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A draft map of the human proteome
Open accessAbstract
The availability of human genome sequence has transformed biomedical research over the past decade. However, an equivalent map for the human proteome with direct measurements of proteins and peptides does not exist yet. Here we present a draft map of the human proteome using high-resolution Fourier-transform mass spectrometry. In-depth proteomic profiling of 30 histologically normal human samples, including 17 adult tissues, 7 fetal tissues and 6 purified primary haematopoietic cells, resulted in identification of proteins encoded by 17,294 genes accounting for approximately 84% of the total annotated protein-coding genes in humans. A unique and comprehensive strategy for proteogenomic analysis enabled us to discover a number of novel protein-coding regions, which includes translated pseudogenes, non-coding RNAs and upstream open reading frames. This large human proteome catalogue (available as an interactive web-based resource at http://www.humanproteomemap.org) will complement available human genome and transcriptome data to accelerate biomedical research in health and disease.
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In the citing paper
“this situation has changed with the development of more sensitive and powerful high-resolution mass spectrometry (MS) technologies that allow in-depth coverage of nearly complete proteomes of mammalian cells 13–17.”
From Cell type- and brain region-resolved mouse brain proteome (2015) · cites this paper as [17]
Experimental — accuracy not yet measuredThe cited source says what the claim attributes to it.
In the citing paper
“Because only 9 of the 953 genes lack confirmed expression in any of the 34 neuro-related tissues tracked by IDG KMC (for example, GTEx40,41, HPA42 and HPM43), these data suggest that the remaining 80% of this set have the potential to be associated with human neurobehavioural phenotypes, paving the way for new research avenues in this direction (see Supplementary Table S8).”
From Unexplored therapeutic opportunities in the human genome (2018) · cites this paper as [43]
The cited source says what the claim attributes to it.
In the citing paper
“Recent efforts to describe the composition and spatial distribution of proteins have advanced in draft maps of the human proteome 40,41 and the Human Protein Atlas 2 , respectively.”
From How many human proteoforms are there? (2018) · cites this paper as [40]
In the citing paper
“Since protein expression levels span around 4 to 5 orders of magnitude (13, 16, 37, 38)”
From Dynamic profiling of the protein life cycle in response to pathogens (2015) · cites this paper as [37]
In the citing paper
“Recently, the protein products of 17,294 genes were identified and mapped in the draft of human proteome using 30 human samples of tissues and cells (Kim et al., 2014).”
From Integrative Analysis of Multi-omics Data for Discovery and Functional Studies of Complex Human Diseases (2016) · cites this paper as Kim et al., 2014
In the citing paper
“Although, highly abundant “housekeeping” proteins from 2,350 genes constitute approximately 75% of total protein mass, low-abundance proteins constitute the majority of the protein species in human (Kim et al., 2014).”
From Integrative Analysis of Multi-omics Data for Discovery and Functional Studies of Complex Human Diseases (2016) · cites this paper as Kim et al., 2014
In the citing paper
“This draft proteome demonstrated the feasibility of building a complete human proteome encompassing over 200 cell types and all body fluids.”
From Integrative Analysis of Multi-omics Data for Discovery and Functional Studies of Complex Human Diseases (2016) · cites this paper as Kim et al., 2014
In the citing paper
“Despite this limitation, it is now possible to reliably obtain quantitative observations for tens of thousands of peptides derived from up to 10,000 proteins per sample22, and very recently important steps have been taken toward profiling the entire human proteome23,24.”
From Decoding neuroproteomics: integrating the genome, translatome and functional anatomy (2014) · cites this paper as [24]
In the citing paper
“As a result, proteins can be resolved and quantified relatively and absolutely, culminating in a near-comprehensive mass spectrometry-based expression map of the human proteome (Kim et al., 2014, Wilhelm et al., 2014).”
From A Multi-layered Quantitative In Vivo Expression Atlas of the Podocyte Unravels Kidney Disease Candidate Genes (2018) · cites this paper as Kim et al., 2014
In the citing paper
“In addition, cell line expression data was added from HPA and the Human Proteome Map (15) and expression data was collected for orthologous genes from 17 different species.”
From TCRD and pharos 2021: mining the human proteome for disease biology (2021) · cites this paper as [15]
In the citing paper
“The E3 ligase expression pattern in many E3 ligases can be validated by the immunohistochemistry (IHC) data from the Human Protein Atlas (THPA) (https://www.proteinatlas.org/) or the human tissue proteomic data [95].”
From PROteolysis TArgeting Chimeras (PROTACs) as emerging anticancer therapeutics (2020) · cites this paper as [95]
In the citing paper
“Prior initiatives such as those describing first drafts of the human proteome in 2014 ( 33 , 34 ) and ongoing work under the aegis of the Human Protein Atlas and the Human Proteome Project ( 35 ) have accomplished a great deal over the past several years,”
From The Human Proteoform Project: Defining the human proteome (2021) · cites this paper as [33]
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Citations
Cites
An integrated encyclopedia of DNA elements in the human genome
The ENCODE Project Consortium (2012) · Nature · doi:10.1038/nature11247 · Cited by 18,072
Perkins, D. N., Pappin, D., Creasy, D. M., & Cottrell, J. S. (1999) · Electrophoresis · doi:10.1002/(sici)1522-2683(19991201)20:18 · Cited by 8,264
An integrated map of genetic variation from 1,092 human genomes
The 1000 Genomes Project Consortium (2012) · Nature · doi:10.1038/nature11632 · Cited by 7,711
Mass spectrometry-based proteomics
Aebersold, R., & Mann, M. (2003) · Nature · doi:10.1038/nature01511 · Cited by 6,955
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
In-gel digestion for mass spectrometric characterization of proteins and proteomes
Shevchenko, A., Tomas, H., Havli, J., Olsen, J. V., & Mann, M. (2006) · Nature Protocols · doi:10.1038/nprot.2006.468 · Cited by 4,947
TANDEM: matching proteins with tandem mass spectra
Craig, R., & Beavis, R. C. (2004) · Bioinformatics · doi:10.1093/bioinformatics/bth092 · Cited by 2,546
Towards a knowledge-based Human Protein Atlas
Uhlen, M., Oksvold, P., Fagerberg, L., Lundberg, E., Jonasson, K., Forsberg, M., Zwahlen, M., Kampf, C., Wester, K., Hober, S., et al. (2010) · Nature Biotechnology · doi:10.1038/nbt1210-1248 · Cited by 2,440
Semi-supervised learning for peptide identification from shotgun proteomics datasets
Käll, L., Canterbury, J. D., Weston, J., Noble, W. S., & MacCoss, M. J. (2007) · Nature Methods · doi:10.1038/nmeth1113 · Cited by 2,424
The Proteomics Identifications (PRIDE) database and associated tools: status in 2013
Vizcaíno, J. A., Côté, R. G., Csordas, A., Dianes, J. A., Fabregat, A., Foster, J. M., Griss, J., Alpi, E., Birim, M., Contell, J., et al. (2012) · Nucleic Acids Research · doi:10.1093/nar/gks1262 · Cited by 1,918
Flagged first, then by citations
Cited by
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Items 501–600 of 1,002
PGTools: A Software Suite for Proteogenomic Data Analysis and Visualization
Nagaraj, S. H., Waddell, N., Madugundu, A. K., Wood, S., Jones, A., Mandyam, R. A., Nones, K., Pearson, J. V., & Grimmond, S. M. (2015) · Journal of Proteome Research · doi:10.1021/acs.jproteome.5b00029 · Cited by 55
Self-citationUBB pseudogene 4 encodes functional ubiquitin variants
Dubois, M., Meller, A., Samandi, S., Brunelle, M., Frion, J., Brunet, M. A., Toupin, A., Beaudoin, M. C., Jacques, J., Lévesque, D., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-15090-6 · Cited by 58
Aballo, T. J., Roberts, D. S., Melby, J. A., Buck, K. M., Brown, K. A., & Ge, Y. (2021) · Journal of Proteome Research · doi:10.1021/acs.jproteome.1c00446 · Cited by 54
π-HuB: the proteomic navigator of the human body
He, F., Aebersold, R. H., Baker, M. S., Bian, X., Bo, X., Chan, D. W., Chang, C., Chen, L., Chen, X., Chen, Y., et al. (2024) · Nature · doi:10.1038/s41586-024-08280-5 · Cited by 59
Interactome disassembly during apoptosis occurs independent of caspase cleavage
Scott, N. E., Rogers, L. D., Prudova, A., Brown, N. F., Fortelny, N., Overall, C. M., & Foster, L. J. (2017) · Molecular Systems Biology · doi:10.15252/msb.20167067 · Cited by 52
Hu, D. G., Hulin, J.-A., Nair, P. C., Haines, A. Z., McKinnon, R. A., Mackenzie, P. I., & Meech, R. (2019) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2019.107414 · Cited by 55
Quest for Missing Proteins: Update 2015 on Chromosome-Centric Human Proteome Project
Horvatovich, P. L., Lundberg, E. K., Chen, Y., Sung, T.-Y., He, F., Nice, E. C., Goode, R. J. A., Yu, S., Ranganathan, S., Baker, M. S., et al. (2015) · Journal of Proteome Research · doi:10.1021/pr5013009 · Cited by 54
Yang, S., Chen, F., Lian, X., Dong, X., & Zhang, Z. (2019) · mSystems · doi:10.1128/msystems.00303-18 · Cited by 54
Wu, Q., Shi, M., Meng, W., Wang, Y., Hui, P., & Ma, J. (2019) · Journal of Cellular Physiology · doi:10.1002/jcp.28752 · Cited by 54
Workability of mRNA Sequencing for Predicting Protein Abundance
Ponomarenko, E. A., Krasnov, G. S., Kiseleva, O. I., Kryukova, P. A., Arzumanian, V. A., Dolgalev, G. V., Ilgisonis, E. V., Lisitsa, A., & Poverennaya, E. V. (2023) · Genes · doi:10.3390/genes14112065 · Cited by 59
Proteomics of Human Aqueous Humor
Murthy, K. R., Rajagopalan, P., Pinto, S. M., Advani, J., Murthy, P. R., Goel, R., Subbannayya, Y., Balakrishnan, L., Dash, M., Anil, A. K., et al. (2015) · OMICS A Journal of Integrative Biology · doi:10.1089/omi.2015.0029 · Cited by 54
Self-citationFrom the Human Genome to the Human Proteome
Muñoz, J., & Heck, A. J. R. (2014) · Angewandte Chemie International Edition · doi:10.1002/anie.201406545 · Cited by 54
Knockout of BRD7 results in impaired spermatogenesis and male infertility
Wang, H., Zhao, R., Guo, C., Jiang, S., Yang, J., Xu, Y., Liu, Y., Fan, L., Xiong, W., Ma, J., et al. (2016) · Scientific Reports · doi:10.1038/srep21776 · Cited by 54
Identification of differentially expressed peptides in high-throughput proteomics data
van Ooijen, M. P., Jong, V. L., Eijkemans, M. J. C., Heck, A. J. R., Andeweg, A. C., Binai, N. A., & van den Ham, H. (2017) · Briefings in Bioinformatics · doi:10.1093/bib/bbx031 · Cited by 63
Zagorac, I., Fernandez-Gaitero, S., Penning, R., Post, H., Bueno, M. J., Mouron, S. A., Manso, L., Morente, M. M., Alonso, S. R., Serra, V., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-05742-z · Cited by 59
TRPM5 in the battle against diabetes and obesity
Vennekens, R., Mesuere, M., & Philippaert, K. (2017) · Acta Physiologica · doi:10.1111/apha.12949 · Cited by 52
RNA profiling of human testicular cells identifies syntenic lncRNAs associated with spermatogenesis
Rolland, A. D., Evrard, B., Darde, T., Béguec, C. L., Bras, Y. L., Bensalah, K., Lavoué, S., Jost, B., Primig, M., Dejucq‐Rainsford, N., et al. (2019) · Human Reproduction · doi:10.1093/humrep/dez063 · Cited by 54
The regulation properties of RNA secondary structure in alternative splicing
Bartyś, N., Kierzek, R., & Lisowiec‐Wąchnicka, J. (2019) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2019.07.002 · Cited by 54
Nuclear Periphery Takes Center Stage: The Role of Nuclear Pore Complexes in Cell Identity and Aging
Cho, U. H., & Hetzer, M. W. (2020) · Neuron · doi:10.1016/j.neuron.2020.05.031 · Cited by 54
Origins, Technological Development, and Applications of Peptidomics
Schrader, M. (2018) · Methods in molecular biology · doi:10.1007/978-1-4939-7537-2_1 · Cited by 54
Gu, L., Casserly, D., Brady, G., Carpenter, S. B., Bracken, A. P., Fitzgerald, K. A., Unterholzner, L., & Bowie, A. (2022) · Nature Communications · doi:10.1038/s41467-021-27701-x · Cited by 52
The Impact of PIK3R1 Mutations and Insulin–PI3K–Glycolytic Pathway Regulation in Prostate Cancer
Chakraborty, G., Nandakumar, S., Hirani, R., Nguyen, B., Stopsack, K. H., Kreitzer, C. K., Rajanala, S. H., Ghale, R., Mazzu, Y. Z., Pillarsetty, N., et al. (2022) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-21-4272 · Cited by 54
Cao, X., Zhu, L., Song, X., Hu, Z., & Cronan, J. E. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1805862115 · Cited by 51
Spatiotemporal changes in the human lens proteome: Critical insights into long-lived proteins
Schey, K. L., Wang, Z., Friedrich, M. G., Garland, D. L., & Truscott, R. J. W. (2019) · Progress in Retinal and Eye Research · doi:10.1016/j.preteyeres.2019.100802 · Cited by 53
The tissue proteome in the multi-omic landscape of kidney disease
Rinschen, M. M., & Sáez-Rodríguez, J. (2020) · Nature Reviews Nephrology · doi:10.1038/s41581-020-00348-5 · Cited by 56
Conserved Epigenetic Regulatory Logic Infers Genes Governing Cell Identity
Shim, W. J., Sinniah, E., Xu, J., Vitrinel, B., Alexanian, M., Andreoletti, G., Shen, S., Sun, Y., Balderson, B., Boix, C. A., et al. (2020) · Cell Systems · doi:10.1016/j.cels.2020.11.001 · Cited by 50
Tune instead of destroy: How proteolysis keeps OXPHOS in shape
Szczepanowska, K., & Trifunović, A. (2021) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2020.148365 · Cited by 51
Quantitative proteome comparison of human hearts with those of model organisms
Linscheid, N., Santos, A., Poulsen, P. C., Mills, R. W., Calløe, K., Leurs, U., Ye, J. Z., Calløe, K., Thomsen, M. B., Bentzen, B. H., et al. (2021) · PLoS Biology · doi:10.1371/journal.pbio.3001144 · Cited by 56
Assessing the functional relevance of splice isoforms
del Pozo, F. C., Gómez, L. M., Walsh, T., Rodrı́guez, J. M., Domenico, T. D., Abascal, F., Vázquez, J., & Tress, M. L. (2021) · NAR Genomics and Bioinformatics · doi:10.1093/nargab/lqab044 · Cited by 46
Metabolon formation regulates branched-chain amino acid oxidation and homeostasis
Patrick, M., Gu, Z., Zhang, G., Wynn, R., Kaphle, P., Cao, H., Vu, H., Cai, F., Gao, X., Zhang, Y., et al. (2022) · Nature Metabolism · doi:10.1038/s42255-022-00689-4 · Cited by 53
Proteomics of human mitochondria
Palmfeldt, J., & Bross, P. (2016) · Mitochondrion · doi:10.1016/j.mito.2016.07.006 · Cited by 55
Radhakrishnan, A., Nanjappa, V., Raja, R., Sathe, G. J., Puttamallesh, V. N., Jain, A., Pinto, S. M., Andugulapati, S. B., Chavan, S., Sahasrabuddhe, N. A., et al. (2016) · Scientific Reports · doi:10.1038/srep36132 · Cited by 52
Self-citationA Comprehensive Guide for Performing Sample Preparation and Top-Down Protein Analysis
Padula, M. P., Berry, I. J., O’Rourke, M. B., Raymond, B. B. A., Santos, J., & Djordjevic, S. P. (2017) · Proteomes · doi:10.3390/proteomes5020011 · Cited by 53
Generic membrane-spanning features endow IRE1α with responsiveness to membrane aberrancy
Kono, N., Amin-Wetzel, N., & Ron, D. (2017) · Molecular Biology of the Cell · doi:10.1091/mbc.e17-03-0144 · Cited by 50
Xu, R., Tang, J., Deng, Q., He, W., Sun, X., Xia, L., Cheng, Z., He, L., You, S., Hu, J., et al. (2018) · Analytical Chemistry · doi:10.1021/acs.analchem.8b00596 · Cited by 52
Feng, J. T., Xu, Y., Huang, W., Kong, H., Li, Y., Cheng, H., & Li, L. (2019) · Analytica Chimica Acta · doi:10.1016/j.aca.2019.11.004 · Cited by 52
Srivastava, R., Daulatabad, S. V., Srivastava, M., & Janga, S. C. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21197090 · Cited by 52
Yang, M., Lin, X., Liu, X., Zhang, J., & Ge, F. (2018) · Molecular Plant · doi:10.1016/j.molp.2018.08.005 · Cited by 53
Proteomic Detection and Validation of Translated Small Open Reading Frames
Khitun, A., & Slavoff, S. A. (2019) · Current Protocols in Chemical Biology · doi:10.1002/cpch.77 · Cited by 49
Basha, O., Flom, D., Barshir, R., Smoly, I. Y., Tirman, S., & Yeger‐Lotem, E. (2015) · Nucleic Acids Research · doi:10.1093/nar/gkv515 · Cited by 50
Proteomic characterization of post-translational modifications in drug discovery
Zhai, L., Chen, K., Hao, B., & Tan, M. (2022) · Acta Pharmacologica Sinica · doi:10.1038/s41401-022-01017-y · Cited by 53
Analysis of human upstream open reading frames and impact on gene expression
Ye, Y., Liang, Y., Yu, Q., Hu, L., Li, H., Zhang, Z., & Xu, X. (2015) · Human Genetics · doi:10.1007/s00439-015-1544-7 · Cited by 50
Metzler‐Guillemain, C., Victoréro, G., Lepoivre, C., Bergon, A., Yammine, M., Perrin, J., Sari-Minodier, I., Boulanger, N., Rihet, P., & Nguyen, C. (2015) · Systems Biology in Reproductive Medicine · doi:10.3109/19396368.2015.1022835 · Cited by 52
Positional proteomics in the era of the human proteome project on the doorstep of precision medicine
Eckhard, U., Marino, G., Butler, G. S., & Overall, C. M. (2015) · Biochimie · doi:10.1016/j.biochi.2015.10.018 · Cited by 50
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Leitner, A. (2015) · Methods in molecular biology · doi:10.1007/978-1-4939-3049-4_7 · Cited by 50
Development of a Microflow System for In-Cell Footprinting Coupled with Mass Spectrometry
Rinas, A., Mali, V. S., Espino, J. A., & Jones, L. M. (2016) · Analytical Chemistry · doi:10.1021/acs.analchem.6b02357 · Cited by 50
Lian, Y., Xu, Y., Xiao, C., Xia, R., Gong, H., Yang, P., Chen, T., Wu, D., Cai, Z., Zhang, J., et al. (2017) · Scientific Reports · doi:10.1038/s41598-017-07954-7 · Cited by 52
Deep learning for image analysis: Personalizing medicine closer to the point of care
Xie, Q. Y., Faust, K., Ommeren, R. V., Sheikh, A., Djuric, U., & Diamandis, P. (2019) · Critical Reviews in Clinical Laboratory Sciences · doi:10.1080/10408363.2018.1536111 · Cited by 50
Proteomics in cancer research: Are we ready for clinical practice?
Maes, E., Mertens, I., Valkenborg, D., Pauwels, P., Rolfo, C. D., & Baggerman, G. (2015) · Critical Reviews in Oncology/Hematology · doi:10.1016/j.critrevonc.2015.07.006 · Cited by 49
Mendelian disorders of PI metabolizing enzymes
Staiano, L., Leo, M. G. D., Persico, M., & Matteis, M. A. D. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2014.12.001 · Cited by 54
Park, G. W., Hwang, H., Kim, K. H., Lee, J. Y., Lee, H. K., Park, J. Y., Ji, E. S., Park, S. K. R., Yates, J. R., Kwon, K., et al. (2016) · Journal of Proteome Research · doi:10.1021/acs.jproteome.6b00376 · Cited by 48
Biosynthetic energy cost for amino acids decreases in cancer evolution
Zhang, H., Wang, Y., Li, J., Chen, H., He, X., Zhang, H., Liang, H., & Lü, J. (2018) · Nature Communications · doi:10.1038/s41467-018-06461-1 · Cited by 49
Bittremieux, W., Laukens, K., & Noble, W. S. (2019) · Journal of Proteome Research · doi:10.1021/acs.jproteome.9b00291 · Cited by 49
Ravarani, C. N. J., Flock, T., Chavali, S., Anandapadamanaban, M., Babu, M. M., & Santhanam, B. (2020) · Nature Communications · doi:10.1038/s41467-020-16182-z · Cited by 48
Serrano, L. R., Peters-Clarke, T. M., Arrey, T. N., Damoc, E., Robinson, M. L., Lancaster, N. M., Shishkova, E., Moss, C. E., Pashkova, A., Sinitcyn, P. G., et al. (2024) · Molecular & Cellular Proteomics · doi:10.1016/j.mcpro.2024.100760 · Cited by 48
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Witzmann, F. A., Evan, A. P., Coe, F. L., Worcester, E. M., Lingeman, J. E., & Williams, J. C. (2016) · Proteome Science · doi:10.1186/s12953-016-0093-x · Cited by 46
Li, H., Joh, Y. S., Kim, H., Paek, E., Lee, S., & Hwang, K. (2016) · BMC Genomics · doi:10.1186/s12864-016-3327-5 · Cited by 50
Pineau, C., Hikmet, F., Zhang, C., Oksvold, P., Chen, S., Fagerberg, L., Uhlén, M., & Lindskog, C. (2019) · Journal of Proteome Research · doi:10.1021/acs.jproteome.9b00351 · Cited by 48
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Kim, T. H., Hong, D.-G., & Yang, Y. M. (2021) · Biomedicines · doi:10.3390/biomedicines9121903 · Cited by 57
Chen, D., Shen, X., & Sun, L. (2018) · Analytica Chimica Acta · doi:10.1016/j.aca.2018.01.037 · Cited by 47
TMEM16E regulates endothelial cell procoagulant activity and thrombosis
Schmaier, A. A., Anderson, P. F., Chen, S. M., El-Darzi, E., Aivasovsky-Trotta, I., Kaushik, M. P., Sack, K. D., Hartzell, H. C., Parikh, S. M., Flaumenhaft, R. C., et al. (2023) · Journal of Clinical Investigation · doi:10.1172/jci163808 · Cited by 47
Fekete, R., Simats, A., Bíró, E., Pósfai, B., Cserép, C., Schwarcz, A. D., Szabadits, E., Környei, Z., Tóth, K., Fichó, E., et al. (2025) · Nature Neuroscience · doi:10.1038/s41593-025-01871-z · Cited by 59
Tissue-Based Proteogenomics Reveals that Human Testis Endows Plentiful Missing Proteins
Zhang, Y., Li, Q., Wu, F., Zhou, R., Qi, Y., Su, N., Chen, L., Xu, S., Jiang, T., Zhang, C., et al. (2015) · Journal of Proteome Research · doi:10.1021/acs.jproteome.5b00435 · Cited by 47
Vanderperre, B., Cermakova, K., Escoffier, J., Kaba, M., Bender, T., Nef, S., & Martinou, J. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.733840 · Cited by 52
Guo, L., Wu, Y., Huang, Q., Qiang, J., Hart, J. R., Wang, W., Hu, J., Zhu, J., Liu, N., & Zhang, Y. (2018) · Cell chemical biology · doi:10.1016/j.chembiol.2018.08.006 · Cited by 47
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Lamadema, N., Burr, S., & Brewer, A. C. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.12.009 · Cited by 50
Wormser, O., Gradstein, L., Yogev, Y., Perez, Y., Kadir, R., Goliand, I., Sadaka, Y., Riati, S. E., Flusser, H., Nachmias, D., et al. (2019) · European Journal of Human Genetics · doi:10.1038/s41431-019-0347-z · Cited by 48
Wang, D., Zou, L., Jin, Q., Guan, X., Yu, Y., Zhu, Y.-D., Huang, J., Gao, P., Wang, P., Ge, G., et al. (2020) · ACS Sensors · doi:10.1021/acssensors.0c00384 · Cited by 47
Lesurf, R., Said, A., Akinrinade, O., Breckpot, J., Delfosse, K., Liu, T., Yao, R., Persad, G., McKenna, F., Noche, R. R., et al. (2022) · npj Genomic Medicine · doi:10.1038/s41525-022-00288-y · Cited by 49
Viewing the proteome: How to visualize proteomics data?
Oveland, E., Muth, T., Rapp, E., Martens, L., Berven, F. S., & Barsnes, H. (2014) · PROTEOMICS · doi:10.1002/pmic.201400412 · Cited by 46
Jarnuczak, A. F., Lee, D. C. H., Lawless, C., Holman, S. W., Eyers, C. E., & Hubbard, S. J. (2016) · Journal of Proteome Research · doi:10.1021/acs.jproteome.6b00048 · Cited by 43
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Tain, L. S., Sehlke, R., Jain, C., Chokkalingam, M., Nagaraj, N., Essers, P., Rassner, M., Grönke, S., Froelich, J., Dieterich, C., et al. (2017) · Molecular Systems Biology · doi:10.15252/msb.20177663 · Cited by 44
Gel-based proteomics in disease research: Is it still valuable?
Kim, Y., & Cho, J. (2018) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2018.08.001 · Cited by 48
Lso2 is a conserved ribosome-bound protein required for translational recovery in yeast
Wang, Y. J., Vaidyanathan, P. P., Rojas-Durán, M. F., Udeshi, N. D., Bartoli, K. M., Carr, S. A., & Gilbert, W. V. (2018) · PLoS Biology · doi:10.1371/journal.pbio.2005903 · Cited by 44
An, Z., Zhai, L., Ying, W., Qian, X., Gong, F., Tan, M., & Fu, Y. (2018) · Molecular & Cellular Proteomics · doi:10.1074/mcp.ra118.000812 · Cited by 46
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Kulbe, H., Otto, R., Darb‐Esfahani, S., Lammert, H., Abobaker, S., Welsch, G., Chekerov, R., Schäfer, R., Dragun, D., Hummel, M., et al. (2019) · Cells · doi:10.3390/cells8070713 · Cited by 46
Linscheid, N., Poulsen, P. C., Pedersen, I. D., Gregers, E., Svendsen, J. H., OLESEN, M. S., Olsen, J. V., Delmar, M., & Lundby, A. (2020) · Molecular & Cellular Proteomics · doi:10.1074/mcp.ra119.001878 · Cited by 46
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Curry, O. S., Alfano, M., Brandt, M. J., & Pelican, C. (2021) · Review of Philosophy and Psychology · doi:10.1007/s13164-021-00540-x · Cited by 58
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Gil, J., Betancourt, L. H., Pla, I., Sanchez, A., Appelqvist, R., Miliotis, T., Kuras, M., Oskolas, H., Kim, Y., Horvath, Z., et al. (2019) · Cell Biology and Toxicology · doi:10.1007/s10565-019-09468-6 · Cited by 45
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Malty, R. H., Jessulat, M., Jin, K., Musso, G. A., Vlasblom, J., Phanse, S., Zhang, Z., & Babu, M. (2014) · Journal of Proteome Research · doi:10.1021/pr500813f · Cited by 45
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Chernobrovkin, A. L., Marín‐Vicente, C., Visa, N., & Zubarev, R. A. (2015) · Scientific Reports · doi:10.1038/srep11176 · Cited by 49
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A deep generative model of 3D single-cell organization
Donovan-Maiye, R. M., Brown, J. M., Chan, C. K., Ding, L., Yan, C., Gaudreault, N., Theriot, J. A., Maleckar, M. M., Knijnenburg, T. A., & Johnson, G. R. (2022) · PLOS Computational Biology · doi:10.1371/journal.pcbi.1009155 · Cited by 44
Carapito, C., Lane, L., Benama, M., Opsomer, A., Mouton‐Barbosa, E., Garrigues, L., de Peredo, A. G., Burel, A., Bruley, C., Gateau, A., et al. (2015) · Journal of Proteome Research · doi:10.1021/pr5010345 · Cited by 47
Guillemin, A., Kumar, A., Wencker, M., & Ricci, E. P. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2021.796012 · Cited by 48
Jin, Y., Kim, H., Min, S., Choi, Y. S., Seo, S. J., Jeong, E., Kim, S. K., Lee, H., Jo, S.-H., Park, J.-H., et al. (2022) · Science Advances · doi:10.1126/sciadv.abn5768 · Cited by 44
Song, K. J., Choi, S., Kim, K., Hwang, H. S., Chang, E., Park, J. S., Shim, S. B., Choi, S., Heo, Y. J., Yang, D. Y., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-54434-4 · Cited by 44
Self-citationChemogenetics—A Transformational and Translational Platform
English, J. G., & Roth, B. L. (2015) · JAMA Neurology · doi:10.1001/jamaneurol.2015.1921 · Cited by 46
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Kuljanin, M., Dieters‐Castator, D. Z., Hess, D. A., Postovit, L.-M. M., & Lajoie, G. (2016) · PROTEOMICS · doi:10.1002/pmic.201600337 · Cited by 43
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Signaling by discoidin domain receptor 1 in cancer metastasis
Gadiya, M. M., & Chakraborty, G. (2018) · Cell Adhesion & Migration · doi:10.1080/19336918.2018.1520556 · Cited by 46
Aizat, W. M., & Hassan, M. (2018) · Advances in experimental medicine and biology · doi:10.1007/978-3-319-98758-3_3 · Cited by 46
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Wang, H., Wang, Y., Yang, J., Zhao, Q. C., Tang, N., Chen, C., Li, H., Cheng, C., Xie, M., Yang, Y., et al. (2021) · Nucleic Acids Research · doi:10.1093/nar/gkab482 · Cited by 44
Metadata
- Authors
- Kim, M.-S., Pinto, S. M., Getnet, D., Nirujogi, R. S., Manda, S. S., Chaerkady, R., Madugundu, A. K., Kelkar, D. S., Isserlin, R., Jain, S., Thomas, J. K., Muthusamy, B., Leal-Rojas, P., Kumar, P., Sahasrabuddhe, N. A., Balakrishnan, L., Advani, J., George, B., Renuse, S., Selvan, L. D. N., Patil, A. H., Nanjappa, V., Radhakrishnan, A., Prasad, S., Subbannayya, T., Raju, R., Kumar, M., Sreenivasamurthy, S. K., Marimuthu, A., Sathe, G. J., Chavan, S., Datta, K. K., Subbannayya, Y., Sahu, A., Yelamanchi, S. D., Jayaram, S., Rajagopalan, P., Sharma, J., Murthy, K. R., Syed, N., Goel, R., Khan, A. A., Ahmad, S., Dey, G., Mudgal, K., Chatterjee, A., Huang, T.-C., Zhong, J., Wu, X., Shaw, P. G., Freed, D., Zahari, M. S., Mukherjee, K. K., Shankar, S., Mahadevan, A., Lam, H., Mitchell, C. J., Shankar, S. K., Satishchandra, P., Schroeder, J. T., Sirdeshmukh, R., Maitra, A., Leach, S. D., Drake, C. G., Halushka, M. K., Prasad, T. S. K., Hruban, R. H., Kerr, C. L., Bader, G. D., Iacobuzio-Donahue, C. A., Gowda, H., & Pandey, A.
- Affiliations
- Johns Hopkins University (US)
- Institute of Bioinformatics (IN)
- University of Toronto (CA)
- Imperial College London (GB)
- Post Graduate Institute of Medical Education and Research (IN)
- National Institute of Mental Health and Neurosciences (IN)
- Hong Kong University of Science and Technology (HK)
- Corresponding author
- Gowda, Harsha
- Pandey, Akhilesh
- ORCID
- Kim, Min-Sik
- Pinto, Sneha M.
- Getnet, Derese
- Nirujogi, Raja Sekhar
- Manda, Srikanth S.
- Chaerkady, Raghothama
- Madugundu, Anil K.
- Kelkar, Dhanashree S.
- Isserlin, Ruth
- Muthusamy, Babylakshmi
- Kumar, Praveen
- Balakrishnan, Lavanya
- Advani, Jayshree
- George, Bijesh
- Renuse, Santosh
- Selvan, Lakshmi Dhevi N.
- Patil, Arun H.
- Nanjappa, Vishalakshi
- Prasad, Samarjeet
- Subbannayya, Tejaswini
- Raju, Rajesh
- Kumar, Manish
- Sreenivasamurthy, Sreelakshmi K.
- Sathe, Gajanan J.
- Chavan, Sandip
- Datta, Keshava K.
- Subbannayya, Yashwanth
- Yelamanchi, Soujanya D.
- Jayaram, Savita
- Sharma, Jyoti
- Syed, Nazia
- Khan, Aafaque A.
- Ahmad, Sartaj
- Dey, Gourav
- Mudgal, Keshav
- Chatterjee, Aditi
- Huang, Tai-Chung
- Zhong, Jun
- Wu, Xinyan
- Freed, Donald
- Mukherjee, Kanchan K.
- Shankar, Subramanian
- Mahadevan, Anita
- Lam, Henry
- Schroeder, John T.
- Maitra, Anirban
- Leach, Steven D.
- Drake, Charles G.
- Halushka, Marc K.
- Prasad, T. S. Keshava
- Hruban, Ralph H.
- Bader, Gary D.
- Gowda, Harsha
- Pandey, Akhilesh
- Venue
- Nature
- Published
- 2014-05-28
- Volume
- 509
- Issue
- 7502
- Pages
- 575-581
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- PMC
- PMC4403737
- OpenAlex
- W2056499061
- Cited by
- 2,198
- References
- 45
- Citations by year
- 2026: 59 · 2025: 93 · 2024: 110 · 2023: 150 · 2022: 151 · 2021: 201 · 2020: 177 · 2019: 176 · 2018: 203 · 2017: 244 · 2016: 253 · 2015: 276 · 2014: 102
- FWCI
- 125.37
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- Discovery Research Portal (University of Dundee) (submittedVersion)
- Omeka S (Universidad de La Frontera) (submittedVersion, cc-by-nc-nd)
- Rare & Special e-Zone (The Hong Kong University of Science and Technology) (submittedVersion)
- Funders
- National Institutes of Health
- National Heart, Lung, and Blood Institute (HHS-N268201000032C)
- National Cancer Institute (U24CA160036)
- National Institute of General Medical Sciences (T32GM007814, U54GM103520, P41GM103504)
- Topics
- Physical Sciences › Chemistry › Spectroscopy › Advanced Proteomics Techniques and Applications
- Physical Sciences › Chemistry › Spectroscopy › Mass Spectrometry Techniques and Applications
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Bioinformatics and Genomic Networks
- Keywords
- human proteome, proteome map, proteogenomics, non-coding RNA, upstream open reading frames, protein-coding genes, human tissue, hematopoietic cells, fetal tissue, tissue-specific proteins, long intergenic non-coding RNA, mRNA-protein correlation, Human Protein Atlas
- MeSH terms
- Adult, Cells, Cultured, Fetus, Fourier Analysis, Hematopoietic Stem Cells, Humans, Organ Specificity, Pseudogenes, Mass Spectrometry, Protein Biosynthesis, Reproducibility of Results, Genome, Human, Open Reading Frames, Protein Isoforms, Internet, Untranslated Regions, Proteome, Gene Expression Profiling, Protein Transport, Protein Sorting Signals, RNA, Untranslated, Databases, Protein, Proteomics, Molecular Sequence Annotation
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