The DOI matches its Crossref record; 33 of the 33 references it cites were found in a registry or an index.
Proteome-wide cellular protein concentrations of the human pathogen Leptospira interrogans
Open accessAbstract
Mass-spectrometry-based methods for relative proteome quantification have broadly affected life science research. However, important research directions, particularly those involving mathematical modelling and simulation of biological processes, also critically depend on absolutely quantitative data--that is, knowledge of the concentration of the expressed proteins as a function of cellular state. Until now, absolute protein concentration measurements of a considerable fraction of the proteome (73%) have only been derived from genetically altered Saccharomyces cerevisiae cells, a technique that is not directly portable from yeast to other species. Here we present a mass-spectrometry-based strategy to determine the absolute quantity, that is, the average number of protein copies per cell in a cell population, for a large fraction of the proteome in genetically unperturbed cells. Applying the technology to the human pathogen Leptospira interrogans, a spirochete responsible for leptospirosis, we generated an absolute protein abundance scale for 83% of the mass-spectrometry-detectable proteome, from cells at different states. Taking advantage of the unique cellular dimensions of L. interrogans, we used cryo-electron tomography morphological measurements to verify, at the single-cell level, the average absolute abundance values of selected proteins determined by mass spectrometry on a population of cells. Because the strategy is relatively fast and applicable to any cell type, we expect that it will become a cornerstone of quantitative biology and systems biology.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
The check wasn’t confident either way, so it gives no verdict — never disputed.
In the citing paper
“Tissue-specific amino acid precursor pools and recycling rates, a pervasive problem for in vivo pulse labeling experiments 15,22 , did not appreciably affect our results (Fig. S1).”
From Global quantification of mammalian gene expression control (2011) · cites this paper as [22]
Experimental — accuracy not yet measuredIn the citing paper
“Mass spectrometry (MS)-based methods can overcome these difficulties and were recently used to determine protein copy numbers per cell for a significant fraction of the proteome of two bacterial species, namely Mycoplasma pneumonia and Leptospira interrogans (Malmstrom et al, 2009; Maier et al, 2011) and yeast (de Godoy et al, 2008).”
From The quantitative proteome of a human cell line (2011) · cites this paper as Malmstrom et al, 2009
In the citing paper
“We used the same data to calculate three different protein abundance scores as previously described (Ishihama et al, 2005; Silva et al, 2006; Malmstrom et al, 2009) and validated their precision by statistical analysis (Supplementary Figure S1; see Supplementary information for detail).”
From The quantitative proteome of a human cell line (2011) · cites this paper as Malmstrom et al, 2009
In the citing paper
“We and others have previously shown that the dynamic range of protein concentrations spans more than three orders of magnitude in the bacterium L. interrogans (Malmstrom et al, 2009) and five orders of magnitude in yeast (Ghaemmaghami et al, 2003; de Godoy et al, 2008; Picotti et al, 2009).”
From The quantitative proteome of a human cell line (2011) · cites this paper as Malmstrom et al, 2009
In the citing paper
“Those proteins make up the majority of the total protein mass (Malmstrom et al, 2009) and a considerable fraction of the cytoplasmic volume (Beck et al, 2009), while proteins functioning in signaling, protein transport, or regulatory pathways, e.g. transcription factors, comprise a minority of the quantitative proteome.”
From The quantitative proteome of a human cell line (2011) · cites this paper as Malmstrom et al, 2009
In the citing paper
“Interestingly, the bacterium L. interrogans expresses a relatively small number of in very high copy proteins, e.g. proteins of the translation and protein folding system, metabolic enzymes as well as components of the cell wall.”
From The quantitative proteome of a human cell line (2011) · cites this paper as Malmstrom et al, 2009
In the citing paper
“The arbitrary protein abundance indices were calibrated to absolute protein copy numbers per cell their precision validated by bootstrapping analysis as described earlier (Malmstrom et al, 2009).”
From The quantitative proteome of a human cell line (2011) · cites this paper as Malmstrom et al, 2009
In the citing paper
“The MS signal of peptides identifying each protein can be used to estimate its absolute cellular abundance (de Godoy et al, 2008; Malmstrom et al, 2009; Silva et al, 2006)”
From Deep proteome and transcriptome mapping of a human cancer cell line (2011) · cites this paper as Malmstrom et al, 2009
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Gene Ontology: tool for the unification of biology
Ashburner, M., Ball, C. A., Blake, J. A., Botstein, D., Butler, H., Cherry, J. M., Davis, A. P., Dolinski, K., Dwight, S. S., Eppig, J. T., et al. (2000) · Nature Genetics · doi:10.1038/75556 · Cited by 43,206
Eng, J. K., McCormack, A. L., & Yates, J. R. (1994) · Journal of the American Society for Mass Spectrometry · doi:10.1016/1044-0305(94)80016-2 · Cited by 6,484
Keller, A., Nesvizhskii, A., Kolker, E., & Aebersold, R. (2002) · Analytical Chemistry · doi:10.1021/ac025747h · Cited by 4,970
Self-citationGlobal analysis of protein expression in yeast
Ghaemmaghami, S., Huh, W.-K., Bower, K., Howson, R. W., Belle, A., Dephoure, N., O'Shea, E. K., & Weissman, J. S. (2003) · Nature · doi:10.1038/nature02046 · Cited by 3,750
Cryo-electron microscopy of vitrified specimens
Dubochet, J., Adrian, M., Chang, J.-J., Homo, J., Lepault, J., McDowall, A. W., & Schultz, P. (1988) · Quarterly Reviews of Biophysics · doi:10.1017/s0033583500004297 · Cited by 2,397
Ishihama, Y., Oda, Y., Tabata, T., Sato, T., Nagasu, T., Rappsilber, J., & Mann, M. (2005) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m500061-mcp200 · Cited by 2,055
Absolute quantification of proteins and phosphoproteins from cell lysates by tandem MS
Gerber, S. A., Rush, J., Stemman, O., Kirschner, M. W., & Gygi, S. P. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0832254100 · Cited by 1,733
Absolute Quantification of Proteins by LCMSE
Silva, J. C., Gorenstein, M. V., Li, G.-Z., Vissers, J. P. C., & Geromanos, S. J. (2006) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m500230-mcp200 · Cited by 1,529
Lu, P., Vogel, C., Wang, R., Yao, X., & Marcotte, E. M. (2007) · Nature Biotechnology · doi:10.1038/nbt1270 · Cited by 1,139
Desiere, F. (2006) · Nucleic Acids Research · doi:10.1093/nar/gkj040 · Cited by 910
Cited by
Sorted by citations
Global quantification of mammalian gene expression control
Schwanhäusser, B., Busse, D., Li, N., Dittmar, G., Schuchhardt, J., Wolf, J., Chen, W., & Selbach, M. (2011) · Nature · doi:10.1038/nature10098 · Cited by 6,566
Insights into the regulation of protein abundance from proteomic and transcriptomic analyses
Vogel, C., & Marcotte, E. M. (2012) · Nature Reviews Genetics · doi:10.1038/nrg3185 · Cited by 4,195
On the Dependency of Cellular Protein Levels on mRNA Abundance
Liu, Y., Beyer, A., & Aebersold, R. (2016) · Cell · doi:10.1016/j.cell.2016.03.014 · Cited by 3,221
Self-citationMass-spectrometric exploration of proteome structure and function
Aebersold, R., & Mann, M. (2016) · Nature · doi:10.1038/nature19949 · Cited by 2,334
Self-citationCorrelation of mRNA and protein in complex biological samples
Maier, T., Güell, M., & Serrano, L. (2009) · FEBS Letters · doi:10.1016/j.febslet.2009.10.036 · Cited by 1,802
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
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
The quantitative proteome of a human cell line
Beck, M., Schmidt, A., Malmstroem, J., Claassen, M., Ori, A., Szymborska, A., Herzog, F., Rinner, O., Ellenberg, J., & Aebersold, R. (2011) · Molecular Systems Biology · doi:10.1038/msb.2011.82 · Cited by 816
Self-citationQuantitative mass spectrometry in proteomics: critical review update from 2007 to the present
Bantscheff, M., Lemeer, S., Savitski, M. M., & Kuster, B. (2012) · Analytical and Bioanalytical Chemistry · doi:10.1007/s00216-012-6203-4 · Cited by 801
Geiger, T., Wehner, A., Schaab, C., Cox, J., & Mann, M. (2012) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m111.014050 · Cited by 797
The quantitative and condition-dependent Escherichia coli proteome
Schmidt, A., Kochanowski, K., Vedelaar, S. R., Ahrné, E., Volkmer, B., Callipo, L., Knoops, K., Bauer, M., Aebersold, R. H., & Heinemann, M. (2015) · Nature Biotechnology · doi:10.1038/nbt.3418 · Cited by 759
Self-citationLess label, more free: Approaches in label‐free quantitative mass spectrometry
Neilson, K. A., Ali, N., Muralidharan, S., Mirzaei, M., Mariani, M., Assadourian, G., Lee, A., Sluyter, S. C. V., & Haynes, P. A. (2011) · PROTEOMICS · doi:10.1002/pmic.201000553 · Cited by 731
A “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
Quantitative, High-Resolution Proteomics for Data-Driven Systems Biology
Cox, J., & Mann, M. (2011) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-061308-093216 · Cited by 685
Options and considerations when selecting a quantitative proteomics strategy
Domon, B., & Aebersold, R. H. (2010) · Nature Biotechnology · doi:10.1038/nbt.1661 · Cited by 616
Self-citationTranslation efficiency is determined by both codon bias and folding energy
Tuller, T., Waldman, Y. Y., Kupiec, M., & Ruppin, E. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0909910107 · Cited by 584
Decoding signalling networks by mass spectrometry-based proteomics
Choudhary, C., & Mann, M. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2900 · Cited by 592
Shteynberg, 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 554
Self-citationLundby, A., Lage, K., Weinert, B. T., Bekker‐Jensen, D. B., Secher, A., Skovgaard, T., Kelstrup, C. D., Dmytriyev, A., Choudhary, C., Lundby, C., et al. (2012) · Cell Reports · doi:10.1016/j.celrep.2012.07.006 · Cited by 563
Mass spectrometry in high-throughput proteomics: ready for the big time
Nilsson, T., Mann, M., Aebersold, R., Yates, J. R., Bairoch, A., & Bergeron, J. J. M. (2010) · Nature Methods · doi:10.1038/nmeth0910-681 · Cited by 470
Self-citationPaxdb, a database of protein abundance averages across all three domains of life
Wang, M., Weiss, M., Simonovic, M., Haertinger, G., Schrimpf, S. P., Hengartner, M. O., & von Mering, C. (2012) · Molecular & Cellular Proteomics · doi:10.1074/mcp.o111.014704 · Cited by 466
Fraga, T. R., Carvalho, E., Isaac, L., & Barbosa, A. S. (2014) · Elsevier eBooks · doi:10.1016/b978-0-12-397169-2.00107-4 · Cited by 457
Virulence of the zoonotic agent of leptospirosis: still terra incognita?
Picardeau, M. (2017) · Nature Reviews Microbiology · doi:10.1038/nrmicro.2017.5 · Cited by 421
Mass spectrometry–based proteomics in cell biology
Walther, T. C., & Mann, M. (2010) · The Journal of Cell Biology · doi:10.1083/jcb.201004052 · Cited by 425
Mass Spectrometry–Based Proteomics and Network Biology
Bensimon, A., Heck, A. J. R., & Aebersold, R. H. (2012) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-072909-100424 · Cited by 420
Self-citationDepletion of Abundant Plasma Proteins and Limitations of Plasma Proteomics
Tu, C., Rudnick, P. A., Martinez, M. Y., Cheek, K. L., Stein, S. E., Slebos, R. J. C., & Liebler, D. C. (2010) · Journal of Proteome Research · doi:10.1021/pr100646w · Cited by 390
Quantitative proteomic analysis reveals a simple strategy of global resource allocation in bacteria
Hui, S., Silverman, J. M., Chen, S. S., Erickson, D. W., Basan, M., Wang, J., Hwa, T., & Williamson, J. R. (2015) · Molecular Systems Biology · doi:10.15252/msb.20145697 · Cited by 369
Next-generation synthetic gene networks
Lu, T. K., Khalil, A. S., & Collins, J. J. (2009) · Nature Biotechnology · doi:10.1038/nbt.1591 · Cited by 365
Leptospira as an Emerging Pathogen: A Review of its Biology, Pathogenesis and Host Immune Responses
Evangelista, K. V., & Coburn, J. (2010) · Future Microbiology · doi:10.2217/fmb.10.102 · Cited by 354
The Coming Age of Complete, Accurate, and Ubiquitous Proteomes
Mann, M., Kulak, N. A., Nagaraj, N., & Cox, J. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.01.029 · Cited by 350
Quantitative 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
Deep and Highly Sensitive Proteome Coverage by LC-MS/MS Without Prefractionation
Thakur, S. S., Geiger, T., Chatterjee, B., Bandilla, P., Fröhlich, F., Cox, J., & Mann, M. (2011) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m110.003699 · Cited by 349
Cryo-Electron Tomography: Can it Reveal the Molecular Sociology of Cells in Atomic Detail?
Beck, M., & Baumeister, W. P. (2016) · Trends in Cell Biology · doi:10.1016/j.tcb.2016.08.006 · Cited by 322
Self-citationWhat Makes a Bacterial Species Pathogenic?:Comparative Genomic Analysis of the Genus Leptospira
Fouts, D. E., Matthias, M. A., Adhikarla, H., Adler, B., Santos, L. A., Berg, D. E., Bulach, D., Buschiazzo, A., Chang, Y.-F., Galloway, R. L., et al. (2016) · PLoS neglected tropical diseases · doi:10.1371/journal.pntd.0004403 · Cited by 331
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
Quantification of mRNA and protein and integration with protein turnover in a bacterium
Maier, T., Schmidt, A., Güell, M., Kühner, S., Gavin, A., Aebersold, R., & Serrano, L. (2011) · Molecular Systems Biology · doi:10.1038/msb.2011.38 · Cited by 297
Self-citationProteomic and interactomic insights into the molecular basis of cell functional diversity
Bludau, I., & Aebersold, R. (2020) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-020-0231-2 · Cited by 297
Self-citationSAM68 Regulates Neuronal Activity-Dependent Alternative Splicing of Neurexin-1
Iijima, T., Wu, K., Witte, H., Hanno-Iijima, Y., Glatter, T., Richard, S., & Scheiffele, P. (2011) · Cell · doi:10.1016/j.cell.2011.11.028 · Cited by 279
Proteomics on an Orbitrap Benchtop Mass Spectrometer Using All-ion Fragmentation
Geiger, T., Cox, J., & Mann, M. (2010) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m110.001537 · Cited by 264
Chemical Analysis of Single Cells
Lin, Y., Trouillon, R., Рустамовна, С. Г., & Ewing, A. G. (2011) · Analytical Chemistry · doi:10.1021/ac2009838 · Cited by 253
Quantitative Analysis of the Intra- and Inter-Individual Variability of the Normal Urinary Proteome
Nagaraj, N., & Mann, M. (2010) · Journal of Proteome Research · doi:10.1021/pr100835s · Cited by 251
Critical assessment of proteome‐wide label‐free absolute abundance estimation strategies
Ahrné, E., Molzahn, L., Glatter, T., & Schmidt, A. (2013) · PROTEOMICS · doi:10.1002/pmic.201300135 · Cited by 247
Self-citationPhenotypic bistability in Escherichia coli's central carbon metabolism
Kotte, O., Volkmer, B., Radzikowski, J. L., & Heinemann, M. (2014) · Molecular Systems Biology · doi:10.15252/msb.20135022 · Cited by 242
Quaternary dynamics and plasticity underlie small heat shock protein chaperone function
Stengel, F., Baldwin, A. J., Painter, A. J., Jaya, N., Basha, E., Kay, L. E., Vierling, E., Robinson, C. V., & Benesch, J. L. P. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0910126107 · Cited by 247
Saito, M. A., Bertrand, E. M., Dutkiewicz, S., Bulygin, V. V., Moran, D. M., Monteiro, F., Follows, M. J., Valois, F. W., & Waterbury, J. B. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1006943108 · Cited by 241
Synthetic Biology: An Emerging Engineering Discipline
Cheng, A. A., & Lu, T. K. (2012) · Annual Review of Biomedical Engineering · doi:10.1146/annurev-bioeng-071811-150118 · Cited by 241
Proteome of mouse oocytes at different developmental stages
Wang, S., Kou, Z., Jing, Z., Zhang, Y., Guo, X., Dong, M., Wilmut, I., & Gao, S. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1013185107 · Cited by 239
Protein 19 F NMR in Escherichia coli
Li, C., Wang, G.-F., Wang, Y., Creager-Allen, R. L., Lutz, E. A., Scronce, H., Slade, K. M., Ruf, R. A. S., Mehl, R. A., & Pielak, G. J. (2009) · Journal of the American Chemical Society · doi:10.1021/ja907966n · Cited by 226
Shi, T., Fillmore, T., Sun, X., Zhao, R., Schepmoes, A., Hossain, M., Xie, F., Wu, S., Kim, J., Jones, N., et al. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1204366109 · Cited by 220
Multiple nutrient stresses at intersecting Pacific Ocean biomes detected by protein biomarkers
Saito, M. A., McIlvin, M. R., Moran, D. M., Goepfert, T. J., DiTullio, G. R., Post, A. F., & Lamborg, C. H. (2014) · Science · doi:10.1126/science.1256450 · Cited by 217
Rapid tests for diagnosis of leptospirosis: Current tools and emerging technologies
Picardeau, M., Bertherat, E., Jancloes, M., nikolaos, S. A., Durski, K. N., & Hartskeerl, R. A. (2013) · Diagnostic Microbiology and Infectious Disease · doi:10.1016/j.diagmicrobio.2013.09.012 · Cited by 203
Schubert, 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 182
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 171
Self-citationArike, L., Valgepea, K., Peil, L., Nahku, R., Adamberg, K., & Vilu, R. (2012) · Journal of Proteomics · doi:10.1016/j.jprot.2012.06.020 · Cited by 176
An 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
Self-citationVisual proteomics of the human pathogen Leptospira interrogans
Beck, M., Malmström, J. A., Lange, V., Schmidt, A., Deutsch, E. W., & Aebersold, R. (2009) · Nature Methods · doi:10.1038/nmeth.1390 · Cited by 156
Self-citationIdentifier mapping performance for integrating transcriptomics and proteomics experimental results
Day, R., McDade, K. K., Chandran, U. R., Lisovich, A., Conrads, T. P., Hood, B. L., Kolli, V. S. K., Kirchner, D. R., Litzi, T., & Maxwell, G. L. (2011) · BMC Bioinformatics · doi:10.1186/1471-2105-12-213 · Cited by 156
Fraga, T. R., Carvalho, E., Isaac, L., & Barbosa, A. S. (2024) · Elsevier eBooks · doi:10.1016/b978-0-12-818619-0.00159-3 · Cited by 155
Lambert, A., Picardeau, M., Haake, D. A., Sermswan, R. W., Srikram, A., Adler, B., & Murray, G. L. (2012) · Infection and Immunity · doi:10.1128/iai.00131-12 · Cited by 146
Small Heat-Shock Proteins: Paramedics of the Cell
Hilton, G. R., Lioe, H., Stengel, F., Baldwin, A. J., & Benesch, J. L. P. (2012) · Topics in current chemistry · doi:10.1007/128_2012_324 · Cited by 148
Standardization approaches in absolute quantitative proteomics with mass spectrometry
Calderón‐Celis, F., Encinar, J. R., & Sanz‐Medel, A. (2017) · Mass Spectrometry Reviews · doi:10.1002/mas.21542 · Cited by 152
Ludwig, C., Claassen, M., Schmidt, A., & Aebersold, R. H. (2011) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m111.013987 · Cited by 141
Self-citationLiu, L., Yu, M., Zhang, Y., Wang, C., & Lu, H. (2014) · ACS Applied Materials & Interfaces · doi:10.1021/am501110e · Cited by 135
Chavez, J. D., Lee, C. F., Caudal, A., Keller, A., Tian, R., & Bruce, J. E. (2017) · Cell Systems · doi:10.1016/j.cels.2017.10.017 · Cited by 135
Quantitative dissection of the simple repression input–output function
García, H. G., & Phillips, R. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1015616108 · Cited by 127
Eyers, C. E., Lawless, C., Wedge, D. C., Lau, K. W., Gaskell, S. J., & Hubbard, S. J. (2011) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m110.003384 · Cited by 129
Application of targeted mass spectrometry in bottom-up proteomics for systems biology research
Manes, N. P., & Nita‐Lazar, A. (2018) · Journal of Proteomics · doi:10.1016/j.jprot.2018.02.008 · Cited by 130
Scheres, S. H. W., Melero, R., Valle, M., & Carazo, J. M. (2009) · Structure · doi:10.1016/j.str.2009.10.009 · Cited by 117
Computational methods for electron tomography
Fernández, J. (2012) · Micron · doi:10.1016/j.micron.2012.05.003 · Cited by 117
Kraeutler, M. J., Soltis, A. R., & Saucerman, J. J. (2010) · BMC Systems Biology · doi:10.1186/1752-0509-4-157 · Cited by 113
Izard, J., Renken, C. W., Hsieh, C., Desrosiers, D. C., Dunham-Ems, S. M., Vake, C. J. L., Gebhardt, L. L., Limberger, R. J., Cox, D. L., Marko, M., et al. (2009) · Journal of Bacteriology · doi:10.1128/jb.01031-09 · Cited by 111
Mass spectrometry-based proteomics for systems biology
Sabidó, E., Selevsek, N., & Aebersold, R. H. (2011) · Current Opinion in Biotechnology · doi:10.1016/j.copbio.2011.11.014 · Cited by 110
Self-citationGoeminne, L. J. E., Gevaert, K., & Clement, L. (2017) · Journal of Proteomics · doi:10.1016/j.jprot.2017.04.004 · Cited by 106
Absolute quantification of microbial proteomes at different states by directed mass spectrometry
Schmidt, A., Beck, M., Malmström, J. A., Lam, H., Claassen, M., Campbell, D. S., & Aebersold, R. H. (2011) · Molecular Systems Biology · doi:10.1038/msb.2011.37 · Cited by 102
Self-citationMalmström, E., Kilsgård, O., Hauri, S., Smeds, E., Herwald, H., Malmström, L., & Malmström, J. A. (2016) · Nature Communications · doi:10.1038/ncomms10261 · Cited by 103
Self-citationFarley, M. M., Hu, B., Margolin, W., & Liu, J. (2016) · Journal of Bacteriology · doi:10.1128/jb.00901-15 · Cited by 101
Evolutionary meandering of intermolecular interactions along the drift barrier
Lynch, M., & Hagner, K. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1421641112 · Cited by 102
TraML—A Standard Format for Exchange of Selected Reaction Monitoring Transition Lists
Deutsch, E. W., Chambers, M., Neumann, S., Levander, F., Binz, P., Shofstahl, J., Campbell, D. S., Mendoza, L., Ovelleiro, D., Helsens, K., et al. (2011) · Molecular & Cellular Proteomics · doi:10.1074/mcp.r111.015040 · Cited by 100
Self-citationHigh Precision Platelet Releasate Definition by Quantitative Reversed Protein Profiling—Brief Report
Wijten, P., van Holten, T. C., Woo, L. L., Bleijerveld, O. B., Roest, M., Heck, A. J. R., & Scholten, A. (2013) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.113.301147 · Cited by 103
Leptospira interrogans Catalase Is Required for Resistance to H 2 O 2 and for Virulence
Eshghi, A., Lourdault, K., Murray, G. L., Bartpho, T., Sermswan, R. W., Picardeau, M., Adler, B., Snarr, B. D., Zuerner, R. L., & Cameron, C. E. (2012) · Infection and Immunity · doi:10.1128/iai.00466-12 · Cited by 98
OmpL1 Is an Extracellular Matrix- and Plasminogen-Interacting Protein of Leptospira spp
Fernandes, L. G. V., Vieira, M. L., Kirchgatter, K., Alves, I. J., de Morais, Z. M., Vasconcellos, S. A., Romero, E. C., & Nascimento, A. L. T. O. (2012) · Infection and Immunity · doi:10.1128/iai.00474-12 · Cited by 98
A new view into prokaryotic cell biology from electron cryotomography
Oikonomou, C. M., Chang, Y., & Jensen, G. J. (2016) · Nature Reviews Microbiology · doi:10.1038/nrmicro.2016.7 · Cited by 97
Motility Is Crucial for the Infectious Life Cycle of Borrelia burgdorferi
Sultan, S. Z., Manne, A., Stewart, P. E., Bestor, A. C., Rosa, P. A., Charon, N. W., & Motaleb, M. A. (2013) · Infection and Immunity · doi:10.1128/iai.01228-12 · Cited by 96
Muntel, J., Fromion, V., Goelzer, A., Maaß, S., Mäder, U., Büttner, K., Hecker, M., & Becher, D. (2014) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m113.032631 · Cited by 101
Wu, Q., Yuan, H., Zhang, L., & Zhang, Y. (2012) · Analytica Chimica Acta · doi:10.1016/j.aca.2012.04.010 · Cited by 94
Directed mass spectrometry: towards hypothesis-driven proteomics
Schmidt, A., Claassen, M., & Aebersold, R. H. (2009) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2009.08.016 · Cited by 93
Self-citationOliveira, R., de Morais, Z. M., Gonçales, A. P., Romero, E. C., Vasconcellos, S. A., & Nascimento, A. L. T. O. (2011) · PLoS ONE · doi:10.1371/journal.pone.0021962 · Cited by 91
Xue, F., Dong, H., Wu, J., Wu, Z., Hu, W., Sun, A., Troxell, B., Yang, X., & Yan, J. (2010) · PLoS neglected tropical diseases · doi:10.1371/journal.pntd.0000857 · Cited by 91
Protease bias in absolute protein quantitation
Peng, M., Taouatas, N., Cappadona, S., van Breukelen, B., Mohammed, S., Scholten, A., & Heck, A. J. R. (2012) · Nature Methods · doi:10.1038/nmeth.2031 · Cited by 90
Pinne, M., Choy, H. A., & Haake, D. A. (2010) · PLoS neglected tropical diseases · doi:10.1371/journal.pntd.0000815 · Cited by 90
Direct and Absolute Quantification of over 1800 Yeast Proteins via Selected Reaction Monitoring
Lawless, C., Holman, S. W., Brownridge, P., Lanthaler, K., Harman, V. M., Watkins, R. H., Hammond, D. E., Miller, R. L., Sims, P. F. G., Grant, C. M., et al. (2016) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m115.054288 · Cited by 89
Wunder, E. A., Figueira, C. P., Benaroudj, N., Hu, B., Tong, B. A., Trajtenberg, F., Liu, J., dos Reis, M. G., Charon, N. W., Buschiazzo, A., et al. (2016) · Molecular Microbiology · doi:10.1111/mmi.13403 · Cited by 87
The Molecular Basis of Leptospiral Pathogenesis
Murray, G. L. (2014) · Current topics in microbiology and immunology · doi:10.1007/978-3-662-45059-8_7 · Cited by 86
The lipoprotein LipL32, an enigma of leptospiral biology
Murray, G. L. (2012) · Veterinary Microbiology · doi:10.1016/j.vetmic.2012.11.005 · Cited by 86
The Proteome of Cholesteryl-Ester-Enriched Versus Triacylglycerol-Enriched Lipid Droplets
Khor, V. K., Ahrends, R., Lin, Y., Shen, W., Adams, C. M., Roseman, A. N., Cortez, Y., Teruel, M. N., Azhar, S., & Kraemer, F. B. (2014) · PLoS ONE · doi:10.1371/journal.pone.0105047 · Cited by 86
Pinne, M., & Haake, D. A. (2013) · PLoS ONE · doi:10.1371/journal.pone.0051025 · Cited by 85
Classic reaction kinetics can explain complex patterns of antibiotic action
Wiesch, P. A. Z., Abel, S., Gkotzis, S., Ocampo, P., Engelstädter, J., Hinkley, T., Magnus, C., Waldor, M. K., Udekwu, K. I., & Cohen, T. (2015) · Science Translational Medicine · doi:10.1126/scitranslmed.aaa8760 · Cited by 85
Raddi, G., Morado, D. R., Yan, J., Haake, D. A., Yang, X., & Liu, J. (2012) · Journal of Bacteriology · doi:10.1128/jb.06474-11 · Cited by 84
Beck, M., Claassen, M., & Aebersold, R. (2011) · Current Opinion in Biotechnology · doi:10.1016/j.copbio.2010.09.002 · Cited by 83
Self-citationSouza, N. M., Vieira, M. L., Alves, I. J., de Morais, Z. M., Vasconcellos, S. A., & Nascimento, A. L. T. O. (2012) · Microbial Pathogenesis · doi:10.1016/j.micpath.2012.06.001 · Cited by 80
Metadata
- Authors
- Malmström, J., Beck, M., Schmidt, A., Lange, V., Deutsch, E. W., & Aebersold, R.
- Affiliations
- ETH Zurich (CH)
- Institute for Systems Biology (US)
- University of Zurich (CH)
- Corresponding author
- Aebersold, Ruedi
- Venue
- Nature
- Published
- 2009-07-15
- Volume
- 460
- Issue
- 7256
- Pages
- 762-765
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- PMC
- PMC2723184
- OpenAlex
- W2041852635
- Cited by
- 421
- References
- 33
- Citations by year
- 2026: 5 · 2025: 5 · 2024: 10 · 2023: 9 · 2022: 13 · 2021: 11 · 2020: 17 · 2019: 17 · 2018: 28 · 2017: 20 · 2016: 28 · 2015: 23 · 2014: 35 · 2013: 37 · 2012: 60
- FWCI
- 23.35
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- Lund University Publications (Lund University) (submittedVersion)
- MPG.PuRe (Max Planck Society) (submittedVersion)
- Funders
- National Institutes of Health (n01hv28179-12-0-0)
- National Heart, Lung, and Blood Institute (N01 HV028179, N01-HV-28179)
- Topics
- Physical Sciences › Chemistry › Spectroscopy › Advanced Proteomics Techniques and Applications
- Health Sciences › Medicine › Infectious Diseases › Leptospirosis research and findings
- Physical Sciences › Chemistry › Spectroscopy › Mass Spectrometry Techniques and Applications
- Keywords
- Leptospira interrogans, protein copy number, leptospirosis, cryo-electron tomography, quantitative proteomics, spirochetes
- MeSH terms
- Bacterial Proteins, Chromatography, High Pressure Liquid, Chromatography, Liquid, Humans, Leptospira interrogans, Mass Spectrometry, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, Cryoelectron Microscopy, Proteome, Proteomics, Tandem Mass Spectrometry, Electron Microscope Tomography
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.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
