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Structure-based prediction of protein–protein interactions on a genome-wide scale
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The genome-wide identification of pairs of interacting proteins is an important step in the elucidation of cell regulatory mechanisms. Much of our present knowledge derives from high-throughput techniques such as the yeast two-hybrid assay and affinity purification, as well as from manual curation of experiments on individual systems. A variety of computational approaches based, for example, on sequence homology, gene co-expression and phylogenetic profiles, have also been developed for the genome-wide inference of protein-protein interactions (PPIs). Yet comparative studies suggest that the development of accurate and complete repertoires of PPIs is still in its early stages. Here we show that three-dimensional structural information can be used to predict PPIs with an accuracy and coverage that are superior to predictions based on non-structural evidence. Moreover, an algorithm, termed PrePPI, which combines structural information with other functional clues, is comparable in accuracy to high-throughput experiments, yielding over 30,000 high-confidence interactions for yeast and over 300,000 for human. Experimental tests of a number of predictions demonstrate the ability of the PrePPI algorithm to identify unexpected PPIs of considerable biological interest. The surprising effectiveness of three-dimensional structural information can be attributed to the use of homology models combined with the exploitation of both close and remote geometric relationships between proteins.
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“More than 300 000 protein-protein interactions (PPIs) occur in human cells and they are involved in all physiological processes, including disease. 1”
From Chasing molecular glue degraders: screening approaches (2022) · cites this paper as [1]
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Gapped BLAST and PSI-BLAST: a new generation of protein database search programs
Altschul, S. (1997) · Nucleic Acids Research · doi:10.1093/nar/25.17.3389 · Cited by 73,302
Gene Ontology: tool for the unification of biology
Ashburner, M., Ball, C. A., Blake, J. A., Botstein, D., Butler, H., Cherry, J. M., Davis, A. P., Dolinski, K., Dwight, S. S., Eppig, J. T., et al. (2000) · Nature Genetics · doi:10.1038/75556 · Cited by 43,206
Berman, H. M. (2000) · Nucleic Acids Research · doi:10.1093/nar/28.1.235 · Cited by 40,196
Inference of Macromolecular Assemblies from Crystalline State
Krissinel, E., & Henrick, K. (2007) · Journal of Molecular Biology · doi:10.1016/j.jmb.2007.05.022 · Cited by 10,007
UniProt: the Universal Protein knowledgebase
Apweiler, R. (2003) · Nucleic Acids Research · doi:10.1093/nar/gkh131 · Cited by 7,593
Comparative assessment of large-scale data sets of protein–protein interactions
von Mering, C., Krause, R., Snel, ., Cornell, M. J., Oliver, S. G., Fields, S., & Peer Bork, B. (2002) · Nature · doi:10.1038/nature750 · Cited by 2,339
Interactome Networks and Human Disease
Vidal, M., Cusick, M. E., & Barabási, A.-L. (2011) · Cell · doi:10.1016/j.cell.2011.02.016 · Cited by 1,771
von Mering, C. (2004) · Nucleic Acids Research · doi:10.1093/nar/gki005 · Cited by 1,768
High-Quality Binary Protein Interaction Map of the Yeast Interactome Network
Yu, H., Braun, P., Yıldırım, M. A., Lemmens, I., Venkatesan, K., Sahalie, J., Hirozane-Kishikawa, T., Gebreab, F., Li, N., Simonis, N., et al. (2008) · Science · doi:10.1126/science.1158684 · Cited by 1,392
A Bayesian Networks Approach for Predicting Protein-Protein Interactions from Genomic Data
Jansen, R., Yu, H., Greenbaum, D. S., Kluger, Y., Krogan, N. J., Chung, S., Emili, A., Snyder, M. P., Greenblatt, J. F., & Gerstein, M. (2003) · Science · doi:10.1126/science.1087361 · Cited by 1,254
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Zhou, T., Wang, S., Song, X., Liu, W., Dong, F., Huo, Y., Zou, R., Wang, C., Zhang, S., Liu, W., et al. (2022) · Cell Death and Disease · doi:10.1038/s41419-022-04787-9 · Cited by 14
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Baxter, D., Ullman, C. G., & Mason, J. M. (2014) · Future Medicinal Chemistry · doi:10.4155/fmc.14.134 · Cited by 14
Soner, S., Özbek, P., Garzón, J. I., Ben‐Tal, N., & Haliloǧlu, T. (2015) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1004461 · Cited by 14
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Gaínza, P., Sverrisson, F., Monti, F., Rodolà, E., Bronstein, M., & Correia, B. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/606202 · Cited by 13
Chakravarty, D., McElfresh, G., Kundrotas, P. J., & Vakser, I. A. (2020) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.25875 · Cited by 13
Emvirus: An embedding-based neural framework for human-virus protein-protein interactions prediction
Xie, P., Zhuang, J., Tian, G., & Yang, J. (2023) · Biosafety and Health · doi:10.1016/j.bsheal.2023.04.003 · Cited by 13
Prediction of protein‐protein interactions using stacked auto‐encoder
Jha, K., Saha, S., & Tanveer, M. (2021) · Transactions on Emerging Telecommunications Technologies · doi:10.1002/ett.4256 · Cited by 13
Normalized L3-based link prediction in protein–protein interaction networks
Yuen, H. Y., & Jansson, J. (2023) · BMC Bioinformatics · doi:10.1186/s12859-023-05178-3 · Cited by 13
Improved Protein–Protein Interaction Assay FlimPIA by the Entrapment of Luciferase Conformation
Ohmuro‐Matsuyama, Y., Hara, Y., & Ueda, H. (2013) · Analytical Chemistry · doi:10.1021/ac403065v · Cited by 14
Ramakrishnan, G., Srinivasan, N., Padmapriya, P., & Vasant Natarajan, A. (2015) · Bioinformatics and Biology Insights · doi:10.4137/bbi.s31880 · Cited by 12
Review of Recent Protein-Protein Interaction Techniques
Shatnawi, M. (2015) · Elsevier eBooks · doi:10.1016/b978-0-12-802508-6.00006-5 · Cited by 13
Protein–Protein Interface and Disease: Perspective from Biomolecular Networks
Hu, G., Xiao, F., Li, Y., Li, Y., & Vongsangnak, W. (2016) · Advances in biochemical engineering, biotechnology · doi:10.1007/10_2016_40 · Cited by 13
Leveraging Stacked Denoising Autoencoder in Prediction of Pathogen-Host Protein-Protein Interactions
Chen, H., Shen, J., Wang, L., & Song, J. (2017) · IEEE International Congress on Big Data (BigData Congress) · doi:10.1109/bigdatacongress.2017.54 · Cited by 13
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Zeng, J., Yang, Z., Xu, D., Song, J., Liu, Y., Qin, J., & Weng, Z. (2023) · Inflammation · doi:10.1007/s10753-023-01893-4 · Cited by 12
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Ballerini, C., Amoriello, R., Maghrebi, O., Bellucci, G., Addazio, I., Betti, M., Aprea, M. G., Masciulli, C., Caporali, A., Penati, V., et al. (2025) · Frontiers in Immunology · doi:10.3389/fimmu.2025.1557483 · Cited by 12
Isvoran, A., Crăciun, D., Martiny, V. Y., Spérandio, O., & Miteva, M. A. (2013) · BMC Pharmacology and Toxicology · doi:10.1186/2050-6511-14-31 · Cited by 12
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Chen, H., Shen, J., Wang, L., & Song, J. (2020) · Journal of Ambient Intelligence and Humanized Computing · doi:10.1007/s12652-020-01715-7 · Cited by 12
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Pei, F., Shi, Q., Zhang, H., & Bahar, İ. (2021) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.1c00173 · Cited by 14
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Hsieh, J., Molusky, M. M., McCabe, K. M., Fotakis, P., Xiao, T., Tascau, L., Zeana-Schliep, L., DaSilva-Jardine, P. A., & Tall, A. R. (2021) · Journal of Hepatology · doi:10.1016/j.jhep.2021.09.021 · Cited by 12
Khandelwal, M., Rout, R. K., & Umer, S. (2022) · International Conference on Cloud Computing, Data Science & Engineering (Confluence) · doi:10.1109/confluence52989.2022.9734190 · Cited by 12
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Vangone, A., Oliva, R., Cavallo, L., & Bonvin, A. M. J. J. (2017) · Springer eBooks · doi:10.1007/978-94-024-1069-3_8 · Cited by 13
Proteome-level assessment of origin, prevalence and function of leucine-aspartic acid (LD) motifs
Alam, T., Alazmi, M., Naser, R., Huser, F., Momin, A. A., Astro, V., Hong, S., Walkiewicz, K. W., Canlas, C. G., Huser, R., et al. (2019) · Bioinformatics · doi:10.1093/bioinformatics/btz703 · Cited by 12
Emery, A., Hardwick, B. S., Crooks, A. T., Milech, N., Watt, P. M., Mithra, C., Kumar, V., Giridharan, S., Sadasivam, G., Mathivanan, S., et al. (2021) · Cell chemical biology · doi:10.1016/j.chembiol.2021.05.009 · Cited by 12
From local structure to a global framework: recognition of protein folds
Joseph, A. P., & de Brevern, A. G. (2014) · Journal of The Royal Society Interface · doi:10.1098/rsif.2013.1147 · Cited by 13
ZEPPI: Proteome-scale sequence-based evaluation of protein–protein interaction models
Zhao, H., Petrey, D. S., Murray, D., & Honig, B. H. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2400260121 · Cited by 13
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Nilsson, A., Meimetis, N., & Lauffenburger, D. A. (2025) · npj Precision Oncology · doi:10.1038/s41698-025-00822-y · Cited by 11
Fick, A., Fick, J. L. M., Swart, V., & van den Berg, N. (2025) · The Plant Journal · doi:10.1111/tpj.70169 · Cited by 16
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Lin, S., Yin, Y. A., Jiang, X., Sahni, N., & Yi, S. S. (2016) · BioMed Research International · doi:10.1155/2016/6186281 · Cited by 12
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Zeng, C., Zhan, W., & Deng, L. (2018) · Database · doi:10.1093/database/bay064 · Cited by 11
Self-citationChen, Z., You, Z., Zhang, W., Wang, Y.-B., Cheng, L., & Alghazzawi, D. (2019) · Genes · doi:10.3390/genes10110924 · Cited by 11
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Pérez-Bercoff, Å., Hudson, C. M., & Conant, G. C. (2013) · PLoS ONE · doi:10.1371/journal.pone.0052581 · Cited by 11
Ohmuro‐Matsuyama, Y., Nakano, K., Kimura, A., Ayabe, K., Ihara, M., Wada, T., & Ueda, H. (2013) · Analytical Chemistry · doi:10.1021/ac4016825 · Cited by 12
Tan, X., Worley, J., Turunen, M. M., Wong, K., Fernández, E. C., Paull, E., Jones, S. J., Wang, J., Noh, H., Salvatori, B., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.06.28.449297 · Cited by 12
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Huang, J., Li, W., Xiao, B., Zhao, C., Zheng, H., Li, Y., & Wang, J. (2024) · iScience · doi:10.1016/j.isci.2024.110850 · Cited by 10
Samarasinghe, K., Kotlyar, M., Vallet, S. D., Hayes, C. A., Naba, A., Jurišica, I., Lisacek, F., & Ricard‐Blum, S. (2024) · Nucleic Acids Research · doi:10.1093/nar/gkae1088 · Cited by 10
Li, P., Shao, B., Zhao, G., & Liu, Z.-P. (2025) · BMC Biology · doi:10.1186/s12915-025-02231-w · Cited by 10
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Laer, B. V., Kapp, U., Soler‐López, M., Moczulska, K. E., Pääbo, S., Leonard, G. A., & Mueller‐Dieckmann, C. (2018) · Scientific Reports · doi:10.1038/s41598-018-36195-5 · Cited by 10
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Larsen, S. J., Schmidt, H. H. H. W., & Baumbach, J. (2020) · Systems Medicine · doi:10.1089/sysm.2019.0008 · Cited by 10
Palfi, A., Yesmambetov, A., Humphries, P., Hokamp, K., & Farrar, G. J. (2020) · Frontiers in Neuroscience · doi:10.3389/fnins.2020.00656 · Cited by 10
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Stokes, M. E., Vasciaveo, A., Small, J. C., Zask, A., Reznik, E., Smith, N., Wang, Q., Daniels, J., Forouhar, F., Rajbhandari, P., et al. (2023) · Cell chemical biology · doi:10.1016/j.chembiol.2023.11.007 · Cited by 9
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Rogers, J. R., Nikolényi, G., & AlQuraishi, M. (2023) · Protein Engineering Design and Selection · doi:10.1093/protein/gzad023 · Cited by 12
Liu, Q., Cantu, J. C., Zhu, J., Liebler, D. C., Marnett, L. J., & Zhang, B. (2013) · Molecular BioSystems · doi:10.1039/c3mb70114j · Cited by 9
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Avella-Oliver, M., Giménez-Romero, D., Morais, S., Martínez, M. Á. G., Bueno, P. R., Puchades, R., & Maquieira, Á. (2013) · Chemical Communications · doi:10.1039/c3cc44018d · Cited by 9
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Shelanski, M. L., Shin, W., Aubry, S., Sims, P. A., Alvarez, M. J., & Califano, A. (2015) · Neurotherapeutics · doi:10.1007/s13311-014-0335-5 · Cited by 9
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Kundrotas, P. J., Kotthoff, I., Choi, S. W., Copeland, M. M., & Vakser, I. A. (2020) · Methods in molecular biology · doi:10.1007/978-1-0716-0708-4_17 · Cited by 8
Xu, H., Xu, D., Zhang, N., Zhang, Y., & Gao, R. (2021) · Journal of Proteome Research · doi:10.1021/acs.jproteome.0c00871 · Cited by 9
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Li, Y., Xu, J., Chen, H., Zhao, Z., Li, S., Bai, J., Wu, A., Jiang, C., Wang, Y., Su, B., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0065871 · Cited by 9
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Zhao, S., Yang, X., Zeng, Z., Qian, P., Zhao, Z., Dai, L., Prabhu, N., Nordlund, P., & Tam, W. L. (2024) · Scientific Reports · doi:10.1038/s41598-024-51193-6 · Cited by 8
Marinis, Y. Z. D., Sun, J., Bompada, P., Omella, J. D., Luan, C., Halu, A., Renström, E., Sharma, A., & Ridderstråle, M. (2017) · Obesity · doi:10.1002/oby.21899 · Cited by 8
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Dhusia, K., Raja, K., Thomas, P. P. M., Yadav, P. K., & Ramteke, P. W. (2018) · Infection Genetics and Evolution · doi:10.1016/j.meegid.2018.11.001 · Cited by 8
Li, F., Du, Z., Huang, X., Dong, C., & Ren, J. (2021) · Analytical Chemistry · doi:10.1021/acs.analchem.0c03521 · Cited by 9
Khazen, G., Gyulkhandanian, A., Issa, T., & Maroun, R. C. (2021) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2021.09.013 · Cited by 8
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Johnson, M. E., & Hummer, G. (2013) · The Journal of Physical Chemistry B · doi:10.1021/jp402944e · Cited by 8
Daou, L., & Hanna, E. M. (2024) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2024.10.009 · Cited by 8
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Mou, M., Lu, M., Zhou, Z., Ren, Y., Yu, X., Pan, Z., Zhou, Y., Yang, H., Zheng, L., Shukai, G., et al. (2025) · Advanced Science · doi:10.1002/advs.202516530 · Cited by 9
Huang, L., Liao, L., & Wu, C. H. (2016) · BMC Systems Biology · doi:10.1186/s12918-016-0296-x · Cited by 7
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Andrews, F. H., Rogers, M. P., Paul, L. N., & McLeish, M. J. (2014) · Biochemistry · doi:10.1021/bi500081r · Cited by 7
Zhang, H., Wu, P.-Y., Ma, M., Ye, Y., Yang, H., Yang, J., Yin, S., Sun, C., Phan, J. H., Wang, M. D., et al. (2013) · Nanomedicine Nanotechnology Biology and Medicine · doi:10.1016/j.nano.2013.05.015 · Cited by 7
Wang, S., Fu, L., Zhang, S. Y., Tian, M., Zhang, L., Zheng, Y., Wang, J., Huang, J. M., & Ouyang, L. (2014) · Cell Proliferation · doi:10.1111/cpr.12157 · Cited by 7
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Qin, S., & Zhou, H. (2013) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.24366 · Cited by 7
Structure‐based protein‐protein interaction networks and drug design
Naveed, H., & Han, J. J. (2013) · Quantitative Biology · doi:10.1007/s40484-013-0018-y · Cited by 8
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Ma, W., Bao, W., Cao, Y., Yang, B., & Chen, Y. (2021) · Lecture notes in computer science · doi:10.1007/978-3-030-84532-2_59 · Cited by 7
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Janin, J., Wodak, S. J., Lensink, M. F., & Velankar, S. S. (2015) · Reviews in computational chemistry · doi:10.1002/9781118889886.ch4 · Cited by 7
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Hamon, V., & Morelli, X. (2013) · doi:10.4155/ebo.13.193 · Cited by 7
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Mohseni, A., Fan, L., Gao, L., Segal, J., & Roddick, F. (2024) · Environmental Science Water Research & Technology · doi:10.1039/d4ew00160e · Cited by 6
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Chen, Z., You, Z., Li, L., Wang, Y., Qiu, Y., & Hu, P. (2019) · BMC Genomics · doi:10.1186/s12864-019-6301-1 · Cited by 6
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Mewara, B., & Lalwani, S. (2023) · Research on Biomedical Engineering · doi:10.1007/s42600-023-00273-z · Cited by 6
Huang, L., Liao, L., & Wu, C. H. (2015) · IEEE International Conference on Bioinformatics and Biomedicine (BIBM) · doi:10.1109/bibm.2015.7359681 · Cited by 6
Predicting physiologically relevant SH3 domain mediated protein–protein interactions in yeast
Jain, S., & Bader, G. D. (2016) · Bioinformatics · doi:10.1093/bioinformatics/btw045 · Cited by 6
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Metadata
- Authors
- Zhang, Q. C., Petrey, D., Deng, L., Qiang, L., Shi, Y., Thu, C. A., Bisikirska, B., Lefebvre, C., Accili, D., Hunter, T., Maniatis, T., Califano, A., & Honig, B.
- Affiliations
- Howard Hughes Medical Institute (US)
- Tongji University (CN)
- Salk Institute for Biological Studies (US)
- Columbia University (US)
- Corresponding author
- Califano, Andrea
- Honig, Barry
- ORCID
- Venue
- Nature
- Published
- 2012-09-30
- Volume
- 490
- Issue
- 7421
- Pages
- 556-560
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- PMC
- PMC3482288
- OpenAlex
- W2039473152
- Cited by
- 723
- References
- 45
- Citations by year
- 2026: 23 · 2025: 35 · 2024: 42 · 2023: 30 · 2022: 55 · 2021: 62 · 2020: 47 · 2019: 43 · 2018: 52 · 2017: 56 · 2016: 59 · 2015: 81 · 2014: 62 · 2013: 71 · 2012: 5
- FWCI
- 28.39
- Type
- journal article
- Language
- en
- Update notices
- correction (2013-03-06)
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- Funders
- Howard Hughes Medical Institute
- National Cancer Institute (U54CA121852, CA082683, CA121852., R01CA082683)
- National Institute of General Medical Sciences (R01GM030518, GM030518, R37GM030518, GM094597, U54GM094597)
- National Institute of Diabetes and Digestive and Kidney Diseases (R01DK057539, DK057539)
- National Institute of Neurological Disorders and Stroke (R01NS043915)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Bioinformatics and Genomic Networks
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Machine Learning in Bioinformatics
- Keywords
- protein-protein interaction, protein-protein interaction prediction, protein structure, protein-protein interaction network, homology model, remote homology, yeast, human interactome, cell regulation
- MeSH terms
- Algorithms, Animals, Bayes Theorem, Brain, Humans, Models, Molecular, Phylogeny, Protein Binding, Protein Conformation, Protein Kinases, Proteins, ROC Curve, Saccharomyces cerevisiae, Transcription Factors, Reproducibility of Results, Cadherins, Proteome, Protein Interaction Mapping, Matrix Attachment Region Binding Proteins, Proteomics, PPAR gamma, Suppressor of Cytokine Signaling Proteins, Mice, High-Throughput Screening Assays, Protein Interaction Maps
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