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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]
The check wasn’t confident either way, so it gives no verdict — never disputed.
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]
Experimental — accuracy not yet measuredIn 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
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Shiferaw, G. A., Vandermarliere, E., Hulstaert, N., Gabriels, R., Martens, L., & Volders, P. (2020) · Journal of Proteome Research · doi:10.1021/acs.jproteome.9b00743 · Cited by 23
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Takemori, A., Ishizaki, J., Nakashima, K., Shibata, T., Kato, H., Kodera, Y., Suzuki, T., Hasegawa, H., & Takemori, N. (2020) · Journal of Proteome Research · doi:10.1021/acs.jproteome.0c00749 · Cited by 23
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Hong, J. M., Gibbons, M., Bashir, A., Wu, D., Shao, S. J., Cutts, Z., Chavarha, M., Chen, Y., Schiff, L., Foster, M., et al. (2021) · iScience · doi:10.1016/j.isci.2021.103586 · Cited by 23
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Martínez‐Val, A., Guzmán, U. H., & Olsen, J. V. (2022) · Annual Review of Genomics and Human Genetics · doi:10.1146/annurev-genom-112921-024948 · Cited by 23
Hou, Y., Sun, X., Gheinani, P. T., Guan, X., Sharma, S., Zhou, Y., Jin, C., Yang, Z., Naren, A. P., Yin, J., et al. (2022) · Cellular and Molecular Gastroenterology and Hepatology · doi:10.1016/j.jcmgh.2022.05.006 · Cited by 23
Dowling, P., Swandulla, D., & Ohlendieck, K. (2023) · Cells · doi:10.3390/cells12212560 · Cited by 22
Adeola, H. A., Soares, N. C., Paccez, J. D., Kaestner, L., Blackburn, J. M., & Zerbini, L. F. (2015) · PROTEOMICS - CLINICAL APPLICATIONS · doi:10.1002/prca.201400197 · Cited by 23
Li, J., Zhao, W., Shen, Z., Yuan, T., Liu, S., Liu, Q., Fu, Y., & Sun, W. (2015) · PLoS ONE · doi:10.1371/journal.pone.0119350 · Cited by 23
Olow, A., Chen, Z., Niedner, R. H., Wolf, D. M., Yau, C. S. F., Pankov, A., Lee, E. P. R., Swigart, L. B., Veer, L. V. ‘., & Coppé, J. (2016) · Cancer Research · doi:10.1158/0008-5472.can-15-2325-t · Cited by 22
Yang, C. L., Liu, Y., Zhang, Y., Wang, J., Tian, L., Yan, Y., Cao, W., & Wang, Y. (2017) · PROTEOMICS · doi:10.1002/pmic.201600284 · Cited by 23
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Igarashi, M., Takeuchi, K., & Sugiyama, S. (2017) · Neurochemistry International · doi:10.1016/j.neuint.2017.10.001 · Cited by 22
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Shu, W., & Du, H. (2020) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2020.188465 · Cited by 23
Degroeve, S., Gabriels, R., Velghe, K., Bouwmeester, R., Tichshenko, N., & Martens, L. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.07.02.450686 · Cited by 24
Fang, X., Yang, Y., Wang, H., & Xu, H. Y. (2024) · Mechanobiology in Medicine · doi:10.1016/j.mbm.2024.100063 · Cited by 21
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Zhu, K., Shao, J., Tao, H., Yan, X., Luo, C., Zhang, H., & Duan, W. (2019) · Journal of Computer-Aided Molecular Design · doi:10.1007/s10822-019-00214-y · Cited by 23
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Caligiore, F., Zangelmi, E., Vetro, C., Kentache, T., Dewulf, J. P., Veiga‐da‐Cunha, M., SCHAFTINGEN, E. V., Bommer, G. T., & Peracchi, A. (2022) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-022-04439-3 · Cited by 23
Cobley, J. N. (2023) · BioEssays · doi:10.1002/bies.202200248 · Cited by 25
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Banks, C. A. S., Boanca, G., Lee, Z. T., Florens, L. A., & Washburn, M. P. (2015) · Scientific Reports · doi:10.1038/srep08530 · Cited by 22
Liu, X., Wang, Y., Yang, W., Guan, Z., Yu, W., & Liao, D. J. (2016) · Progress in Histochemistry and Cytochemistry · doi:10.1016/j.proghi.2016.11.001 · Cited by 22
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Yang, Y. Z., Zhao, Y., Yang, L., Yu, L. P., Wang, H., & Ji, X. S. (2017) · Comparative Biochemistry and Physiology Part B Biochemistry and Molecular Biology · doi:10.1016/j.cbpb.2017.12.012 · Cited by 22
Espinoza, J. A., Riquelme, I., Sagredo, E. A., Rosa, L., García, P., Bizama, C., Apud‐Bell, M., Leal, P., Weber, H. L., Benavente, F. M., et al. (2018) · Histopathology · doi:10.1111/his.13797 · Cited by 22
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Chakraborty, S., Andrieux, G., Hasan, A. M. M., Ahmed, M., Hosen, M. I., Rahman, T., Hossain, M. A., & Boerries, M. (2019) · Scientific Reports · doi:10.1038/s41598-019-48774-1 · Cited by 23
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Mitchell, C. J., Kim, M., Zhong, J., Nirujogi, R. S., Bose, A. K., & Pandey, A. (2016) · Molecular Oncology · doi:10.1016/j.molonc.2016.03.003 · Cited by 22
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BURT, C. H., & Simons, R. L. (2015) · Criminology · doi:10.1111/1745-9125.12060 · Cited by 21
Michel, A. M., Ahern, A. M., Donohue, C. A., & Baranov, P. V. (2015) · PROTEOMICS · doi:10.1002/pmic.201400603 · Cited by 21
Fu, S., Liu, X., Luo, M., Xie, K., Nice, E. C., Zhang, H., & Huang, C. (2017) · Expert Review of Proteomics · doi:10.1080/14789450.2017.1299006 · Cited by 22
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Lin, A., Howbert, J. J., & Noble, W. S. (2018) · Journal of Proteome Research · doi:10.1021/acs.jproteome.8b00206 · Cited by 21
Gale, T. V., Horton, T. M., Hoffmann, A. R., Branco, L. M., & Garry, R. F. (2018) · Journal of Proteome Research · doi:10.1021/acs.jproteome.8b00204 · Cited by 22
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Claridge, B., Kastaniegaard, K., Stensballe, A., & Greening, D. W. (2018) · Expert Review of Proteomics · doi:10.1080/14789450.2019.1551135 · Cited by 21
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Suhre, K., & Zaghlool, S. B. (2021) · Journal of Internal Medicine · doi:10.1111/joim.13306 · Cited by 23
Zhong, L. L. D., Zhu, L., & Cai, Z. (2021) · Journal of Analysis and Testing · doi:10.1007/s41664-021-00197-6 · Cited by 22
Protein Lipidation Types: Current Strategies for Enrichment and Characterization
Wang, R., & Chen, Y. Q. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23042365 · Cited by 25
Shabestari, S. A. S., Nassir, N., Sopariwala, S., Karimov, I., Tambi, R., Zehra, B., Kosaji, N., Akter, H., Berdiev, B. K., & Uddin, M. J. (2022) · Human Genetics · doi:10.1007/s00439-022-02482-5 · Cited by 21
Carreras‐Badosa, G., Maslovskaja, J., Vaher, H., Pajusaar, L., Annilo, T., Lättekivi, F., Hübenthal, M., Rodríguez, E., Weidinger, S., Kingo, K., et al. (2022) · Scientific Reports · doi:10.1038/s41598-022-27235-2 · Cited by 21
Proteomics: A groundbreaking development in cancer biology
Mir, M. A., Qayoom, H., Sofi, S., & Jan, N. (2023) · Elsevier eBooks · doi:10.1016/b978-0-323-95072-5.00004-3 · Cited by 21
Linares-Pineda, T., Peña-Montero, N., Fragoso-Bargas, N., Gutiérrez-Repiso, C., Lima-Rubio, F., Suárez-Arana, M., Sánchez-Pozo, A., Tinahones, F., Molina-Vega, M., Picón-César, M. J., et al. (2023) · Clinical Epigenetics · doi:10.1186/s13148-023-01523-8 · Cited by 23
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Kurgan, N., Larsen, J. K., & Deshmukh, A. S. (2024) · Diabetologia · doi:10.1007/s00125-024-06097-5 · Cited by 22
Lichti, C. F., Mostovenko, E., Wadsworth, P. A., Lynch, G. C., Pettitt, B. M., Sulman, E. P., Wang, Q., Lang, F. F., Rezeli, M., Marko‐Varga, G., et al. (2014) · Journal of Proteome Research · doi:10.1021/pr500810g · Cited by 21
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Rizzo, J. M., Romano, R., Bard, J., & Sinha, S. (2014) · Journal of Investigative Dermatology · doi:10.1038/jid.2014.384 · Cited by 21
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Liu, C., Atkinson, M. A., & Zhang, Q. (2016) · PROTEOMICS · doi:10.1002/pmic.201500333 · Cited by 21
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Trpevski, I., Dimitrova, T., Boshkovski, T., Stikov, N., & Kocarev, L. (2016) · Scientific Reports · doi:10.1038/srep37057 · Cited by 21
Jia, Y., Chen, L., Ma, Y., Zhang, J., Xu, N., & Liao, D. J. (2015) · International Journal of Biological Sciences · doi:10.7150/ijbs.13436 · Cited by 21
Pang, R., Qiu, J., Li, T., Pan, Y., Yue, L., Pan, Y., & Zhang, W. (2017) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2017.03.011 · Cited by 21
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Zhou, L., Wong, L., & Goh, W. W. B. (2017) · Drug Discovery Today · doi:10.1016/j.drudis.2017.11.011 · Cited by 22
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Szklanna, P. B., Parsons, M. E. M., Wynne, K. J., O’Connor, H., Egan, K., Allen, S., Áinle, F. N., & Maguire, P. B. (2018) · PROTEOMICS - CLINICAL APPLICATIONS · doi:10.1002/prca.201800162 · Cited by 22
Mandad, S., Rahman, R., Centeno, T. P., Vidal, R. O., Wildhagen, H., Rammner, B., Keihani, S., Opazo, F., Urban, I., Ischebeck, T., et al. (2018) · Scientific Reports · doi:10.1038/s41598-018-35277-8 · Cited by 21
Zhou, Q., Andersson, R. E., Hu, D., Bauden, M. P., Sasor, A., Bygott, T., Pawłowski, K., Plá, I., Marko‐Varga, G., & Ansari, D. (2019) · Translational research · doi:10.1016/j.trsl.2019.06.003 · Cited by 21
Kim, H., Dan, K., Shin, H., Lee, J. H., Wang, J. I., & Han, D. (2019) · Analytical Methods · doi:10.1039/c9ay01269a · Cited by 21
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Slater, O., Miller, B., & Kontoyianni, M. (2020) · Current Topics in Medicinal Chemistry · doi:10.2174/1568026620666200226105312 · Cited by 21
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Jiang, X. G., Lai, X., Lu, J., Tang, L.-Z., Zhang, J., & Liu, H. (2021) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2020.12.108 · Cited by 21
Zhang, Y., Xu, T., Shan, B., Hart, J. R., Aslanian, A., Han, X., Zong, C., Li, H., Choi, H., Wang, D., et al. (2015) · Journal of Proteomics · doi:10.1016/j.jprot.2015.07.006 · Cited by 21
Vidalain, P., Jacob, Y., Hagemeijer, M. C., Jones, L. M., Neveu, G., Roussarie, J.-P., Rottier, P. J. M., Tangy, F., & de Haan, C. A. M. (2015) · Methods in molecular biology · doi:10.1007/978-1-4939-2438-7_18 · Cited by 21
Fondrie, W. E., & Noble, W. S. (2020) · Journal of Proteome Research · doi:10.1021/acs.jproteome.9b00780 · Cited by 21
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Self-citationLiu, Y., Liu, N., & Liu, Q. (2021) · Aging · doi:10.18632/aging.202486 · Cited by 20
Stuparević, I., Novačić, A., Rahmouni, A. R., Fernandez, A., Lamb, N. J. C., & Primig, M. (2021) · Biological reviews/Biological reviews of the Cambridge Philosophical Society · doi:10.1111/brv.12693 · Cited by 23
Lu, Y., 宁波大学海洋学院, 浙. 宁. 3., Liu, Q., Liu, K., Wang, H., Li, C., Wang, Q., Shao, C., 中国水产科学院黄海水产研究所, 农., 青岛海洋科学与技术试点国家实验室, 海., et al. (2022) · 动物学研究 · doi:10.24272/j.issn.2095-8137.2021.406 · Cited by 20
Zhou, Q., Shu, X., Chai, Y., Liu, W., Li, Z., & Xi, Y. (2023) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2023.114807 · Cited by 21
Metabolic-Associated Fatty Liver Disease and Insulin Resistance: A Review of Complex Interlinks
Barber, T. M., Kabisch, S., Pfeiffer, A. F. H., & Weickert, M. O. (2023) · Metabolites · doi:10.3390/metabo13060757 · Cited by 22
A peptide resource for the analysis of Staphylococcus aureus in host–pathogen interaction studies
Depke, M., Michalik, S., Rabe, A., Surmann, K., Brinkmann, L., Jehmlich, N., Bernhardt, J., Hecker, M., Wollscheid, B., Sun, Z., et al. (2015) · PROTEOMICS · doi:10.1002/pmic.201500091 · Cited by 20
Forward Individualized Medicine from Personal Genomes to Interactomes
Zhang, X., Kuivenhoven, J. A., & Groen, A. K. (2015) · Frontiers in Physiology · doi:10.3389/fphys.2015.00364 · Cited by 22
Tenzer, S., Leidinger, P., Backes, C., Huwer, H., Hildebrandt, A., Lenhof, H., Wesse, T., Franke, A., Meese, E. U., & Keller, A. (2016) · Oncotarget · doi:10.18632/oncotarget.7562 · Cited by 20
Alternative splicing shapes transcriptome but not proteome diversity in Physcomitrella patens
Fesenko, I. A., Khazigaleeva, R., Kirov, I. V., Kniazev, A., Glushenko, O. E., Babalyan, K., Arapidi, G. P., Shashkova, T., Butenko, I., Zgoda, V. G., et al. (2017) · Scientific Reports · doi:10.1038/s41598-017-02970-z · Cited by 19
Booth, K. T. A., Azaiez, H., Jahan, I., Smith, R. J., & Fritzsch, B. (2018) · Frontiers in Genetics · doi:10.3389/fgene.2018.00156 · Cited by 20
Systems biology and gene networks in Alzheimer’s disease
Wang, Z.-T., Tan, C., Tan, L., & Yu, J. (2018) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2018.11.007 · Cited by 20
Kim, N., Yu, L., Dawe, R. J., Petyuk, V., Gaiteri, C., Jager, P. L. D., Schneider, J. A., Arfanakis, K., & Bennett, D. A. (2019) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2019.07.013 · Cited by 20
Chen, D., Ning, Z., Chen, H., Lu, C., Liu, X., Xia, T., Qi, H., Wang, W., Ling, T., Guo, X., et al. (2019) · Oncogene · doi:10.1038/s41388-019-1002-4 · Cited by 20
Ding, Y., Zhong, T., Wang, M., Xiang, X., Ren, G., Jia, Z., Lin, Q., Liu, Q., Dong, J., Li, L., et al. (2019) · Frontiers in Oncology · doi:10.3389/fonc.2019.00956 · Cited by 20
Engineered ChymotrypsiN for Mass Spectrometry-Based Detection of Protein Glycosylation
Ramesh, B., Abnouf, S., Mali, S., Moree, W. J., Patil, U., Bark, S. J., & Varadarajan, N. (2019) · ACS Chemical Biology · doi:10.1021/acschembio.9b00506 · Cited by 20
Kitazawa, M., Hatta, T., Sasaki, Y., Fukui, K., Ogawa, K., Fukuda, E., Goshima, N., Okita, N. T., Yamada, Y., Nakagama, H., et al. (2019) · Cancer Science · doi:10.1111/cas.14275 · Cited by 20
Wei, R., Gao, B., Shih, F. F., Ranger, A. M., Dearth, A. T., Mischak, H., Siwy, J., Wisniacki, N., Petri, M., & Burkly, L. C. (2016) · Nephrology Dialysis Transplantation · doi:10.1093/ndt/gfw446 · Cited by 20
Lee, S., Hadipour‐Lakmehsari, S., Kim, D. H., Paola, M. D., Kuzmanov, U., Shah, S., Lee, J., Kislinger, T., Sharma, P., Oudit, G. Y., et al. (2020) · Scientific Data · doi:10.1038/s41597-020-00762-1 · Cited by 20
Hasenauer, A., Bevc, K., McCabe, M. C., Chansoria, P., Saviola, A. J., Hansen, K. C., Christman, K. L., & Zenobi‐Wong, M. (2025) · Science Advances · doi:10.1126/sciadv.adu5793 · Cited by 19
Colangelo, C. M., Ivosev, G., Chung, L. M., Abbott, T. B., Shifman, M. A., Sakaue, F., Cox, D., Kitchen, R. R., Burton, L., Tate, S. A., et al. (2014) · PROTEOMICS · doi:10.1002/pmic.201400353 · Cited by 19
Phenome-genome association studies of pancreatic cancer: new targets for therapy and diagnosis.
Narayanan, R. (2015) · PubMed · Cited by 18
Prediction of a Missing Protein Expression Map in the Context of the Human Proteome Project
Guruceaga, E., del Pino, M. M. S., Corrales, F. J., & Segura, V. (2015) · Journal of Proteome Research · doi:10.1021/pr500850u · Cited by 19
Szulik, M. W., Davis, K., Bakhtina, A. A., Azarcon, P., Bia, R. D., Horiuchi, E., & Franklin, S. (2020) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00382.2020 · Cited by 19
Praissman, J. L., & Wells, L. (2021) · Molecular & Cellular Proteomics · doi:10.1016/j.mcpro.2021.100103 · Cited by 19
The next “sweet” spot for pancreatic ductal adenocarcinoma: Glycoprotein for early detection
Xu, Y., Wang, Y., Höti, N., Clark, D. J., Chen, S., & Zhang, H. (2021) · Mass Spectrometry Reviews · doi:10.1002/mas.21748 · Cited by 22
Myokine-mediated exercise effects: the role of myokine meteorin-like hormone (Metrnl)
Alizadeh, H. (2021) · Growth Factors · doi:10.1080/08977194.2022.2032689 · Cited by 22
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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