The DOI matches its Crossref record; 45 of the 45 references it cites were found in a registry or an index.
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.
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 source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
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]
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
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
Cited by
Sorted by citations
Items 701–800 of 1,002
Hasin-Brumshtein, Y., Khan, A. H., Hormozdiari, F., Pan, C., Parks, B. W., Petyuk, V., Piehowski, P., Brümmer, A., Pellegrini, M. A., Xiao, X. G., et al. (2016) · eLife · doi:10.7554/elife.15614 · Cited by 34
Self-citationOnco-proteogenomics: Multi-omics level data integration for accurate phenotype prediction
Dimitrakopoulos, L., Prassas, I., Diamandis, E. P., & Charames, G. S. (2017) · Critical Reviews in Clinical Laboratory Sciences · doi:10.1080/10408363.2017.1384446 · Cited by 36
Proteomic Landscape of Patient-Derived CD4+ T Cells in Recent-Onset Type 1 Diabetes
Lepper, M. F., Ohmayer, U., von Toerne, C., Maison, N., Ziegler, A., & Hauck, S. M. (2017) · Journal of Proteome Research · doi:10.1021/acs.jproteome.7b00712 · Cited by 36
Massa, D., Baran, M., Bengoechea, J. A., & Bowie, A. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.011400 · Cited by 32
Evidence for a novel overlapping coding sequence in POLG initiated at a CUG start codon
Khan, Y. A., Jungreis, I., Wright, J. C., Mudge, J. M., Choudhary, J. S., Firth, A. E., & Kellis, M. (2020) · BMC Genetics · doi:10.1186/s12863-020-0828-7 · Cited by 33
Thomas, S. N., Friedrich, B., Schnaubelt, M., Chan, D. W., Zhang, H., & Aebersold, R. H. (2020) · iScience · doi:10.1016/j.isci.2020.101079 · Cited by 34
Molecular Dynamics Simulation-assisted Ionic Liquid Screening for Deep Coverage Proteome Analysis
Fang, F., Zhao, Q., Chu, H., Liu, M., Zhao, B., Liang, Z., Zhang, L., Li, G., Wang, L., Qin, J., et al. (2020) · Molecular & Cellular Proteomics · doi:10.1074/mcp.tir119.001827 · Cited by 35
Integration of omics sciences to advance biology and medicine
Boja, E. S., Kinsinger, C. R., Rodriguez, H., & Srinivas, P. R. (2014) · Clinical Proteomics · doi:10.1186/1559-0275-11-45 · Cited by 38
Kumar, D., Yadav, A. K., Jia, X., Mulvenna, J. P., & Dash, D. (2015) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m114.047126 · Cited by 35
Laplacian paths in complex networks: Information core emerges from entropic transitions
Villegas, P., Gabrielli, A., Santucci, F., Caldarelli, G., & Gili, T. (2022) · Physical Review Research · doi:10.1103/physrevresearch.4.033196 · Cited by 37
Miao, X., Alidadipour, A., Saed, V., Sayyadi, F., Jadidi, Y., Davoudi, M., Amraee, F., Jadidi, N., & Afrisham, R. (2024) · Acta Diabetologica · doi:10.1007/s00592-024-02335-9 · Cited by 37
Ishige, T., Nishimura, M., Satoh, M., Fujimoto, M., Fukuyo, M., Semba, T., Kado, S., Tsuchida, S., Sawai, S., Matsushita, K., et al. (2016) · Scientific Reports · doi:10.1038/srep21681 · Cited by 35
Alvarellos, M. L., Sangkuhl, K., Daneshjou, R., Whirl‐Carrillo, M., Altman, R. B., & Klein, T. E. (2014) · Pharmacogenetics and Genomics · doi:10.1097/fpc.0000000000000100 · Cited by 34
Woo, S., Cha, S. W., Bonissone, S. R., Na, S., Tabb, D. L., Pevzner, P. A., & Bafna, V. (2015) · Journal of Proteome Research · doi:10.1021/acs.jproteome.5b00264 · Cited by 34
Why proteomics is not the new genomics and the future of mass spectrometry in cell biology
Sidoli, S., Kulej, K., & Garcia, B. A. (2016) · The Journal of Cell Biology · doi:10.1083/jcb.201612010 · Cited by 38
Kumar, B., Yadav, A., Brown, N. V., Zhao, S., Cipolla, M. J., Wakely, P. E., Schmitt, A. C., Baiocchi, R. A., Teknos, T. N., Old, M. O., et al. (2017) · Oncotarget · doi:10.18632/oncotarget.14682 · Cited by 34
Self-citationSingh, H., Yu, Y., Suh, M., Torralba, M., Stenzel, R. D., Tovchigrechko, A., Thovarai, V., Harkins, D. M., Rajagopala, S. V., Osborne, W., et al. (2017) · Theranostics · doi:10.7150/thno.19679 · Cited by 33
Ren, L., Li, Z., Shao, W., Lin, W., He, F., & Jiang, Y. (2017) · Journal of Proteome Research · doi:10.1021/acs.jproteome.7b00520 · Cited by 32
Understanding Ovarian Cancer: iTRAQ-Based Proteomics for Biomarker Discovery
Światły‐Błaszkiewicz, A., Horała, A., Matysiak, J., Hajduk, J., Nowak‐Markwitz, E., & Kokot, Z. J. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19082240 · Cited by 34
Dynamics of the transcriptional landscape during human fetal testis and ovary development
Lecluze, E., Rolland, A. D., Filis, P., Evrard, B., Leverrier, S., Maamar, M. B., Coiffec, I., Lavoué, V., Fowler, P., Mazaud‐Guittot, S., et al. (2020) · Human Reproduction · doi:10.1093/humrep/deaa041 · Cited by 36
PP2A/B55α substrate recruitment as defined by the retinoblastoma-related protein p107
Fowle, H. A., Zhao, Z., Xu, Q., Wasserman, J. S., Wang, X., Adeyemi, M., Feiser, F., Kurimchak, A., Atar, D., McEwan, B. C., et al. (2021) · eLife · doi:10.7554/elife.63181 · Cited by 31
A note on the false discovery rate of novel peptides in proteogenomics
Zhang, K., Fu, Y., Zeng, W., He, K., Chi, H., Liu, C., Li, Y., Gao, Y., Xu, P., & He, S. (2015) · Bioinformatics · doi:10.1093/bioinformatics/btv340 · Cited by 34
Cotton, R. W., & Fisher, M. B. (2015) · Forensic Science International Genetics · doi:10.1016/j.fsigen.2015.03.009 · Cited by 35
Habuka, M., Fagerberg, L., Hallström, B. M., Pontén, F., Yamamoto, T., & Uhlén, M. (2015) · PLoS ONE · doi:10.1371/journal.pone.0145301 · Cited by 33
Proteomic Analysis of Human Fetal Atria and Ventricle
Lu, Z. Q., Sinha, A., Sharma, P., Kislinger, T., & Gramolini, A. O. (2014) · Journal of Proteome Research · doi:10.1021/pr5007685 · Cited by 34
Novel biomarker signatures for idiopathic REM sleep behavior disorder
Mondello, S., Kobeissy, F. H., Mechref, Y. S., Zhao, J., Talih, F. R., Cosentino, F., Antelmi, E., Moresco, M., Plazzi, G., & Ferri, R. (2018) · Neurology · doi:10.1212/wnl.0000000000006439 · Cited by 34
Mitchell, K., & Steidl, U. G. (2019) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a036251 · Cited by 37
The HLA Ligand Atlas - A resource of natural HLA ligands presented on benign tissuesPreprint
Marcu, A., Bichmann, L., Kuchenbecker, L., Kowalewski, D. J., Freudenmann, L. K., Backert, L., Mühlenbruch, L., Szolek, A., Lübke, M., Wagner, P., et al. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/778944 · Cited by 34
A Quantitative Proteome Map of the Human BodyPreprint
Jiang, L., Wang, M., Lin, S., Jian, R., Li, X., Chan, J., Fang, H., Dong, G., Tang, H., & Snyder, M. P. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/797373 · Cited by 35
Laan, L., Klar, J., Sobol, M., Hoeber, J., Shahsavani, M., Kele, M., Fatima, A., Zakaria, M., Annerén, G., Falk, A., et al. (2020) · Clinical Epigenetics · doi:10.1186/s13148-019-0803-1 · Cited by 33
Park, H., Bae, J., Kim, H., Kim, S., Kim, H., Mun, D., Joh, Y. S., Lee, W., Chae, S., Lee, S., et al. (2014) · PROTEOMICS · doi:10.1002/pmic.201400225 · Cited by 33
Fan, J., Saha, S., Barker, G., Heesom, K. J., Ghali, F., Jones, A. R., Matthews, D. A., & Bessant, C. (2015) · Molecular & Cellular Proteomics · doi:10.1074/mcp.o115.048777 · Cited by 33
Proteomics of Skeletal Muscle: Focus on Insulin Resistance and Exercise Biology
Deshmukh, A. S. (2016) · Proteomes · doi:10.3390/proteomes4010006 · Cited by 35
Dysregulation of splicing proteins in head and neck squamous cell carcinoma
Radhakrishnan, A., Nanjappa, V., Raja, R., Sathe, G. J., Chavan, S., Nirujogi, R. S., Patil, A. H., Solanki, H. S., Renuse, S., Sahasrabuddhe, N. A., et al. (2016) · Cancer Biology & Therapy · doi:10.1080/15384047.2016.1139234 · Cited by 34
Self-citationLounis, M. A., Lalonde, S., Rial, S. A., Bergeron, K., Ralston, J. C., Mutch, D. M., & Mounier, C. (2016) · Lipids · doi:10.1007/s11745-016-4210-5 · Cited by 31
Param-Medic: A Tool for Improving MS/MS Database Search Yield by Optimizing Parameter Settings
May, D., Tamura, K., & Noble, W. S. (2017) · Journal of Proteome Research · doi:10.1021/acs.jproteome.7b00028 · Cited by 33
Advanced bioinformatics methods for practical applications in proteomics
Goh, W. W. B., & Wong, L. (2017) · Briefings in Bioinformatics · doi:10.1093/bib/bbx128 · Cited by 33
Drug Repurposing of Metabolic Agents in Malignant Glioma
Seliger, C., & Hau, P. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19092768 · Cited by 36
Context-specific interactions in literature-curated protein interaction databases
Stacey, R. G., Skinnider, M. A., Chik, J. H. L., & Foster, L. J. (2018) · BMC Genomics · doi:10.1186/s12864-018-5139-2 · Cited by 33
Averaging Strategy To Reduce Variability in Target-Decoy Estimates of False Discovery Rate
Keich, U., Tamura, K., & Noble, W. S. (2018) · Journal of Proteome Research · doi:10.1021/acs.jproteome.8b00802 · Cited by 32
Janda, E., Nepveu, F., Calamini, B., Ferry, G., & Boutin, J. A. (2020) · Molecular Pharmacology · doi:10.1124/molpharm.120.000105 · Cited by 33
Bassignani, A., Plancade, S., Berland, M., Blein‐Nicolas, M., Guillot, A., Chevret, D., Moritz, C., Huet, S., Rizkalla, S. W., Clément, K., et al. (2021) · Journal of Proteome Research · doi:10.1021/acs.jproteome.0c00669 · Cited by 32
Gao, J., Liu, Y., Yang, F., Chen, X., Cravatt, B. F., & Wang, C. (2021) · Journal of Proteome Research · doi:10.1021/acs.jproteome.1c00455 · Cited by 32
The, M., Samaras, P., Küster, B., & Wilhelm, M. (2022) · Molecular & Cellular Proteomics · doi:10.1016/j.mcpro.2022.100437 · Cited by 36
Challenges and developments in protein identification using mass spectrometry
Szabó, Z., & Janáky, T. (2015) · TrAC Trends in Analytical Chemistry · doi:10.1016/j.trac.2015.03.007 · Cited by 34
Exome-Driven Characterization of the Cancer Cell Lines at the Proteome Level: The NCI-60 Case Study
Karpova, M. A., Karpov, D. S., Ivanov, M. V., Pyatnitskiy, M. A., Chernobrovkin, A. L., Lobas, A. A., Lisitsa, A., Archakov, A. I., Gorshkov, M. V., & Moshkovskii, S. A. (2014) · Journal of Proteome Research · doi:10.1021/pr500531x · Cited by 33
Panwar, B., Menon, R., Eksi, R., Li, H.-D., Omenn, G. S., & Guan, Y. (2016) · Journal of Proteome Research · doi:10.1021/acs.jproteome.5b00883 · Cited by 32
Integrative analysis of human omics data using biomolecular networks
Robinson, J. L., & Nielsen, J. (2016) · Molecular BioSystems · doi:10.1039/c6mb00476h · Cited by 33
The Human Adrenal Gland Proteome Defined by Transcriptomics and Antibody-Based Profiling
Bergman, J., Botling, J., Fagerberg, L., Hallström, B. M., Djureinovic, D., Uhlén, M., & Pontén, F. (2016) · Endocrinology · doi:10.1210/en.2016-1758 · Cited by 32
Komorowski, A., James, G. M., Philippe, C., Gryglewski, G., Bauer, A., Hienert, M., Spies, M., Kautzky, A., Vanicek, T., Hahn, A., et al. (2016) · Cerebral Cortex · doi:10.1093/cercor/bhw355 · Cited by 32
Myeloid-derived growth factor is a resident endoplasmic reticulum protein
Bortnov, V., Annis, D. S., Fogerty, F. J., Barretto, K. T., Turton, K. B., & Mosher, D. F. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ac118.002052 · Cited by 32
Comparing SRM and SWATH Methods for Quantitation of Bovine Muscle Proteomes
Wu, W., Dai, R., & Bendixen, E. (2019) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.8b05459 · Cited by 32
Galano‐Frutos, J. J., García‐Cebollada, H., & Sancho, J. (2019) · Briefings in Bioinformatics · doi:10.1093/bib/bbz146 · Cited by 32
Zhao, Z., Kurimchak, A., Nikonova, A. S., Feiser, F., Wasserman, J. S., Fowle, H. A., Varughese, T., Connors, M., Johnson, K. J., Makhov, P. B., et al. (2019) · Oncogenesis · doi:10.1038/s41389-019-0180-9 · Cited by 31
Emerging Roles of Activity-Dependent Alternative Splicing in Homeostatic Plasticity
Thalhammer, A., Jaudon, F., & Cingolani, L. A. (2020) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2020.00104 · Cited by 32
Zhou, Y., Wang, P., Yan, B., Chen, X., Landeck, L., Wang, Z., Li, X., Zhang, J., Zheng, M., & Man, X. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.01432 · Cited by 32
Large‐scale tandem mass spectrum clustering using fast nearest neighbor searching
Bittremieux, W., Laukens, K., Noble, W. S., & Dorrestein, P. C. (2021) · Rapid Communications in Mass Spectrometry · doi:10.1002/rcm.9153 · Cited by 31
Kitata, R. B., Dimayacyac-Esleta, B. R. T., Choong, W.-K., Tsai, C.-F., Lin, T., Tsou, C., Weng, S.-H., Chen, Y., Yang, P.-C., Arco, S. D., et al. (2015) · Journal of Proteome Research · doi:10.1021/acs.jproteome.5b00477 · Cited by 32
Clinical proteomics: Promises, challenges and limitations of affinity arrays
Betzen, C., Alhamdani, M. S. S., Lueong, S., Schröder, C., Stang, A., & Hoheisel, J. D. (2015) · PROTEOMICS - CLINICAL APPLICATIONS · doi:10.1002/prca.201400156 · Cited by 36
Francisco‐Velilla, R., Fernández-Chamorro, J., Dotú, I., & Martı́nez-Salas, E. (2018) · Nucleic Acids Research · doi:10.1093/nar/gky361 · Cited by 32
The Yin and Yang of cancer genes
Bashyam, M. D., Animireddy, S., Bala, P., Naz, A., & George, S. A. (2019) · Gene · doi:10.1016/j.gene.2019.04.025 · Cited by 31
Cobley, J. N., & Husi, H. (2020) · Antioxidants · doi:10.3390/antiox9040315 · Cited by 33
Gene expression and protein abundance: Just how associated are these molecular traits?
Samih, A., Ferreira, M. A. D. M., & Nikoloski, Z. (2025) · Biotechnology Advances · doi:10.1016/j.biotechadv.2025.108720 · Cited by 35
Information processing in the CNS: a supramolecular chemistry?
Tozzi, A. (2015) · Cognitive Neurodynamics · doi:10.1007/s11571-015-9337-1 · Cited by 32
TNF Superfamily Protein-Protein Interactions: Feasibility of Small- Molecule Modulation
Song, Y., & Buchwald, P. (2015) · Current Drug Targets · doi:10.2174/1389450116666150223115628 · Cited by 32
Wang, X., Slebos, R. J. C., Chambers, M., Tabb, D. L., Liebler, D. C., & Zhang, B. (2015) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m115.052860 · Cited by 31
Chen, Y., Li, Y., Zhong, J., Zhang, J., Chen, Z., Yang, L., Cao, X., He, Q., Zhang, G., & Wang, T. (2015) · Journal of Proteome Research · doi:10.1021/pr501103r · Cited by 31
Self-citationdbSAP: single amino-acid polymorphism database for protein variation detection
Cao, R., Shi, Y. Y., Chen, S., Ma, Y.-M., Chen, J., Yang, J., Chen, G., & Shi, T. (2016) · Nucleic Acids Research · doi:10.1093/nar/gkw1096 · Cited by 31
Liu, C., Chi, L., Tu, P., Xue, J., Ru, H., & Lü, K. (2019) · Journal of Proteomics · doi:10.1016/j.jprot.2019.01.011 · Cited by 31
Quantitative proteomics characterization of cancer biomarkers and treatment
Yang, X., Shi, Y., Zhang, D., Xin, R., Deng, J., Wu, T., Wang, H., Wang, P., Liu, J., Li, W., et al. (2021) · Molecular Therapy — Oncolytics · doi:10.1016/j.omto.2021.04.006 · Cited by 31
Suresh, V., Mohanty, V., Avula, K., Ghosh, A., Singh, B., Reddy, R. K., Parida, D., Suryawanshi, A. R., Raghav, S. K., Chattopadhyay, S., et al. (2021) · The FASEB Journal · doi:10.1096/fj.202100431r · Cited by 32
Microbial proteasomes as drug targets
Zhang, H., & Lin, G. (2021) · PLoS Pathogens · doi:10.1371/journal.ppat.1010058 · Cited by 31
Nutritional systems biology of type 2 diabetes
Zhao, Y., Barrere‐Cain, R., & Yang, X. (2015) · Genes & Nutrition · doi:10.1007/s12263-015-0481-3 · Cited by 31
Using Quantitative Seroproteomics to Identify Antibody Biomarkers in Pancreatic Cancer
Jhaveri, D. T., Kim, M., Thompson, E. D., Huang, L., Sharma, R. B., Klein, A. P., Zheng, L., Le, D. T., Laheru, D. A., Pandey, A., et al. (2016) · Cancer Immunology Research · doi:10.1158/2326-6066.cir-15-0200-t · Cited by 31
Self-citationComputation and application of tissue-specific gene set weights
Frost, H. R. (2018) · Bioinformatics · doi:10.1093/bioinformatics/bty217 · Cited by 30
Endothelial PRMT5 plays a crucial role in angiogenesis after acute ischemic injury
Ye, Q., Zhang, J., Zhang, C., Yi, B., Kazama, K., Liu, W., Sun, X., Liu, Y., & Sun, J. (2022) · JCI Insight · doi:10.1172/jci.insight.152481 · Cited by 31
Recent advances in large-scale protein interactome mapping
Mehta, V., & Trinkle‐Mulcahy, L. (2016) · F1000Research · doi:10.12688/f1000research.7629.1 · Cited by 34
A High-Efficiency Cellular Extraction System for Biological Proteomics
Dhabaria, A., Cifani, P., Reed, C., Steen, H., & Kentsis, A. (2015) · Journal of Proteome Research · doi:10.1021/acs.jproteome.5b00547 · Cited by 30
Immunoproteasome β5i‐Selective Dipeptidomimetic Inhibitors
Singh, P. K., Fan, H., Jiang, X., Shi, L., Nathan, C., & Lin, G. (2016) · ChemMedChem · doi:10.1002/cmdc.201600384 · Cited by 30
In-depth proteomic profiling of left ventricular tissues in human end-stage dilated cardiomyopathy
Liu, S., Xia, Y., Liu, X., Wang, Y., Chen, Z., Xie, J., Qian, J., Shen, H., & Yang, P. (2017) · Oncotarget · doi:10.18632/oncotarget.15689 · Cited by 30
Musunuru, K., Ingelsson, E., Fornage, M., Liu, P. X., Murphy, A. M., Newby, L. K., Newton‐Cheh, C., Perez, M. V., Voora, D., & Woo, D. (2017) · Circulation Cardiovascular Genetics · doi:10.1161/hcg.0000000000000037 · Cited by 31
Jaravine, V., Mösch, A., Raffegerst, S. H., Schendel, D. J., & Frishman, D. (2017) · BMC Cancer · doi:10.1186/s12885-017-3854-8 · Cited by 30
Platelet proteomics: from discovery to diagnosis
Looße, C., Swieringa, F., Heemskerk, J. W. M., Sickmann, A., & Lorenz, C. (2018) · Expert Review of Proteomics · doi:10.1080/14789450.2018.1480111 · Cited by 30
Omenn, G. S. (2021) · Molecular & Cellular Proteomics · doi:10.1016/j.mcpro.2021.100062 · Cited by 33
Alternative RNA Splicing—The Trojan Horse of Cancer Cells in Chemotherapy
Mehterov, N. H., Kazakova, M., Sbirkov, Y., Vladimirov, B., Belev, N., Yaneva, G. A., Todorova, K. O., Hayrabedyan, S., & Sarafian, V. S. (2021) · Genes · doi:10.3390/genes12071085 · Cited by 31
Towards Building a Quantitative Proteomics Toolbox in Precision Medicine: A Mini-Review
Rojo, A. C., Heylen, D., Aerts, J. A., Thas, O., Hooyberghs, J., Ertaylan, G., & Valkenborg, D. (2021) · Frontiers in Physiology · doi:10.3389/fphys.2021.723510 · Cited by 30
Propargylic Se-adenosyl- l -selenomethionine: A Chemical Tool for Methylome Analysis
Sohtome, Y., Shimazu, T., Shinkai, Y., & Sodeoka, M. (2021) · Accounts of Chemical Research · doi:10.1021/acs.accounts.1c00395 · Cited by 30
Serum Proteome Profiles in Stricturing Crohnʼs Disease
Townsend, P., Zhang, Q., Shapiro, J. M., Webb‐Robertson, B., Bramer, L., Schepmoes, A., Weitz, K., Mallette, M. M., Moniz, H., Bright, R., et al. (2015) · Inflammatory Bowel Diseases · doi:10.1097/mib.0000000000000445 · Cited by 30
Distler, U., Kuharev, J., & Tenzer, S. (2014) · Expert Review of Proteomics · doi:10.1586/14789450.2014.971114 · Cited by 31
Petit, F. G., Kervarrec, C., Jamin, S. P., Smagulova, F. O., Hao, C., Becker, E., Jégou, B., Chalmel, F., & Primig, M. (2015) · Biology of Reproduction · doi:10.1095/biolreprod.114.126250 · Cited by 30
Mining Large Scale Tandem Mass Spectrometry Data for Protein Modifications Using Spectral Libraries
Horlacher, O., Lisacek, F., & Müller, M. (2015) · Journal of Proteome Research · doi:10.1021/acs.jproteome.5b00877 · Cited by 31
Lautz, J. D., Brown, E., VanSchoiack, A., & Smith, S. E. P. (2018) · Journal of Neurochemistry · doi:10.1111/jnc.14466 · Cited by 29
Proteomic profiling of liver tissue from the mdx-4cv mouse model of Duchenne muscular dystrophy
Murphy, S., Zweyer, M., Henry, M. A., Meleady, P., Mundegar, R. R., Swandulla, D., & Ohlendieck, K. (2018) · Clinical Proteomics · doi:10.1186/s12014-018-9212-2 · Cited by 30
Functional unfoldomics: Roles of intrinsic disorder in protein (multi)functionality
Uversky, V. N. (2023) · Advances in protein chemistry and structural biology · doi:10.1016/bs.apcsb.2023.11.001 · Cited by 31
Yin, H., Duo, H., Li, S., Qin, D., Xie, L., Xiao, Y., Sun, J., Tao, J., Zhang, X., Li, Y., et al. (2024) · Journal of Advanced Research · doi:10.1016/j.jare.2024.12.004 · Cited by 34
The coming era of proteomics-driven precision medicine
Jiang, Y., Wang, J., Sun, A., Zhang, H., Yu, X., Qin, W., Ying, W., Li, Y., Chang, C., Wang, X., et al. (2025) · National Science Review · doi:10.1093/nsr/nwaf278 · Cited by 34
Spencer, C. T., Bezbradica, J. S., Ramos, M., Arico, C. D., Conant, S. B., Gilchuk, P., Gray, J. J., Zheng, M., Niu, X., Hildebrand, W. H., et al. (2015) · PROTEOMICS - CLINICAL APPLICATIONS · doi:10.1002/prca.201500106 · Cited by 30
Krisp, C., Yang, H., van Soest, R., & Molloy, M. P. (2015) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m114.046425 · Cited by 29
SKA1 overexpression is associated with poor prognosis in hepatocellular carcinoma
Chen, Y., Zhao, J., Jiao, Z., Wang, W., Wang, D., Yu, X., Shi, Z., Ge, N., Pan, Q., Xia, J., et al. (2018) · BMC Cancer · doi:10.1186/s12885-018-5119-6 · Cited by 29
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
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