The DOI matches its Crossref record.
Crystal Structures of c-Src Reveal Features of Its Autoinhibitory Mechanism
Open accessOverview
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
No references could be resolved yet.
Research works printed but not linked: 36
- Alexandropoulos, 1996, Coordinate activation of c-Src by SH3- and SH2- binding sites on a novel p130CAS-related protein, Sin, Genes Dev, 10, 1341, 10.1101/gad.10.11.1341 · DOI
- Boerner, 1996, Correlation of the phosphorylation states of pp60 c-src with tyrosine kinase activity, Biochemistry, 35, 9519, 10.1021/bi960248u · DOI
- Brown, 1996, Regulation, substrates and functions of src, Biochim. Biophys. Acta, 1287, 121
- Canagarajah, 1997, Activation mechanism of the MAP kinase ERK2 by dual phosphorylation, Cell, 90, 859, 10.1016/S0092-8674(00)80351-7 · DOI · Paper page
- De Bondt, 1993, Crystal structure of cyclin-dependent kinase 2, Nature, 363, 595, 10.1038/363595a0 · DOI · Paper page
- Erpel, 1995, Src family protein tyrosine kinases and cellular signal transduction pathways, Curr. Opin. Cell Biol, 7, 176, 10.1016/0955-0674(95)80025-5 · DOI · Paper page
- Gonfloni, 1997, The role of the linker between the SH2 domain and catalytic domain in the regulation and function of Src, EMBO J, 16, 7261, 10.1093/emboj/16.24.7261 · DOI
- Hardwick, 1997, The activated form of the Lck tyrosine protein kinase in cells exposed to hydrogen peroxide is phosphorylated at both Tyr-394 and Tyr-505, J. Biol. Chem, 272, 25429, 10.1074/jbc.272.41.25429 · DOI
- Hubbard, 1997, Crystal structure of the activated insulin receptor tyrosine kinase in complex with peptide substrate and ATP analog, EMBO J, 16, 5572, 10.1093/emboj/16.18.5572 · DOI · Paper page
- Hubbard, 1994, Crystal structure of the tyrosine kinase domain of the human insulin receptor, Nature, 372, 746, 10.1038/372746a0 · DOI · Paper page
- Hubbard, 1998, Autoregulatory mechanisms in protein-tyrosine kinases, J. Biol. Chem, 273, 11987, 10.1074/jbc.273.20.11987 · DOI · Paper page
- Hunter, 1987, A tail of two src’s, Cell, 49, 1, 10.1016/0092-8674(87)90745-8 · DOI · Paper page
- Jeffrey, 1995, Mechanism of CDK activation revealed by the structure of a cyclinA-CDK2 complex, Nature, 376, 313, 10.1038/376313a0 · DOI · Paper page
- Johnson, 1996, Active and inactive protein kinases, Cell, 85, 149, 10.1016/S0092-8674(00)81092-2 · DOI · Paper page
- Jones, T.A., Bergdoll, M., and Kjeldgaard, M. (1989). In Crystallographic Computing and Modeling Methods in Molecular Design, C. Bugg and S. Ealick, eds. (New York: Springer).
- Kabsch, 1988, Evaluation of single crystal diffraction data from a position sensitive detector, J. Appl. Crystallogr, 21, 916, 10.1107/S0021889888007903 · DOI · Paper page
- Knighton, 1991, Crystal structure of the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase, Science, 253, 407, 10.1126/science.1862342 · DOI · Paper page
- Kraulis, 1991, MOLSCRIPT, J. Appl. Crystallogr, 24, 946, 10.1107/S0021889891004399 · DOI · Paper page
- Krebs, 1989, The Albert Lasker medical awards. Role of the cyclic AMP-dependent protein kinase in signal transduction, JAMA, 262, 1815, 10.1001/jama.1989.03430130091040 · DOI
- LaFevre-Bernt, 1998, Intramolecular regulatory interactions in the Src family kinase Hck probed by mutagenesis of a conserved tryptophan residue, J. Biol. Chem, 273, 32129, 10.1074/jbc.273.48.32129 · DOI
- Lamzin, 1993, Automated refinement of protein models, Acta Crystallogr. D, 49, 129, 10.1107/S0907444992008886 · DOI · Paper page
- Matsuda, 1990, Binding of transforming protein, P47gag-crk, to a broad range of phosphotyrosine-containing proteins, Science, 248, 1537, 10.1126/science.1694307 · DOI · Paper page
- Mohammadi, 1996, Structure of the FGF receptor tyrosine kinase domain reveals a novel autoinhibitory mechanism, Cell, 86, 577, 10.1016/S0092-8674(00)80131-2 · DOI · Paper page
- Morgan, 1995, Principles of CDK regulation, Nature, 374, 131, 10.1038/374131a0 · DOI · Paper page
- Morgan, 1994, Protein kinase regulation, Curr. Opin. Cell Biol, 6, 239, 10.1016/0955-0674(94)90142-2 · DOI
- Russo, 1996, Structural basis of cyclin-dependent kinase activation by phosphorylation, Nat. Struct. Biol, 3, 696, 10.1038/nsb0896-696 · DOI · Paper page
- Schindler, 1999, Crystal structure of Hck in complex with a Src family–selective tyrosine kinase inhibitor, Mol. Cell, 3, 639, 10.1016/S1097-2765(00)80357-3 · DOI · Paper page
- Sicheri, 1997, Crystal structure of the Src family tyrosine kinase Hck, Nature, 385, 602, 10.1038/385602a0 · DOI · Paper page
- Superti-Furga, 1993, Csk inhibition of c-Src activity requires both the SH2 and SH3 domains of Src, EMBO J, 12, 2625, 10.1002/j.1460-2075.1993.tb05923.x · DOI
- Superti-Furga, 1995, Structure-function relationships in Src family and related protein tyrosine kinases, Bioessays, 17, 321, 10.1002/bies.950170408 · DOI
- Taylor, 1990, cAMP-dependent protein kinase, Annu. Rev. Biochem, 59, 971, 10.1146/annurev.bi.59.070190.004543 · DOI · Paper page
- Thomas, 1998, SH2- and SH3-mediated interactions between focal adhesion kinase and Src, J. Biol. Chem, 273, 577, 10.1074/jbc.273.1.577 · DOI · Paper page
- Williams, 1997, The 2.35 Å crystal structure of the inactivated form of chicken Src, J. Mol. Biol, 274, 757, 10.1006/jmbi.1997.1426 · DOI
- Xu, 1997, Three-dimensional structure of the tyrosine kinase c-Src, Nature, 385, 595, 10.1038/385595a0 · DOI · Paper page
- Yamaguchi, 1996, Structural basis for activation of the human lymphocyte kinase Lck upon tyrosine phosphorylation, Nature, 384, 484, 10.1038/384484a0 · DOI · Paper page
- Zheng, 1993, Crystal structure of the catalytic subunit of cAMP-dependent protein kinase complexed with MgATP and peptide inhibitor, Biochemistry, 32, 2154, 10.1021/bi00060a005 · DOI
Cited by
Cell Signaling by Receptor Tyrosine Kinases
Lemmon, M. A., & Schlessinger, J. (2010) · Cell · doi:10.1016/j.cell.2010.06.011 · Cited by 7,929
Cell Signaling by Receptor Tyrosine Kinases
Schlessinger, J. (2000) · Cell · doi:10.1016/s0092-8674(00)00114-8 · Cited by 3,774
Hunter, T. (2000) · Cell · doi:10.1016/s0092-8674(00)81688-8 · Cited by 2,586
An allosteric mechanism for activation of the kinase domain of epidermal growth factor receptor
Zhang, X., Gureasko, J., Shen, K., Cole, P. A., & Kuriyan, J. (2006) · Cell · doi:10.1016/j.cell.2006.05.013 · Cited by 1,650
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
Intrinsic Disorder in Cell-signaling and Cancer-associated Proteins
Iakoucheva, L. M., Brown, C. J., Lawson, J. D., Obradović, Z., & Dunker, A. K. (2002) · Journal of Molecular Biology · doi:10.1016/s0022-2836(02)00969-5 · Cited by 1,214
Structure and regulation of Src family kinases
Boggon, T. J., & Eck, M. J. (2004) · Oncogene · doi:10.1038/sj.onc.1208081 · Cited by 712
Self-citationc-Src and cooperating partners in human cancer
Ishizawar, R., & Parsons, S. J. (2004) · Cancer Cell · doi:10.1016/j.ccr.2004.09.001 · Cited by 617
Defining a new nomenclature for the structures of active and inactive kinases
Modi, V., & Dunbrack, R. L. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1814279116 · Cited by 367
Structural analysis of the catalytically inactive kinase domain of the human EGF receptor 3
Jura, N., Shan, Y., Cao, X., Shaw, D. E., & Kuriyan, J. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0912101106 · Cited by 338
Activation pathway of Src kinase reveals intermediate states as targets for drug design
Shukla, D., Meng, Y., Roux, B., & Pande, V. S. (2014) · Nature Communications · doi:10.1038/ncomms4397 · Cited by 333
Catalytic Control in the EGF Receptor and Its Connection to General Kinase Regulatory Mechanisms
Jura, N., Zhang, X., Endres, N. F., Seeliger, M. A., Schindler, T., & Kuriyan, J. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.03.004 · Cited by 310
Heme is involved in microRNA processing
Faller, M., Matsunaga, M., Yin, S., Loo, J. A., & Guo, F. (2007) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1182 · Cited by 295
Structural Basis for the Inhibition of Tyrosine Kinase Activity of ZAP-70
Deindl, S., Kadlecek, T. A., Brdicka, T., Cao, X., Weiss, A., & Kuriyan, J. (2007) · Cell · doi:10.1016/j.cell.2007.03.039 · Cited by 234
Receptor Mechanisms Mediating Non-Genomic Actions of Sex Steroids
Boonyaratanakornkit, V., & Edwards, D. (2007) · Seminars in Reproductive Medicine · doi:10.1055/s-2007-973427 · Cited by 178
PTP1B Contributes to the Oncogenic Properties of Colon Cancer Cells through Src Activation
Zhu, S., Bjorge, J. D., & Fujita, D. J. (2007) · Cancer Research · doi:10.1158/0008-5472.can-06-4338 · Cited by 168
Wheeler, D. L., Iida, M., Kruser, T. J., Nechrebecki, M. M., Dunn, E. F., Armstrong, E. A., Huang, S., & Harari, P. M. (2009) · Cancer Biology & Therapy · doi:10.4161/cbt.8.8.7903 · Cited by 157
Dasatinib sensitizes KRAS mutant colorectal tumors to cetuximab
Dunn, E. F., Iida, M., Myers, R. A., Campbell, D. A., Hintz, K. A., Armstrong, E. A., Li, C., & Wheeler, D. L. (2011) · Oncogene · doi:10.1038/onc.2010.430 · Cited by 133
“This interaction results in a conformational change in the SFK and leads to autophophorylation at Y419 and transient activity (Xu et al., 1999).”
BackgroundLittlefield, P., Liu, L., Mysore, V., Shan, Y., Shaw, D. E., & Jura, N. (2014) · Science Signaling · doi:10.1126/scisignal.2005786 · Cited by 126
Schmidt, M. H. H., Dikic, I., & Bögler, O. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m409839200 · Cited by 76
Towards simple kinetic models of functional dynamics for a kinase subfamily
Sultan, M. M., Kiss, G., & Pande, V. S. (2018) · Nature Chemistry · doi:10.1038/s41557-018-0077-9 · Cited by 68
Chemical Proteomics and Structural Biology Define EPHA2 Inhibition by Clinical Kinase Drugs
Heinzlmeir, S., Kudlinzki, D., Sreeramulu, S., Klaeger, S., Gande, S. L., Linhard, V., Wilhelm, M., Qiao, H., Helm, D., Ruprecht, B., et al. (2016) · ACS Chemical Biology · doi:10.1021/acschembio.6b00709 · Cited by 56
Paradoxical activation of c-Src as a drug-resistant mechanism
Higuchi, M., Ishiyama, K., Maruoka, M., Kanamori, R., Takaori-Kondo, A., & Watanabe, N. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.108876 · Cited by 31
M-CSF induces the stable interaction of cFms with αVβ3 integrin in osteoclasts
Elsegood, C. L., Zhuo, Y., Wesolowski, G. A., Hamilton, J. A., Rodan, G. A., & Duong, L. T. (2006) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2006.02.011 · Cited by 28
MacGowan, S. A., Madeira, F., Britto-Borges, T., & Barton, G. J. (2024) · Communications Biology · doi:10.1038/s42003-024-06117-5 · Cited by 8
Metadata
- Authors
- Xu, W., Doshi, A., Lei, M., Eck, M. J., & Harrison, S. C.
- Venue
- Molecular Cell
- Publisher
- Elsevier BV
- Published
- 1999-05
- Volume
- 3
- Issue
- 5
- Pages
- 629-638
- ISSN
- 1097-2765 (ISSN-L)
- OpenAlex
- W2156480395
- Cited by
- 870
- References
- 0
- FWCI
- 13.92
- Type
- journal article
- Language
- en
- Open access
- bronze
- Licence
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
- www.elsevier.com/open-access/userlicense/1.0/ (vor, 5191 d)
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.