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Crystal structure of the tyrosine kinase domain of the human insulin receptor
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PROCHECK: a program to check the stereochemical quality of protein structures
Laskowski, R. A., MacArthur, M. W., Moss, D. S., & Thornton, J. M. (1993) · Journal of Applied Crystallography · doi:10.1107/s0021889892009944 · Cited by 24,581
Kabsch, W., & Sander, C. (1983) · Biopolymers · doi:10.1002/bip.360221211 · Cited by 15,320
Chou, C. K., Dull, T. J., Russell, D. S., Gherzi, R., Lebwohl, D., Ullrich, A., & Rosen, O. M. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)75716-0 · Cited by 640
Atomic structure of the MAP kinase ERK2 at 2.3 A resolution
Zhang, F., Strand, A., Robbins, D., Cobb, M. H., & Goldsmith, E. J. (1994) · Nature · doi:10.1038/367704a0 · Cited by 592
Cited by
Free Radicals in the Physiological Control of Cell Function
Dröge, W. (2002) · Physiological Reviews · doi:10.1152/physrev.00018.2001 · Cited by 9,855
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
Mechanisms of Insulin Action and Insulin Resistance
Petersen, M. C., & Shulman, G. I. (2018) · Physiological Reviews · doi:10.1152/physrev.00063.2017 · Cited by 3,028
Brogiolo, W., Stocker, H., Ikeya, T., Rintelen, F., Fernandez, R., & Hafen, E. (2001) · Current Biology · doi:10.1016/s0960-9822(01)00068-9 · Cited by 1,255
The molecular details of cytokine signaling via the JAK/STAT pathway
Morris, R., Kershaw, N. J., & Babon, J. J. (2018) · Protein Science · doi:10.1002/pro.3519 · Cited by 943
Structure and regulation of Src family kinases
Boggon, T. J., & Eck, M. J. (2004) · Oncogene · doi:10.1038/sj.onc.1208081 · Cited by 712
Biscardi, J. S., Maa, M.-C., Tice, D. A., Cox, M. E., Leu, T.-H., & Parsons, S. J. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.12.8335 · Cited by 649
Current views on type 2 diabetes
Lin, Y., & Sun, Z. (2010) · Journal of Endocrinology · doi:10.1677/joe-09-0260 · Cited by 457
The molecular basis of JAK/STAT inhibition by SOCS1
Liau, N. P. D., Laktyushin, A., Lucet, I. S., Murphy, J. M., Yao, S., Whitlock, E., Callaghan, K., Nicola, N. A., Kershaw, N. J., & Babon, J. J. (2018) · Nature Communications · doi:10.1038/s41467-018-04013-1 · Cited by 456
Insulin signaling in health and disease
Saltiel, A. R. (2021) · Journal of Clinical Investigation · doi:10.1172/jci142241 · Cited by 446
Insulin and its receptor: structure, function and evolution
De Meyts, P. (2004) · BioEssays · doi:10.1002/bies.20151 · Cited by 345
The structure of mitogen-activated protein kinase p38 at 2.1-Å resolution
Wang, Z., Harkins, P. C., Ulevitch, R. J., Han, J., Cobb, M. H., & Goldsmith, E. J. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.6.2327 · Cited by 275
Conformational states dynamically populated by a kinase determine its function
Xie, T., Saleh, T., Rossi, P., & Kalodimos, C. G. (2020) · Science · doi:10.1126/science.abc2754 · Cited by 266
Potential of insulin nanoparticle formulations for oral delivery and diabetes treatment.
Wong, C. Y., Al-Salami, H., & Dass, C. R. (2017) · Journal of Controlled Release · doi:10.1016/j.jconrel.2017.09.003 · Cited by 257
The intrinsic substrate specificity of the human tyrosine kinome
Yaron-Barir, T. M., Joughin, B. A., Huntsman, E. M., Kerelsky, A., Cizin, D. M., Cohen, B. M., Regev, A., Song, J., Vasan, N., Lin, T.-Y., et al. (2024) · Nature · doi:10.1038/s41586-024-07407-y · Cited by 189
Leukocyte Tyrosine Kinase Functions in Pigment Cell Development
Lopes, S. S., Yang, X., Müller, J., Carney, T. J., McAdow, A. R., Rauch, G.-J., Jacoby, A. S., Hurst, L. D., Delfino-Machín, M., Haffter, P., et al. (2008) · PLoS Genetics · doi:10.1371/journal.pgen.1000026 · Cited by 163
syk kinase activation by a src kinase-initiated activation loop phosphorylation chain reaction
El-Hillal, O., Kurosaki, T., Yamamura, H., Kinet, J.-P., & Scharenberg, A. M. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.5.1919 · Cited by 130
Caffrey, D. R., O'Neill, L. A. J., & Shields, D. C. (1999) · Journal of Molecular Evolution · doi:10.1007/pl00006578 · Cited by 124
Piao, X., & Bernstein, A. (1996) · Blood · doi:10.1182/blood.v87.8.3117.bloodjournal8783117 · Cited by 112
A novel insulin receptor-signaling platform and its link to insulin resistance and type 2 diabetes
Alghamdi, F., Guo, M., Abdulkhalek, S., Crawford, N., Amith, S. R., & Szewczuk, M. R. (2014) · Cellular Signalling · doi:10.1016/j.cellsig.2014.02.015 · Cited by 87
Storozhevykh, T. P., Senilova, Y. E., Persiyantseva, N. A., Pinelis, V. G., & Pomytkin, I. A. (2007) · BMC Neuroscience · doi:10.1186/1471-2202-8-84 · Cited by 69
Nikou, S.-A., Zhou, C., Griffiths, J. S., Kotowicz, N. K., Coleman, B. M., Green, M. J., Moyes, D. L., Gaffen, S. L., Naglik, J. R., & Parker, P. J. (2022) · Science Signaling · doi:10.1126/scisignal.abj6915 · Cited by 65
Insulin Signaling in Arthritis
Tripolino, C., Ciaffi, J., Pucino, V., Ruscitti, P., van Leeuwen, N., Borghi, C., Giacomelli, R., Meliconi, R., & Ursini, F. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.672519 · Cited by 46
Witthuhn, B. A., Williams, M. D., Kerawalla, H., & Uckun, F. M. (1999) · Leukemia & Lymphoma · doi:10.3109/10428199909167389 · Cited by 28
Quantitatively accounting for protein reorganization in computer-aided drug design
Fajer, M., Borrelli, K., Abel, R., & Wang, L. (2023) · Journal of Chemical Theory and Computation · doi:10.1021/acs.jctc.3c00009 · Cited by 18
PKD autoinhibition in trans regulates activation loop autophosphorylation in cis
Reinhardt, R., Hirzel, K., Link, G., Eisler, S. A., Hägele, T., Parson, M. A. H., Burke, J. E., Hausser, A., & Leonard, T. A. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2212909120 · Cited by 13
Metadata
- Authors
- Hubbard, S. R., Wei, L., & Hendrickson, W. A.
- Venue
- Nature
- Published
- 1994-12
- Volume
- 372
- Issue
- 6508
- Pages
- 746-754
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W2141743775
- Cited by
- 1,080
- References
- 4
- FWCI
- 67.51
- Type
- journal article
- Language
- en
- Open access
- closed
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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.