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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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“APID (Agile Protein Interaction Data Analyzer) (Alonso-Lopez et al. 2019) provides a collection of known experimentally validated PPIs for more than 400 organisms from DIP (Sal-winski et al. 2004), IntAct, MINT, HPRD (Keshava Prasad et al. 2009), BioGRID, BioPlex (Huttlin et al. 2015), and also from experimentally res…”
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“Identification of INF2 as a novel FBXO7 interacting protein The affinity-purification mass spectrometry (AP-MS) result from two proteomics studies hint the potential interacted proteins of FBXO7 including INF2, a key factor in DRP1-associated mitochondrial division [21, 22].”
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A network-based meta-analysis for characterizing the genetic landscape of human aging
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“BioPlex is an ongoing effort to unravel the landscape of all human protein complexes (Huttlin et al. 2015).”
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Decrypting protein surfaces by combining evolution, geometry, and molecular docking
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“Our knowledge 35 of protein-protein interaction (PPI) networks [2] is largely incomplete, since the experimental assessment of 36 all possible interactions of a protein is very challenging [3, 4].”
BackgroundThe True Story of Yeti, the “Abominable” Heterochromatic Gene of Drosophila melanogaster
Prozzillo, Y., Monache, F. D., Ferreri, D., Cuticone, S., Dimitri, P., & Messina, G. (2019) · Frontiers in Physiology · doi:10.3389/fphys.2019.01093 · Cited by 16
“Studies on the cp27 protein (later called mCFDP1) have shown specific interaction with NF-Y nuclear factor which bind CCAAT box (Luan et al., 2010; Ito et al., 2011), and with the TFII-I transcription factors involved in craniofacial development and osteo-differentiation Frontiers in Physiology |…”
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“The BioPlex database (Huttlin et al., 2015) identifies with 99% probability that KLHL26 interacts with Cullin-3 (CUL3), an important subunit of E3 ubiquitin ligase.”
BackgroundExperimental Approaches in Delineating mTOR Signaling
Qian, J., Su, S., & Liu, P. (2020) · Genes · doi:10.3390/genes11070738 · Cited by 17
“searched the BioPlex database (a human protein-protein interaction database [96]) for GATOR2 binding proteins and found GATSL3 (CASTOR1) as a GATOR2 binding partner, while GATSL2 (CASTOR2) interacted with GATOR1 [97].”
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“Interestingly, an interaction of TTC39A with P2RY12, a receptor involved in platelet aggregation, regarded to be a potential target of thromboembolism treatment, was supposed [33].”
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“For example, PantherDB [66] and David [67] enable GO annotation based on protein/gene names, KEGG [68] or Ingenuity Pathway Analysis (Agilent) infer on gene set enrichment, and STRING [69] and recently BioPlex [70] can help build protein interaction networks.”
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Autophagy-independent role of ATG9A vesicles as carriers for galectin-9 secretion
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Investigation and Prediction of Human Interactome Based on Quantitative Features
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“They were defined in three previous studies (Hein et al., 2015; Huttlin et al., 2015; Wan et al., 2015) and represented various biological characteristics of PPI.”
BackgroundMethodInfluentialBiotin Proximity Labeling for Protein–Protein Interaction Discovery: The BioID Method
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“Clusterin binds to TNF-a in the BioPlex human interactome network (141).”
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“In plants, NDL proteins were first reported in sunflower (SF21) as stigma and transmitting tissue cell specific proteins (Kräuter-Canham et al., 1997).”
Backgroundp37/UBXN2B regulates spindle orientation by limiting cortical NuMA recruitment via PP1/Repo-Man
Lee, B. H., Schwager, F., Meraldi, P., & Gotta, M. (2017) · The Journal of Cell Biology · doi:10.1083/jcb.201707050 · Cited by 16
“This model is compatible with proteomic studies, which reported interactions between several PP1 subunits and p37 (Huttlin et al., 2015, 2017; Raman et al., 2015).”
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“4 interaction networks and form predictions of unknown protein function based on these networks (6,7), for gene annotation enrichment analyses, and are now being leveraged for the creation of predictive disease models in the scope of systems biochemistry (8).”
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“(2015) using affinity chromatography and anti-tag co-immunoprecipitation (co-IP) technologies showed that CRHBP may bind to p62 [14].”
BackgroundInfluentialProteomics profiling of interactome dynamics by colocalisation analysis (COLA)
Mardakheh, F. K., Sailem, H., Kuemper, S., Tape, C. J., McCully, R. R., Paul, A., Anjomani‐Virmouni, S., Jørgensen, C., Poulogiannis, G., Marshall, C. J., et al. (2016) · Molecular BioSystems · doi:10.1039/c6mb00701e · Cited by 15
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Identification and characterization of the BRI2 interactome in the brain
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“Both of these transcription factors are highly expressed in the brain (Fagerberg et al. 2014) and involved in forming the AP1 transcription factor complex (Huttlin et al. 2015), which responds to cytokines and growth factor signaling.”
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“Both CYFIP proteins incorporate into WAVE complexes [44-46].”
BackgroundStructure of LRRK1 and mechanisms of autoinhibition and activation
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“4a,b), and that no peptides for either LRRK1 or LRRK2 were found in the 293T cell proteome in a previous study 22 .”
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Challenges and Opportunities for Bayesian Statistics in Proteomics
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TREAT: Therapeutic RNAs exploration inspired by artificial intelligence technology
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“Coding gene-related relationships are from HURI [23], Bio-plex [26], PhosphoSitePlus [27], BioGRID [28], InnateDB [29], MINT [30], INSIDER [31], and DIP [32].”
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“Researchers have also attempted to use high-throughput, mass spectrometry-based methods to perform comprehensive analyses of protein‒protein interaction networks [169, 170] to identify the nucleolar proteome [171].”
Serrano, L. R., Pelin, A., Arrey, T. N., Damoc, N. E., Richards, A., Zhou, Y. M., Lancaster, N. M., Peters-Clarke, T. M., Pashkova, A., Jang, G. Μ., et al. (2025) · Journal of Proteome Research · doi:10.1021/acs.jproteome.4c01040 · Cited by 14
Import mechanism of peroxisomal proteins with an N-terminal signal sequence
Skowyra, M. L., & Rapoport, T. A. (2025) · Nature Cell Biology · doi:10.1038/s41556-025-01662-5 · Cited by 16
“A possible mechanism was suggested by large-scale protein-interaction studies in yeast 40,41 and mammalian cells 42–44 , which had identified an uncharacterized binding partner of PEX7 in the cytosol that has recently been named PEX39 (ref.”
Halu, A., Wang, J., Iwata, H., Mojcher, A., Abib, A. L., Singh, S. A., Aikawa, M., & Sharma, A. (2018) · eLife · doi:10.7554/elife.37059 · Cited by 12
“0 (http://bioplex.hms.harvard.edu/; Huttlin et al., 2015) contained 56,553 interactions and (Hein et al.”
BackgroundLi, H., Zhou, D., Chang, H., Wang, L., Liu, W., Dai, S., Zhang, C., Cai, J., Liu, W., Li, X., et al. (2019) · Journal of Psychiatric Research · doi:10.1016/j.jpsychires.2019.05.024 · Cited by 14
Explore Protein–Protein Interactions for Cancer Target Discovery Using the OncoPPi Portal
Ivanov, A. A. (2019) · Methods in molecular biology · doi:10.1007/978-1-4939-9873-9_12 · Cited by 14
Bon-Baret, V., Chignon, A., Boulanger, M., Li, Z., Argaud, D., Arsenault, B. J., Thériault, S., Bossé, Y., & Mathieu, P. (2021) · Circulation Genomic and Precision Medicine · doi:10.1161/circgen.120.003196 · Cited by 13
Discovery–Versus Hypothesis–Driven Detection of Protein–Protein Interactions and Complexes
Bludau, I. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22094450 · Cited by 11
“, kinases [8]), and to even larger scale studies, such as the effort to map PPIs across all human ORFs [6,9,10].”
BackgroundInfluentialAxon-Specific Mitochondrial Pathology in SPG11 Alpha Motor Neurons
Güner, F., Pozner, T., Krach, F., Prots, I., Loskarn, S., Schlötzer-Schrehardt, U. M., Winkler, J., Winner, B., & Regensburger, M. (2021) · Frontiers in Neuroscience · doi:10.3389/fnins.2021.680572 · Cited by 14
Metabolic endophenotype associated with right ventricular glucose uptake in pulmonary hypertension
Farha, S., COMHAIR, S. A. A., Hou, Y., Park, M. M., Sharp, J., Peterson, L., Willard, B. B., Zhang, R., DiFilippo, F. P., Neumann, D. R., et al. (2021) · Pulmonary Circulation · doi:10.1177/20458940211054325 · Cited by 14
“0;(42) and (5) protein complexes data (56,000 candidate interactions) identified by a robust affinity purification-mass spectrometry methodology were collected from BioPlex V2.(43) The genes were mapped to their Entrez ID based on the NCBI database as well as their official gene symbols based on GeneCards (http://www.”
MethodSartori, G., Napoli, S., Cascione, L., Chung, E. Y., Priebe, V., Arribas, A. J., Mensah, A. A., Dall’Angelo, M., Falzarano, C., Barnabei, L., et al. (2021) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-021-02159-3 · Cited by 17
Construction and contextualization approaches for protein-protein interaction networks
Badkas, A., Landtsheer, S. D., & Sauter, T. (2022) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2022.06.040 · Cited by 14
“A database of cell-line specific networks, BioPLEX, is also under construction [27].”
BackgroundMclean, C. (2016) · Journal of Proteomics & Bioinformatics · doi:10.4172/jpb.1000383 · Cited by 14
“To test how our findings translate to other large proteome datasets we looked at the BioPlex network [17].”
BackgroundMethodInfluentialFitzsimmons, R., Amin, N. E., & Uversky, V. N. (2016) · Intrinsically Disordered Proteins · doi:10.1080/21690707.2016.1248273 · Cited by 14
Gene co-opening network deciphers gene functional relationships
Li, W., Wang, M., Sun, J., Wang, Y., & Jiang, R. (2017) · Molecular BioSystems · doi:10.1039/c7mb00430c · Cited by 14
The Notch Interactome: Complexity in Signaling Circuitry
Ho, D. M., Guruharsha, K. G., & Artavanis‐Tsakonas, S. (2018) · Advances in experimental medicine and biology · doi:10.1007/978-3-319-89512-3_7 · Cited by 14
Chen, J., & Kuhn, L. A. (2019) · Journal of Molecular Graphics and Modelling · doi:10.1016/j.jmgm.2019.04.003 · Cited by 15
“However, the binding of hSerpinB12 to RNA pol II [113] suggests an alternative role in RNA rather than DNA binding.”
BackgroundC20orf27 Promotes Cell Growth and Proliferation of Colorectal Cancer via the TGFβR-TAK1-NFĸB Pathway
Gao, J., Wang, Y., Zhang, W., Zhang, J., Lu, S., Meng, K., Yin, X., Sun, Z., & He, Q. (2020) · Cancers · doi:10.3390/cancers12020336 · Cited by 14
“According to the mass spectrometry results, the band is the catalytic subunit of serine threonine (PP1c) [8].”
BackgroundContribution of Mass Spectrometry-Based Proteomics to the Understanding of TNF-α Signaling
Ciuffa, R., Caron, É., Leitner, A., Uliana, F., Gstaiger, M., & Aebersold, R. H. (2016) · Journal of Proteome Research · doi:10.1021/acs.jproteome.6b00728 · Cited by 14
An Atlas of Protein-Protein Interactions Across Mammalian TissuesPreprint
Skinnider, M. A., Scott, N. E., Prudova, A., Stoynov, N., Stacey, R. G., Gsponer, J., & Foster, L. J. (2018) · SSRN Electronic Journal · doi:10.1101/351247 · Cited by 14
“To select a precision cutoff for further analysis, we compared each mouse tissue interactome to five recently published high-throughput human interactome maps (Hein et al., 2015; Huttlin et al., 2015; Huttlin et al., 2017; Rolland et al., 2014; Wan et al., 2015).”
BackgroundMethodInfluentialThe p140Cap adaptor protein as a molecular hub to block cancer aggressiveness
Salemme, V., Angelini, C., Chapelle, J., Centonze, G., Natalini, D., Morellato, A., Taverna, D., Turco, E., Ala, U., & Defilippi, P. (2020) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-020-03666-w · Cited by 15
“p140Cap was also identified in the interactome of NUFIP1 (nuclear fragile X mental retardation protein-interacting protein) [40, 41], BCAS4 (breast carcinoma amplified sequence 4) [41], ESR2 (estrogen receptor 2) [42], from human samples.”
BackgroundHe, Z., Gao, K., Dong, L., Liu, L., Qu, X., Zou, Z., Wu, Y., Bu, D., Guo, J., & Zhao, Y. C. (2023) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2023.02.005 · Cited by 13
“To realistically simulate the regulatory relationships of the human molecular network, we collected 11 high-quality molecular interaction databases, including HuRI [9], BioPlex [25], BioGRID [26], DIP [27], MINT [28], InnateDB [29], PhosphoSitePlus [30], INSIDER [31], KnockTF [7], IntAct [32], and TRRUST [33].”
BackgroundGraph databases in systems biology: a systematic review
Mazein, I., Rougny, A., Mazein, A., Henkel, R., Gütebier, L., Michaelis, L., Ostaszewski, M., Schneider, R., Satagopam, V., Jensen, L. J., et al. (2024) · Briefings in Bioinformatics · doi:10.1093/bib/bbae561 · Cited by 15
“Well-established PPI databases are broadly available (including [33–40]).”
Dou, L., Xu, Z., Xu, J., Zang, C., Su, C., Pieper, A. A., Leverenz, J. B., Wang, F., Zhu, X., Cummings, J. L., et al. (2025) · npj Parkinson s Disease · doi:10.1038/s41531-025-00870-y · Cited by 21
Nardone, C., Mintseris, J., He, D., Rutter, J. C., Ebert, B. L., Gygi, S. P., & Rapoport, T. A. (2025) · Nature Structural & Molecular Biology · doi:10.1038/s41594-025-01610-9 · Cited by 15
“Large-scale proteomics studies have reported that WDR7, DMXL1/2 and ROGDI coimmunoprecipitate with each other and with V-ATPase subunits 39,47,48 (Extended Data Fig.”
Translating molecular advances in Down syndrome and Fragile X syndrome into therapies
Faúndez, V., Toma, I. D., Bardoni, B., Bartesaghi, R., Nižetić, D., de la Torre, R., Kadosh, R. C., Hérault, Y., Dierssen, M., Potier, M., et al. (2018) · European Neuropsychopharmacology · doi:10.1016/j.euroneuro.2018.03.006 · Cited by 14
“The interactome was obtained from six published proteome-wide interactomes datasets (Shannon et al. , 2003; Camargo et al. , 2007; Warde-Farley et al. , 2010; Wang et al. , 2011; Havugimana et al. , 2012; Corominas et al. , 2014; Huttlin et al. , 2015; Wan et al. , 2015).”
Meneses‐Salas, E., García-Melero, A., Blanco‐Muñoz, P., Jose, J., Brenner, M.-S., Lu, A., Tebar, F., Grewal, T., Rentero, C., & Enrich, C. (2020) · Cells · doi:10.3390/cells9051152 · Cited by 13
“In support of this, direct protein–protein interactions of annexins with several LE/Lys proteins have been reported, including the two‐pore channel (TPC1/2) [26], NPC1 [27], or the vacuolar proton pump (ATPase H+ transporting VO subunit a2) [28].”
BackgroundKim, S. M., Cho, S. Y., Kim, M. W., Roh, S. R., Shin, H. S., Suh, Y. H., Geum, D., & Lee, M. A. (2020) · PubMed Central · doi:10.14348/molcells.2020.0071 · Cited by 13
“We selected eight genes involved in nervous system development: BAALC binder of MAP3K1 and KLF4 (BAALC) (Wang et al., 2005), calcium/calmodulin dependent protein kinase II inhibitor 1 (CAMK2N1) (Lucchesi et al., 2011; Saha et al., 2006), myosin light chain kinase (MYLK) (Li et al., 2016a), NMU (Kasper et al., 2016), C…”
InfluentialPredicting Functions of Uncharacterized Human Proteins: From Canonical to Proteoforms
Poverennaya, E. V., Kiseleva, O. I., Romanova, A., & Pyatnitskiy, M. A. (2020) · Genes · doi:10.3390/genes11060677 · Cited by 12
“Interactome database BioPlex [38,39] is a developing project on building a human interactome by sequential annotation of human genes using the affinity purification coupled with mass spectrometry approach (AP-MS, [59]).”
BackgroundMethodTissue Proteomic Approaches to Understand the Pathogenesis of Inflammatory Bowel Disease
Martin, M. B., Chaparro, M., & Gisbert, J. P. (2021) · Inflammatory Bowel Diseases · doi:10.1093/ibd/izaa352 · Cited by 13
Mitochondrially localized MPZL3 emerges as a signaling hub of mammalian physiology
Wikramanayake, T. C., Nicu, C., Chéret, J., Czyzyk, T. A., & Paus, R. (2021) · BioEssays · doi:10.1002/bies.202100126 · Cited by 13
Vanderwall, D., Poudel, S., Fu, Y., Cho, J., Shaw, T. I., Mishra, A., High, A. A., Peng, J., & Li, Y. (2021) · Journal of Visualized Experiments · doi:10.3791/62796 · Cited by 16
Herebian, D. A., Alhaddad, B., Seibt, A., Schwarzmayr, T., Danhauser, K., Klee, D., Harmsen, S., Meitinger, T., Strom, T. M., Schulz, A., et al. (2017) · European Journal of Human Genetics · doi:10.1038/ejhg.2017.96 · Cited by 13
Genevini, P., Colombo, M. N., Venditti, R., Marcuzzo, S., Colombo, S. F., Bernasconi, P., Matteis, M. A. D., Borgese, N., & Navone, F. (2019) · Journal of Cell Science · doi:10.1242/jcs.220061 · Cited by 15
“To be noted, the sets of binding partners ofVAPA and VAPB overlap to a large extent (Huttlin et al., 2015; Murphy and Levine, 2016), and specific roles that functionally distinguish the two VAP isoforms have not been identified yet.”
BackgroundInteger Linear Programming in Computational and Systems Biology: An Entry-Level Text and Course
Gusfield, D. (2019) · Cited by 13
Kong, Q., Huang, P., Chu, B., Ke, M., Chen, W., Zheng, Z., Ji, S., Cai, Z., Li, P., & Tian, R. (2020) · Analytical Chemistry · doi:10.1021/acs.analchem.0c00839 · Cited by 13
Pal, R. R., Kumar, A., & Misra, G. (2021) · Briefings in Bioinformatics · doi:10.1093/bib/bbab007 · Cited by 13
Tankyrase regulates epithelial lumen formation via suppression of Rab11 GEFs
Chandrakumar, A. A., Coyaud, É., Marshall, C. B., Ikura, M., Raught, B., & Rottapel, R. K. (2021) · The Journal of Cell Biology · doi:10.1083/jcb.202008037 · Cited by 13
“…be a novel Tankyrase substrate since it contains a conserved Tankyrase binding motif RxxxxG and was observed in several independent Tankyrase immuno-precipitation mass spectrometry experiments (Guettler et al., 2011; Wang et al., 2015; Li et al., 2017; Huttlin et al., 2015; Bhardwaj et al., 2017).”
BackgroundQuantitative proteomics of model organisms
Feng, Y., Cappelletti, V., & Picotti, P. (2017) · Current Opinion in Systems Biology · doi:10.1016/j.coisb.2017.09.004 · Cited by 12
Spatially resolved proteomics in osteoarthritis: State of the art and new perspectives.
Eveque-Mourroux, M., Rocha, B., Barré, F. P. Y., Heeren, R., & Cillero-Pastor, B. (2020) · Journal of Proteomics · doi:10.1016/j.jprot.2020.103637 · Cited by 12
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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