A brain serine/threonine protein kinase activated by Cdc42 and Rac1

Manser, Edward, Leung, Thomas, Salihuddin, Harfizah, Zhao, Zhuo-shen, Lim, Louis·1994·Nature

DOI 10.1038/367040a0

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Whitmarsh, A. J., & Davis, R. J. (1996) · Journal of Molecular Medicine · doi:10.1007/s001090050063 · Cited by 1,543
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Coso, O. A., Chiariello, M., Yu, J.-C., Teramoto, H., Crespo, P., Xu, N., Miki, T., & Silvio Gutkind, J. (1995) · Cell · doi:10.1016/s0092-8674(05)80018-2 · Cited by 1,397
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Jordens, I., Fernandez-Borja, M., Marsman, M., Dusseljee, S., Janssen, L., Calafat, J., Janssen, H., Wubbolts, R., & Neefjes, J. (2001) · Current Biology · doi:10.1016/s0960-9822(01)00531-0 · Cited by 811
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Su, B., & Karin, M. (1996) · Current Opinion in Immunology · doi:10.1016/s0952-7915(96)80131-2 · Cited by 747
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Sells, M. A., Knaus, U. G., Bagrodia, S., Ambrose, D. M., Bokoch, G. M., & Chernoff, J. (1997) · Current Biology · doi:10.1016/s0960-9822(97)70091-5 · Cited by 603
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Lang, P., Gesbert, F., Delespine‐Carmagnat, M., Stancou, R., Pouchelet, M., & Bertoglio, J. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb00383.x · Cited by 558
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Perona, R., Montaner, S., Saniger, L., Sánchez-Pérez, I., Bravo, R., & Lacal, J. C. (1997) · Genes & Development · doi:10.1101/gad.11.4.463 · Cited by 519
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Cerione, R. A., & Zheng, Y. (1996) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(96)80068-8 · Cited by 437
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Yang, Y., Kim, S. C., Yu, T., Yi, Y.-S., Rhee, M. H., Sung, G.-H., Yoo, B. C., & Cho, J. Y. (2014) · Mediators of Inflammation · doi:10.1155/2014/352371 · Cited by 406
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Chou, M. M., & Blenis, J. (1996) · Cell · doi:10.1016/s0092-8674(00)81257-x · Cited by 292
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Dolan, B. M., Duron, S. G., Campbell, D. A., Vollrath, B., Rao, B. S. S., Ko, H.-Y., Lin, G. G., Govindarajan, A., Choi, S.-Y., & Tonegawa, S. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1219383110 · Cited by 260
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Kwong, C. H., Adams, A. G., & Leto, T. L. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.34.19868 · Cited by 76
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Authors: Manser, E., Leung, T., Salihuddin, H., Zhao, Z.-S., & Lim, L.
Venue: Nature
Publisher: Springer Science and Business Media LLC
Published: 1994-01
Volume: 367
Issue: 6458
Pages: 40-46
ISSN: 0028-0836 (ISSN-L)
1476-4687
DOI: 10.1038/367040a0
OpenAlex: W2011756230
Cited by: 1,538
References: 0
FWCI: 37.38
Type: journal article
Language: en
Open access: closed

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