The DOI matches its Crossref record; 20 of the 20 references it cites were found in a registry or an index.
Domains, Motifs, and Scaffolds: The Role of Modular Interactions in the Evolution and Wiring of Cell Signaling Circuits
Abstract
Living cells display complex signal processing behaviors, many of which are mediated by networks of proteins specialized for signal transduction. Here we focus on the question of how the remarkably diverse array of eukaryotic signaling circuits may have evolved. Many of the mechanisms that connect signaling proteins into networks are highly modular: The core catalytic activity of a signaling protein is physically and functionally separable from molecular domains or motifs that determine its linkage to both inputs and outputs. This high degree of modularity may make these systems more evolvable—in principle, novel circuits, and therefore highly innovative regulatory behaviors, can arise from relatively simple genetic events such as recombination, deletion, or insertion. In support of this hypothesis, recent studies show that such modular systems can be exploited to engineer nonnatural signaling proteins and pathways with novel behavior.
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
AKAP signalling complexes: focal points in space and time
Wong, W., & Scott, J. D. (2004) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1527 · Cited by 1,073
Evolution at Two Levels: On Genes and Form
Carroll, S. B. (2005) · PLoS Biology · doi:10.1371/journal.pbio.0030245 · Cited by 882
Benner, S. A., & Sismour, A. M. (2005) · Nature Reviews Genetics · doi:10.1038/nrg1637 · Cited by 834
A conserved docking motif in MAP kinases common to substrates, activators and regulators
Tanoue, T., Adachi, M., Moriguchi, T., & Nishida, E. (2000) · Nature Cell Biology · doi:10.1038/35000065 · Cited by 816
A Mammalian Scaffold Complex That Selectively Mediates MAP Kinase Activation
Whitmarsh, A. J., Cavanagh, J., Tournier, C., Yasuda, J., & Davis, R. J. (1998) · Science · doi:10.1126/science.281.5383.1671 · Cited by 652
Bow ties, metabolism and disease
Csete, M., & Doyle, J. (2004) · Trends in biotechnology · doi:10.1016/j.tibtech.2004.07.007 · Cited by 468
Evolution of Key Cell Signaling and Adhesion Protein Families Predates Animal Origins
King, N., Hittinger, C. T., & Carroll, S. B. (2003) · Science · doi:10.1126/science.1083853 · Cited by 424
Rotation of photoreceptor clusters in the developing drosophila eye requires the nemo gene
Choi, K.-W., & Benzer, S. (1994) · Cell · doi:10.1016/0092-8674(94)90579-7 · Cited by 339
Signalling specificity of Ser/Thr protein kinases through docking-site-mediated interactions
BIONDI, R. M., & NEBREDA, A. R. (2003) · Biochemical Journal · doi:10.1042/bj20021641 · Cited by 334
Chang, C.-I., Xu, B.-E., Akella, R., Cobb, M. H., & Goldsmith, E. J. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00525-7 · Cited by 302
Ory, S., Zhou, M., Conrads, T. P., Veenstra, T. D., & Morrison, D. K. (2003) · Current Biology · doi:10.1016/s0960-9822(03)00535-9 · Cited by 296
Structure, function, and biology of SHIP proteins
Rohrschneider, L. R., Fuller, J. F., Wolf, I., Liu, Y., & Lucas, D. M. (2000) · Genes & Development · doi:10.1101/gad.14.5.505 · Cited by 294
Regulation of actin dynamics by WASP and WAVE family proteins
Stradal, T. E. B., Rottner, K., Disanza, A., Confalonieri, S., Innocenti, M., & Scita, G. (2004) · Trends in Cell Biology · doi:10.1016/j.tcb.2004.04.007 · Cited by 286
Docking Motif Interactions in MAP Kinases Revealed by Hydrogen Exchange Mass Spectrometry
Lee, T., Hoofnagle, A. N., Kabuyama, Y., Stroud, J., Min, X., Goldsmith, E. J., Chen, L., Resing, K. A., & Ahn, N. G. (2004) · Molecular Cell · doi:10.1016/s1097-2765(04)00161-3 · Cited by 282
Structural basis for the selective inhibition of JNK1 by the scaffolding protein JIP1 and SP600125
Heo, Y., Kim, S., Seo, C. I., Kim, Y. K., Sung, B., Lee, H. S., Lee, J. I., Park, S., Kim, J. H., Hwang, K. Y., et al. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600212 · Cited by 275
Custom zinc-finger nucleases for use in human cells
Alwin, S., Gere, M. B., Guhl, E., Effertz, K., Barbas, C. F., Segal, D. J., Weitzman, M. D., & Cathomen, T. (2005) · Molecular Therapy · doi:10.1016/j.ymthe.2005.06.094 · Cited by 165
Bardwell, L., Cook, J. G., Chang, E. C., Cairns, B. R., & Thorner, J. (1996) · Molecular and Cellular Biology · doi:10.1128/mcb.16.7.3637 · Cited by 161
Ho, D. T., Bardwell, A. J., Abdollahi, M., & Bardwell, L. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m304229200 · Cited by 108
A conserved protein interaction network involving the yeast MAP kinases Fus3 and Kss1
Kusari, A. B., Molina, D. M., Sabbagh, W., Lau, C. S., & Bardwell, L. (2004) · The Journal of Cell Biology · doi:10.1083/jcb.200310021 · Cited by 81
Research works printed but not linked: 138
- 10.1038/35057062 · DOI · Paper page
- 10.1038/35057277 · DOI
- 10.1038/35011540 · DOI · Paper page
- 10.1038/nsmb820 · DOI · Paper page
- Ptashne M, 2002, Genes and Signals
- 10.1126/science.1113833 · DOI
- 10.1073/pnas.95.15.8420 · DOI · Paper page
- 10.1016/S0022-2836(63)80091-1 · DOI
- 10.1038/scientificamerican1278-92 · DOI
- 10.1126/science.1083653 · DOI · Paper page
- 10.1038/nmeth731 · DOI · Paper page
- 10.1002/cber.18940270364 · DOI
- 10.1111/j.1538-7836.2004.01021.x · DOI
- 10.1385/MB:22:1:051 · DOI
- 10.1016/S0960-9822(99)80205-X · DOI
- 10.1073/pnas.72.9.3448 · DOI
- 10.1038/nmeth708 · DOI
- 10.1016/S0960-9822(00)00221-9 · DOI
- 10.1021/ar020116v · DOI
- 10.1126/science.278.5337.455 · DOI
- 10.1016/S0968-0004(00)01627-3 · DOI · Paper page
- 10.1101/gad.13.20.2678 · DOI · Paper page
- 10.1016/j.molcel.2005.10.030 · DOI · Paper page
- 10.1016/j.cellsig.2005.04.001 · DOI
- 10.1091/mbc.02-03-0043 · DOI
- 10.1093/emboj/20.3.466 · DOI · Paper page
- 10.1016/0968-0004(96)30032-7 · DOI
- 10.1074/jbc.M108145200 · DOI
- 10.1074/jbc.M102512200 · DOI
- 10.1074/jbc.M010271200 · DOI
- 10.1016/j.molcel.2005.04.001 · DOI
- 10.1093/emboj/cdg353 · DOI
- 10.1093/emboj/19.5.979 · DOI · Paper page
- 10.1093/emboj/19.12.2924 · DOI · Paper page
- 10.1093/emboj/cdf437 · DOI
- 10.1016/0003-9861(88)90089-6 · DOI
- 10.1016/S0092-8674(01)00374-9 · DOI · Paper page
- 10.1016/S1097-2765(01)00253-2 · DOI
- 10.1016/S0960-9822(01)00370-0 · DOI
- 10.1126/stke.2422004re10 · DOI
- 10.1016/S0014-5793(01)03294-X · DOI · Paper page
- 10.1016/j.tibs.2004.09.010 · DOI
- Harris BZ, 2001, J. Cell Sci., 114, 3219, 10.1242/jcs.114.18.3219 · DOI · Paper page
- 10.1042/0264-6021:3500001 · DOI · Paper page
- 10.1016/S0962-8924(01)02154-7 · DOI · Paper page
- 10.1126/stke.2003.191.re12 · DOI · Paper page
- 10.1016/j.cell.2005.04.001 · DOI
- 10.1126/stke.2003.179.re8 · DOI
- 10.1242/jcs.1994.Supplement_18.14 · DOI
- 10.1016/j.sbi.2004.10.004 · DOI
- 10.1016/S0959-440X(02)00290-7 · DOI · Paper page
- 10.1126/science.290.5492.801 · DOI · Paper page
- 10.1083/jcb.150.6.1299 · DOI
- 10.1038/385602a0 · DOI · Paper page
- 10.1006/jmbi.1997.1426 · DOI
- 10.1038/385595a0 · DOI · Paper page
- 10.1093/nar/gkh088 · DOI · Paper page
- 10.1073/pnas.95.11.5857 · DOI
- 10.1016/S0960-9822(02)01038-2 · DOI · Paper page
- 10.1093/emboj/cdg258 · DOI · Paper page
- 10.1016/S1097-2765(03)00046-7 · DOI · Paper page
- 10.1074/jbc.M402745200 · DOI · Paper page
- 10.1016/S0092-8674(03)00314-3 · DOI
- 10.1016/S0960-9822(00)80080-9 · DOI
- 10.1016/j.cell.2005.02.019 · DOI
- 10.1073/pnas.92.11.5106 · DOI
- 10.1126/science.7509083 · DOI · Paper page
- 10.1074/jbc.270.7.2897 · DOI · Paper page
- 10.1038/nature02178 · DOI · Paper page
- 10.1371/journal.pbio.0020014 · DOI
- 10.1126/science.278.5346.2075 · DOI · Paper page
- 10.1021/bi0268910 · DOI
- 10.1038/nature03329 · DOI · Paper page
- 10.1016/S0955-0674(99)00078-2 · DOI
- Elion EA, 2001, J. Cell Sci., 114, 3967, 10.1242/jcs.114.22.3967 · DOI
- 10.1016/S0955-0674(99)80028-3 · DOI · Paper page
- 10.1146/annurev.cellbio.19.111401.091942 · DOI · Paper page
- 10.1016/S0968-0004(98)01309-7 · DOI · Paper page
- 10.1016/j.molcel.2004.06.011 · DOI
- 10.1073/pnas.91.16.7762 · DOI
- 10.1126/science.276.5319.1702 · DOI · Paper page
- Printen JA, 1994, Genetics, 138, 609, 10.1093/genetics/138.3.609 · DOI · Paper page
- 10.1128/MCB.26.3.912-928.2006 · DOI
- 10.1016/S0960-9822(01)00567-X · DOI
- 10.1038/sj.onc.1204782 · DOI
- 10.1021/ar020210b · DOI
- 10.1006/jmbi.2001.4585 · DOI · Paper page
- 10.1128/MCB.20.15.5529-5539.2000 · DOI
- 10.1016/j.brainresrev.2004.06.002 · DOI
- 10.1016/S1074-7613(00)80422-7 · DOI
- 10.1074/jbc.M000404200 · DOI · Paper page
- 10.1016/S1097-2765(01)00383-5 · DOI · Paper page
- 10.1128/MCB.22.9.3035-3045.2002 · DOI · Paper page
- 10.1038/nature02237 · DOI
- 10.1074/jbc.M405681200 · DOI
- 10.1126/science.1120941 · DOI
- 10.1074/jbc.M207324200 · DOI
- 10.1074/jbc.M501926200 · DOI
- 10.1126/science.7528941 · DOI
- 10.1126/science.271.5255.1589 · DOI
- 10.1016/S0960-9822(99)80141-9 · DOI
- 10.1093/emboj/20.8.1921 · DOI · Paper page
- 10.1016/j.cellsig.2005.04.003 · DOI
- 10.1038/27448 · DOI
- 10.1038/40805 · DOI · Paper page
- 10.1054/ceca.1999.0070 · DOI
- 10.1016/j.febslet.2005.02.013 · DOI
- 10.1126/science.1076979 · DOI
- 10.1073/pnas.1934711100 · DOI
- 10.1126/science.1085945 · DOI · Paper page
- 10.1074/jbc.M301226200 · DOI
- 10.1126/science.2420005 · DOI
- 10.1016/0092-8674(87)90756-2 · DOI · Paper page
- 10.1016/0092-8674(87)90757-4 · DOI
- 10.1016/S0962-8924(00)01834-1 · DOI
- 10.1126/science.288.5463.88 · DOI · Paper page
- 10.1073/pnas.0503610102 · DOI
- 10.1016/j.tig.2005.02.008 · DOI
- 10.1038/nbt796 · DOI
- 10.1074/jbc.M102604200 · DOI · Paper page
- 10.1074/jbc.M506654200 · DOI
- 10.1006/jmbi.2000.4133 · DOI
- 10.1073/pnas.96.6.2758 · DOI · Paper page
- 10.1126/science.8303274 · DOI · Paper page
- 10.1006/jmbi.1999.3007 · DOI
- 10.1021/bi026806o · DOI
- 10.1073/pnas.95.25.14628 · DOI
- 10.1073/pnas.040552697 · DOI · Paper page
- 10.1073/pnas.0501162102 · DOI
- 10.1016/j.febslet.2004.10.104 · DOI
- 10.1074/jbc.M400349200 · DOI
- 10.1128/JVI.78.3.1301-1313.2004 · DOI
- 10.1038/nature03556 · DOI · Paper page
- 10.1016/S0969-2126(01)00679-7 · DOI
- 10.1093/emboj/cdg068 · DOI · Paper page
- 10.1016/S0092-8674(00)00043-X · DOI
- 10.1038/nature03650 · DOI · Paper page
- 10.1016/j.cub.2004.12.050 · DOI
Cited by
Mechanisms of specificity in protein phosphorylation
Ubersax, J. A., & Ferrell Jr, J. E. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2203 · Cited by 1,451
Membrane recognition by phospholipid-binding domains
Lemmon, M. A. (2008) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2328 · Cited by 1,419
Putnam, C. D., Hammel, M., Hura, G. L., & Tainer, J. A. (2007) · Quarterly Reviews of Biophysics · doi:10.1017/s0033583507004635 · Cited by 1,184
Tight Regulation of Unstructured Proteins: From Transcript Synthesis to Protein Degradation
Gsponer, J., Futschik, M. E., Teichmann, S. A., & Babu, M. M. (2008) · Science · doi:10.1126/science.1163581 · Cited by 466
Docking interactions in protein kinase and phosphatase networks
Reményi, A., Good, M. C., & Lim, W. A. (2006) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2006.10.008 · Cited by 188
Self-citation
Metadata
- Authors
- Bhattacharyya, R. P., Reményi, A., Yeh, B. J., & Lim, W. A.
- Venue
- Annual Review of Biochemistry
- Publisher
- Annual Reviews
- Published
- 2006-06-01
- Volume
- 75
- Issue
- 1
- Pages
- 655-680
- ISSN
- 0066-4154 (ISSN-L)
- 1545-4509
- OpenAlex
- W2152854378
- Cited by
- 454
- References
- 20
- FWCI
- 1.89
- 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.