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Journal articles on the topic 'Voie des MAP kinases'

Author: Grafiati

Published: 5 October 2024

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1

Dereure, O. "La voie des MAP-kinases dans les génodermatoses : de nouveaux développements." Annales de Dermatologie et de Vénéréologie 133, no. 12 (December 2006): 1031. http://dx.doi.org/10.1016/s0151-9638(06)71096-1.

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2

Mourah, S. "Étude la voie MAP kinases dans la pathogénie de l’histiocytose Langheransienne pulmonaire de l’adulte." Revue des Maladies Respiratoires 31 (January 2014): A203. http://dx.doi.org/10.1016/j.rmr.2013.10.151.

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3

Fierrard, H., and M. L. Raffin-Sanson. "Un nouveau mécanisme d'activation de la voie des MAP kinases dans le cancer papillaire thyroïdien." EMC - Endocrinologie - Nutrition 2, no. 1 (January 2005): 1–2. http://dx.doi.org/10.1016/s1155-1941(05)44140-2.

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4

Fierrard, H., and M. L. Raffin-Sanson. "Un nouveau mécanisme d'activation de la voie des MAP kinases dans le cancer papillaire thyroïdien." EMC - Endocrinologie 2, no. 4 (December 2005): 265–67. http://dx.doi.org/10.1016/j.emcend.2005.09.002.

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5

Dereure, O. "Implication de la voie des MAP-kinases dans les nævus sébacés et le syndrome de Schimmelpenning." Annales de Dermatologie et de Vénéréologie 140, no. 4 (April 2013): 326–27. http://dx.doi.org/10.1016/j.annder.2013.02.009.

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6

Dereure, O. "Anomalies de la voie des MAP Kinases dans le mélanome : B-RAF n’est pas seul en cause." Annales de Dermatologie et de Vénéréologie 139, no. 10 (October 2012): 691–92. http://dx.doi.org/10.1016/j.annder.2012.04.157.

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7

Bouskine, A., M. Nebout, B. Mograbi, S. Lambard, G. Pointis, S. Carreau, and P. Fénichel. "CO17 - Contrôle estrogénique de la prolifération des cellules séminomateuses humaines par une voie non génomique impliquant les map-kinases." Annales d'Endocrinologie 65, no. 4 (September 2004): 261–62. http://dx.doi.org/10.1016/s0003-4266(04)95698-3.

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8

Dereure, O. "Mutation du promoteur de Tert dans le mélanome : la voie des MAP-kinases n’est décidément pas seule en cause." Annales de Dermatologie et de Vénéréologie 140, no. 6-7 (June 2013): 487–88. http://dx.doi.org/10.1016/j.annder.2013.04.071.

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9

Frouin, E., B. Guillot, M. Larrieux, A. Tempier, N. Boulle, C. Girard, V. Costes, and J. Solassol. "Étude moléculaire de lésions épithéliales cutanées induites par vemurafenib chez des patients atteints de mélanome métastatique : une activation de la voie des MAP-Kinases." Annales de Dermatologie et de Vénéréologie 140, no. 12 (December 2013): S395. http://dx.doi.org/10.1016/j.annder.2013.09.075.

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10

Hanauer, A., E. Trivier, D. De Cesare, S. Jacquot, S. Pannetier, P. Sassone-Corsi, and JL Mandel. "Le syndrome de Coffin-Lowry : une anomalie de la transduction du signal (voie Ras/MAP kinase)." médecine/sciences 13, no. 1 (1997): 107. http://dx.doi.org/10.4267/10608/317.

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11

Oberlé, Marion, Anna Greliak, Clotilde Descarpentries, Olivier Farchi, Sandrine Mansard, Laurent Machet, Nora Kramkimel, David Dudoignon, Laurent Mortier, and Philippe Jamme. "Réponse clinique et radiologique de mélanomes BRAF p.Thr599dup mutés, sous inhibiteurs de la voie MAP kinase." Annales de Dermatologie et de Vénéréologie - FMC 1, no. 8 (December 2021): A72—A73. http://dx.doi.org/10.1016/j.fander.2021.09.469.

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12

Le Quement, C., J. Y. Gillon, V. Lagente, and E. Boichot. "088 L’élastase du macrophage (MMP-12) induit une production d’IL-8/CXCL8 par des cellules épithéliales alvéolaires, via la voie des MAP (Mitogen-Activated Protein) Kinases." Revue des Maladies Respiratoires 23, no. 5 (November 2006): 558. http://dx.doi.org/10.1016/s0761-8425(06)71916-7.

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13

Amouyal, C., E. Capel, E. Pussard, J. Capeau, C. Vigouroux, M. Caron-Debarle, and J. Young. "CA-146: Hypoglycémies induites par des auto-anticorps anti récepteur de l'insuline stimulant les voies de signalisation AKT/PKB et MAP kinases." Diabetes & Metabolism 42 (March 2016): A75. http://dx.doi.org/10.1016/s1262-3636(16)30278-6.

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14

Chen, Zhu, Tara Beers Gibson, Fred Robinson, Loraine Silvestro, Gray Pearson, Bing-e. Xu, Angelique Wright, Colleen Vanderbilt, and Melanie H. Cobb. "MAP Kinases." Chemical Reviews 101, no. 8 (August 2001): 2449–76. http://dx.doi.org/10.1021/cr000241p.

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15

Wilsbacher, Julie L., Elizabeth J. Goldsmith, and Melanie H. Cobb. "Phosphorylation of MAP kinases by MAP/ERK kinases involves multiple regions of MAP kinases." Journal of Biological Chemistry 274, no. 34 (August 1999): 24440. http://dx.doi.org/10.1016/s0021-9258(19)55580-6.

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16

Wilsbacher, Julie L., Elizabeth J. Goldsmith, and Melanie H. Cobb. "Phosphorylation of MAP Kinases by MAP/ERK Involves Multiple Regions of MAP Kinases." Journal of Biological Chemistry 274, no. 24 (June 11, 1999): 16988–94. http://dx.doi.org/10.1074/jbc.274.24.16988.

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17

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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18

LEE, S., T. ZHOU, and E. GOLDSMITH. "Crystallization of MAP kinases." Methods 40, no. 3 (November 2006): 224–33. http://dx.doi.org/10.1016/j.ymeth.2006.05.003.

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19

Murray, Andrew W. "MAP Kinases in Meiosis." Cell 92, no. 2 (January 1998): 157–59. http://dx.doi.org/10.1016/s0092-8674(00)80910-1.

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20

Nebreda, Angel R. "Inactivation of MAP kinases." Trends in Biochemical Sciences 19, no. 1 (January 1994): 1–2. http://dx.doi.org/10.1016/0968-0004(94)90163-5.

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21

Pryciak, Peter M. "MAP Kinases Bite Back." Developmental Cell 1, no. 4 (October 2001): 449–51. http://dx.doi.org/10.1016/s1534-5807(01)00066-1.

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22

Dong, Chen, Roger J. Davis, and Richard A. Flavell. "MAP KINASES IN THEIMMUNERESPONSE." Annual Review of Immunology 20, no. 1 (April 2002): 55–72. http://dx.doi.org/10.1146/annurev.immunol.20.091301.131133.

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23

Chen, Zhu, Tara Beers Gibson, Fred Robinson, Loraine Silvestro, Gray Pearson, Bing-e. Xu, Angelique Wright, Colleen Vanderbilt, and Melanie H. Cobb. "ChemInform Abstract: MAP Kinases." ChemInform 32, no. 40 (May 24, 2010): no. http://dx.doi.org/10.1002/chin.200140296.

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24

Thibault, T., C. Auvens, T. Rogier, G. Muller, A. Turcu, J. Lecluse, S. Mouries-Martin, et al. "Analyse de classification des uvéites secondaires aux inhibiteurs de check-points et aux inhibiteurs de la voie MAP-kinase (inhibiteurs de BRAF et MEK) à partir des cas issus de la base nationale de pharmacovigilance." La Revue de Médecine Interne 43 (December 2022): A371—A372. http://dx.doi.org/10.1016/j.revmed.2022.10.079.

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25

Tan, Xin, Da-Yuan Chen, Zhe Yang, Yong-Chao Wang, Manyu Li, Heide Schatten, and Qing-Yuan Sun. "Phosphorylation of p90rsk during meiotic maturation and parthenogenetic activation of rat oocytes: correlation with MAP kinases." Zygote 9, no. 3 (August 2001): 269–76. http://dx.doi.org/10.1017/s0967199401001290.

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This paper reports on the activation of p90rsk during meiotic maturation and the inactivation of p90rsk after electrical parthenogenetic activation of rat oocytes. In addition, the correlation between p90rsk and MAP kinases after different treatments was studied. We assessed p90rsk activity by examining its electrophoretic mobility shift on SDS-PAGE and evaluated ERK1+2 activity by both mobility shift and a specific antibody against phospho-MAP kinase. The phosphorylation of p90rsk during rat oocyte maturation was a sequential process that may be divided into two stages: the first stage was partial phosphorylation, which was irrelevant with MAP kinases because p90rsk phosphorylation took place prior to activation of MAP kinases. The second stage inferred full activation occurred at the time when MAP kinases began to be activated (3 h after germinal visicle breakdown). Evidence for the involvement of MAP kinases in the p90rsk phosphorylation was further obtained by the following approaches: (1) okadaic acid (OA) accelerated the phosphorylation of both MAP kinases and p90rsk; (2) OA induced phosphorylation of both MAP kinases and p90rsk in the presence of IBMX; (3) when activation of MAP kinases was inhibited by cycloheximide, p90rsk phosphorylation was also abolished; (4) dephosphorylation of p90rsk began to take place at 3 h post-activation, temporally correlated with the completion of MAP kinase inactivation; (5) phosphorylation of both kinases was maintained in oocytes that failed to form pronuclei after stimulation; (6) OA abolished the dephosphorylation of both kinases after parthenogenetic activation. Our data suggest that MAP kinases are not required for early partial activation of p90rsk but are required for full activation of p90rsk during rat oocyte maturation, and that p90rsk dephosphorylation occurs following MAP kinase inactivation after parthenogenetic activation of rat oocytes.

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26

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

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27

Ueno, Yoshihisa, Riichiro Yoshida, Mitsuko Kishi-Kaboshi, Akane Matsushita, Chang-Jie Jiang, Shingo Goto, Akira Takahashi, Hirohiko Hirochika, and Hiroshi Takatsuji. "MAP kinases phosphorylate rice WRKY45." Plant Signaling & Behavior 8, no. 6 (June 2013): e24510. http://dx.doi.org/10.4161/psb.24510.

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28

Rodríguez-Berriguete, Gonzalo, Benito Fraile, Pilar Martínez-Onsurbe, Gabriel Olmedilla, Ricardo Paniagua, and Mar Royuela. "MAP Kinases and Prostate Cancer." Journal of Signal Transduction 2012 (October 20, 2012): 1–9. http://dx.doi.org/10.1155/2012/169170.

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The three major mitogen-activated protein kinases (MAPKs) p38, JNK, and ERK are signal transducers involved in a broad range of cell functions including survival, apoptosis, and cell differentiation. Whereas JNK and p38 have been generally linked to cell death and tumor suppression, ERK plays a prominent role in cell survival and tumor promotion, in response to a broad range of stimuli such as cytokines, growth factors, ultraviolet radiation, hypoxia, or pharmacological compounds. However, there is a growing body of evidence supporting that JNK and p38 also contribute to the development of a number of malignances. In this paper we focus on the involvement of the MAPK pathways in prostate cancer, including the less-known ERK5 pathway, as pro- or antitumor mediators, through their effects on apoptosis, survival, metastatic potential, and androgen-independent growth.

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29

Huang, C. "MAP kinases and cell migration." Journal of Cell Science 117, no. 20 (October 15, 2004): 4619–28. http://dx.doi.org/10.1242/jcs.01481.

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30

Stanton, Lee-Anne, T. Michael Underhill, and Frank Beier. "MAP kinases in chondrocyte differentiation." Developmental Biology 263, no. 2 (November 2003): 165–75. http://dx.doi.org/10.1016/s0012-1606(03)00321-x.

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31

Somssich, Imre E. "MAP kinases and plant defence." Trends in Plant Science 2, no. 11 (November 1997): 406–8. http://dx.doi.org/10.1016/s1360-1385(97)01121-7.

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32

Suganuma, T., and J. L. Workman. "MAP kinases and histone modification." Journal of Molecular Cell Biology 4, no. 5 (July 24, 2012): 348–50. http://dx.doi.org/10.1093/jmcb/mjs043.

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33

Cobb, Melanie H., and Elizabeth J. Goldsmith. "How MAP Kinases Are Regulated." Journal of Biological Chemistry 270, no. 25 (June 23, 1995): 14843–46. http://dx.doi.org/10.1074/jbc.270.25.14843.

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34

Xu, Jin-Rong. "MAP Kinases in Fungal Pathogens." Fungal Genetics and Biology 31, no. 3 (December 2000): 137–52. http://dx.doi.org/10.1006/fgbi.2000.1237.

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35

Davis, Roger J. "Transcriptional regulation by MAP kinases." Molecular Reproduction and Development 42, no. 4 (December 1995): 459–67. http://dx.doi.org/10.1002/mrd.1080420414.

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36

Yamboliev, Ilia A., Jason C. Hedges, Jack L. M. Mutnick, Leonard P. Adam, and William T. Gerthoffer. "Evidence for modulation of smooth muscle force by the p38 MAP kinase/HSP27 pathway." American Journal of Physiology-Heart and Circulatory Physiology 278, no. 6 (June 1, 2000): H1899—H1907. http://dx.doi.org/10.1152/ajpheart.2000.278.6.h1899.

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Mitogen-activated protein (MAP) kinases signal to proteins that could modify smooth muscle contraction. Caldesmon is a substrate for extracellular signal-related kinases (ERK) and p38 MAP kinases in vitro and has been suggested to modulate actin-myosin interaction and contraction. Heat shock protein 27 (HSP27) is downstream of p38 MAP kinases presumably participating in the sustained phase of muscle contraction. We tested the role of caldesmon and HSP27 phosphorylation in the contractile response of vascular smooth muscle by using inhibitors of both MAP kinase pathways. In intact smooth muscle, PD-098059 abolished endothelin-1 (ET-1)-stimulated phosphorylation of ERK MAP kinases and caldesmon, but p38 MAP kinase activation and contractile response remained unaffected. SB-203580 reduced muscle contraction and inhibited p38 MAP kinase and HSP27 phosphorylation but had no effect on ERK MAP kinase and caldesmon phosphorylation. In permeabilized muscle fibers, SB-203580 and a polyclonal anti-HSP27 antibody attenuated ET-1-dependent contraction, whereas PD-098059 had no effect. These results suggest that ERK MAP kinases phosphorylate caldesmon in vivo but that activation of this pathway is unnecessary for force development. The generation of maximal force may be modulated by the p38 MAP kinase/HSP27 pathway.

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37

Yamboliev, Ilia A., Kevin M. Wiesmann, Cherie A. Singer, Jason C. Hedges, and William T. Gerthoffer. "Phosphatidylinositol 3-kinases regulate ERK and p38 MAP kinases in canine colonic smooth muscle." American Journal of Physiology-Cell Physiology 279, no. 2 (August 1, 2000): C352—C360. http://dx.doi.org/10.1152/ajpcell.2000.279.2.c352.

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In canine colon, M2/M3 muscarinic receptors are coupled to extracellular signal-regulated kinase (ERK) and p38 mitogen-activated protein (MAP) kinases. We tested the hypothesis that this coupling is mediated by enzymes of the phosphatidylinositol (PI) 3-kinase family. RT-PCR and Western blotting demonstrated expression of two isoforms, PI 3-kinase-α and PI 3-kinase-γ. Muscarinic stimulation of intact muscle strips (10 μM ACh) activated PI 3-kinase-γ, ERK and p38 MAP kinases, and MAP kinase-activated protein kinase-2, whereas PI 3-kinase-α activation was not detected. Wortmannin (25 μM) abolished the activation of PI 3-kinase-γ, ERK, and p38 MAP kinases. MAP kinase inhibition was a PI 3-kinase-γ-specific effect, since wortmannin did not inhibit recombinant activated murine ERK2 MAP kinase, protein kinase C, Raf-1, or MAP kinase kinase. In cultured muscle cells, newborn calf serum (3%) activated PI 3-kinase-α and PI 3-kinase-γ isoforms, ERK and p38 MAP kinases, and stimulated chemotactic cell migration. Using wortmannin and LY-294002 to inhibit PI 3-kinase activity and PD-098059 and SB-203580 to inhibit ERK and p38 MAP kinases, we established that these enzymes are functionally important for regulation of chemotactic migration of colonic myocytes.

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38

Cook, Amy K., Michael Carty, Cherie A. Singer, Ilia A. Yamboliev, and William T. Gerthoffer. "Coupling of M2 muscarinic receptors to ERK MAP kinases and caldesmon phosphorylation in colonic smooth muscle." American Journal of Physiology-Gastrointestinal and Liver Physiology 278, no. 3 (March 1, 2000): G429—G437. http://dx.doi.org/10.1152/ajpgi.2000.278.3.g429.

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Coupling of M2 and M3 muscarinic receptors to activation of mitogen-activated protein (MAP) kinases and phosphorylation of caldesmon was studied in canine colonic smooth muscle strips in which M3 receptors were selectively inactivated by N, N-dimethyl-4-piperidinyl diphenylacetate (4-DAMP) mustard (40 nM). ACh elicited activation of extracellular signal-regulated kinase (ERK) 1, ERK2, and p38 MAP kinases in control muscles and increased phosphorylation of caldesmon (Ser789), a putative downstream target of MAP kinases. Alkylation of M3 receptors with 4-DAMP had only a modest inhibitory effect on ERK activation, p38 MAP kinase activation, and caldesmon phosphorylation. Subsequent treatment with 1 μM AF-DX 116 completely prevented activation of ERK and p38 MAP kinase and prevented caldesmon phosphorylation. Caldesmon phosphorylation was blocked by the MAP kinase/ERK kinase inhibitor PD-98509 but not by the p38 MAP kinase inhibitor SB-203580. These results indicate that colonic smooth muscle M2 receptors are coupled to ERK and p38 MAP kinases. Activation of ERK, but not p38 MAP kinases, results in phosphorylation of caldesmon in vivo, which is a novel function for M2receptor activation in smooth muscle.

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39

CHIARIELLO, Mario, Eliana GOMEZ, and J. Silvio GUTKIND. "Regulation of cyclin-dependent kinase (Cdk) 2 Thr-160 phosphorylation and activity by mitogen-activated protein kinase in late G1 phase." Biochemical Journal 349, no. 3 (July 25, 2000): 869–76. http://dx.doi.org/10.1042/bj3490869.

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Mitogen-activated protein (MAP) kinases, p42MAPK and p44MAPK, are central components of growth-promoting signalling pathways. However, how stimulation of MAP kinases culminates in cell-cycle progression is still poorly understood. Here we show that mitogenic stimulation of NIH 3T3 cells causes a sustained activation of MAP kinases, which lasts until cells begin progressing through the G1/S boundary. Furthermore, we observed that disruption of the MAP-kinase pathway with a selective MEK (MAP kinase/extracellular-signal-regulated protein kinase kinase) inhibitor, PD98059, prevents the activation of cyclin-dependent kinase (Cdk) 2 and DNA synthesis, even when added during late G1 phase, once the known mechanisms by which MAP kinase controls G1 progression, accumulation of G1 cyclins and degradation of Cdk inhibitors have already taken place. Moreover, we provide evidence indicating that MAP kinases control Cdk2 Thr-160 activating phosphorylation and function, possibly by regulating the activity of a Cdk-activating kinase, thus promoting the re-initiation of DNA synthesis. These findings suggest the existence of a novel mechanism whereby signal-transducing pathways converging on MAP kinases can affect the cell-cycle machinery and, ultimately, participate in cell-growth control.

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40

Gerthoffer, W. T., I. A. Yamboliev, J. Pohl, R. Haynes, S. Dang, and J. McHugh. "Activation of MAP kinases in airway smooth muscle." American Journal of Physiology-Lung Cellular and Molecular Physiology 272, no. 2 (February 1, 1997): L244—L252. http://dx.doi.org/10.1152/ajplung.1997.272.2.l244.

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To test the hypothesis that mitogen-activated protein (MAP) kinases are activated by contractile agonists in intact nonproliferating airway smooth muscle, kinase activities were compared in resting and stimulated canine tracheal smooth muscle. Kinase activities in sodium dodecyl sulfate extracts were assayed by a gel renaturation method. Myelin basic protein kinase activities corresponding to ERK1 and ERK2 immunoreactive proteins were activated twofold above the basal level within 5 min by 1 microM carbachol. MAP kinase activity assayed in crude homogenates using a synthetic peptide substrate (APRTPGGRR) also increased twofold above basal in muscles stimulated with 1 microM carbachol. Two protein kinases separated by Mono-Q chromatography were identified on Western blots as ERK1 and ERK2 MAP kinases. Carbachol stimulation increased caldesmon phosphorylation in intact muscle, and purified caldesmon was a substrate for activated murine ERK2 MAP kinase. Activated ERK2 MAP kinase added to Triton X-100-permeabilized fibers potentiated Ca2+-induced contraction. The results show that ERK MAP kinases are activated after stimulation of muscarinic receptors in airway smooth muscle, which is consistent with coupling of MAP kinases to phosphorylation of caldesmon in vivo.

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41

Chen, R. H., C. Sarnecki, and J. Blenis. "Nuclear localization and regulation of erk- and rsk-encoded protein kinases." Molecular and Cellular Biology 12, no. 3 (March 1992): 915–27. http://dx.doi.org/10.1128/mcb.12.3.915-927.1992.

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We demonstrate that members of the erk-encoded family of mitogen-activated protein (MAP) kinases (pp44/42mapk/erk) and members of the rsk-encoded protein kinases (RSKs or pp90rsk) are present in the cytoplasm and nucleus of HeLa cells. Addition of growth factors to serum-deprived cells results in increased tyrosine and threonine phosphorylation and in the activation of cytosolic and nuclear MAP kinases. Activated MAP kinases then phosphorylate (serine/threonine) and activate RSKs. Concurrently, a fraction of the activated MAP kinases and RSKs enter the nucleus. In addition, a distinct growth-regulated RSK-kinase activity (an enzyme[s] that phosphorylates recombinant RSK in vitro and that may be another member of the erk-encoded family of MAP kinases) was found associated with a postnuclear membrane fraction. Regulation of nuclear MAP kinase and RSK activities by growth factors and phorbol ester is coordinate with immediate-early gene expression. Indeed, in vitro, MAP kinase and/or RSK phosphorylates histone H3 and the recombinant c-Fos and c-Jun polypeptides, transcription factors phosphorylated in a variety of cells in response to growth stimuli. These in vitro studies raise the possibility that the MAP kinase/RSK signal transduction pathway represents a protein-Tyr/Ser/Thr phosphorylation cascade with the spatial distribution and temporal regulation that can account for the rapid transmission of growth-regulating information from the membrane, through the cytoplasm, and to the nucleus.

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42

Chen, R. H., C. Sarnecki, and J. Blenis. "Nuclear localization and regulation of erk- and rsk-encoded protein kinases." Molecular and Cellular Biology 12, no. 3 (March 1992): 915–27. http://dx.doi.org/10.1128/mcb.12.3.915.

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We demonstrate that members of the erk-encoded family of mitogen-activated protein (MAP) kinases (pp44/42mapk/erk) and members of the rsk-encoded protein kinases (RSKs or pp90rsk) are present in the cytoplasm and nucleus of HeLa cells. Addition of growth factors to serum-deprived cells results in increased tyrosine and threonine phosphorylation and in the activation of cytosolic and nuclear MAP kinases. Activated MAP kinases then phosphorylate (serine/threonine) and activate RSKs. Concurrently, a fraction of the activated MAP kinases and RSKs enter the nucleus. In addition, a distinct growth-regulated RSK-kinase activity (an enzyme[s] that phosphorylates recombinant RSK in vitro and that may be another member of the erk-encoded family of MAP kinases) was found associated with a postnuclear membrane fraction. Regulation of nuclear MAP kinase and RSK activities by growth factors and phorbol ester is coordinate with immediate-early gene expression. Indeed, in vitro, MAP kinase and/or RSK phosphorylates histone H3 and the recombinant c-Fos and c-Jun polypeptides, transcription factors phosphorylated in a variety of cells in response to growth stimuli. These in vitro studies raise the possibility that the MAP kinase/RSK signal transduction pathway represents a protein-Tyr/Ser/Thr phosphorylation cascade with the spatial distribution and temporal regulation that can account for the rapid transmission of growth-regulating information from the membrane, through the cytoplasm, and to the nucleus.

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43

Goldsmith, E. J. "MAP kinases and their activating enzymes." Acta Crystallographica Section A Foundations of Crystallography 52, a1 (August 8, 1996): C95. http://dx.doi.org/10.1107/s010876739609530x.

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44

Adjei, Alex A. "E-2. Inhibitors of MAP kinases." Lung Cancer 41 (August 2003): S5. http://dx.doi.org/10.1016/s0169-5002(03)90409-0.

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45

Clarke, Paul R. "Signal Transduction: Switching off MAP kinases." Current Biology 4, no. 7 (July 1994): 647–50. http://dx.doi.org/10.1016/s0960-9822(00)00144-5.

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46

Jonak, C., W. Ligterink, and H. Hirt. "MAP kinases in plant signal transduction." Cellular and Molecular Life Sciences CMLS 55, no. 2 (February 1999): 204–13. http://dx.doi.org/10.1007/s000180050285.

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47

Pelech, S., and J. Sanghera. "MAP kinases: charting the regulatory pathways." Science 257, no. 5075 (September 4, 1992): 1355–56. http://dx.doi.org/10.1126/science.1382311.

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48

Magnelli, Lucia, Nicola Schiavone, Fabio Staderini, Alessio Biagioni, and Laura Papucci. "MAP Kinases Pathways in Gastric Cancer." International Journal of Molecular Sciences 21, no. 8 (April 21, 2020): 2893. http://dx.doi.org/10.3390/ijms21082893.

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Gastric cancer (GC) is turning out today to be one of the most important welfare issues for both Asian and European countries. Indeed, while the vast majority of the disease burden is located in China and in Pacific and East Asia, GC in European countries still account for about 100,000 deaths per year. With this review article, we aim to focus the attention on one of the most complex cellular pathways involved in GC proliferation, invasion, migration, and metastasis: the MAP kinases. Such large kinases family is to date constantly studied, since their discovery more than 30 years ago, due to the important role that it plays in the regulation of physiological and pathological processes. Interactions with other cellular proteins as well as miRNAs and lncRNAs may modulate their expression influencing the cellular biological features. Here, we summarize the most important and recent studies involving MAPK in GC. At the same time, we need to underly that, differently from cancers arising from other tissues, where MAPK pathways seems to be a gold target for anticancer therapies, GC seems to be unique in any aspect. Our aim is to review the current knowledge in MAPK pathways alterations leading to GC, including H. pylori MAPK-triggering to derail from gastric normal epithelium to GC and to encourage researches involved in MAPK signal transduction, that seems to definitely sustain GC development.

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Huang, Ching-Yu, and Tse-Hua Tan. "DUSPs, to MAP kinases and beyond." Cell & Bioscience 2, no. 1 (2012): 24. http://dx.doi.org/10.1186/2045-3701-2-24.

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Moustafa, Khaled. "MAP kinases nomenclature: Time for curation." Plant Signaling & Behavior 12, no. 12 (December 2, 2017): e1388974. http://dx.doi.org/10.1080/15592324.2017.1388974.

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