Insights into the regulation of protein abundance from proteomic and transcriptomic analyses
Open accessAbstract
Recent advances in next-generation DNA sequencing and proteomics provide an unprecedented ability to survey mRNA and protein abundances. Such proteome-wide surveys are illuminating the extent to which different aspects of gene expression help to regulate cellular protein abundances. Current data demonstrate a substantial role for regulatory processes occurring after mRNA is made — that is, post-transcriptional, translational and protein degradation regulation — in controlling steady-state protein abundances. Intriguing observations are also emerging in relation to cells following perturbation, single-cell studies and the apparent evolutionary conservation of protein and mRNA abundances. Here, we summarize current understanding of the major factors regulating protein expression.
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Other estimates for the contribution of mRNA levels in determining protein expression in mammals are lower than ours, suggesting that mRNA levels contribute 10%-40%.
“Other estimates for the contribution of mRNA levels in determining protein expression in mammals are lower than ours, suggesting that mRNA levels contribute 10%–40% (Maier, Guell & Serrano, 2009; Vogel & Marcotte, 2012).”
From System wide analyses have underestimated protein abundances and the importance of transcription in mammals (2014) · cites this paper as Vogel & Marcotte, 2012
In “Concentrations, production and turnover rates of mRNA and proteins at steady state” (page unavailable), the review says mRNA abundance explains approximately 40% of variation in protein concentration and includes mammalian cells among the organisms discussed. It does not provide the 10% estimate attributed to the cited sources collectively. (LLM, conf=0.87)
Experimental — accuracy not yet measuredThe regulation of senescence extends beyond transcription, and prior work has reported cases in which transcriptomic changes do not align with proteomic readouts.
“the regulation of senescence extends beyond transcription, and prior work has reported cases in which transcriptomic changes do not align with proteomic readouts [11,46,47,48].”
From Fluorescence-Guided Spatial Mapping of p21-Expressing Senescent Cells in Aged Liver at Single-Cell Resolution (2026) · cites this paper as [47]
The section “mRNA and protein levels in response to perturbation” reports cases in yeast and bacteria where changes in mRNA and protein abundance do not align. The Conclusions also describe regulation beyond transcription. Neither passage addresses senescence specifically, so the senescence-specific framing is not supported by this source. Page numbers are unavailable in our copy. (LLM, conf=0.86)
Experimental — accuracy not yet measuredpQTL associations may capture regulatory mechanisms specific to proteins, explaining low correlations between mRNAs and their protein products.
“pQTL associations may capture regulatory mechanisms specific to proteins, explaining low correlations between mRNAs and their protein products (7).”
From Low overlap of plasma and CSF protein quantitative trait loci affects protein discovery for neurological disease (2026) · cites this paper as [7]
The section on steady-state mRNA and protein levels reports that mRNA abundance explains only part of the variation in protein abundance and discusses regulation downstream of transcription. However, the passages do not address pQTL associations or say that those associations capture the regulatory mechanisms; that specific attribution is unsupported. (LLM, conf=0.84)
Experimental — accuracy not yet measuredMessenger RNA and protein quantities often correlate poorly, emphasizing post-transcriptional control of protein synthesis and degradation.
“Several studies have reported that quantities of messenger RNA and proteins often correlate poorly, emphasizing the importance of post-transcriptional processes that control protein synthesis and degradation11.”
From Cell type- and brain region-resolved mouse brain proteome (2015) · cites this paper as [11]
mRNA abundance is not always a faithful proxy of protein expression across various organisms.
“Although transcriptomic profiling has provided insights into Tex cell biology, mRNA abundance is not always a faithful proxy of protein expression across various organisms18–22.”
From Proteotoxic stress response drives T cell exhaustion and immune evasion (2025) · cites this paper as [18]
The correlation between mRNA levels and their encoded protein levels is weak.
“Additionally, the correlation between levels of mRNA and their encoded proteins is weak8,9, while proteins are typically the molecule that most-directly act on disease.”
From Proteogenomic analysis of human cerebrospinal fluid identifies neurologically relevant regulation and implicates causal proteins for Alzheimer’s disease (2024) · cites this paper as [8]
mRNA and protein levels were modestly correlated, but over two thirds of these correlations were not statistically significant in the TCGA tumor set.
“mRNA and protein levels were modestly correlated, as earlier cell and animal model studies suggest36, but over two thirds of these correlations were not statistically significant in the TCGA tumor set.”
From Proteogenomic characterization of human colon and rectal cancer (2014) · cites this paper as [36]
Protein half-lives can vary many orders of magnitude and proteins have different translational rates.
“This is not surprising, since it known that protein half‐lives can vary many orders of magnitude and that proteins also have different translational rates (Schwanhäusser et al, 2011; Vogel & Marcotte, 2012).”
From Gene‐specific correlation of RNA and protein levels in human cells and tissues (2016) · cites this paper as Vogel & Marcotte, 2012
Comparisons of steady-state mRNA and protein abundances have revealed a large mismatch between mRNA and protein levels.
“comparing steady state mRNA and protein abundances has indicated a considerable discrepancy between mRNA and protein levels (5, 7–13).”
From Dynamic profiling of the protein life cycle in response to pathogens (2015) · cites this paper as [5]
How much each step of RNA and protein turnover contributes to shifts in protein expression is still unclear and disputed.
“the quantitative contribution of each process to changes in protein expression levels (Fig. 1A) remains largely unknown and much debated (5, 6).”
From Dynamic profiling of the protein life cycle in response to pathogens (2015) · cites this paper as [5]
Few studies have examined how mRNA, translation, and degradation changes shape differential protein expression during dynamic responses, and none has fully accounted for measurement error or disentangled interdependencies in the data.
“only a few studies (5, 12, 17–20) have attempted to shed light on how changes in each of these processes determine differential protein expression – either relative (ratios) or absolute (differences) – during dynamic responses and only one recent report (20) has attempted to quantitate each process. However, none of these has comprehensively accounted for experimental measurement errors, nor have”
From Dynamic profiling of the protein life cycle in response to pathogens (2015) · cites this paper as [5]
The consensus across studies holds that, in a wide array of organisms, transcriptional regulation explains 30-50% of the variation in steady-state protein levels, leaving half or more to be explained by post-transcriptional regulatory processes.
“The consensus across these studies holds that, in a wide array of organisms, transcriptional regulation explains 30–50% of the variation in steady-state protein levels, leaving half or more to be explained by post-transcriptional regulatory processes [3, 7, 9–16].”
Between-study correlations are modest, with median r = 0.62 for mRNA measurements and 0.57 for protein measurements.
“Although correlations of replicates within studies are quite high [9], with median r = 0.97 for mRNA and 0.93 for protein levels, between-study correlations are far more modest, r = 0.62 for mRNA measurements and 0.57 for protein measurements (Fig 1C).”
Most quantification methods are biased toward detection of more abundant mRNAs and proteins.
“However, most quantification methods are biased toward detection of more abundant mRNAs and proteins [9].”
Noise in measurements can cause many of the observations attributed to post-transcriptional regulation.
“However, as frequently noted [1, 7, 9, 10, 19–21], noise in measurements can cause many of the observations attributed to post-transcriptional regulation.”
Within-study replicate correlations are high, with median r = 0.97 for mRNA and 0.93 for protein levels.
“Although correlations of replicates within studies are quite high [9], with median r = 0.97 for mRNA and 0.93 for protein levels, between-study correlations are far more modest, r = 0.62 for mRNA measurements and 0.57 for protein measurements (Fig 1C).”
Data that are not missing at random due to biased detection have reduced variance or restricted range.
“Data which are not missing at random (NMAR) in this way have reduced variance or restricted range.”
The largest pair of datasets covers 4,367 genes and shows an mRNA-protein correlation of r = 0.618 (r^2 = 0.38).
“The largest pair of datasets covers 4,367 genes and shows an mRNA–protein correlation of r = 0.618 (r 2 = 0.38, 38% of protein-level variance explained by mRNA levels), close to consensus values [9].”
Dynamic-range amplification must involve post-transcriptional variation.
“As previously noted [9], this dynamic-range amplification must involve post-transcriptional variation.”
Integration of RNA-seq with proteomics is controversial because the two measurements show generally low correlation (~0.40).
“Integration of RNA-seq with proteomics is controversial because the two measurements show generally low correlation (~0.40 [158, 159]).”
From A survey of best practices for RNA-seq data analysis (2016) · cites this paper as [159]
Protein abundances are more direct determinants of cellular functions than transcript levels.
“Yet protein abundances are more direct determinants of cellular functions (4)”
From Impact of regulatory variation from RNA to protein (2015) · cites this paper as [4]
Transcript levels can explain only one- to two-thirds of protein levels.
“Indeed, transcript levels can only explain one- to two-thirds of protein levels, underlining the importance of post-transcriptional control (Liu et al., 2016, Vogel and Marcotte, 2012).”
From A Multi-layered Quantitative In Vivo Expression Atlas of the Podocyte Unravels Kidney Disease Candidate Genes (2018) · cites this paper as Vogel and Marcotte, 2012
Absolute abundances of mRNA and protein correlate only moderately.
“However, several studies from different fields found that absolute abundances of mRNA and protein abundances correlate only moderately.”
From A Multi-layered Quantitative In Vivo Expression Atlas of the Podocyte Unravels Kidney Disease Candidate Genes (2018) · cites this paper as Vogel and Marcotte, 2012
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Cites
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 · cited 1× · see citing works
“Both techniques enable the absolute quantification of proteins in the sample, providing that the resulting intensities or counts are suitably calibrated to molecular concentration”
Ong, 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 · see citing works
Ross, P. L., Huang, Y. N., Marchese, J. N., Williamson, B., Parker, K., Hattan, S., Khainovski, N., Pillai, S., Dey, S., Daniels, S., et al. (2004) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m400129-mcp200 · Cited by 4,401 · see citing works
Genome-Wide Analysis in Vivo of Translation with Nucleotide Resolution Using Ribosome Profiling
Ingolia, N. T., Ghaemmaghami, S., Newman, J. R. S., & Weissman, J. S. (2009) · Science · doi:10.1126/science.1168978 · Cited by 3,853 · see citing works
Global 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 · see citing works
The impact of microRNAs on protein output
Baek, D., Villén, J., Shin, C., Camargo, F. D., Gygi, S. P., & Bartel, D. P. (2008) · Nature · doi:10.1038/nature07242 · Cited by 3,592 · see citing works
Widespread changes in protein synthesis induced by microRNAs
Selbach, M., Schwanhäusser, B., Thierfelder, N., Fang, Z., Khanin, R., & Rajewsky, N. (2008) · Nature · doi:10.1038/nature07228 · Cited by 3,429 · cited 1× · see citing works
“Indeed, miRNAs have been found to fine-regulate protein expression levels, rather than to cause large expression change”
Ingolia, N. T., Lareau, L. F., & Weissman, J. S. (2011) · Cell · doi:10.1016/j.cell.2011.10.002 · Cited by 2,187 · see citing works
Taniguchi, Y., Choi, P. J., Li, G.-W., Chen, H., Babu, M., Hearn, J., Emili, A., & Xie, X. S. (2010) · Science · doi:10.1126/science.1188308 · Cited by 1,982 · cited 1× · see citing works
“Such strains provide a direct readout of protein abundance and have led to large-scale surveys of protein expression within single cell”
Correlation 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 · see citing works
Stochastic mRNA Synthesis in Mammalian Cells
Raj, A., Peskin, C. S., Tranchina, D., Vargas, D. Y., & Tyagi, S. (2006) · PLoS Biology · doi:10.1371/journal.pbio.0040309 · Cited by 1,737 · see citing works
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 · see citing works
Quantitative mass spectrometry in proteomics: a critical review
Bantscheff, M., Schirle, M., Sweetman, G. M. A., Rick, J. M., & Küster, B. (2007) · Analytical and Bioanalytical Chemistry · doi:10.1007/s00216-007-1486-6 · Cited by 1,659 · see citing works
Mayr, C., & Bartel, D. P. (2009) · Cell · doi:10.1016/j.cell.2009.06.016 · Cited by 1,613 · see citing works
Single-cell proteomic analysis of S. cerevisiae reveals the architecture of biological noise
Newman, J. R. S., Ghaemmaghami, S., Ihmels, J., Breslow, D. K., Noble, M., DeRisi, J. L., & Weissman, J. S. (2006) · Nature · doi:10.1038/nature04785 · Cited by 1,483 · see citing works
Real-Time Kinetics of Gene Activity in Individual Bacteria
Golding, I., Paulsson, J., Zawilski, S. M., & Cox, E. C. (2005) · Cell · doi:10.1016/j.cell.2005.09.031 · Cited by 1,468 · see citing works
Sandberg, R., Neilson, J. R., Sarma, A., Sharp, P. A., & Burge, C. B. (2008) · Science · doi:10.1126/science.1155390 · Cited by 1,349 · see citing works
The Orbitrap: a new mass spectrometer
Hu, Q., Noll, R. J., Li, H., Makarov, A., Hardman, M., & Cooks, R. G. (2005) · Journal of Mass Spectrometry · doi:10.1002/jms.856 · Cited by 1,338 · see citing works
Next-generation transcriptome assembly
Martin, J. A., & Wang, Z. (2011) · Nature Reviews Genetics · doi:10.1038/nrg3068 · Cited by 1,254 · see citing works
Global signatures of protein and mRNA expression levels
de Sousa Abreu, R., Penalva, L. O., Marcotte, E. M., & Vogel, C. (2009) · Molecular BioSystems · doi:10.1039/b908315d · Cited by 1,248 · see citing works
Self-citationLu, P., Vogel, C., Wang, R., Yao, X., & Marcotte, E. M. (2007) · Nature Biotechnology · doi:10.1038/nbt1270 · Cited by 1,139 · see citing works
Self-citationComprehensive mass-spectrometry-based proteome quantification of haploid versus diploid yeast
de Godoy, L. M. F., Olsen, J. V., Cox, J., Nielsen, M. L., Hubner, N. C., Fröhlich, F., Walther, T. C., & Mann, M. (2008) · Nature · doi:10.1038/nature07341 · Cited by 873 · see citing works
Quantification of protein half-lives in the budding yeast proteome
Belle, A., Tanay, A., Bitincka, L., Shamir, R., & O’Shea, E. K. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0605420103 · Cited by 678 · see citing works
MicroRNAs can generate thresholds in target gene expression
Mukherji, S., Ebert, M. S., Zheng, G. X. Y., Tsang, J. S., Sharp, P. A., & van Oudenaarden, A. (2011) · Nature Genetics · doi:10.1038/ng.905 · Cited by 628 · see citing works
Vogel, C., de Sousa Abreu, R., Ko, D., Le, S., Shapiro, B. A., Burns, S. C., Sandhu, D., Boutz, D. R., Marcotte, E. M., & Penalva, L. O. (2010) · Molecular Systems Biology · doi:10.1038/msb.2010.59 · Cited by 608 · see citing works
Self-citationSharova, L. V., Sharov, A. A., Nedorezov, T., Piao, Y., Shaik, N., & Ko, M. S. H. (2009) · DNA Research · doi:10.1093/dnares/dsn030 · Cited by 591 · see citing works
Global Protein Stability Profiling in Mammalian Cells
Yen, H.-C. S., Xu, Q., Chou, D. M., Zhao, Z., & Elledge, S. J. (2008) · Science · doi:10.1126/science.1160489 · Cited by 482 · see citing works
Central dogma at the single-molecule level in living cells
Li, G., & Xie, X. S. (2011) · Nature · doi:10.1038/nature10315 · Cited by 442 · see citing works
Proteomics: a pragmatic perspective
Mallick, P., & Küster, B. (2010) · Nature Biotechnology · doi:10.1038/nbt.1658 · Cited by 428 · see citing works
Proteome-wide cellular protein concentrations of the human pathogen Leptospira interrogans
Malmström, J., Beck, M., Schmidt, A., Lange, V., Deutsch, E. W., & Aebersold, R. (2009) · Nature · doi:10.1038/nature08184 · Cited by 421 · see citing works
Noise Minimization in Eukaryotic Gene Expression
Fraser, H. B., Hirsh, A. E., Giaever, G. N., Kumm, J., & Eisen, M. B. (2004) · PLoS Biology · doi:10.1371/journal.pbio.0020137 · Cited by 419 · see citing works
Defining the transcriptome and proteome in three functionally different human cell lines
Lundberg, E., Fagerberg, L., Klevebring, D., Matic, I., Geiger, T., Cox, J., Älgenäs, C., Lundeberg, J., Mann, M., & Uhlen, M. (2010) · Molecular Systems Biology · doi:10.1038/msb.2010.106 · Cited by 373 · see citing works
Selinger, D. W., Saxena, R. M., Cheung, K. J., Church, G. M., & Rosenow, C. (2003) · Genome Research · doi:10.1101/gr.912603 · Cited by 361 · see citing works
Proteome Half-Life Dynamics in Living Human Cells
Eden, E., Geva‐Zatorsky, N., Issaeva, I., Cohen, A. A., Dekel, E., Danon, T., Cohen, L., Mayo, A., & Alon, U. S. (2011) · Science · doi:10.1126/science.1199784 · Cited by 320 · see citing works
Utilizing Human Blood Plasma for Proteomic Biomarker Discovery
Jacobs, J., Adkins, J., Qian, W., Liu, T., Shen, Y., Camp, D., & Smith, R. D. (2005) · Journal of Proteome Research · doi:10.1021/pr0500657 · Cited by 315 · see citing works
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 · see citing works
A dynamic model of proteome changes reveals new roles for transcript alteration in yeast
Lee, M. V., Topper, S. E., Hubler, S. L., Hose, J., Wenger, C. D., Coon, J. J., & Gasch, A. P. (2011) · Molecular Systems Biology · doi:10.1038/msb.2011.48 · Cited by 290 · see citing works
RNA sequencing reveals two major classes of gene expression levels in metazoan cells
Hebenstreit, D., Fang, M., Gu, M., Charoensawan, V., van Oudenaarden, A., & Teichmann, S. A. (2011) · Molecular Systems Biology · doi:10.1038/msb.2011.28 · Cited by 289 · see citing works
Comparative Functional Analysis of the Caenorhabditis elegans and Drosophila melanogaster Proteomes
Schrimpf, S. P., Weiss, M., Reiter, L., Ahrens, C. H., Jovanovic, M., Malmström, J., Brunner, E., Mohanty, S., Lercher, M. J., Hunziker, P. E., et al. (2009) · PLoS Biology · doi:10.1371/journal.pbio.1000048 · Cited by 229 · see citing works
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 · see citing works
Quantifying E. coli Proteome and Transcriptome with Single-molecule Sensitivity in Single Cells
Taniguchi, Y. (2011) · Seibutsu Butsuri · doi:10.2142/biophys.51.136 · Cited by 157 · see citing works
Protein abundances are more conserved than mRNA abundances across diverse taxa
Laurent, J. M., Vogel, C., Kwon, T., Craig, S. A., Boutz, D. R., Huse, H. K., Nozue, K., Walia, H., Whiteley, M., Ronald, P. C., et al. (2010) · PROTEOMICS · doi:10.1002/pmic.201000327 · Cited by 156 · see citing works
Self-citationProtein Expression Regulation under Oxidative Stress
Vogel, C., Silva, G. M., & Marcotte, E. M. (2011) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m111.009217 · Cited by 144 · see citing works
Self-citationUncovering Genes with Divergent mRNA-Protein Dynamics in Streptomyces coelicolor
Jayapal, K. P., Philp, R. J., Kok, Y. J., Yap, M. G. S., Sherman, D. H., Griffin, T. J., & Hu, W. (2008) · PLoS ONE · doi:10.1371/journal.pone.0002097 · Cited by 113 · see citing works
Transcription of functionally related constitutive genes is not coordinated
Gandhi, S. J., Zenklusen, D., Lionnet, T., & Singer, R. H. (2010) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1934 · Cited by 109 · see citing works
Regulatory mechanisms and networks couple the different phases of gene expression
Dahan, O., Gingold, H., & Pilpel, Y. (2011) · Trends in Genetics · doi:10.1016/j.tig.2011.05.008 · Cited by 88 · see citing works
Integrating shotgun proteomics and mRNA expression data to improve protein identification
Ramakrishnan, S. R., Vogel, C., Prince, J. T., Wang, R., Li, Z., Penalva, L. O. F., Myers, M., Marcotte, E. M., & Miranker, D. P. (2009) · Bioinformatics · doi:10.1093/bioinformatics/btp168 · Cited by 79 · see citing works
Self-citationWeiss, M., Schrimpf, S., Hengartner, M. O., Lercher, M. J., & von Mering, C. (2010) · PROTEOMICS · doi:10.1002/pmic.200900414 · Cited by 64 · see citing works
No Splicing, No Dicing: Non-proteolytic Roles of the Ubiquitin-Proteasome System in Transcription*
Kodadek, T. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.r109.077883 · Cited by 61 · see citing works
Noise in Biological Systems: Pros, Cons, and Mechanisms of Control
Pilpel, Y. (2011) · Methods in molecular biology · doi:10.1007/978-1-61779-173-4_23 · Cited by 47 · see citing works
Transcriptional regulation is only half the story
Plotkin, J. B. (2010) · Molecular Systems Biology · doi:10.1038/msb.2010.63 · Cited by 46 · see citing works
Cells of the yeast Saccharomyces cerevisiae are transformable by DNA under non‐artificial conditions
Nevoigt, E., Faßbender, A., & Ståhl, U. (2000) · Yeast · doi:10.1002/1097-0061(20000915)16:12 · Cited by 45 · see citing works
Transcriptional Regulation by the Proteasome as a Mechanism for Cellular Protein
Auld, K. L., & Silver, P. (2006) · Cell Cycle · doi:10.4161/cc.5.14.2979 · Cited by 42 · see citing works
Smythe, W. R., & Mattauch, J. (1932) · Physical Review · doi:10.1103/physrev.40.429 · Cited by 38 · see citing works
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Proteogenomic characterization of human colon and rectal cancer
CPTAC, T. N., Zhang, B., Wang, J., Wang, X., Zhu, J., Liu, Q., Shi, Z., Chambers, M. C., Zimmerman, L. J., Shaddox, K. F., et al. (2014) · Nature · doi:10.1038/nature13438 · Cited by 1,462 · see citing works
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Integrated Proteogenomic Characterization of Human High-Grade Serous Ovarian Cancer
Zhang, H., Liu, T., Zhang, Z., Payne, S. H., Zhang, B., McDermott, J. E., Zhou, J.-Y., Petyuk, V. A., Chen, L., Ray, D., et al. (2016) · Cell · doi:10.1016/j.cell.2016.05.069 · Cited by 1,029 · see citing works
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Liu, Y., Yang, M., Deng, Y., Su, G., Enninful, A., Guo, C. C., Tebaldi, T., Zhang, D., Kim, D., Bai, Z., et al. (2020) · Cell · doi:10.1016/j.cell.2020.10.026 · Cited by 966 · see citing works
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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 871 · see citing works
Targeting the translation machinery in cancer
Bhat, M., Robichaud, N., Hulea, L., Sonenberg, N., Pelletier, J., & Topisirovic, I. (2015) · Nature Reviews Drug Discovery · doi:10.1038/nrd4505 · Cited by 799 · see citing works
Marguerat, S., Schmidt, A., Codlin, S., Chen, W., Aebersold, R., & Bähler, J. (2012) · Cell · doi:10.1016/j.cell.2012.09.019 · Cited by 571 · see citing works
Gene‐specific correlation of RNA and protein levels in human cells and tissues
Edfors, F., Danielsson, F., Hallström, B. M., Käll, L., Lundberg, E., Pontén, F., Forsström, B., & Uhlén, M. (2016) · Molecular Systems Biology · doi:10.15252/msb.20167144 · Cited by 493 · see citing works
A Quantitative Proteome Map of the Human Body
Jiang, L., Wang, M., Lin, S., Jian, R., Li, X., Chan, J., Dong, G., Fang, H., Robinson, A. E., Aguet, F., et al. (2020) · Cell · doi:10.1016/j.cell.2020.08.036 · Cited by 458 · see citing works
Transcriptional and Translational Differences of Microglia from Male and Female Brains
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Jovanovic, M., Rooney, M. S., Mertins, P., Przybylski, D., Chevrier, N., Satija, R., Rodriguez, E. H., Fields, A. P., Schwartz, S., Raychowdhury, R., et al. (2015) · Science · doi:10.1126/science.1259038 · Cited by 460 · see citing works
Defining the consequences of genetic variation on a proteome-wide scale
Chick, J. M., Munger, S. C., Simecek, P., Huttlin, E. L., Choi, K., Gatti, D. M., Raghupathy, N., Svenson, K. L., Churchill, G. A., & Gygi, S. P. (2016) · Nature · doi:10.1038/nature18270 · Cited by 361 · see citing works
A multidimensional systems biology analysis of cellular senescence in aging and disease
Avelar, R. A., Ortega, J. G., Tacutu, R., Tyler, E. J., Bennett, D., Binetti, P., Budovsky, A., Chatsirisupachai, K., Johnson, E., Murray, A., et al. (2020) · Genome Biology · doi:10.1186/s13059-020-01990-9 · Cited by 399 · see citing works
New frontiers in translational control of the cancer genome
Truitt, M. L., & Ruggero, D. (2016) · Nature Reviews Cancer · doi:10.1038/nrc.2016.27 · Cited by 378 · see citing works
Chaperone-mediated autophagy prevents collapse of the neuronal metastable proteome
Bourdenx, M., Martín-Segura, A., Scrivo, A., Rodriguez-Navarro, J. A., Kaushik, S., Tasset, I., Diaz, A., Storm, N. J., Xin, Q., Juste, Y. R., et al. (2021) · Cell · doi:10.1016/j.cell.2021.03.048 · Cited by 337 · see citing works
Li, J. J., Bickel, P. J., & Biggin, M. D. (2014) · PeerJ · doi:10.7717/peerj.270 · Cited by 279 · see citing works
The glutamate hypothesis of schizophrenia: evidence from human brain tissue studies
Hu, W., MacDonald, M. L., Elswick, D. E., & Sweet, R. A. (2015) · Annals of the New York Academy of Sciences · doi:10.1111/nyas.12547 · Cited by 286 · see citing works
Disentangling neural cell diversity using single-cell transcriptomics
Poulin, J.-F., Tasic, B., Hjerling-Leffler, J., Trimarchi, J. M., & Awatramani, R. (2016) · Nature Neuroscience · doi:10.1038/nn.4366 · Cited by 293 · see citing works
Medulloblastomics revisited: biological and clinical insights from thousands of patients
Hovestadt, V., Ayrault, O., Swartling, F. J., Robinson, G. W., Pfister, S. M., & Northcott, P. A. (2020) · Nature Reviews Cancer · doi:10.1038/s41568-019-0223-8 · Cited by 271 · see citing works
Transcriptome analysis of human tissues and cell lines reveals one dominant transcript per gene
Gonzàlez-Porta, M., Frankish, A., Rung, J., Harrow, J., & Brazma, A. (2013) · Genome Biology · doi:10.1186/gb-2013-14-7-r70 · Cited by 266 · see citing works
Primate Transcript and Protein Expression Levels Evolve Under Compensatory Selection Pressures
Khan, Z., Ford, M. J., Cusanovich, D. A., Mitrano, A., Pritchard, J. K., & Gilad, Y. (2013) · Science · doi:10.1126/science.1242379 · Cited by 240 · see citing works
Schlotter, F., Halu, A., Goto, S., Blaser, M. C., Body, S. C., Lee, L. H., Higashi, H., DeLaughter, D. M., Hutcheson, J. D., Vyas, P., et al. (2018) · Circulation · doi:10.1161/circulationaha.117.032291 · Cited by 256 · see citing works
Tunable and reversible drug control of protein production via a self-excising degron
Chung, H. K., Jacobs, C. L., Huo, Y., Yang, J., Krumm, S. A., Plemper, R. K., Tsien, R. Y., & Lin, M. Z. (2015) · Nature Chemical Biology · doi:10.1038/nchembio.1869 · Cited by 233 · see citing works
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 · see citing works
Self-citationMicroglia affect α-synuclein cell-to-cell transfer in a mouse model of Parkinson’s disease
George, S., Rey, N. L., Tyson, T., Esquibel, C., Meyerdirk, L., Schulz, E., Pierce, S., Burmeister, A. R., Madaj, Z., Steiner, J. A., et al. (2019) · Molecular Neurodegeneration · doi:10.1186/s13024-019-0335-3 · Cited by 229 · see citing works
Impact of Alternative Splicing on the Human Proteome
Liu, Y., Gonzàlez-Porta, M., Santos, S., Brazma, A., Marioni, J. C., Aebersold, R., Venkitaraman, A. R., & Wickramasinghe, V. O. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.07.025 · Cited by 190 · see citing works
Csárdi, G., Franks, A., Choi, D. S., Airoldi, E. M., & Drummond, D. A. (2015) · PLOS Genetics · doi:10.1371/journal.pgen.1005206 · Cited by 181 · see citing works
Liu, A., Trairatphisan, P., Gjerga, E., Didangelos, A., Barratt, J., & Saez-Rodriguez, J. (2019) · npj Systems Biology and Applications · doi:10.1038/s41540-019-0118-z · Cited by 151 · see citing works
The ribosome-engaged landscape of alternative splicing
Weatheritt, R. J., Sterne-Weiler, T., & Blencowe, B. J. (2016) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.3317 · Cited by 162 · see citing works
Martin, E., Boucher, C., Fontaine, B., & Delarasse, C. (2017) · Aging Cell · doi:10.1111/acel.12522 · Cited by 156 · see citing works
Marcellin, E., Behrendorff, J. B., Nagaraju, S., DeTissera, S., Segovia, S., Palfreyman, R. W., Daniell, J., Licona-Cassani, C., Quek, L.-E., Speight, R., et al. (2016) · Green Chemistry · doi:10.1039/c5gc02708j · Cited by 159 · see citing works
Gunn, B. G., Cunningham, L., Cooper, M. A., Corteen, N. L., Seifi, M., Swinny, J. D., Lambert, J. J., & Belelli, D. (2013) · The Journal of Neuroscience · doi:10.1523/jneurosci.1337-13.2013 · Cited by 151 · see citing works
Linking microbiota to human diseases: a systems biology perspective
Wu, H., Tremaroli, V., & Bäckhed, F. (2015) · Trends in Endocrinology & Metabolism · doi:10.1016/j.tem.2015.09.011 · Cited by 150 · see citing works
Circulating Proteomic Signatures of Chronological Age
Menni, C., Kiddle, S. J., Mangino, M., Viñuela, A., Psatha, M., Steves, C., Sattlecker, M., Buil, A., Newhouse, S., Nelson, S., et al. (2015) · The Journals of Gerontology: Series A · doi:10.1093/gerona/glu121 · Cited by 144 · see citing works
McGlory, C., Devries, M. C., & Phillips, S. M. (2017) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00613.2016 · Cited by 135 · see citing works
Cuadrado, E., van den Biggelaar, M., de Kivit, S., Chen, Y.-Y., Slot, M., Doubal, I., Meijer, A., van Lier, R. A. W., Borst, J., & Amsen, D. (2018) · Immunity · doi:10.1016/j.immuni.2018.04.008 · Cited by 132 · see citing works
Borsini, A., Cattaneo, A., Malpighi, C., Thuret, S., Harrison, N. A., MRC ImmunoPsychiatry Consortium, Zunszain, P. A., & Pariante, C. M. (2018) · International Journal of Neuropsychopharmacology · doi:10.1093/ijnp/pyx083 · Cited by 113 · see citing works
Nielsen, D. S. G., Jensen, B. B., Theil, P. K., Nielsen, T. S., Knudsen, K. E. B., & Purup, S. (2018) · Journal of Functional Foods · doi:10.1016/j.jff.2017.10.023 · Cited by 115 · see citing works
Rinschen, M. M., Gödel, M., Grahammer, F., Zschiedrich, S., Helmstädter, M., Kretz, O., Zarei, M., Braun, D. A., Dittrich, S., Pahmeyer, C., et al. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.04.059 · Cited by 105 · see citing works
Western, D., Timsina, J., Wang, L., Wang, C., Yang, C., Phillips, B., Wang, Y., Liu, M., Ali, M., Beric, A., et al. (2024) · Nature Genetics · doi:10.1038/s41588-024-01972-8 · Cited by 111 · see citing works
Gillespie, M. A., Palii, C. G., Sanchez-Taltavull, D., Shannon, P., Longabaugh, W. J. R., Downes, D. J., Sivaraman, K., Espinoza, H. M., Hughes, J. R., Price, N. D., et al. (2020) · Molecular Cell · doi:10.1016/j.molcel.2020.03.031 · Cited by 110 · see citing works
Trzupek, D., Dunstan, M., Cutler, A. J., Lee, M., Godfrey, L., Jarvis, L., Rainbow, D. B., Aschenbrenner, D., Jones, J. L., Uhlig, H. H., et al. (2020) · Genome Medicine · doi:10.1186/s13073-020-00756-z · Cited by 105 · see citing works
Roussos, P., Katsel, P., Fam, P., Tan, W., Purohit, D. P., & Haroutunian, V. (2015) · Alzheimer's & Dementia · doi:10.1016/j.jalz.2014.10.013 · Cited by 103 · see citing works
Orosco, L. A., Ross, A. P., Cates, S. L., Scott, S. E., Wu, D., Sohn, J., Pleasure, D., Pleasure, S. J., Adamopoulos, I. E., & Zarbalis, K. S. (2014) · Nature Communications · doi:10.1038/ncomms5692 · Cited by 90 · see citing works
Sex differences in brain protein expression and disease
Wingo, A. P., Liu, Y., Gerasimov, E. S., Vattathil, S. M., Liu, J., Cutler, D. J., Epstein, M. P., Blokland, G. A. M., Thambisetty, M., Troncoso, J. C., et al. (2023) · Nature Medicine · doi:10.1038/s41591-023-02509-y · Cited by 94 · see citing works
Pacheco, N. L., Heaven, M. R., Holt, L. M., Crossman, D. K., Boggio, K. J., Shaffer, S. A., Flint, D. L., & Olsen, M. L. (2017) · Molecular Autism · doi:10.1186/s13229-017-0174-4 · Cited by 90 · see citing works
Into the multiverse: advances in single-cell multiomic profiling
Ogbeide, S., Giannese, F., Mincarelli, L., & Macaulay, I. C. (2022) · Trends in Genetics · doi:10.1016/j.tig.2022.03.015 · Cited by 82 · see citing works
Bayesian sparse regression analysis documents the diversity of spinal inhibitory interneurons
Gabitto, M. I., Pakman, A., Bikoff, J. B., Abbott, L. F., Jessell, T. M., & Paninski, L. (2016) · Cell · doi:10.1016/j.cell.2016.01.026 · Cited by 73 · see citing works
Aviner, R., Geiger, T., & Elroy-Stein, O. (2014) · Nature Protocols · doi:10.1038/nprot.2014.051 · Cited by 76 · see citing works
Rayaprolu, S., Gao, T., Xiao, H., Ramesha, S., Weinstock, L. D., Shah, J., Duong, D. M., Dammer, E. B., Webster, J. A., Lah, J. J., et al. (2019) · doi:10.1101/802694 · Cited by 71 · see citing works
Alanazi, B., Munje, C. R., Rastogi, N., Williamson, A. J. K., Taylor, S., Hole, P. S., Hodges, M., Doyle, M., Baker, S., Gilkes, A. F., et al. (2020) · Leukemia · doi:10.1038/s41375-019-0596-4 · Cited by 64 · see citing works
Species comparison of liver proteomes reveals links to naked mole-rat longevity and human aging
Heinze, I., Bens, M., Calzia, E., Holtze, S., Dakhovnik, O., Sahm, A., Kirkpatrick, J. M., Szafranski, K., Romanov, N., Sama, S. N., et al. (2018) · BMC Biology · doi:10.1186/s12915-018-0547-y · Cited by 65 · see citing works
Proteotoxic stress response drives T cell exhaustion and immune evasion
Wang, Y., Ma, A., Song, N.-J., Shannon, A. E., Amankwah, Y. S., Chen, X., Wu, W., Wang, Z., Saadey, A. A., Yousif, A., et al. (2025) · Nature · doi:10.1038/s41586-025-09539-1 · Cited by 68 · see citing works
Nicolet, B. P., & Wolkers, M. C. (2022) · PLOS ONE · doi:10.1371/journal.pone.0276294 · Cited by 62 · see citing works
Doolittle, M. L., Saul, D., Kaur, J., Rowsey, J. L., Vos, S. J., Pavelko, K. D., Farr, J. N., Monroe, D. G., & Khosla, S. (2023) · Nature Communications · doi:10.1038/s41467-023-40393-9 · Cited by 57 · see citing works
Vardas, K., Ilia, S., Sertedaki, A., Charmandari, E., Briassouli, E., Goukos, D., Apostolou, K., Psarra, K., Botoula, E., Tsagarakis, S., et al. (2017) · Intensive Care Medicine Experimental · doi:10.1186/s40635-017-0123-8 · Cited by 58 · see citing works
Doolittle, M. L., Saul, D., Kaur, J., Rowsey, J. L., Vos, S. J., Pavelko, K. D., Farr, J. N., Monroe, D. G., & Khosla, S. (2023) · doi:10.1101/2023.01.12.523760 · Cited by 57 · see citing works
Expression and localization of GPR91 and GPR99 in murine organs
Diehl, J., Gries, B., Pfeil, U., Goldenberg, A., Mermer, P., Kummer, W., & Paddenberg, R. (2016) · Cell and Tissue Research · doi:10.1007/s00441-015-2318-1 · Cited by 50 · see citing works
Lephart, E. D. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18061193 · Cited by 50 · see citing works
Marthandan, S., Priebe, S., Baumgart, M., Groth, M., Cellerino, A., Guthke, R., Hemmerich, P., & Diekmann, S. (2015) · BioMed Research International · doi:10.1155/2015/731938 · Cited by 47 · see citing works
Januszyk, M., Wong, V. W., Bhatt, K. A., Vial, I. N., Paterno, J., Longaker, M. T., & Gurtner, G. C. (2014) · Organogenesis · doi:10.4161/org.28818 · Cited by 43 · see citing works
Proteogenomics: emergence and promise
Faulkner, S., Dun, M. D., & Hondermarck, H. (2015) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-015-1837-y · Cited by 36 · see citing works
Wang, G., Zhao, J., Lin, Y., Liu, T., Zhao, Y., & Zhao, H. (2025) · Nature Communications · doi:10.1038/s41467-025-60333-z · Cited by 29 · see citing works
Analysis of Differential Expression of Synaptic Vesicle Protein 2A in the Adult Rat Brain
Mendoza-Torreblanca, J. G., García-Cruz, M. E., Sánchez-Cruz, I., Gomez-Gonzalez, B., Juárez-Méndez, S., & Gómez-Lira, G. (2019) · Neuroscience · doi:10.1016/j.neuroscience.2019.09.004 · Cited by 18 · see citing works
Lee, J., Wang, Z., Messi, M. L., Milligan, C., Furdui, C. M., & Delbono, O. (2024) · Acta Physiologica · doi:10.1111/apha.14123 · Cited by 15 · see citing works
Vattathil, S. M., Gerasimov, E. S., Canon, S. M., Lori, A., Tan, S. S. M., Kim, P. J., Liu, Y., Lai, E. C., Bennett, D. A., Wingo, T. S., et al. (2024) · Nature Aging · doi:10.1038/s43587-024-00778-x · Cited by 14 · see citing works
Pinto, A. P., Muñoz, V. R., da Rocha, A. L., Rovina, R. L., Ferrari, G. D., Alberici, L. C., Simabuco, F. M., Teixeira, G. R., Pauli, J. R., de Moura, L. P., et al. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.953272 · Cited by 14 · see citing works
Expression of estrogen receptor α in the mouse cerebral cortex
Dietrich, A. K., Humphreys, G. I., & Nardulli, A. M. (2015) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2015.02.013 · Cited by 10 · see citing works
Ribosomal flavours: An acquired taste for specific mRNAs?
Bates, C., Hubbard, S. J., & Ashe, M. P. (2018) · Biochemical Society Transactions · doi:10.1042/bst20180160 · Cited by 8 · see citing works
Forés-Martos, J., Forte, A., García-Martínez, J., & Pérez-Ortín, J. E. (2021) · Cells · doi:10.3390/cells10020334 · Cited by 8 · see citing works
Lephart, E. D. (2018) · Journal of Cosmetic Dermatology · doi:10.1111/jocd.12362 · Cited by 6 · see citing works
Single-molecule imaging of transcription dynamics, RNA localization and fate in human T cells
Lattanzio, M. V., Šoštarić, N., Kanagasabesan, N., Popović, B., Bradarić, A., Wardak, L., Guislain, A., Savakis, P., Tutucci, E., & Wolkers, M. C. (2025) · The EMBO Journal · doi:10.1038/s44318-025-00592-0 · Cited by 3 · see citing works
Western, D., Yang, C., Timsina, J., Liu, M., Wang, C., Campbell, M. C., Kotzbauer, P., Perlmutter, J. S., Schindler, S. E., Morris, J. C., et al. (2026) · Science Translational Medicine · doi:10.1126/scitranslmed.adz2016 · Cited by 1 · see citing works
Hsu, J.-E., Wang, B., Hwang, Y., Cheng, W., Zhao, Q., Si, Y., Xu, M., Kang, H.-M., & Lee, J. H. (2026) · Biomolecules · doi:10.3390/biom16040579
Zanoaga, M.-D., Cavinato, T., Latrille, T., Liska, O., Schoeler, T., Papp, B., & Kutalik, Z. (2026) · doi:10.64898/2026.10.16.759432
- Authors
- Vogel, C., & Marcotte, E. M.
- Affiliations
- New York University (US)
- The University of Texas at Austin (US)
- Corresponding author
- Vogel, Christine
- Marcotte, Edward M.
- Venue
- Nature Reviews Genetics
- Published
- 2012-03-13
- Volume
- 13
- Issue
- 4
- Pages
- 227-232
- ISSN
- 1471-0056 (ISSN-L)
- 1471-0064
- PMC
- PMC3654667
- OpenAlex
- W1973268693
- Semantic Scholar
- 119839d2861f7293f7a982a421a577799a9dcac6
- Cited by
- 4,195
- References
- 54
- Citations by year
- 2026: 409 · 2025: 312 · 2024: 278 · 2023: 258 · 2022: 338 · 2021: 343 · 2020: 382 · 2019: 303 · 2018: 302 · 2017: 301 · 2016: 293 · 2015: 271 · 2014: 254 · 2013: 119 · 2012: 26
- FWCI
- 20.15
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature Reviews Genetics (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- Welch Foundation
- National Institute of General Medical Sciences (DP1GM106408, R01GM076536)
- Topics
- Physical Sciences › Chemistry › Spectroscopy › Advanced Proteomics Techniques and Applications
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Research and Splicing
- Keywords
- protein abundance, mRNA levels, post-transcriptional regulation, translational regulation, protein degradation, gene expression regulation, mRNA-protein correlation, single-cell transcriptomics
- MeSH terms
- Proteins, RNA, Messenger, Proteome, Gene Expression Profiling, Proteomics
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