The DOI matches its Crossref record; 14 of the 14 references it cites were found in a registry or an index.
Assembly of Cell Regulatory Systems Through Protein Interaction Domains
Abstract
The sequencing of complete genomes provides a list that includes the proteins responsible for cellular regulation. However, this does not immediately reveal what these proteins do, nor how they are assembled into the molecular machines and functional networks that control cellular behavior. The regulation of many different cellular processes requires the use of protein interaction domains to direct the association of polypeptides with one another and with phospholipids, small molecules, or nucleic acids. The modular nature of these domains, and the flexibility of their binding properties, have likely facilitated the evolution of cellular pathways. Conversely, aberrant interactions can induce abnormal cellular behavior and disease. The fundamental properties of protein interaction domains are discussed in this review and in detailed reviews on individual domains at Science 's STKE at http://www.sciencemag.org/cgi/content/full/300/5618/445/DC1 .
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
The sequence of the human genome
Venter, J. C., Adams, M. D., Myers, E. W., Li, P. W., Mural, R. J., Sutton, G. G., Smith, H. O., Yandell, M., Evans, C. A., Holt, R. A., et al. (2001) · Science · doi:10.1126/science.1058040 · Cited by 13,909
Error and attack tolerance of complex networks
Albert, R., Jeong, H., & Barabási, A.-L. (2000) · Nature · doi:10.1038/35019019 · Cited by 7,534
Takeda, K., Kaisho, T., & Akira, S. (2003) · Annual Review of Immunology · doi:10.1146/annurev.immunol.21.120601.141126 · Cited by 6,143
Death Receptors: Signaling and Modulation
Ashkenazi, A., & Dixit, V. M. (1998) · Science · doi:10.1126/science.281.5381.1305 · Cited by 5,866
Jaakkola, P., Mole, D. R., Tian, Y.-M., Wilson, M. I., Gielbert, J., Gaskell, S. J., Kriegsheim, A. V., Hebestreit, H. F., Mukherji, M., Schofield, C. J., et al. (2001) · Science · doi:10.1126/science.1059796 · Cited by 5,535
HIFα Targeted for VHL-Mediated Destruction by Proline Hydroxylation: Implications for O 2 Sensing
Ivan, M., Kondo, K., Yang, H., Kim, W., Valiando, J., Ohh, M., Salic, A., Asara, J. M., Lane, W. S., & Kaelin Jr., W. G. (2001) · Science · doi:10.1126/science.1059817 · Cited by 4,735
Protein modules and signalling networks
Pawson, T. (1995) · Nature · doi:10.1038/373573a0 · Cited by 2,420
Self-citationStructure of the Cul1–Rbx1–Skp1–F boxSkp2 SCF ubiquitin ligase complex
Zheng, N., Schulman, B. A., Song, L., Miller, J. J., Jeffrey, P. D., Wang, P., Chu, C., Koepp, D. M., Elledge, S. J., Pagano, M., et al. (2002) · Nature · doi:10.1038/416703a · Cited by 1,507
Recognition of Unique Carboxyl-Terminal Motifs by Distinct PDZ Domains
Songyang, Z., Fanning, A. S., Fu, C., Xu, J., Marfatia, S. M., Chishti, A. H., Crompton, A., Chan, A. C., Anderson, J. M., & Cantley, L. C. (1997) · Science · doi:10.1126/science.275.5296.73 · Cited by 1,385
The cell-polarity protein Par6 links Par3 and atypical protein kinase C to Cdc42
Joberty, G., Petersen, C., Gao, L., & Macara, I. G. (2000) · Nature Cell Biology · doi:10.1038/35019573 · Cited by 928
Cited by
BioGRID: a general repository for interaction datasets
Stark, C. (2006) · Nucleic Acids Research · doi:10.1093/nar/gkj109 · Cited by 3,960
Quantifying similarity between motifs
Gupta, S., Stamatoyannopoulos, J. A., Bailey, T. L., & Noble, W. S. (2007) · Genome Biology · doi:10.1186/gb-2007-8-2-r24 · Cited by 2,058
Molecular determinants of the response of glioblastomas to EGFR kinase inhibitors
Mellinghoff, I. K., Wang, M. Y., Vivanco, I., Haas-Kogan, D. A., Zhu, S., Dia, E. Q., Lu, K. V., Yoshimoto, K., Huang, J. H. Y., Chute, D. J., et al. (2005) · New England Journal of Medicine · doi:10.1056/nejmoa051918 · Cited by 1,442
Cell-signalling dynamics in time and space
Kholodenko, B. N. (2006) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1838 · Cited by 1,347
LDL receptor-related proteins 5 and 6 in Wnt/β-catenin signaling:Arrows point the way
He, X., Semenov, M., Tamai, K., & Zeng, X. (2004) · Development · doi:10.1242/dev.01117 · Cited by 1,044
RAS Interaction with PI3K: More Than Just Another Effector Pathway
Castellano, E., & Downward, J. (2011) · Genes & Cancer · doi:10.1177/1947601911408079 · Cited by 762
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
Structure and regulation of Src family kinases
Boggon, T. J., & Eck, M. J. (2004) · Oncogene · doi:10.1038/sj.onc.1208081 · Cited by 712
Calculation of absolute protein–ligand binding free energy from computer simulations
Woo, H.-J., & Roux, B. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0409005102 · Cited by 661
BRCT Repeats As Phosphopeptide-Binding Modules Involved in Protein Targeting
Manke, I. A., Lowery, D. M., Nguyen, A., & Yaffe, M. B. (2003) · Science · doi:10.1126/science.1088877 · Cited by 651
Structure and function of plant photoreceptors
Möglich, A., Yang, X., Ayers, R. A., & Moffat, K. (2010) · Annual Review of Plant Biology · doi:10.1146/annurev-arplant-042809-112259 · Cited by 499
A Specificity Map for the PDZ Domain Family
Tonikian, R., Zhang, Y., Sazinsky, S. L., Currell, B., Yeh, J.-H., Reva, B., Held, H. A., Appleton, B. A., Evangelista, M., Wu, Y., et al. (2008) · PLoS Biology · doi:10.1371/journal.pbio.0060239 · Cited by 476
Brain endothelial cells and the glio-vascular complex
Wolburg, H., Noell, S., Mack, A., Wolburg-Buchholz, K., & Fallier-Becker, P. (2009) · Cell and Tissue Research · doi:10.1007/s00441-008-0658-9 · Cited by 438
YAP/TAZ as mechanosensors and mechanotransducers in regulating organ size and tumor growth
Low, B. C., Pan, C. Q., Shivashankar, G. V., Bershadsky, A., Sudol, M., & Sheetz, M. (2014) · FEBS Letters · doi:10.1016/j.febslet.2014.04.012 · Cited by 412
Systematic Discovery of New Recognition Peptides Mediating Protein Interaction Networks
Neduva, V., Linding, R., Su-Angrand, I., Stark, A., Masi, F. D., Gibson, T. J., Lewis, J., Serrano, L., & Russell, R. B. (2005) · PLoS Biology · doi:10.1371/journal.pbio.0030405 · Cited by 359
Rules for Modeling Signal-Transduction Systems
Hlavacek, W. S., Faeder, J. R., Blinov, M. L., Posner, R. G., Hucka, M., & Fontana, W. (2006) · Science's STKE · doi:10.1126/stke.3442006re6 · Cited by 350
SAM domains: uniform structure, diversity of function
Kim, C. (2003) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2003.11.001 · Cited by 259
Polyelectrostatic interactions of disordered ligands suggest a physical basis for ultrasensitivity
Borg, M., Mittag, T., Pawson, T., Tyers, M., Forman-Kay, J. D., & Chan, H. S. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0702580104 · Cited by 245
Self-citationSaccharomyces cerevisiae Rad9 acts as a Mec1 adaptor to allow Rad53 activation
Sweeney, F. D., Yang, F., Chi, A., Shabanowitz, J., Hunt, D. F., & Durocher, D. (2005) · Current Biology · doi:10.1016/j.cub.2005.06.063 · Cited by 237
Distinct enzyme combinations in AKAP signalling complexes permit functional diversity
Hoshi, N., Langeberg, L. K., & Scott, J. D. (2005) · Nature Cell Biology · doi:10.1038/ncb1315 · Cited by 183
Sheng, R., Chen, Y., Yung Gee, H., Stec, E., Melowic, H. R., Blatner, N. R., Tun, M. P., Kim, Y., Källberg, M., Fujiwara, T. K., et al. (2012) · Nature Communications · doi:10.1038/ncomms2221 · Cited by 179
London, N., Raveh, B., Movshovitz‐Attias, D., & Schueler‐Furman, O. (2010) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.22785 · Cited by 164
Structure of a BCOR Corepressor Peptide in Complex with the BCL6 BTB Domain Dimer
Ghetu, A. F., Corcoran, C. M., Cerchietti, L., Bardwell, V. J., Melnick, A., & Privé, G. G. (2008) · Molecular Cell · doi:10.1016/j.molcel.2007.12.026 · Cited by 168
Bae, J. H., Lew, E. D., Yuzawa, S., Tomé, F., Lax, I., & Schlessinger, J. (2009) · Cell · doi:10.1016/j.cell.2009.05.028 · Cited by 158
Loops Govern SH2 Domain Specificity by Controlling Access to Binding Pockets
Kaneko, T., Huang, H., Zhao, B., Li, L., Liu, H., Voss, C. K., Wu, C., Schiller, M. R., & Li, S. S.-C. (2010) · Science Signaling · doi:10.1126/scisignal.2000796 · Cited by 146
Spatially Separate Docking Sites on ERK2 Regulate Distinct Signaling Events In Vivo
Dimitri, C. A., Dowdle, W., MacKeigan, J. P., Blenis, J., & Murphy, L. O. (2005) · Current Biology · doi:10.1016/j.cub.2005.06.037 · Cited by 114
Quantifying the mechanisms of domain gain in animal proteins
Buljan, M., Frankish, A., & Bateman, A. (2010) · Genome Biology · doi:10.1186/gb-2010-11-7-r74 · Cited by 112
Clark, A. J., Negron, C., Hauser, K., Sun, M., Wang, L., Abel, R., & Friesner, R. A. (2019) · Journal of Molecular Biology · doi:10.1016/j.jmb.2019.02.003 · Cited by 91
Phospholipase C families: Common themes and versatility in physiology and pathology
Katan, M., & Cockcroft, S. (2020) · Progress in Lipid Research · doi:10.1016/j.plipres.2020.101065 · Cited by 89
Systems biology—an engineering perspective
Kremling, A., & Saez-Rodriguez, J. (2007) · Journal of Biotechnology · doi:10.1016/j.jbiotec.2007.02.009 · Cited by 76
Initial characterization of the human central proteome
Burkard, T. R., Planyavsky, M., Kaupe, I., Breitwieser, F. P., Bürckstümmer, T., Bennett, K. L., Superti-Furga, G., & Colinge, J. (2011) · BMC Systems Biology · doi:10.1186/1752-0509-5-17 · Cited by 67
Quantitative Analysis of ERK2 Interactions with Substrate Proteins
Burkhard, K. A., Chen, F., & Shapiro, P. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.177899 · Cited by 62
Quantitative fragmentomics allow affinity mapping of interactomes
Gogl, G., Zambo, B., Kostmann, C., Cousido-Siah, A., Morlet, B., Durbesson, F., Negroni, L., Eberling, P., Jané, P., Nominé, Y., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-33018-0 · Cited by 51
Evolving specificity from variability for protein interaction domains
Kaneko, T., Sidhu, S. S., & Li, S. S. C. (2011) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2010.12.001 · Cited by 45
Identifying polymer‐forming SAM domains
Meruelo, A. D., & Bowie, J. U. (2009) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.22232 · Cited by 40
Koveal, D., Schuh-Nuhfer, N., Ritt, D., Page, R., Morrison, D. K., & Peti, W. (2012) · Science Signaling · doi:10.1126/scisignal.2003289 · Cited by 36
Hartmann, C., Schwietzer, Y. A., Kummer, D., Kirschnick, N., Hoppe, E., Thüring, E.-M., Glaesner-Ebnet, M., Brinkmann, F., Gerke, V., Reuter, S., et al. (2020) · BMC Molecular and Cell Biology · doi:10.1186/s12860-020-00274-1 · Cited by 32
Blinov, M. L., Ruebenacker, O., & Moraru, I. I. (2008) · IET Systems Biology · doi:10.1049/iet-syb:20080092 · Cited by 25
Metadata
- Authors
- Pawson, T., & Nash, P.
- Venue
- Science
- Published
- 2003-04-18
- Volume
- 300
- Issue
- 5618
- Pages
- 445-452
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2145080853
- Cited by
- 1,422
- References
- 14
- FWCI
- 32.49
- Type
- journal article
- Language
- en
- Open access
- closed
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.