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The BioPlex Network: A Systematic Exploration of the Human Interactome
Open accessAbstract
Protein interactions form a network whose structure drives cellular function and whose organization informs biological inquiry. Using high-throughput affinity-purification mass spectrometry, we identify interacting partners for 2,594 human proteins in HEK293T cells. The resulting network (BioPlex) contains 23,744 interactions among 7,668 proteins with 86% previously undocumented. BioPlex accurately depicts known complexes, attaining 80%-100% coverage for most CORUM complexes. The network readily subdivides into communities that correspond to complexes or clusters of functionally related proteins. More generally, network architecture reflects cellular localization, biological process, and molecular function, enabling functional characterization of thousands of proteins. Network structure also reveals associations among thousands of protein domains, suggesting a basis for examining structurally related proteins. Finally, BioPlex, in combination with other approaches, can be used to reveal interactions of biological or clinical significance. For example, mutations in the membrane protein VAPB implicated in familial amyotrophic lateral sclerosis perturb a defined community of interactors.
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“It comprises two sub-assemblies: Retriever composed of VPS35L, VPS26C, and VPS29; and the CCC complex which contains twelve subunits: COMMD1-COMMD10 and the coiled-coil domain-containing (CCDC) proteins CCDC22 and CCDC93.”
From Structure of the endosomal Commander complex linked to Ritscher-Schinzel syndrome (2023) · cites this paper as [19]
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In the citing paper
“The CCC complex comprises twelve components, the coiled coil domain-containing proteins CCDC22 and CCDC93 and ten COMMD (copper metabolism MURR1 [Mouse U2af1-rs1 region 1) domain) family members COMMD1-COMMD10.2,16,17,18,19”
From Structure of the endosomal Commander complex linked to Ritscher-Schinzel syndrome (2023) · cites this paper as [19]
Experimental — accuracy not yet measuredIn the citing paper
“The community detection approach was well illustrated in recent analyses of protein-protein interaction networks in yeast (Dutkowski et al., 2013) and human (Huttlin et al., 2015).”
From Mapping the multiscale structure of biological systems (2021) · cites this paper as Huttlin et al., 2015
In the citing paper
“In the human study, the authors first performed clique percolation to determine high-level protein communities; subsequently, they ran modularity-based clustering to further subdivide these communities into more granular subsystems, resulting in a multi-layer hierarchical structure (Figure 3A).”
From Mapping the multiscale structure of biological systems (2021) · cites this paper as Huttlin et al., 2015
In the citing paper
“several high throughput studies using robust affinity purification-mass spectrometry methodologies to elucidate protein interaction networks have revealed the interaction of ABCD1 with AT2B2 [ 167 ] and ABCD3 with AT2B2 and AT2A2 [ 168 , 169 ]”
From Peroxisomal ABC Transporters: An Update (2021) · cites this paper as [169]
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TTC39B destabilizes retinoblastoma protein promoting hepatic lipogenesis in a sex-specific fashion
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“…characterization in biomedicine has shifted from defining the sequence [1, 2] to characterizing protein modifications [3] to identifying proteins in reference to genomics information [4, 5] to quantifying proteins [6, 7] to analyzing protein networks [8, 9] and identifying proteoforms [10, 11].”
The protein-interaction network with functional roles in tumorigenesis, neurodegeneration, and aging
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“…of the Drosophila and human Protein Interaction Map, and studies coupling genetic manipulation to the analysis of kinase–phosphatase networks, will considerably advance our capacity to define the in vivo function of these genes (Guruharsha et al. 2011; Huttlin et al. 2015; Sopko et al. 2014).”
BackgroundFunctional proteomics of cellular mechanosensing mechanisms
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Protein interactions study through proximity-labeling
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“As available data from high-throughput proteomics analysis (Huttlin et al., 2015) suggest, the most probable interaction partners of FAHD1 are carnitine palmitoyltransferase 2 (CPT2), clustered mitochondria homolog (CLUH), NADH dependent ubiquinone oxidoreductase subunit S6 (NDUFS6),…”
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The Biochemical Evolution of Protein Complexes
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Proteomic Investigation of Murine Neuronal α7-Nicotinic Acetylcholine Receptor Interacting Proteins
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“Notably, the top hits included proteins crucial for 40S ribosome biogenesis, such as nucleolar complex protein 4 homolog (NOC4L), bystin-like (BYSL), EMG1, poly(A)-speci fi c ribonuclease (PARN), ribosomal RNA processing 12 homolog (RRP12) and DEAH-box helicase 37 (DHX37) (Fig.”
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“With the expanding understanding of PPIs, the human protein interactome is increasingly being recognized as a rich source of potential targets for disease treatment 14,15 .”
PHLPP2 is a pseudophosphatase that lost activity in the metazoan ancestor
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Network-Based Approaches for Drug Target Identification
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Multi-OMICs and Genome Editing Perspectives on Liver Cancer Signaling Networks
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“However, a number of experimental strategies have been employed in large-scale human interactome mapping, such as yeast twohybrid [79, 101, 102], cofractionation [103], and affinity purification followed by mass spectrometry (AP-MS) [104].”
BackgroundMethodComplex network theory for the identification and assessment of candidate protein targets
McGarry, K., & McDonald, S. (2018) · Computers in Biology and Medicine · doi:10.1016/j.compbiomed.2018.04.015 · Cited by 11
Chan, J. Y., Ng, A. Y. J., Cheng, C. L., Nairismägi, M., Venkatesh, B., Cheah, D. M. Z., Li, S.-T., Chan, S. H., Ngeow, J. Y. Y., Laurensia, Y., et al. (2018) · Blood Cancer Journal · doi:10.1038/s41408-018-0149-5 · Cited by 11
Tissue specific expression of sialic acid metabolic pathway: role in GNE myopathy
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Integrative network analysis interweaves the missing links in cardiomyopathy diseasome
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“Several PDIA5 substrates have being identified over the years, including α1-antitrypsin [39], Neudesin (NENF) [40,41], Protein phosphatase inhibitor 2 (PPP1R2) [42], DNA-directed RNA polymerase II subunit RPB7 (POLR2G) [43], Pleiotropic regulator 1 (PLRG1) [43] and Cell division cycle 5-like protein (CDC5L) [42].”
BackgroundGlobal Interactome Mapping Reveals Pro-tumorigenic Interactions of NF-κB in Breast Cancer
Lapčík, P., Stacey, R. G., Potěšil, D., Kulhánek, P., Foster, L. J., & Bouchal, P. (2024) · Molecular & Cellular Proteomics · doi:10.1016/j.mcpro.2024.100744 · Cited by 10
Modern Prometheus: editing the human genome with Crispr-Cas9
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Dissecting the Keap1/Nrf2 pathway through proteomics
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C11ORF74 interacts with the IFT-A complex and participates in ciliary BBSome localization
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“In addition, the PPI data were derived from InBio (Li et al., 2017) (version 2016_05_31, https://www.intomics.com/inbio/map/#home) and BioPlex 2.0 (Huttlin et al., 2015) (http://bioplex.hms.harvard.edu/index.php).”
InfluentialSpt5 Phosphorylation and the Rtf1 Plus3 Domain Promote Rtf1 Function through Distinct Mechanisms
Chen, J. J., Mbogning, J., Hancock, M. A., Majdpour, D., Madhok, M., Nassour, H., Dallagnol, J. C. C., Pagé, V., Chatenet, D., & Tanny, J. C. (2020) · Molecular and Cellular Biology · doi:10.1128/mcb.00150-20 · Cited by 11
“We detect 469 interaction between multiple PAF subunits and the Plus3 domain in vitro, but interactions 470 between Prf1 and the PAF complex are weak or undetectable in extracts (as is the case in 471 metazoans), further complicating efforts to dissect the function of the interaction in vivo (16,44).”
BackgroundRole of Antizyme Inhibitor Proteins in Cancers and Beyond
Tulluri, V., & Nemmara, V. V. (2021) · OncoTargets and Therapy · doi:10.2147/ott.s281157 · Cited by 11
Proximity labeling and other novel mass spectrometric approaches for spatiotemporal protein dynamics
Pino, L. K., & Schilling, B. (2021) · Expert Review of Proteomics · doi:10.1080/14789450.2021.1976149 · Cited by 11
A proximity labeling method for protein–protein interactions on cell membrane
Li, Q., Xie, Y., Rice, R., Maverakis, E. M., & Lebrilla, C. B. (2022) · Chemical Science · doi:10.1039/d1sc06898a · Cited by 11
“6 9 However, weak and transient interactions are di ffi cult to be captured by this technique.”
BackgroundLi, Y., Sahni, N., & Yi, S. S. (2016) · Oncotarget · doi:10.18632/oncotarget.12879 · Cited by 11
“generated a proteome-scale interactome dataset in human using high-throughput affinity-purification mass spectrometry (AP-MS), resulting in 23,744 interactions among 7,688 proteins [21].”
BackgroundA learned embedding for efficient joint analysis of millions of mass spectraPreprint
Bittremieux, W., May, D., Bilmes, J. A., & Noble, W. S. (2018) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/483263 · Cited by 11
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A phospho-harmonic orchestra plays the NLRP3 score
Bornancin, F., & Dekker, C. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1281607 · Cited by 10
“…it is notable that both PRKAs and A-kinase anchor proteins have been reported to harbor a Two-Phenylalanines-in-an Acidic-Tract (FFAT) motif, which is recognized by the VAP (VAMP-associated proteins) family of transmembrane proteins from the ER, involved in tethering other organelles (89, 90).”
BackgroundThe SMN-ribosome interplay: a new opportunity for Spinal Muscular Atrophy therapies
Sharma, G., Paganin, M., Lauria, F., Perenthaler, E., & Viero, G. (2024) · Biochemical Society Transactions · doi:10.1042/bst20231116 · Cited by 11
“The majority of these studies were conducted at symptomatic stages of the disease, thus the IP + LC – MS/MS[14,37] AP-MS[36] Proximity biotinylation assay [25] Co-IP[7,38 – 41] TAP-MS [42] ,large subunit x x cause-effect relationship between SMN de fi ciency and proteome reorganization is not obvious.”
BackgroundGetting to Grips with the Oxysterol-Binding Protein Family – a Forty Year Perspective
Olkkonen, V. M., & Ikonen, E. (2024) · Contact · doi:10.1177/25152564241273598 · Cited by 9
“…in a neutral tract (FFNT) and phospho-FFAT motifs] have been discovered (James and Kehlenbach, 2021; Mikitova and Levine, 2012), and over 250 proteins have been found to bind to VAPs (Cabukusta et al., 2020; Huttlin et al., 2021; Huttlin et al., 2017; Huttlin et al., 2015; James et al., 2019).”
BackgroundRegulation of volume-regulated anion channels alters sensitivity to platinum chemotherapy
Feldman, L. E., Mohapatra, S., Jones, R. T., Scholtes, M., Tilton, C. B., Orman, M. V., Joshi, M. U., Deiter, C. S., Broneske, T. P., Qu, F., et al. (2024) · Science Advances · doi:10.1126/sciadv.adr9364 · Cited by 9
“…2 to 5 were derived from the transurethral resection of bladder tumor samples before the patients received nAc. embryonic kidney (HEK) 293T cells, the cell type reported in the BioPlex database to have NPEPPS- LRRC8A-E interactions ( 35 ), to establish an NPEPPS-KO phenotype in noncancer cells.”
On the multiplicity of Laplacian eigenvalues and Fiedler partitions
Andreotti, E., Remondini, D., Servizi, G., & Bazzani, A. (2018) · Linear Algebra and its Applications · doi:10.1016/j.laa.2018.01.009 · Cited by 10
“in the case of proteins with a similar neighborhood structure in interactome networks[17], with implications on biomedical and Systems Biology applications [21].”
BackgroundOpen Science Resources for the Mass Spectrometry-Based Analysis of SARS-CoV-2
Bittremieux, W., Adams, C., Laukens, K., Dorrestein, P. C., & Bandeira, N. (2021) · Journal of Proteome Research · doi:10.1021/acs.jproteome.0c00929 · Cited by 11
Kattan, R. E., Ayesh, D., & Wang, W. (2023) · Briefings in Bioinformatics · doi:10.1093/bib/bbad010 · Cited by 11
Hsu, Y.-H. H., Pintacuda, G., Liu, R., Nacu, E., Kim, A., Tsafou, K., Petrossian, N., Crotty, W. J., Suh, J. M., Riseman, J., et al. (2023) · iScience · doi:10.1016/j.isci.2023.106701 · Cited by 11
Chen, Y., Jiao, D., He, H., Sun, H., Liu, Y., Shi, Q., Zhang, P., Li, Y., Mo, R., Gao, K., et al. (2023) · Redox Biology · doi:10.1016/j.redox.2023.102872 · Cited by 13
“Notably, the potential interaction between mLST8 and Keap1 was also revealed via a large-scale proteome mapping analysis; however, the biological function of this interaction was not analyzed further [16].”
BackgroundSolid support resins and affinity purification mass spectrometry
Havis, S., Moree, W. J., Mali, S., & Bark, S. J. (2017) · Molecular BioSystems · doi:10.1039/c6mb00735j · Cited by 10
“cerevisiae and have been expanded to Drosophila and mammalian cell types.(3,4) Typically, the antibody to a native protein or overexpressed tagged protein is attached to a resin matrix by either noncovalent (Protein A or G) or covalent methods (Figure 1).”
MethodEvolution of peroxisomal trans-2-enoyl-CoA reductase ( PECR ) as candidate gene for meat quality
Piórkowska, K., Tyra, M., Ropka‐Molik, K., & Podbielska, A. (2017) · Livestock Science · doi:10.1016/j.livsci.2017.05.004 · Cited by 10
A mass spectrometry-based proteomic analysis of Homer2-interacting proteins in the mouse brain
Goulding, S. P., Szumlinski, K. K., Contet, C., MacCoss, M. J., & Wu, C. C. (2017) · Journal of Proteomics · doi:10.1016/j.jprot.2017.07.008 · Cited by 10
Zou, X., An, K., Wu, Y., & Ye, Z. (2018) · BMC Systems Biology · doi:10.1186/s12918-018-0567-9 · Cited by 11
Han, X., Dong, Q., Wu, J., Luo, Y., Rong, X., Han, Q., Zheng, X., & Wang, E. (2019) · Molecular Carcinogenesis · doi:10.1002/mc.23000 · Cited by 10
Shi, T., Yao, L., Han, Y., Hao, P., & Lu, P. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20215400 · Cited by 10
Emerging tools to investigate bromodomain functions
Tchara, P.-E. K., Filippakopoulos, P., & Lambert, J. (2019) · Methods · doi:10.1016/j.ymeth.2019.11.003 · Cited by 12
Wang, X., Li, Y., Hu, H., Zhou, F., Chen, J., & Zhang, D. (2020) · Genetics and Molecular Biology · doi:10.1590/1678-4685-gmb-2019-0164 · Cited by 10
Kim, S. A., Jo, S.-H., Cho, J. H., Yu, M. Y., Shin, H., Kim, J., Park, B. C., Park, B. C., Kim, J., & Kim, J. (2020) · Molecules and Cells · doi:10.14348/molcells.2020.0122 · Cited by 10
“DCAF15 interacts with ARNT Affinity purification-mass spectrometry studies on the human interactome have disclosed potential associations of DCAF15 with ARNT (Huttlin et al., 2015; 2017).”
BackgroundA Structural Perspective on Gene Repression by Polycomb Repressive Complex 2
Liu, X. (2020) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-3-030-58971-4_17 · Cited by 11
Recombinant Human SCARB2 Expressed in Escherichia coli and its Potential in Enterovirus 71 Blockage
Vo-Nguyen, H.-V., Nguyen, T.-T., Vu, H.-T. T., Nguyen, T.-T. T., Hoang, Q. C., Tran, T. L., & Tran‐Van, H. (2021) · Iranian Journal of Science and Technology Transactions A Science · doi:10.1007/s40995-020-01025-9 · Cited by 10
Peptide array–based interactomics
Pérez-Hernández, D., & Dittmar, G. (2021) · Analytical and Bioanalytical Chemistry · doi:10.1007/s00216-021-03367-8 · Cited by 9
Protein Complex Affinity Capture from Cryomilled Mammalian Cells
LaCava, J., Jiang, H., & Rout, M. P. (2016) · Journal of Visualized Experiments · doi:10.3791/54518-v · Cited by 10
HiQuant: Rapid Postquantification Analysis of Large-Scale MS-Generated Proteomics Data
Bryan, K. R., Jarboui, M. A., Raso, C., Llinares, M. B., McCann, B., Rauch, J., Boldt, K., & Lynn, D. J. (2016) · Journal of Proteome Research · doi:10.1021/acs.jproteome.5b01008 · Cited by 10
Federspiel, J. D., & Cristea, I. M. (2019) · Methods in molecular biology · doi:10.1007/978-1-4939-9232-4_9 · Cited by 10
Identification of the iduronate-2-sulfatase proteome in wild-type mouse brain
Cardona, C., Benincore, E., Pimentel, N., Reyes, L. H., Patarroyo, C., Rodríguez‐López, A., Martín‐Rufián, M., Barrera, L. A., & Alméciga-Díaz, C. J. (2019) · Heliyon · doi:10.1016/j.heliyon.2019.e01667 · Cited by 10
Analyses of Protein Interaction Networks Using Computational Tools
Dong, S., & Provart, N. J. (2018) · Methods in molecular biology · doi:10.1007/978-1-4939-7871-7_7 · Cited by 10
Correction: DOORS syndrome and a recurrent truncating ATP6V1B2 variant
Beauregard‐Lacroix, É., Pacheco-Cuellar, G., Ajeawung, N. F., Tardif, J., Dieterich, K. D., Dabir, T. A., Vind-Kezunovic, D., White, S. M., Zádori, D., Claudia Castiglioni, T., et al. (2020) · Genetics in Medicine · doi:10.1038/s41436-020-00969-y · Cited by 10
Liu, X., Zhang, Y., Wen, Z., Hao, Y., Banks, C. A. S., Cesare, J., Bhattacharya, S., Arvindekar, S., Lange, J. J., Xie, Y., et al. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2318601121 · Cited by 9
Next Generation Sequencing and Electromyography Reveal the Involvement of the P2RX6 Gene in Myopathy
Vinci, M., Vitello, G. A., Greco, D., Treccarichi, S., Ragalmuto, A., Musumeci, A., Fallea, A., Federico, C., Calı̀, F., Saccone, S., et al. (2024) · Current Issues in Molecular Biology · doi:10.3390/cimb46020073 · Cited by 9
“The interaction among our target P2RX6 and the previously mentioned proteins was also revealed by high-throughput affinity-purification mass spectrometry, showing a robust protein–protein interaction [79].”
BackgroundWang, K., Zhang, L., Zhang, S., Liu, Y., Mao, J., Liu, Z., Xu, L., Li, K., Wang, J., Ma, Y., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-51979-2 · Cited by 10
“22).”
The NF1 tumor suppressor regulates PD-L1 and immune evasion in melanoma
Berry, D., Moldoveanu, D., Rajkumar, S., Lajoie, M., Lin, T., Tchelougou, D., Sakthivel, S., Sharon, I., Bernard, A., Pelletier, S., et al. (2025) · Cell Reports · doi:10.1016/j.celrep.2025.115365 · Cited by 11
Broderick, K., Moutaoufik, M. T., Saccon, T. D., Malty, R. H., Amin, S., Phanse, S., Joseph, T. P., Zilocchi, M., Hosseinnia, A., Istace, Z., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-60949-1 · Cited by 9
“For each cell line, outputs from these search engines were scored independently using CompPASS-Plus (Comparative Proteomic Analysis Software Suite 13 ) and MiST (Mass spectrometry interaction STatistics 14 ) scoring procedures to assign con fi dence scores for viral bait-human prey associations (Fig.”
Eyckerman, S., Impens, F., Quickelberghe, E. V., Samyn, N., Vandemoortele, G., Sutter, D. D., Tavernier, J. H., & Gevaert, K. (2016) · Journal of Proteome Research · doi:10.1021/acs.jproteome.6b00517 · Cited by 9
The magic of MAGI‐1: A scaffolding protein with multi signalosomes and functional plasticity
Excoffon, K. J. D. A., Avila, C. L., Alghamri, M. S., & Kolawole, A. O. (2022) · Biology of the Cell · doi:10.1111/boc.202200014 · Cited by 9
Kumar, S., Sarmah, D. T., Asthana, S., & Chatterjee, S. (2022) · Bioinformatics · doi:10.1093/bioinformatics/btac815 · Cited by 9
Preparing to strike: Acute events in signaling by the serpentine receptor for thromboxane A2
Ashton, A. W. (2023) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2023.108478 · Cited by 9
Mapping the Multiscale Proteomic Organization of Cellular and Disease Phenotypes
Cesnik, A. J., Schaffer, L. V., Gaur, I., Jain, M., Ideker, T., & Lundberg, E. K. (2024) · Annual Review of Biomedical Data Science · doi:10.1146/annurev-biodatasci-102423-113534 · Cited by 9
“In our recent work, a multiscale integrated cell map (36) systematically integrated an imaging proteomic dataset from the HPA Subcellular Atlas (20) for HEK293T with the global BioPlex AP-MS interaction network (11).”
BackgroundMethodCrossCheck: an open-source web tool for high-throughput screen data analysis
Najafov, J., & Najafov, A. (2017) · Scientific Reports · doi:10.1038/s41598-017-05960-3 · Cited by 9
A transcriptome-based protein network that identifies new therapeutic targets in colorectal cancer
Durand, S., Trillet, K., Uguen, A., Saint-Pierre, A., Jossic-Corcos, C. L., & Corcos, L. (2017) · BMC Genomics · doi:10.1186/s12864-017-4139-y · Cited by 9
“A recent publication identified ADH1B and XYLT1 (an enzyme implicated in the biosynthesis of glycosaminoglycan chains) as interaction partners of ADH1C using highthroughput affinity purification [42].”
BackgroundInfluentialThe interaction networks of the budding yeast and human DNA replication-initiation proteins
Wu, R., Amin, A., Wang, Z., Huang, Y., Cheung, M. H., Yu, Z., Yang, W., & Liang, C. (2019) · Cell Cycle · doi:10.1080/15384101.2019.1586509 · Cited by 9
“Refer to Figure 1 for the meaning of the symbols. interactions of hNOC3 with hMCM2, hMCM3 and hMCM7 by co-IP (Supplementary Figure S12E and Table 3). hMCM2, hMCM3 and hMCM7 were found to be co-immunoprecipitated with HAhNOC3 by the anti-HA antibody, but not the control IgG, from DNase I treated extracts of HEK-293T ce…”
BackgroundInfluentialContribution of Mass Spectrometry-Based Proteomics to Discoveries in Developmental Biology
Hashimoto, Y., Greco, T. M., & Cristea, I. M. (2019) · Advances in experimental medicine and biology · doi:10.1007/978-3-030-15950-4_8 · Cited by 9
Worming into the Uncharacterized Human Proteome
Duek, P. D., & Lane, L. (2019) · Journal of Proteome Research · doi:10.1021/acs.jproteome.9b00435 · Cited by 9
Benchmarking network algorithms for contextualizing genes of interest
Hill, A. S., Gleim, S., Kiefer, F., Sigoillot, F. D., Loureiro, J., Jenkins, J. L., & Morris, M. K. (2019) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1007403 · Cited by 9
“Three different network sources were used for this work: (1) The “Composite network” consisting of high-confidence, PPI or transcription factor-gene interactions from the Metabase manually curated network, STRING [13, 14] and BioPlex [15]; (2) “MetabaseSD” consisting of signed and directed high confidence interactions…”
MethodMei, L., Montoya, M. R., Quanrud, G. M., Tran, M., Villa-Sharma, A., Huang, M., & Genereux, J. C. (2020) · Journal of Proteome Research · doi:10.1021/acs.jproteome.9b00825 · Cited by 8
“TMT-AP-MS allows direct quantitative comparisons of prey recovery across multiple replicates in a single run, simplifying evaluation of whether potential interactors are preferentially recovered with the bait 22,28 .”
BackgroundSjögren syndrome/scleroderma autoantigen 1 is a direct Tankyrase binding partner in cancer cells
Perdreau‐Dahl, H., Progida, C., Barfeld, S. J., Guldsten, H., Thiede, B., Arntzen, M. Ø., Bakke, O., Mills, I. G., Krauss, S. J. K., & Morth, J. P. (2020) · Communications Biology · doi:10.1038/s42003-020-0851-2 · Cited by 9
The Cardiac Syndecan-2 Interactome
Mathiesen, S. B., Lunde, M., Stensland, M., Martinsen, M., Nyman, T. A., Christensen, G., & Carlson, C. R. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.00792 · Cited by 9
Metadata
- Authors
- Huttlin, E. L., Ting, L., Bruckner, R. J., Gebreab, F., Gygi, M. P., Szpyt, J., Tam, S., Zarraga, G., Colby, G., Baltier, K., Dong, R., Guarani, V., Vaites, L. P., Ordureau, A., Rad, R., Erickson, B. K., Wühr, M., Chick, J., Zhai, B., Kolippakkam, D., Mintseris, J., Obar, R. A., Harris, T., Artavanis-Tsakonas, S., Sowa, M. E., De Camilli, P., Paulo, J. A., Harper, J. W., & Gygi, S. P.
- Affiliations
- Harvard University (US)
- Howard Hughes Medical Institute (US)
- Biogen (United States) (US)
- Corresponding author
- Harper, J. Wade
- Gygi, Steven P.
- ORCID
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2015-07
- Volume
- 162
- Issue
- 2
- Pages
- 425-440
- ISSN
- 0092-8674 (ISSN-L)
- PMC
- PMC4617211
- OpenAlex
- W1611787727
- Cited by
- 1,425
- References
- 41
- Citations by year
- 2026: 46 · 2025: 82 · 2024: 116 · 2023: 105 · 2022: 98 · 2021: 162 · 2020: 159 · 2019: 197 · 2018: 171 · 2017: 147 · 2016: 122 · 2015: 18
- FWCI
- 66.47
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cell (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- Funders
- Howard Hughes Medical Institute
- Damon Runyon Cancer Research Foundation
- Biogen
- Charles A. King Trust
- National Institutes of Health (HG006673)
- National Human Genome Research Institute (U41HG006673)
- National Institute of Diabetes and Digestive and Kidney Diseases (K01DK098285)
- National Institute of Neurological Disorders and Stroke (R37NS036251)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Bioinformatics and Genomic Networks
- Physical Sciences › Chemistry › Spectroscopy › Advanced Proteomics Techniques and Applications
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Biotin and Related Studies
- Keywords
- BioPlex, human interactome, protein-protein interaction, protein complexes, protein domain interactions, community structure, HEK293T cells, VAPB, amyotrophic lateral sclerosis
- MeSH terms
- Amyotrophic Lateral Sclerosis, Humans, Proteins, Mass Spectrometry, Protein Interaction Mapping, Proteomics, Protein Interaction Maps
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