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Functional organization of the yeast proteome by systematic analysis of protein complexes
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Most cellular processes are carried out by multiprotein complexes. The identification and analysis of their components provides insight into how the ensemble of expressed proteins (proteome) is organized into functional units. We used tandem-affinity purification (TAP) and mass spectrometry in a large-scale approach to characterize multiprotein complexes in Saccharomyces cerevisiae. We processed 1,739 genes, including 1,143 human orthologues of relevance to human biology, and purified 589 protein assemblies. Bioinformatic analysis of these assemblies defined 232 distinct multiprotein complexes and proposed new cellular roles for 344 proteins, including 231 proteins with no previous functional annotation. Comparison of yeast and human complexes showed that conservation across species extends from single proteins to their molecular environment. Our analysis provides an outline of the eukaryotic proteome as a network of protein complexes at a level of organization beyond binary interactions. This higher-order map contains fundamental biological information and offers the context for a more reasoned and informed approach to drug discovery.
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Cites
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
A comprehensive analysis of protein–protein interactions in Saccharomyces cerevisiae
Uetz, P., Giot, L., Cagney, G., Mansfield, T. A., Judson, R. S., Knight, J. R., Lockshon, D., Narayan, V., Srinivasan, M., Pochart, P., et al. (2000) · Nature · doi:10.1038/35001009 · Cited by 4,706
Global Analysis of Protein Activities Using Proteome Chips
Zhu, H., Bilgin, M., Bangham, R., Hall, D., Casamayor, A., Bertone, P., Lan, N., Jansen, R., Bidlingmaier, S., Houfek, T., et al. (2001) · Science · doi:10.1126/science.1062191 · Cited by 1,884
Comparative Genomics of the Eukaryotes
Rubin, G. M., Yandell, M. D., Wortman, J. R., Gabor, G. L., Miklos, Nelson, C. R., Hariharan, I. K., Fortini, M. E., Li, P. W., Apweiler, R., et al. (2000) · Science · doi:10.1126/science.287.5461.2204 · Cited by 1,698
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Mass spectrometry-based proteomics
Aebersold, R., & Mann, M. (2003) · Nature · doi:10.1038/nature01511 · Cited by 6,955
Uncovering the overlapping community structure of complex networks in nature and society
Palla, G., Derényi, I., Farkas, I., & Vicsek, T. (2005) · Nature · doi:10.1038/nature03607 · Cited by 5,373
Global analysis of protein localization in budding yeast
Huh, W.-K., Falvo, J. V., Gerke, L. C., Carroll, A. S., Howson, R. W., Weissman, J. S., & O'Shea, E. K. (2003) · Nature · doi:10.1038/nature02026 · Cited by 4,248
Anderson, N. L., & Anderson, N. G. (2002) · Molecular & Cellular Proteomics · doi:10.1074/mcp.r200007-mcp200 · Cited by 4,414
BioGRID: a general repository for interaction datasets
Stark, C. (2006) · Nucleic Acids Research · doi:10.1093/nar/gkj109 · Cited by 3,960
Global analysis of protein expression in yeast
Ghaemmaghami, S., Huh, W.-K., Bower, K., Howson, R. W., Belle, A., Dephoure, N., O'Shea, E. K., & Weissman, J. S. (2003) · Nature · doi:10.1038/nature02046 · Cited by 3,750
Specificity and Stability in Topology of Protein Networks
Maslov, S., & Sneppen, K. (2002) · Science · doi:10.1126/science.1065103 · Cited by 3,051
The Database of Interacting Proteins: 2004 update
Salwinski, L. (2004) · Nucleic Acids Research · doi:10.1093/nar/gkh086 · Cited by 2,271
A Protein Interaction Map of Drosophila melanogaster
Giot, L., Bader, J. S., Brouwer, C., Chaudhuri, A., Kuang, B., Li, Y., Hao, Y. L., Ooi, C. E., Godwin, B., Vitols, E., et al. (2003) · Science · doi:10.1126/science.1090289 · Cited by 1,863
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
A vision for the future of genomics research
Collins, F. S., Green, E. D., Guttmacher, A. E., Guyer, M. S., & on behalf of the US National Human Genome Research Institute (2003) · Nature · doi:10.1038/nature01626 · Cited by 1,752
Phosphoinositides: Tiny Lipids With Giant Impact on Cell Regulation
Balla, T. (2013) · Physiological Reviews · doi:10.1152/physrev.00028.2012 · Cited by 1,638
Mass spectrometry–based proteomics turns quantitative
Ong, S.-E., & Mann, M. (2005) · Nature Chemical Biology · doi:10.1038/nchembio736 · Cited by 1,572
Protein Analysis by Shotgun/Bottom-up Proteomics
Zhang, Y., Fonslow, B. R., Shan, B., Baek, M.-C., & Yates, J. R. (2013) · Chemical Reviews · doi:10.1021/cr3003533 · Cited by 1,491
The BioPlex network: a systematic exploration of the human interactome
Huttlin, E. L., Ting, L., Bruckner, R. J., Gebreab, F., Gygi, M. P., Szpyt, J., Tam, S., Zarraga, G., Colby, G., Baltier, K., et al. (2015) · Cell · doi:10.1016/j.cell.2015.06.043 · Cited by 1,425
“AP-MS has previously mapped a substantial fraction of yeast (Gavin et al., 2002; Ho et al., 2002; Krogan et al., 2006) and Drosophila (Guruharsha et al.”
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
Interaction network containing conserved and essential protein complexes in Escherichia coli
Butland, G., Peregrín-Alvarez, J. M., Li, J., Yang, W., Yang, X., Canadien, V., Starostine, A., Richards, D., Beattie, B., Krogan, N., et al. (2005) · Nature · doi:10.1038/nature03239 · Cited by 1,201
Discovering regulatory and signalling circuits in molecular interaction networks
Ideker, T., Ozier, O., Schwikowski, B., & Siegel, A. F. (2002) · Bioinformatics · doi:10.1093/bioinformatics/18.suppl_1.s233 · Cited by 1,197
Dual proteome-scale networks reveal cell-specific remodeling of the human interactome
Huttlin, E. L., Bruckner, R. J., Navarrete-Perea, J., Cannon, J. R., Baltier, K., Gebreab, F., Gygi, M. P., Thornock, A., Zarraga, G., Tam, S., et al. (2020) · doi:10.1101/2020.01.19.905109 · Cited by 960
Functional and quantitative proteomics using SILAC
Mann, M. (2006) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2067 · Cited by 931
Complete sequencing and characterization of 21,243 full-length human cDNAs
Ota, T., Suzuki, Y., Nishikawa, T., Otsuki, T., Sugiyama, T., Irie, R., Wakamatsu, A., Hayashi, K., Sato, H., Nagai, K., et al. (2004) · Nature Genetics · doi:10.1038/ng1285 · Cited by 925
Choreography of the DNA Damage Response
Lisby, M., Barlow, J. H., Burgess, R. C., & Rothstein, R. (2004) · Cell · doi:10.1016/j.cell.2004.08.015 · Cited by 891
Schuldiner, M., Collins, S. R., Thompson, N. J., Denic, V., Bhamidipati, A., Punna, T., Ihmels, J., Andrews, B., Boone, C., Greenblatt, J. F., et al. (2005) · Cell · doi:10.1016/j.cell.2005.08.031 · Cited by 870
Evolutionary Rate in the Protein Interaction Network
Fraser, H. B., Hirsh, A. E., Steinmetz, L. M., Scharfe, C., & Feldman, M. W. (2002) · Science · doi:10.1126/science.1068696 · Cited by 869
AIP1/ALIX Is a Binding Partner for HIV-1 p6 and EIAV p9 Functioning in Virus Budding
Strack, B., Calistri, A., Craig, S., Popova, E., & Göttlinger, H. G. (2003) · Cell · doi:10.1016/s0092-8674(03)00653-6 · Cited by 825
Protein-Protein Interaction Detection: Methods and Analysis
Rao, V. S., Srinivas, K., Sujini, G. N., & Kumar, G. N. S. (2014) · International Journal of Proteomics · doi:10.1155/2014/147648 · Cited by 811
Quantitative mass spectrometry in proteomics: critical review update from 2007 to the present
Bantscheff, M., Lemeer, S., Savitski, M. M., & Kuster, B. (2012) · Analytical and Bioanalytical Chemistry · doi:10.1007/s00216-012-6203-4 · Cited by 801
Toward a Comprehensive Atlas of the Physical Interactome of Saccharomyces cerevisiae
Collins, S. R., Kemmeren, P., Zhao, X.-C., Greenblatt, J. F., Spencer, F., Holstege, F. C. P., Weissman, J. S., & Krogan, N. J. (2007) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m600381-mcp200 · Cited by 795
Phosphotyrosine interactome of the ErbB‐receptor kinase family
Schulze, W. X., Deng, L., & Mann, M. (2005) · Molecular Systems Biology · doi:10.1038/msb4100012 · Cited by 753
Dosage sensitivity and the evolution of gene families in yeast
Papp, B., Pál, C., & Hurst, L. D. (2003) · Nature · doi:10.1038/nature01771 · Cited by 753
The enzymes and control of eukaryotic mRNA turnover
Parker, R., & Song, H. (2004) · Nature Structural & Molecular Biology · doi:10.1038/nsmb724 · Cited by 730
Henry, K. W., Wyce, A., Lo, W.-S., Duggan, L. J., Emre, N. C. T., Kao, C.-F., Pillus, L., Shilatifard, A., Osley, M. A., & Berger, S. L. (2003) · Genes & Development · doi:10.1101/gad.1144003 · Cited by 714
CAPRI: A Critical Assessment of PRedicted Interactions
Janin, J., Henrick, K., Moult, J., Eyck, L. T., Sternberg, M. J. E., Vajda, S., Vakser, I., & Wodak, S. J. (2003) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.10381 · Cited by 703
Principles of Protein−Protein Interactions: What are the Preferred Ways For Proteins To Interact?
Keskin, O., Gursoy, A., Ma, B., & Nussinov, R. (2008) · Chemical Reviews · doi:10.1021/cr040409x · Cited by 697
Quantitative, High-Resolution Proteomics for Data-Driven Systems Biology
Cox, J., & Mann, M. (2011) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-061308-093216 · Cited by 685
Multidimensional Drug Profiling By Automated Microscopy
Perlman, Z. E., Slack, M. D., Feng, Y., Mitchison, T. J., Wu, L. F., & Altschuler, S. J. (2004) · Science · doi:10.1126/science.1100709 · Cited by 660
Histone acetylation and deacetylation in yeast
Kurdistani, S. K., & Grunstein, M. (2003) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1075 · Cited by 677
Exploring genetic interactions and networks with yeast
Boone, C., Bussey, H., & Andrews, B. J. (2007) · Nature Reviews Genetics · doi:10.1038/nrg2085 · Cited by 661
Exploration of Essential Gene Functions via Titratable Promoter Alleles
Mnaimneh, S., Davierwala, A. P., Haynes, J., Moffat, J., Peng, W.-T., Zhang, W., Yang, X., Pootoolal, J., Chua, G., Lopez, A., et al. (2004) · Cell · doi:10.1016/j.cell.2004.06.013 · Cited by 604
Doyon, Y., Selleck, W., Lane, W. S., Tan, S., & Côté, J. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.5.1884-1896.2004 · Cited by 597
A systems approach to measuring the binding energy landscapes of transcription factors.
Maerkl, S. J., & Quake, S. R. (2007) · Science · doi:10.1126/science.1131007 · Cited by 584
Protein interaction mapping: A Drosophila case study
Formstecher, E., Aresta, S., Collura, V., Hamburger, A., Meil, A., Trehin, A., Reverdy, C., Betin, V., Maire, S., Brun, C., et al. (2005) · Genome Research · doi:10.1101/gr.2659105 · Cited by 542
Proteome organization in a genome-reduced bacterium
Kühner, S., van Noort, V., Betts, M. J., Leo-Macias, A., Batisse, C., Rode, M., Yamada, T., Maier, T., Bader, S., Beltran-Alvarez, P., et al. (2009) · Science · doi:10.1126/science.1176343 · Cited by 471
Self-citationFranke, L., Bakel, H. V., Fokkens, L., de Jong, E. D., Egmont-Petersen, M., & Wijmenga, C. (2006) · The American Journal of Human Genetics · doi:10.1086/504300 · Cited by 476
Comprehensive Identification of Human bZIP Interactions with Coiled-Coil Arrays
Newman, J. R. S., & Keating, A. E. (2003) · Science · doi:10.1126/science.1084648 · Cited by 449
Systematic interpretation of genetic interactions using protein networks
Kelley, R., & Ideker, T. (2005) · Nature Biotechnology · doi:10.1038/nbt1096 · Cited by 437
Zhang, X.-Y., Varthi, M., Sykes, S. M., Phillips, C., Warzecha, C., Zhu, W., Wyce, A., Thorne, A. W., Berger, S. L., & McMahon, S. B. (2008) · Molecular Cell · doi:10.1016/j.molcel.2007.12.015 · Cited by 427
Large-scale identification of protein–protein interaction of Escherichia coli K-12
Arifuzzaman, M., Maeda, M., Itoh, A., Nishikata, K., Takita, C., Saito, R., Ara, T., Nakahigashi, K., Huang, H.-C., Hirai, A., et al. (2006) · Genome Research · doi:10.1101/gr.4527806 · Cited by 403
Structure-Based Assembly of Protein Complexes in Yeast
Aloy, P., Böttcher, B., Ceulemans, H., Leutwein, C., Mellwig, C., Fischer, S., Gavin, A.-C., Bork, P., Superti-Furga, G., Serrano, L., et al. (2004) · Science · doi:10.1126/science.1092645 · Cited by 383
Self-citationGoudreault, M., D'Ambrosio, L. M., Kean, M. J., Mullin, M. J., Larsen, B. G., Sanchez, A., Chaudhry, S., Chen, G. I., Sicheri, F., Nesvizhskii, A. I., et al. (2009) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m800266-mcp200 · Cited by 359
Affinity-purification coupled to mass spectrometry: basic principles and strategies
Dunham, W. H., Mullin, M., & Gingras, A. (2012) · PROTEOMICS · doi:10.1002/pmic.201100523 · Cited by 368
A Systematic Mammalian Genetic Interaction Map Reveals Pathways Underlying Ricin Susceptibility
Bassik, M. C., Kampmann, M., Lebbink, R. J., Wang, S., Hein, M. Y., Poser, I., Weibezahn, J., Horlbeck, M. A., Chen, S., Mann, M., et al. (2013) · Cell · doi:10.1016/j.cell.2013.01.030 · Cited by 365
Conservation and Rewiring of Functional Modules Revealed by an Epistasis Map in Fission Yeast
Roguev, A., Bandyopadhyay, S., Zofall, M., Zhang, K., Fischer, T., Collins, S. R., Qu, H., Shales, M., Park, H.-O., Hayles, J., et al. (2008) · Science · doi:10.1126/science.1162609 · Cited by 352
Messenger RNA Turnover in Eukaryotes: Pathways and Enzymes
Meyer, S., Temme, C., & Wahle, E. (2004) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409230490513991 · Cited by 342
Disorder and Sequence Repeats in Hub Proteins and Their Implications for Network Evolution
Dosztányi, Z., Chen, J., Dunker, A. K., Simon, I., & Tompa, P. (2006) · Journal of Proteome Research · doi:10.1021/pr060171o · Cited by 341
Comprehensive curation and analysis of global interaction networks in Saccharomyces cerevisiae
Reguly, T., Breitkreutz, A., Boucher, L., Breitkreutz, B.-J., Hon, G. C., Myers, C. L., Parsons, A., Friesen, H., Oughtred, R., Tong, A., et al. (2006) · Journal of Biology · doi:10.1186/jbiol36 · Cited by 326
Quantification of mRNA and protein and integration with protein turnover in a bacterium
Maier, T., Schmidt, A., Güell, M., Kühner, S., Gavin, A., Aebersold, R., & Serrano, L. (2011) · Molecular Systems Biology · doi:10.1038/msb.2011.38 · Cited by 297
Self-citationGenome-wide analysis of Notch signalling in Drosophila by transgenic RNAi
Mummery-Widmer, J. L., Yamazaki, M., Stoeger, T., Novatchkova, M., Bhalerao, S., Chen, D., Dietzl, G., Dickson, B. J., & Knoblich, J. A. (2009) · Nature · doi:10.1038/nature07936 · Cited by 305
Lage, K., Hansen, N. T., Karlberg, E. O., Eklund, A. C., Roque, F. S., Donahoe, P. K., Szallasi, Z., Jensen, T. S., & Brunak, S. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0810772105 · Cited by 292
Cryo-electron microscopy--a primer for the non-microscopist
Milne, J. L. S., Borgnia, M. J., Bartesaghi, A., Tran, E. E. H., Earl, L. A., Schauder, D. M., Lengyel, J., Pierson, J., Patwardhan, A., & Subramaniam, S. (2013) · The FEBS Journal · doi:10.1111/febs.12078 · Cited by 277
Bridging structural biology and genomics: assessing protein interaction data with known complexes
Edwards, A. M., Kus, B., Jansen, R., Greenbaum, D., Greenblatt, J., & Gerstein, M. (2002) · Trends in Genetics · doi:10.1016/s0168-9525(02)02763-4 · Cited by 276
Ca2+-Activated K+Channels: From Protein Complexes to Function
Berkefeld, H., Fakler, B., & Schulte, U. (2010) · Physiological Reviews · doi:10.1152/physrev.00049.2009 · Cited by 274
Systematic gene tagging using CRISPR/Cas9 in human stem cells to illuminate cell organization
Roberts, B., Haupt, A., Tucker, A., Grancharova, T., Arakaki, J., Fuqua, M. A., Nelson, A., Hookway, C., Ludmann, S. A., Mueller, I. A., et al. (2017) · Molecular Biology of the Cell · doi:10.1091/mbc.e17-03-0209 · Cited by 262
A Systems Biology Approach for the Investigation of the Heparin/Heparan Sulfate Interactome
Ori, A., Wilkinson, M. C., & Fernig, D. G. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.228114 · Cited by 251
Combining biological networks to predict genetic interactions
Wong, S. L., Zhang, L. V., Tong, A. H. Y., Li, Z., Goldberg, D. S., King, O. D., Lesage, G., Vidal, M., Andrews, B., Bussey, H., et al. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0406614101 · Cited by 245
Henriksen, P., Wagner, S. A., Weinert, B. T., Sharma, S., Bačinskaja, G., Rehman, M., Juffer, A. H., Walther, T. C., Lisby, M., & Choudhary, C. (2012) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m112.017251 · Cited by 246
Clathrin-mediated endocytosis in budding yeast
Weinberg, J., & Drubin, D. G. (2012) · Trends in Cell Biology · doi:10.1016/j.tcb.2011.09.001 · Cited by 236
Probabilistic assembly of human protein interaction networks from label-free quantitative proteomics
Sardiu, M. E., Cai, Y., Jin, J., Swanson, S. K., Conaway, R. C., Conaway, J. W., Florens, L., & Washburn, M. P. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0706983105 · Cited by 226
The diverse and expanding role of mass spectrometry in structural and molecular biology
Lössl, P., van de Waterbeemd, M., & Heck, A. J. (2016) · The EMBO Journal · doi:10.15252/embj.201694818 · Cited by 222
The interaction network of the chaperonin CCT
Dekker, C., Stirling, P. C., McCormack, E. A., Filmore, H., Paul, A., Brost, R. L., Costanzo, M., Boone, C., Leroux, M. R., & Willison, K. R. (2008) · The EMBO Journal · doi:10.1038/emboj.2008.108 · Cited by 220
Integrating physical and genetic maps: from genomes to interaction networks
Beyer, A., Bandyopadhyay, S., & Ideker, T. (2007) · Nature Reviews Genetics · doi:10.1038/nrg2144 · Cited by 207
Green plants as intelligent organisms
Trewavas, A. (2005) · Trends in Plant Science · doi:10.1016/j.tplants.2005.07.005 · Cited by 212
Protein-protein interaction networks: probing disease mechanisms using model systems
Kuzmanov, U., & Emili, A. (2013) · Genome Medicine · doi:10.1186/gm441 · Cited by 197
Powering through ribosome assembly
Strunk, B. S., & Karbstein, K. (2009) · RNA · doi:10.1261/rna.1792109 · Cited by 191
Biochemical approaches for discovering protein–protein interactions
Miernyk, J. A., & Thelen, J. J. (2008) · The Plant Journal · doi:10.1111/j.1365-313x.2007.03316.x · Cited by 165
Adkins, M. W., & Tyler, J. K. (2006) · Molecular Cell · doi:10.1016/j.molcel.2005.12.010 · Cited by 162
Identification of Protein Interactions Involved in Cellular Signaling
Westermarck, J., Ivaska, J., & Corthals, G. L. (2013) · Molecular & Cellular Proteomics · doi:10.1074/mcp.r113.027771 · Cited by 143
Protein–protein interaction networks: how can a hub protein bind so many different partners?
Tsai, C.-J., Ma, B., & Nussinov, R. (2009) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2009.07.007 · Cited by 138
Wakabayashi, T., Craessaerts, K., Bammens, L., Bentahir, M., Borgions, F., Herdewijn, P., Staes, A., Timmerman, E., Vandekerckhove, J., Rubinstein, E., et al. (2009) · Nature Cell Biology · doi:10.1038/ncb1978 · Cited by 135
I-DIRT, A General Method for Distinguishing between Specific and Nonspecific Protein Interactions
Tackett, A. J., DeGrasse, J. A., Sekedat, M. D., Oeffinger, M., Rout, M. P., & Chait, B. T. (2005) · Journal of Proteome Research · doi:10.1021/pr050225e · Cited by 131
The Revolution and Evolution of Shotgun Proteomics for Large-Scale Proteome Analysis
Yates, J. R. (2013) · Journal of the American Chemical Society · doi:10.1021/ja3094313 · Cited by 131
Macromolecular complexes as depots for releasable regulatory proteins
RAY, P., ARIF, A., & FOX, P. (2007) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2007.02.003 · Cited by 129
The social and structural architecture of the yeast protein interactome
Michaelis, A. C., Brunner, A.-D., Zwiebel, M., Meier, F., Strauss, M. T., Bludau, I., & Mann, M. (2023) · Nature · doi:10.1038/s41586-023-06739-5 · Cited by 119
“The large-scale study of cellular interactomes using mass spectrometry-based proteomics dates back over 20 years 3,4 , culminating in 2 studies in which nearly half the expressed yeast proteome was successfully purified with identified interactors 5,6 .”
BackgroundNi, D., Lu, S., & Zhang, J. (2019) · Medicinal Research Reviews · doi:10.1002/med.21585 · Cited by 116
Dosage suppression genetic interaction networks enhance functional wiring diagrams of the cell
Magtanong, L., Ho, C. H., Barker, S. L., Jiao, W., Baryshnikova, A., Bahr, S., Smith, A. M., Heisler, L. E., Choy, J. S., Kuzmin, E., et al. (2011) · Nature Biotechnology · doi:10.1038/nbt.1855 · Cited by 108
Lasserre, J., Beyne, E., Pyndiah, S., Lapaillerie, D., Claverol, S., & Bonneu, M. (2006) · ELECTROPHORESIS · doi:10.1002/elps.200500912 · Cited by 103
Fernández‐Montalván, A., Bouwmeester, T., Joberty, G., Mader, R., Mahnke, M., Pierrat, B., Schlaeppi, J., Worpenberg, S., & Gerhartz, B. (2007) · The FEBS Journal · doi:10.1111/j.1742-4658.2007.05952.x · Cited by 96
Self-citationGupta, I., Clauder‐Münster, S., Klaus, B., Järvelin, A. I., Aiyar, R. S., Benes, V., Wilkening, S., Huber, W., Pelechano, V., & Steinmetz, L. M. (2014) · Molecular Systems Biology · doi:10.1002/msb.135068 · Cited by 95
A credit-card library approach for disrupting protein–protein interactions
Xu, Y., Shi, J., Yamamoto, N., Moss, J. A., Vogt, P. K., & Janda, K. D. (2006) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2005.11.052 · Cited by 93
The LAP family: a phylogenetic point of view
Santoni, M.-J., Pontarotti, P., Birnbaum, D., & Borg, J.-P. (2002) · Trends in Genetics · doi:10.1016/s0168-9525(02)02738-5 · Cited by 88
McConnell, J. L., Gomez, R. J., McCorvey, L. R. A., Law, B. K., & Wadzinski, B. E. (2007) · Oncogene · doi:10.1038/sj.onc.1210406 · Cited by 80
Valouev, I. A., Kushnirov, V. V., & Ter‐Avanesyan, M. D. (2002) · Cell Motility · doi:10.1002/cm.10040 · Cited by 81
Camera, P., Da Silva, J. S., Griffiths, G., Giuffrida, M. G., Ferrara, L., Schubert, V., Imarisio, S., Silengo, L., Dotti, C. G., & Di Cunto, F. (2003) · Nature Cell Biology · doi:10.1038/ncb1064 · Cited by 78
VisANT 3.0: new modules for pathway visualization, editing, prediction and construction
Hu, Z., Ng, D. M., Yamada, T., Chen, C., Kawashima, S., Mellor, J., Linghu, B., Kanehisa, M., Stuart, J. M., & DeLisi, C. (2007) · Nucleic Acids Research · doi:10.1093/nar/gkm295 · Cited by 76
Cornet, M., Bidard, F., Schwarz, P., Da Costa, G., Blanchin-Roland, S., Dromer, F., & Gaillardin, C. (2005) · Infection and Immunity · doi:10.1128/iai.73.12.7977-7987.2005 · Cited by 70
Integrative structure modeling of macromolecular assemblies from proteomics data
Lasker, K., Phillips, J. L., Russel, D., Velázquez-Muriel, J., Schneidman-Duhovny, D., Tjioe, E., Webb, B., Schlessinger, A., & Sali, A. (2010) · Molecular & Cellular Proteomics · doi:10.1074/mcp.r110.000067 · Cited by 71
Temporal patterns of genes in scientific publications
Pfeiffer, T., & Hoffmann, R. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0701315104 · Cited by 64
Choi, H., Glatter, T., Gstaiger, M., & Nesvizhskii, A. I. (2012) · Journal of Proteome Research · doi:10.1021/pr201185r · Cited by 68
A Novel Requirement for C. elegans Alix/ALX-1 in RME-1-Mediated Membrane Transport
Shi, A., Pant, S., Balklava, Z., Chen, C. C.-H., Figueroa, V., & Grant, B. D. (2007) · Current Biology · doi:10.1016/j.cub.2007.10.045 · Cited by 64
Song, W.-M., Agrawal, P., Von Itter, R., Fontanals-Cirera, B., Wang, M., Zhou, X., Mahal, L. K., Hernando, E., & Zhang, B. (2021) · Nature Communications · doi:10.1038/s41467-021-21457-0 · Cited by 62
Metadata
- Authors
- Gavin, A.-C., Bösche, M., Krause, R., Grandi, P., Marzioch, M., Bauer, A., Schultz, J., Rick, J. M., Michon, A.-M., Cruciat, C.-M., Remor, M., Höfert, C., Schelder, M., Brajenovic, M., Ruffner, H., Merino, A., Klein, K., Hudak, M., Dickson, D., Rudi, T., Gnau, V., Bauch, A., Bastuck, S., Huhse, B., Leutwein, C., Heurtier, M.-A., Copley, R. R., Edelmann, A., Querfurth, E., Rybin, V., Drewes, G., Raida, M., Bouwmeester, T., Bork, P., Seraphin, B., Kuster, B., Neubauer, G., & Superti-Furga, G.
- Venue
- Nature
- Published
- 2002-01
- Volume
- 415
- Issue
- 6868
- Pages
- 141-147
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W2084619201
- Cited by
- 4,759
- References
- 4
- FWCI
- 157.24
- Type
- journal article
- Language
- en
- Open access
- green
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
