundby, A., Secher, A., Lage, K., Nordsborg, N. B., Dmytriyev, A., Lundby, C., & Olsen, J. V. (2012) · Nature Communications · doi:10.1038/ncomms1871 · Cited by 343
Self-citationCooperative and independent roles of the Drp1 adaptors Mff, MiD49 and MiD51 in mitochondrial fission
Osellame, L. D., Singh, A. P., Stroud, D. A., Palmer, C. S., Stojanovski, D., Ramachandran, R., & Ryan, M. T. (2016) · Journal of Cell Science · doi:10.1242/jcs.185165 · Cited by 336
Mauvoisin, D., Wang, J., Jouffe, C., Martin, E., Atger, F., Waridel, P., Quadroni, M., Gachon, F., & Naef, F. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1314066111 · Cited by 329
Global Proteome Analysis of the NCI-60 Cell Line Panel
Gholami, A. M., Hahne, H., Wu, Z., Auer, F. J., Meng, C., Wilhelm, M., & Kuster, B. (2013) · Cell Reports · doi:10.1016/j.celrep.2013.07.018 · Cited by 302
Gillet, L. C., Leitner, A., & Aebersold, R. (2016) · Annual Review of Analytical Chemistry · doi:10.1146/annurev-anchem-071015-041535 · Cited by 323
Single Muscle Fiber Proteomics Reveals Fiber-Type-Specific Features of Human Muscle Aging
Murgia, M., Toniolo, L., Nagaraj, N., Ciciliot, S., Vindigni, V., Schiaffino, S., Reggiani, C., & Mann, M. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.05.054 · Cited by 315
Self-citationThe gut microbiota promotes hepatic fatty acid desaturation and elongation in mice
Kindt, A., Liebisch, G., Clavel, T., Haller, D., Hörmannsperger, G., Yoon, H., Kolmeder, D., Sigruener, A., Krautbauer, S., Seeliger, C., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-05767-4 · Cited by 311
Secretome protein enrichment identifies physiological BACE1 protease substrates in neurons
Kuhn, P., Koroniak, K., Hogl, S., Colombo, A., Zeitschel, U., Willem, M., Volbracht, C., Schepers, U., Imhof, A., Hoffmeister, A., et al. (2012) · The EMBO Journal · doi:10.1038/emboj.2012.173 · Cited by 301
A Review on Quantitative Multiplexed Proteomics
Pappireddi, N., Martin, L., & Wühr, M. (2019) · ChemBioChem · doi:10.1002/cbic.201800650 · Cited by 299
The EGFR-specific antibody cetuximab combined with chemotherapy triggers immunogenic cell death
Pozzi, C., Cuomo, A., Spadoni, I., Magni, E., Silvola, A., Conte, A., Sigismund, S., Ravenda, P. S., Bonaldi, T., Zampino, M. G., et al. (2016) · Nature Medicine · doi:10.1038/nm.4078 · Cited by 292
Rørvig, S., Østergaard, O., Heegaard, N. H. H., & Borregaard, N. (2013) · Journal of Leukocyte Biology · doi:10.1189/jlb.1212619 · Cited by 289
UV-sensitive syndrome protein UVSSA recruits USP7 to regulate transcription-coupled repair
Schwertman, P., Lagarou, A., Dekkers, D. H. W., Raams, A., van der Hoek, A. C., Laffeber, C., Hoeijmakers, J. H. J., Demmers, J. A. A., Fousteri, M., Vermeulen, W., et al. (2012) · Nature Genetics · doi:10.1038/ng.2230 · Cited by 279
Bioinformatics Methods for Mass Spectrometry-Based Proteomics Data Analysis
Chen, C., Hou, J., Tanner, J. J., & Cheng, J. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21082873 · Cited by 280
Neufeld-Cohen, A., Robles, M. S., Aviram, R., Manella, G., Adamovich, Y., Ladeuix, B., Nir, D., Rousso-Noori, L., Kuperman, Y., Golik, M., et al. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1519650113 · Cited by 262
Self-citationExtensive quantitative remodeling of the proteome between normal colon tissue and adenocarcinoma
Wiśniewski, J. R., Ostasiewicz, P., Duś, K., Zielińska, D. F., Gnad, F., & Mann, M. (2012) · Molecular Systems Biology · doi:10.1038/msb.2012.44 · Cited by 248
Self-citationSchiller, H. B., Fernandez, I. E., Burgstaller, G., Schaab, C., Scheltema, R. A., Schwarzmayr, T., Strom, T. M., Eickelberg, O., & Mann, M. (2015) · Molecular Systems Biology · doi:10.15252/msb.20156123 · Cited by 261
Self-citationVariant ribosomal RNA alleles are conserved and exhibit tissue-specific expression
Parks, M. M., Kurylo, C. M., Dass, R. A., Bojmar, L., Lyden, D., Vincent, C. T., & Blanchard, S. C. (2018) · Science Advances · doi:10.1126/sciadv.aao0665 · Cited by 260
A selective ER‐phagy exerts procollagen quality control via a Calnexin‐FAM134B complex
Forrester, A., De Leonibus, C., Grumati, P., Fasana, E., Piemontese, M., Staiano, L., Fregno, I., Raimondi, A., Marazza, A., Bruno, G., et al. (2019) · The EMBO Journal · doi:10.15252/embj.201899847 · Cited by 259
He, J., Ford, H. C., Carroll, J., Ding, S., Fearnley, I. M., & Walker, J. E. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1702357114 · Cited by 251
Mick, D. U., Dennerlein, S., Wiese, H., Reinhold, R., Pacheu-Grau, D., Lorenzi, I., Sasarman, F., Weraarpachai, W., Shoubridge, E. A., Warscheid, B., et al. (2012) · Cell · doi:10.1016/j.cell.2012.11.053 · Cited by 250
Selective enrichment of newly synthesized proteins for quantitative secretome analysis
Eichelbaum, K., Winter, M., Diaz, M. B., Herzig, S., & Krijgsveld, J. (2012) · Nature Biotechnology · doi:10.1038/nbt.2356 · Cited by 248
Henriksen, P., Wagner, S. A., Weinert, B. T., Sharma, S., Bačinskaja, G., Rehman, M., Juffer, A. H., Walther, T. C., Lisby, M., & Choudhary, C. (2012) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m112.017251 · Cited by 246
Mitochondrial protein synthesis adapts to influx of nuclear-encoded protein
Richter-Dennerlein, R., Oeljeklaus, S., Lorenzi, I., Ronsör, C., Bareth, B., Schendzielorz, A. B., Wang, C., Warscheid, B., Rehling, P., & Dennerlein, S. (2016) · Cell · doi:10.1016/j.cell.2016.09.003 · Cited by 232
Glutamine methylation in histone H2A is an RNA-polymerase-I-dedicated modification
Tessarz, P., Santos-Rosa, H., Robson, S. C., Sylvestersen, K. B., Nelson, C. J., Nielsen, M. L., & Kouzarides, T. (2014) · Nature · doi:10.1038/nature12819 · Cited by 243
Initial Quantitative Proteomic Map of 28 Mouse Tissues Using the SILAC Mouse
Geiger, T., Velic, A., Macek, B., Lundberg, E., Kampf, C., Nagaraj, N., Uhlen, M., Cox, J., & Mann, M. (2013) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m112.024919 · Cited by 235
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Howden, A. J. M., Hukelmann, J. L., Brenes, A., Spinelli, L., Sinclair, L. V., Lamond, A. I., & Cantrell, D. A. (2019) · Nature Immunology · doi:10.1038/s41590-019-0495-x · Cited by 231
Differential dynamics of the mammalian mRNA and protein expression response to misfolding stress
Cheng, Z., Teo, G., Krueger, S., Rock, T. M., Koh, H. W., Choi, H., & Vogel, C. (2016) · Molecular Systems Biology · doi:10.15252/msb.20156423 · Cited by 227
Extensive identification and analysis of conserved small ORFs in animals
Mackowiak, S. D., Zauber, H., Bielow, C., Thiel, D., Kutz, K., Calviello, L., Mastrobuoni, G., Rajewsky, N., Kempa, S., Selbach, M., et al. (2015) · Genome Biology · doi:10.1186/s13059-015-0742-x · Cited by 227
Sun, L., Zhu, G., Zhang, Z., Mou, S., & Dovichi, N. J. (2015) · Journal of Proteome Research · doi:10.1021/acs.jproteome.5b00100 · Cited by 216
Tumour-selective activity of RAS-GTP inhibition in pancreatic cancer
Wasko, U. N., Jiang, J., Dalton, T. C., Curiel-Garcia, A., Edwards, A. C., Wang, Y., Lee, B., Orlen, M., Tian, S., Stalnecker, C. A., et al. (2024) · Nature · doi:10.1038/s41586-024-07379-z · Cited by 209
VDAC2 enables BAX to mediate apoptosis and limit tumor development
Chin, H. S., Li, M. X., Tan, I. K. L., Ninnis, R. L., Reljic, B., Scicluna, K., Dagley, L. F., Sandow, J. J., Kelly, G. L., Samson, A. L., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-07309-4 · Cited by 196
A streamlined mass spectrometry–based proteomics workflow for large-scale FFPE tissue analysis
Coscia, F., Doll, S., Bech, J. M., Schweizer, L., Mund, A., Lengyel, E., Lindebjerg, J., Madsen, G. I., Moreira, J. M., & Mann, M. (2020) · The Journal of Pathology · doi:10.1002/path.5420 · Cited by 200
Self-citationJUMP: a tag-based database search tool for peptide identification with high sensitivity and accuracy
Wang, X., Li, Y., Wu, Z., Wang, H., Tan, H., & Peng, J. (2014) · Molecular & Cellular Proteomics · doi:10.1074/mcp.o114.039586 · Cited by 194
A PP2A-B55 recognition signal controls substrate dephosphorylation kinetics during mitotic exit
Cundell, M. J., Hutter, L. H., Nunes Bastos, R., Poser, E., Holder, J., Mohammed, S., Novak, B., & Barr, F. A. (2016) · Journal of Cell Biology · doi:10.1083/jcb.201606033 · Cited by 193
Cell-Type-Resolved Quantitative Proteomics of Murine Liver
Azimifar, S. B., Nagaraj, N., Cox, J., & Mann, M. (2014) · Cell Metabolism · doi:10.1016/j.cmet.2014.11.002 · Cited by 173
Self-citationAn evaluation of blood compatibility of silver nanoparticles
Huang, H., Lai, W., Cui, M., Liang, L., Lin, Y., Fang, Q., Liu, Y., & Xie, L. (2016) · Scientific Reports · doi:10.1038/srep25518 · Cited by 186
Zeiler, M., Straube, W. L., Lundberg, E., Uhlen, M., & Mann, M. (2012) · Molecular & Cellular Proteomics · doi:10.1074/mcp.o111.009613 · Cited by 168
Self-citationKinase-impaired BTK mutations are susceptible to clinical-stage BTK and IKZF1/3 degrader NX-2127
Montoya, S., Bourcier, J., Noviski, M., Lu, H., Thompson, M. C., Chirino, A., Jahn, J., Sondhi, A. K., Gajewski, S., Tan, Y. S. (., et al. (2024) · Science · doi:10.1126/science.adi5798 · Cited by 175
De novo derivation of proteomes from transcriptomes for transcript and protein identification
Evans, V. C., Barker, G., Heesom, K. J., Fan, J., Bessant, C., & Matthews, D. A. (2012) · Nature Methods · doi:10.1038/nmeth.2227 · Cited by 166
The neuropeptide complement of the marine annelid Platynereis dumerilii
Conzelmann, M., Williams, E. A., Krug, K., Franz-Wachtel, M., Macek, B., & Jékely, G. (2013) · BMC Genomics · doi:10.1186/1471-2164-14-906 · Cited by 165
Mitochondrial CoQ deficiency is a common driver of mitochondrial oxidants and insulin resistance
Fazakerley, D. J., Chaudhuri, R., Yang, P., Maghzal, G. J., Thomas, K. C., Krycer, J. R., Humphrey, S. J., Parker, B. L., Fisher-Wellman, K. H., Meoli, C. C., et al. (2018) · eLife · doi:10.7554/elife.32111 · Cited by 160
Analysis of High Accuracy, Quantitative Proteomics Data in the MaxQB Database
Schaab, C., Geiger, T., Stoehr, G., Cox, J., & Mann, M. (2012) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m111.014068 · Cited by 164
Self-citationAn automated pipeline for high-throughput label-free quantitative proteomics
Weisser, H., Nahnsen, S., Grossmann, J., Nilse, L., Quandt, A., Brauer, H., Sturm, M., Kenar, E., Kohlbacher, O., Aebersold, R., et al. (2013) · Journal of Proteome Research · doi:10.1021/pr300992u · Cited by 160
Characterization of the E. coli proteome and its modifications during growth and ethanol stress
Soufi, B., Krug, K., Harst, A., & Macek, B. (2015) · Frontiers in Microbiology · doi:10.3389/fmicb.2015.00103 · Cited by 142
AIM2 inflammasome is activated by pharmacological disruption of nuclear envelope integrity
Di Micco, A., Frera, G., Lugrin, J., Jamilloux, Y., Hsu, E.-T., Tardivel, A., De Gassart, A., Zaffalon, L., Bujisic, B., Siegert, S., et al. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1602419113 · Cited by 143
The PhoP-Dependent ncRNA Mcr7 Modulates the TAT Secretion System in Mycobacterium tuberculosis
Solans, L., Gonzalo-Asensio, J., Sala, C., Benjak, A., Uplekar, S., Rougemont, J., Guilhot, C., Malaga, W., Martín, C., & Cole, S. T. (2014) · PLoS Pathogens · doi:10.1371/journal.ppat.1004183 · Cited by 147
A multiregional proteomic survey of the postnatal human brain
Carlyle, B. C., Kitchen, R. R., Kanyo, J. E., Voss, E. Z., Pletikos, M., Sousa, A. M. M., Lam, T. T., Gerstein, M. B., Sestan, N., & Nairn, A. C. (2017) · Nature Neuroscience · doi:10.1038/s41593-017-0011-2 · Cited by 143
Pelka, K., Bertheloot, D., Reimer, E., Phulphagar, K., Schmidt, S. V., Christ, A., Stahl, R., Watson, N., Miyake, K., Hacohen, N., et al. (2018) · Immunity · doi:10.1016/j.immuni.2018.04.011 · Cited by 145
Metadata
- Authors
- Cox, J., Neuhauser, N., Michalski, A., Scheltema, R. A., Olsen, J. V., & Mann, M.
- Venue
- Journal of Proteome Research
- Publisher
- American Chemical Society (ACS)
- Published
- 2011-04
- Volume
- 10
- Issue
- 4
- Pages
- 1794-1805
- ISSN
- 1535-3893 (ISSN-L)
- 1535-3907
- OpenAlex
- W2036321220
- Cited by
- 5,500
- References
- 7
- FWCI
- 81.12
- Type
- journal article
- Language
- en
- Open access
- hybrid
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
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Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.