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1

Marshall, Christopher J. "MAP kinase kinase kinase, MAP kinase kinase and MAP kinase." Current Opinion in Genetics & Development 4, no. 1 (1994): 82–89. http://dx.doi.org/10.1016/0959-437x(94)90095-7.

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2

Matsuda, S., Y. Gotoh, and E. Nishida. "Phosphorylation of Xenopus mitogen-activated protein (MAP) kinase kinase by MAP kinase kinase kinase and MAP kinase." Journal of Biological Chemistry 268, no. 5 (1993): 3277–81. http://dx.doi.org/10.1016/s0021-9258(18)53690-5.

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3

Adams, P. D., and P. J. Parker. "Activation of mitogen-activated protein (MAP) kinase by a MAP kinase-kinase." Journal of Biological Chemistry 267, no. 19 (1992): 13135–37. http://dx.doi.org/10.1016/s0021-9258(18)42181-3.

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4

Kaur, Ramneet, Xia Liu, Ole Gjoerup, et al. "Activation of p21-activated Kinase 6 by MAP Kinase Kinase 6 and p38 MAP Kinase." Journal of Biological Chemistry 280, no. 5 (2004): 3323–30. http://dx.doi.org/10.1074/jbc.m406701200.

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5

Morrison, D. K. "MAP Kinase Pathways." Cold Spring Harbor Perspectives in Biology 4, no. 11 (2012): a011254. http://dx.doi.org/10.1101/cshperspect.a011254.

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6

Fernandes, Juliana D., Ricardo Hsieh, Luiz A. R. de Freitas, et al. "MAP Kinase Pathways." American Journal of Dermatopathology 37, no. 12 (2015): 892–97. http://dx.doi.org/10.1097/dad.0000000000000317.

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7

Qi, M. "MAP kinase pathways." Journal of Cell Science 118, no. 16 (2005): 3569–72. http://dx.doi.org/10.1242/jcs.02470.

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8

Maller, Jim. "MAP kinase activation." Current Biology 1, no. 5 (1991): 334–35. http://dx.doi.org/10.1016/0960-9822(91)90104-5.

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9

Cobb, Melanie H. "MAP kinase pathways." Progress in Biophysics and Molecular Biology 71, no. 3-4 (1999): 479–500. http://dx.doi.org/10.1016/s0079-6107(98)00056-x.

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10

Fukuda, M. "Interaction of MAP kinase with MAP kinase kinase: its possible role in the control of nucleocytoplasmic transport of MAP kinase." EMBO Journal 16, no. 8 (1997): 1901–8. http://dx.doi.org/10.1093/emboj/16.8.1901.

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11

Kosako, H., Y. Gotoh, and E. Nishida. "Requirement for the MAP kinase kinase/MAP kinase cascade in Xenopus oocyte maturation." EMBO Journal 13, no. 9 (1994): 2131–38. http://dx.doi.org/10.1002/j.1460-2075.1994.tb06489.x.

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12

Zhang, Xudong, Yuqing Xiong, Christopher DeFraia, Eric Schmelz, and Zhonglin Mou. "The Arabidopsis MAP kinase kinase 7." Plant Signaling & Behavior 3, no. 4 (2008): 272–74. http://dx.doi.org/10.4161/psb.3.4.5230.

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13

Kyriakis, John M., Harald App, Xian-feng Zhang, et al. "Raf-1 activates MAP kinase-kinase." Nature 358, no. 6385 (1992): 417–21. http://dx.doi.org/10.1038/358417a0.

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14

Matsuda, Satoshi, Yukiko Gotoh, and Eisuke Nishida. "Signaling pathways mediated by the mitogen-activated protein (MAP) kinase kinase/MAP kinase cascade." Journal of Leukocyte Biology 56, no. 5 (1994): 548–53. http://dx.doi.org/10.1002/jlb.56.5.548.

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15

Buxade, Maria. "The Mnks: MAP kinase-interacting kinases (MAP kinase signal-integrating kinases)." Frontiers in Bioscience Volume, no. 13 (2008): 5359. http://dx.doi.org/10.2741/3086.

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16

Posada, J., N. Yew, N. G. Ahn, G. F. Vande Woude, and J. A. Cooper. "Mos stimulates MAP kinase in Xenopus oocytes and activates a MAP kinase kinase in vitro." Molecular and Cellular Biology 13, no. 4 (1993): 2546–53. http://dx.doi.org/10.1128/mcb.13.4.2546-2553.1993.

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Several protein kinases, including Mos, maturation-promoting factor (MPF), mitogen-activated protein (MAP) kinase, and MAP kinase kinase (MAPKK), are activated when Xenopus oocytes enter meiosis. De novo synthesis of the Mos protein is required for progesterone-induced meiotic maturation. Recently, bacterially synthesized maltose-binding protein (MBP)-Mos fusion protein was shown to be sufficient to initiate meiosis I and MPF activation in fully grown oocytes in the absence of protein synthesis. Here we show that MAP kinase is rapidly phosphorylated and activated following injection of wild-ty
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17

Kieran, Mark W., Steve Katz, Brenda Vail, Leonard I. Zon, and Bruce J. Mayer. "Concentration-dependent positive and negative regulation of a MAP kinase by a MAP kinase kinase." Oncogene 18, no. 48 (1999): 6647–57. http://dx.doi.org/10.1038/sj.onc.1203057.

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18

Hammaker, Deepa, David L. Boyle, Katharyn Topolewski, and Gary S. Firestein. "Differential regulation of anti-inflammatory genes by p38 MAP kinase and MAP kinase kinase 6." Journal of Inflammation 11, no. 1 (2014): 14. http://dx.doi.org/10.1186/1476-9255-11-14.

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19

Posada, J., N. Yew, N. G. Ahn, G. F. Vande Woude, and J. A. Cooper. "Mos stimulates MAP kinase in Xenopus oocytes and activates a MAP kinase kinase in vitro." Molecular and Cellular Biology 13, no. 4 (1993): 2546–53. http://dx.doi.org/10.1128/mcb.13.4.2546.

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Several protein kinases, including Mos, maturation-promoting factor (MPF), mitogen-activated protein (MAP) kinase, and MAP kinase kinase (MAPKK), are activated when Xenopus oocytes enter meiosis. De novo synthesis of the Mos protein is required for progesterone-induced meiotic maturation. Recently, bacterially synthesized maltose-binding protein (MBP)-Mos fusion protein was shown to be sufficient to initiate meiosis I and MPF activation in fully grown oocytes in the absence of protein synthesis. Here we show that MAP kinase is rapidly phosphorylated and activated following injection of wild-ty
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20

Merrall, N. W., R. J. Plevin, D. Stokoe, P. Cohen, A. R. Nebreda, and G. W. Gould. "Mitogen-activated protein kinase (MAP kinase), MAP kinase kinase and c-Mos stimulate glucose transport in Xenopus oocytes." Biochemical Journal 295, no. 2 (1993): 351–55. http://dx.doi.org/10.1042/bj2950351.

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Mitogens and growth factors acutely stimulate glucose transport in all cells to supply energy for their growth and division, but little is known about the signalling mechanism by which these agonists promote sugar uptake. Here we show that the transport of deoxyglucose and 3-O-methylglucose into Xenopus laevis oocytes is stimulated about 2.5-fold when mitogen-activated protein kinase (MAP kinase) is microinjected into these oocytes. We also demonstrate that microinjection of the proto-oncogene product c-Mos (an activator of MAP kinase kinase, which activates MAP kinase in Xenopus oocytes), and
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21

NISHIKAWA, Masataka, Akira MYOUI, Tetsuya TOMITA, Koichiro TAKAHI, Akihide NAMPEI, and Hideki YOSHIKAWA. "p38 MAP Kinase inhibitor." Japanese Journal of Clinical Immunology 30, no. 5 (2007): 390–97. http://dx.doi.org/10.2177/jsci.30.390.

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22

Oberst, A. "MAP Kinase Signaling Protocols." Cell Death & Differentiation 11, no. 12 (2004): 1365. http://dx.doi.org/10.1038/sj.cdd.4401518.

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23

Hoek, Jan B. "MAP KINASE SIGNALING PROTOCOLS." Shock 22, no. 2 (2004): 193. http://dx.doi.org/10.1097/01.shk.0000137186.99856.40.

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24

Ji, Ru-Rong, Robert W. Gereau, Marzia Malcangio, and Gary R. Strichartz. "MAP kinase and pain." Brain Research Reviews 60, no. 1 (2009): 135–48. http://dx.doi.org/10.1016/j.brainresrev.2008.12.011.

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25

Buolamwini, John K., and Shantaram Kamath. "Molecule–kinase interaction map." Nature Biotechnology 23, no. 11 (2005): 1346. http://dx.doi.org/10.1038/nbt1105-1346a.

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26

Symons, Antony, Soren Beinke, and Steven C. Ley. "MAP kinase kinase kinases and innate immunity." Trends in Immunology 27, no. 1 (2006): 40–48. http://dx.doi.org/10.1016/j.it.2005.11.007.

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27

Wu, J., J. K. Harrison, L. A. Vincent, et al. "Molecular structure of a protein-tyrosine/threonine kinase activating p42 mitogen-activated protein (MAP) kinase: MAP kinase kinase." Proceedings of the National Academy of Sciences 90, no. 1 (1993): 173–77. http://dx.doi.org/10.1073/pnas.90.1.173.

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28

Ichimura, Kazuya, Tsuyoshi Mizoguchi, Kenji Irie, et al. "Isolation of ATMEKK1 (a MAP Kinase Kinase Kinase)-Interacting Proteins and Analysis of a MAP Kinase Cascade inArabidopsis." Biochemical and Biophysical Research Communications 253, no. 2 (1998): 532–43. http://dx.doi.org/10.1006/bbrc.1998.9796.

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29

Adachi, Makoto, Makoto Fukuda, and Eisuke Nishida. "Nuclear Export of Map Kinase (ERK) Involves a Map Kinase Kinase (Mek-Dependent) Active Transport Mechanism." Journal of Cell Biology 148, no. 5 (2000): 849–56. http://dx.doi.org/10.1083/jcb.148.5.849.

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In response to extracellular stimuli, mitogen-activated protein kinase (MAPK, also known as ERK), which localizes to the cytoplasm in quiescent cells, translocates to the nucleus and then relocalizes to the cytoplasm again. The relocalization of nuclear MAPK to the cytoplasm was not inhibited by cycloheximide, confirming that the relocalization is achieved by nuclear export, but not synthesis, of MAPK. The nuclear export of MAPK was inhibited by leptomycin B (LMB), a specific inhibitor of the nuclear export signal (NES)-dependent transport. We have then shown that MAP kinase kinase (MAPKK, als
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30

Miyata, Yoshihiko, Shungo Adachi, Hiroshi Mizuno, and Eisuke Nishida. "A strategy to make constitutively active MAP kinase by fusing with constitutively active MAP kinase kinase." Biochimica et Biophysica Acta (BBA) - Molecular Cell Research 1451, no. 2-3 (1999): 334–42. http://dx.doi.org/10.1016/s0167-4889(99)00107-x.

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31

Kranenburg, Onno, Ingrid Verlaan, and Wouter H. Moolenaar. "Dynamin Is Required for the Activation of Mitogen-activated Protein (MAP) Kinase by MAP Kinase Kinase." Journal of Biological Chemistry 274, no. 50 (1999): 35301–4. http://dx.doi.org/10.1074/jbc.274.50.35301.

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32

Kondoh, Kunio, and Eisuke Nishida. "Regulation of MAP kinases by MAP kinase phosphatases." Biochimica et Biophysica Acta (BBA) - Molecular Cell Research 1773, no. 8 (2007): 1227–37. http://dx.doi.org/10.1016/j.bbamcr.2006.12.002.

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33

Terada, Y., K. Tomita, M. K. Homma, et al. "Sequential activation of Raf-1 kinase, mitogen-activated protein (MAP) kinase kinase, MAP kinase, and S6 kinase by hyperosmolality in renal cells." Journal of Biological Chemistry 269, no. 49 (1994): 31296–301. http://dx.doi.org/10.1016/s0021-9258(18)47422-4.

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34

Lim, Young-Mi, Leo Tsuda, Yoshihiro H. Inoue, et al. "Dominant Mutations of Drosophila MAP Kinase Kinase and Their Activities in Drosophila and Yeast MAP Kinase Cascades." Genetics 146, no. 1 (1997): 263–73. http://dx.doi.org/10.1093/genetics/146.1.263.

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Eight alleles of Dsor1 encoding a Drosophila homologue of mitogen-activated protein (MAP) kinase kinase were obtained as dominant suppressors of the MAP kinase kinase kinase D-raf. These Dsor1 alleles themselves showed no obvious phenotypic consequences nor any effect on the viability of the flies, although they were highly sensitive to upstream signals and strongly interacted with gain-of-function mutations of upstream factors. They suppressed mutations for receptor tyrosine kinases (RTKs); torso (tor), sevenless (sev) and to a lesser extent Drosophila EGF receptor (DER). Furthermore, the Dso
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35

Kitahara, T., S. Kiryu, K. Ohno, N. Morita, T. Kubo, and H. Kiyama. "Up-regulation of ERK (MAP kinase) and MEK (MAP kinase kinase) transcription after rat facial nerve transection." Neuroscience Research 20, no. 3 (1994): 275–80. http://dx.doi.org/10.1016/0168-0102(94)90097-3.

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36

Singh, Praveen, Sharmistha Ghosh, and Asis Datta. "A novel MAP-kinase kinase from Candida albicans." Gene 190, no. 1 (1997): 99–104. http://dx.doi.org/10.1016/s0378-1119(96)00758-5.

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37

Haystead, Timothy A. J., Paul Dent, Jie Wu, Clare M. M. Haystead, and Thomas W. Sturgill. "Ordered phosphorylation of p42mapk by MAP kinase kinase." FEBS Letters 306, no. 1 (1992): 17–22. http://dx.doi.org/10.1016/0014-5793(92)80828-5.

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38

Mordret, Guy. "MAP kinase kinase: A node connecting multiple pathways." Biology of the Cell 79, no. 3 (1993): 193–207. http://dx.doi.org/10.1016/0248-4900(93)90138-5.

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39

Takenaka, Katsuya, Yukiko Gotoh, and Eisuke Nishida. "MAP Kinase Is Required for the Spindle Assembly Checkpoint but Is Dispensable for the Normal M Phase Entry and Exit in Xenopus Egg Cell Cycle Extracts." Journal of Cell Biology 136, no. 5 (1997): 1091–97. http://dx.doi.org/10.1083/jcb.136.5.1091.

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In Xenopus laevis egg cell cycle extracts that mimic early embryonic cell cycles, activation of MAP kinase and MAP kinase kinase occurs in M phase, slightly behind that of maturation promoting factor. To examine the possible role of MAP kinase in the in vitro cell cycle, we depleted the extracts of MAP kinase by using anti–Xenopus MAP kinase antibody. Like in the mock-treated extracts, the periodic activation and deactivation of MPF occurred normally in the MAP kinase–depleted extracts, suggesting that MAP kinase is dispensable for the normal M phase entry and exit in vitro. It has recently be
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40

GRAHAM, Anne, Angela McLEES, Kevin MALARKEY, Gwyn W. GOULD, and Robin PLEVIN. "Role of receptor desensitization, phosphatase induction and intracellular cyclic AMP in the termination of mitogen-activated protein kinase activity in UTP-stimulated EAhy 926 endothelial cells." Biochemical Journal 315, no. 2 (1996): 563–69. http://dx.doi.org/10.1042/bj3150563.

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We have investigated the mechanisms that bring about the termination of mitogen-activated protein kinase (MAP kinase) activation in response to UTP in EAhy 926 endothelial cells. UTP-stimulated MAP kinase activity was transient, returning to basal values by 60 min. At this time MAP kinase activation was desensitized; re-application of UTP did not further activate MAP kinase, full re-activation of MAP kinase being only apparent after a 1–2 h wash period. However, activation of MAP kinase by UTP could be sustained beyond 60 min by preincubation of the cells with the protein synthesis inhibitor c
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41

Rao, K. Murali Krishna. "MAP kinase activation in macrophages." Journal of Leukocyte Biology 69, no. 1 (2001): 3–10. http://dx.doi.org/10.1189/jlb.69.1.3.

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42

Chang, Lufen, and Michael Karin. "Mammalian MAP kinase signalling cascades." Nature 410, no. 6824 (2001): 37–40. http://dx.doi.org/10.1038/35065000.

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43

Bandyopadhyay, Sourav, Chih-yuan Chiang, Jyoti Srivastava, et al. "A human MAP kinase interactome." Nature Methods 7, no. 10 (2010): 801–5. http://dx.doi.org/10.1038/nmeth.1506.

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44

Ray, L. B. "Memories of MAP Kinase Activation." Science 326, no. 5952 (2009): 503. http://dx.doi.org/10.1126/science.326_503c.

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45

Awazu, M. "MAP kinase in renal development." Nephrology Dialysis Transplantation 17, no. 90009 (2002): 5–7. http://dx.doi.org/10.1093/ndt/17.suppl_9.5.

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46

ter Haar, Ernst. "Activating MAP KAP Kinase 2." Structure 11, no. 6 (2003): 611–12. http://dx.doi.org/10.1016/s0969-2126(03)00104-7.

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47

Drogen, Frank, and Matthias Peter. "MAP kinase dynamics in yeast." Biology of the Cell 93, no. 1-2 (2001): 63–70. http://dx.doi.org/10.1016/s0248-4900(01)01123-6.

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48

COBB, M., and E. GOLDSMITH. "Dimerization in MAP-kinase signaling." Trends in Biochemical Sciences 25, no. 1 (2000): 7–9. http://dx.doi.org/10.1016/s0968-0004(99)01508-x.

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49

L'Allemain, Gilles. "Deciphering the MAP kinase pathway." Progress in Growth Factor Research 5, no. 3 (1994): 291–334. http://dx.doi.org/10.1016/0955-2235(94)90011-6.

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50

Shapiro, Paul. "Discovering New MAP Kinase Inhibitors." Chemistry & Biology 13, no. 8 (2006): 807–9. http://dx.doi.org/10.1016/j.chembiol.2006.08.001.

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