Atypical mitogen-activated protein kinases: Structure, regulation and functions

SWISS‐MODEL and the Swiss‐Pdb Viewer: An environment for comparative protein modeling

Guex, N., & Peitsch, M. C. (1997) · Electrophoresis · doi:10.1002/elps.1150181505 · Cited by 11,312

THE UBIQUITIN SYSTEM

Hershko, A., & Ciechanover, A. (1998) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.67.1.425 · Cited by 8,840

The protein kinase complement of the human genome

Manning, G., Whyte, D. B., Martinez, R., Hunter, T., & Sudarsanam, S. (2002) · Science · doi:10.1126/science.1075762 · Cited by 8,145

Mammalian MAP kinase signalling cascades

Chang, L., & Karin, M. (2001) · Nature · doi:10.1038/35065000 · Cited by 5,118

Mitogen-Activated Protein (MAP) Kinase Pathways: Regulation and Physiological Functions*

Pearson, G. W., Robinson, F. L., Gibson, T. B., Xu, B.-E., Karandikar, M. S., Berman, K. S., & Cobb, M. H. (2001) · Endocrine Reviews · doi:10.1210/edrv.22.2.0428 · Cited by 4,111

Mechanisms Underlying Ubiquitination

Pickart, C. M. (2001) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.70.1.503 · Cited by 3,184

Mitogen-Activated Protein Kinase: Conservation of a Three-Kinase Module From Yeast to Human

Widmann, C., Gibson, S. B., Jarpe, M. B., & Johnson, G. L. (1999) · Physiological Reviews · doi:10.1152/physrev.1999.79.1.143 · Cited by 2,707

ERKs: A family of protein-serine/threonine kinases that are activated and tyrosine phosphorylated in response to insulin and NGF

Boulton, T. G., Nye, S. H., Robbins, D. J., Ip, N. Y., Radzlejewska, E., Morgenbesser, S. D., DePinho, R. A., Panayotatos, N., Cobb, M. H., & Yancopoulos, G. D. (1991) · Cell · doi:10.1016/0092-8674(91)90098-j · Cited by 1,876

Signal Transduction through MAP Kinase Cascades

Lewis, T. S., Shapiro, P. S., & Ahn, N. G. (1998) · Advances in cancer research · doi:10.1016/s0065-230x(08)60765-4 · Cited by 1,759

Pharmacological inhibition of the MEK5/ERK5 and PI3K/Akt signaling pathways synergistically reduces viability in triple‐negative breast cancer

Wright, T. D., Raybuck, C., Bhatt, A. B., Monlish, D. A., Chakrabarty, S., Wendekier, K., Gartland, N., Gupta, M., Burow, M. E., Flaherty, P. T., et al. (2019) · Journal of Cellular Biochemistry · doi:10.1002/jcb.29350 · Cited by 29

A phylogenetic profiling approach identifies novel ciliogenesis genes in Drosophila and C. elegans

Dobbelaere, J., Su, T. Y., Érdi, B., Schleiffer, A., & Dammermann, A. (2023) · The EMBO Journal · doi:10.15252/embj.2023113616 · Cited by 22

ERK5 regulation in naïve T‐cell activation and survival

Ananieva, O., Macdonald, A., Wang, X., McCoy, C. E., McIlrath, J. M., Tournier, C., & Arthur, J. S. C. (2008) · European Journal of Immunology · doi:10.1002/eji.200737867 · Cited by 28

Primary Cilium Formation and Ciliary Protein Trafficking Is Regulated by the Atypical MAP Kinase MAPK15 inCaenorhabditis elegansand Human Cells

Kazatskaya, A., Kuhns, S., Lambacher, N. J., Kennedy, J. E., Brear, A. G., McManus, G., Sengupta, P., & Blacque, O. E. (2017) · Genetics · doi:10.1534/genetics.117.300383 · Cited by 30

The Ser186 phospho-acceptor site within ERK4 is essential for its ability to interact with and activate PRAK/MK5

Perander, M., Åberg, E., Johansen, B., Dreyer, B., Guldvik, I. J., Outzen, H., Keyse, S. M., & Seternes, O. M. (2008) · Biochemical Journal · doi:10.1042/bj20071369 · Cited by 28

Upregulation of miR‐183 represses neuropathic pain through inhibiton of MAP3K4 in CCI rat models

Huang, L., & Wang, L. (2019) · Journal of Cellular Physiology · doi:10.1002/jcp.29276 · Cited by 27

p38β and Cancer: The Beginning of the Road

Roche, O., Fernández‐Aroca, D. M., Arconada‐Luque, E., García-Flores, N., Mellor, L. F., Ruiz‐Hidalgo, M. J., & Sánchez‐Prieto, R. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21207524 · Cited by 27

Activation of the Smk1 Mitogen-Activated Protein Kinase by Developmentally Regulated Autophosphorylation

Whinston, E. R., Omerza, G., Singh, A., Tio, C. W., & Winter, E. (2012) · Molecular and Cellular Biology · doi:10.1128/mcb.00973-12 · Cited by 26

Early Evolution of the Mitogen-Activated Protein Kinase Family in the Plant Kingdom

Kalapos, B., Hlavová, M., Nádai, T. V., Galiba, G., Bišová, K., & Dóczi, R. (2019) · Scientific Reports · doi:10.1038/s41598-019-40751-y · Cited by 25

FBXW7-mediated ERK3 degradation regulates the proliferation of lung cancer cells

An, H., Lee, C., Lee, G.-E., Choi, Y., Jeung, D., Chen, W., Lee, H. S., Kang, H. C., Lee, J. Y., Kim, D. J., et al. (2022) · Experimental & Molecular Medicine · doi:10.1038/s12276-021-00721-9 · Cited by 25

Peptides as Signaling Inhibitors for Mammalian MAP Kinase Cascades

Gaestel, M., & Kracht, M. (2009) · Current Pharmaceutical Design · doi:10.2174/138161209788682299 · Cited by 27

Kinase signaling cascades: an updated mechanistic landscape

Nussinov, R., Regev, C., & Jang, H. (2025) · Chemical Science · doi:10.1039/d5sc04657b · Cited by 28

Dictyostelium Erk2 is an atypical MAPK required for chemotaxis

Schwebs, D. J., Pan, M., Adhikari, N., Kuburich, N. A., Jin, T., & Hadwiger, J. A. (2018) · Cellular Signalling · doi:10.1016/j.cellsig.2018.03.006 · Cited by 25

USF2 enhances the osteogenic differentiation of PDLCs by promoting ATF4 transcriptional activities

Liu, F., Wang, X., Zheng, B., Li, D., Chen, C., Lee, I., Zhong, J., Li, D., & Liu, Y. (2019) · Journal of Periodontal Research · doi:10.1111/jre.12689 · Cited by 24

Fluid Shear Stress Suppresses Osteoclast Differentiation in RAW264.7 Cells through Extracellular Signal-Regulated Kinase 5 (ERK5) Signaling Pathway

Ma, C., Geng, B., Zhang, X., Li, R., Yang, X., & Xia, Y. (2020) · Medical Science Monitor · doi:10.12659/msm.918370 · Cited by 24

Therapeutic effect of neohesperidin on TNF-α-stimulated human rheumatoid arthritis fibroblast-like synoviocytes

Xiao-He, W. A. N. G., Ce, D. A. I., Jun, W. A. N. G., Rui, L. I. U., Li, L., & Yin, Z. (2021) · Chinese Journal of Natural Medicines · doi:10.1016/s1875-5364(21)60107-3 · Cited by 24

Therapeutic Regulation of Cardiac Fibroblast Function: Targeting stress-activated Protein Kinase Pathways

Turner, N. A. (2011) · Future Cardiology · doi:10.2217/fca.11.41 · Cited by 24

Characterization of the expression and regulation of MK5 in the murine ventricular myocardium

Dingar, D. D., Benoît, M.-J., Mamarbachi, A. M., Villeneuve, L. R., Gillis, M., Grandy, S. A., Gaestel, M., Fiset, C., & Allen, B. G. (2010) · Cellular Signalling · doi:10.1016/j.cellsig.2010.02.009 · Cited by 24

Mutant MAPK7-Induced Idiopathic Scoliosis is Linked to Impaired Osteogenesis

Zhou, T., Chen, C., Xu, C., Zhou, H., Gao, B., Su, D., Liao, Z., Li, Y., Yang, S., & Su, P. (2018) · Cellular Physiology and Biochemistry · doi:10.1159/000491956 · Cited by 24

The immuneoreaction and antioxidant status of Chinese mitten crab (Eriocheir sinensis) involve protein metabolism and the response of mTOR signaling pathway to dietary methionine levels

Wang, X., Lei, X., Guo, Z., Wang, S., Wan, J.-W., Liu, H., Chen, Y., Wang, G., Wang, Q., & Zhang, D. (2022) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2022.07.012 · Cited by 23

MAPK15 controls cellular responses to oxidative stress by regulating NRF2 activity and expression of its downstream target genes

Franci, L., Vallini, G., Bertolino, F. M., Cicaloni, V., Inzalaco, G., Cicogni, M., Tinti, L., Calabrese, L., Barone, V., Salvini, L., et al. (2024) · Redox Biology · doi:10.1016/j.redox.2024.103131 · Cited by 22

Dual functions of DP1 promote biphasic Wnt‐on and Wnt‐off states during anteroposterior neural patterning

Kim, W., Kim, H., Katanaev, V. L., Lee, S. J., Ishitani, T., Cha, B., Han, J., & Jho, E. (2012) · The EMBO Journal · doi:10.1038/emboj.2012.181 · Cited by 23

Nemo-like kinase regulates the expression of vascular endothelial growth factor (VEGF) in alveolar epithelial cells

Ke, H., Masoumi, K. C., Ahlqvist, K., Seckl, M. J., Rydell-Törmänen, K., & Massoumi, R. (2016) · Scientific Reports · doi:10.1038/srep23987 · Cited by 22

MAPK15 is part of the ULK complex and controls its activity to regulate early phases of the autophagic process

Colecchia, D., Dapporto, F., Tronnolone, S., Salvini, L., & Chiariello, M. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.002527 · Cited by 21

Corydalis edulis total alkaloids (CETA) ameliorates cognitive dysfunction in rat model of Alzheimer disease through regulation of the antioxidant stress and MAP2/NF-κB

Liang, S., Zheng, Y., Lei, L., Deng, X., Ai, J., Li, Y., Zhang, T.-P., Mei, Z., & Ren, Y. (2020) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2019.112540 · Cited by 22

A walk-through MAPK structure and functionality with the 30-year-old yeast MAPK Slt2

González-Rubio, G., Sellers-Moya, Á., Martı́n, H., & Molina, M. (2021) · International Microbiology · doi:10.1007/s10123-021-00183-z · Cited by 21

Nemo-Like Kinase in Development and Diseases: Insights from Mouse Studies

Daams, R., & Massoumi, R. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21239203 · Cited by 21

Gene expression levels of 4-galactosyltransferase 5 correlate with the tumorigenic potentials of B16-F10 mouse melanoma cells

Shirane, K., Kuji, R., Tareyanagi, C., SATO, T. A., Kobayashi, Y., Furukawa, S., Murata, T., Kubota, S., Ishikawa, Y., Segawa, K., et al. (2014) · Glycobiology · doi:10.1093/glycob/cwu021 · Cited by 21

Major Physiological Signaling Pathways in the Regulation of Cell Proliferation and Survival

Tang, H., & Xue, G. (2017) · Handbook of experimental pharmacology · doi:10.1007/164_2017_4 · Cited by 22

A review of non-classical MAPK family member, MAPK4: A pivotal player in cancer development and therapeutic intervention

Yan, Y., Dai, T., Guo, M., Zhao, X., Chen, C., Zhou, Y., Qin, M., Xu, L., & Zhao, J. (2024) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2024.132686 · Cited by 21

Association of Nuclear-Localized Nemo-Like Kinase with Heat-Shock Protein 27 Inhibits Apoptosis in Human Breast Cancer Cells

Shaw-Hallgren, G., Chmielarska Masoumi, K., Zarrizi, R., Hellman, U., Karlsson, P., Helou, K., & Massoumi, R. (2014) · PLoS ONE · doi:10.1371/journal.pone.0096506 · Cited by 21

The Non-Classical MAP Kinase ERK3 Controls T Cell Activation

Marquis, M., Boulet, S., Mathien, S., Rousseau, J., Thébault, P., Daudelin, J., Rooney, J., Turgeon, B., Beauchamp, C., Meloche, S., et al. (2014) · PLoS ONE · doi:10.1371/journal.pone.0086681 · Cited by 21

Upregulation of ZO-1 in Cultured Human Corneal Epithelial Cells by a Peptide (PHSRN) Corresponding to the Second Cell-Binding Site of Fibronectin

Yanai, R., Ko, J., Nomi, N., Morishige, N., Chikama, T.-I., Hattori, A., Hozumi, K., Nomizu, M., & Nishida, T. (2009) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.08-2341 · Cited by 21

Protective Effects of Lactobacillus plantarum Lac16 on Clostridium perfringens Infection-Associated Injury in IPEC-J2 Cells

Zhou, Y., Wang, B., Wang, Q., Tang, L., Zou, P., Zeng, Z., Zhang, H., Gong, L., & Li, W. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222212388 · Cited by 21

ERK3 Is Required for Metaphase-Anaphase Transition in Mouse Oocyte Meiosis

Li, S., Ou, X., Wang, Z., Xiong, B., Tong, J., Liang, W. P., Li, M., Yuan, J. X., Ouyang, Y., Hou, Y., et al. (2010) · PLoS ONE · doi:10.1371/journal.pone.0013074 · Cited by 20

Extracellular signal-regulated kinases in pain of peripheral origin

White, J. P. M., Cibelli, M., Fidalgo, A. R., & Nagy, I. (2010) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2010.09.077 · Cited by 20

Distinct Docking Mechanisms Mediate Interactions between the Msg5 Phosphatase and Mating or Cell Integrity Mitogen-activated Protein Kinases (MAPKs) in Saccharomyces cerevisiae

Palacios, L., Dickinson, R. J., Sacristán-Reviriego, A., Didmon, M. P., Marín, M. J., Martı́n, H., Keyse, S. M., & Molina, M. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.286948 · Cited by 20

Mitogen activated protein kinases in renal fibrosis

Ma, F. Y. (2009) · Frontiers in Bioscience-Elite · doi:10.2741/e17 · Cited by 19

Hyperosmotic Stress Induces Unconventional Autophagy Independent of the Ulk1 Complex

Tamura, N., Kageyama, S., Komatsu, M., & Waguri, S. (2019) · Molecular and Cellular Biology · doi:10.1128/mcb.00024-19 · Cited by 19

BRAF inhibitors and their immunological effects in malignant melanoma

Adams, R., Coumbe, J. E. M., Coumbe, B. G. T., Thomas, J., Willsmore, Z., Dimitrievska, M., Yasuzawa-Parker, M., Hoyle, M., Ingar, S., Geh, J. L. C., et al. (2022) · Expert Review of Clinical Immunology · doi:10.1080/1744666x.2022.2044796 · Cited by 18

P38 MAPK and Radiotherapy: Foes or Friends?

García-Flores, N., Jiménez‐Suárez, J., Garnés‐García, C., Fernández‐Aroca, D. M., Sabater, S., Andrés, I., Fernández, A., Ruiz‐Hidalgo, M. J., Belandia, B., Sánchez‐Prieto, R., et al. (2023) · Cancers · doi:10.3390/cancers15030861 · Cited by 18

Basic fibroblast growth factor promotes glial cell-derived neurotrophic factor gene expression mediated by activation of ERK5 in rat C6 glioma cells

Obara, Y., Nemoto, W., Kohno, S., Murata, T., Kaneda, N., & Nakahata, N. (2010) · Cellular Signalling · doi:10.1016/j.cellsig.2010.11.020 · Cited by 18

Protein kinase C epsilon‐dependent extracellular signal‐regulated kinase 5 phosphorylation and nuclear translocation involved in cardiomyocyte hypertrophy with angiotensin II stimulation

Zhao, Z., Wang, W., Geng, J., Wang, L., Su, G., Zhang, Y., Ge, Z., & Kang, W. (2010) · Journal of Cellular Biochemistry · doi:10.1002/jcb.22441 · Cited by 18

Advances in ERK1/2 inhibition: a medicinal chemistry perspective on structure and regulation

Sah, V. K., Singh, A. K., Kumar, A. M., Prajapati, V., Kalsi, A. K., Khalilullah, H., Jaremko, M., Emwas, A.-H. M., Verma, A., & Kumar, P. (2025) · Journal of Enzyme Inhibition and Medicinal Chemistry · doi:10.1080/14756366.2025.2555510 · Cited by 17

Metastasis‑associated gene MAPK15 promotes the migration and invasion of osteosarcoma cells via the c‑Jun/MMPs pathway

Su, Z., Yang, B., Zeng, Z., Zhu, S., Wang, C., Lei, S., Jiang, Y., & Lin, L. (2020) · Oncology Letters · doi:10.3892/ol.2020.11544 · Cited by 17

Functional Analysis of p21Cip1/CDKN1A and Its Family Members in Trophoblastic Cells of the Placenta and Its Roles in Preeclampsia

Kreis, N., Friemel, A., Jennewein, L., Hoock, S. C., Hentrich, A. E., Nowak, T., Louwen, F., & Yuan, J. (2021) · Cells · doi:10.3390/cells10092214 · Cited by 17

MK5 haplodeficiency attenuates hypertrophy and preserves diastolic function during remodeling induced by chronic pressure overload in the mouse heart

Nawaito, S. A., Dingar, D. D., Sahadevan, P., Hussein, B., Sahmi, F., Shi, Y., Gillis, M., Gaestel, M., Tardif, J., & Allen, B. G. (2017) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00597.2016 · Cited by 17

The C-Terminus Tail Regulates ERK3 Kinase Activity and Its Ability in Promoting Cancer Cell Migration and Invasion

Elkhadragy, L., Alsaran, H., & Long, W. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21114044 · Cited by 17

Autophosphorylation of the Smk1 MAPK is spatially and temporally regulated by Ssp2 during meiotic development in yeast

Tio, C. W., Omerza, G., Sunder, S., & Winter, E. (2015) · Molecular Biology of the Cell · doi:10.1091/mbc.e15-05-0322 · Cited by 17

Osmoregulation, physiological metabolism, and oxidative stress responses to water salinity in adult males of Chinese mitten crabs (Eriocheir sinensis)

Wang, X., Guo, Z., Lei, X., Wang, S., Wan, J.-W., Liu, H., Chen, Y., Zhao, Y., Wang, G., Wang, Q., et al. (2022) · Aquaculture International · doi:10.1007/s10499-022-00998-1 · Cited by 16

Dissecting the signaling features of the multi-protein complex GPCR/β-arrestin/ERK1/2

Carmona-Rosas, G., Alcántara-Hernández, R., & Hernández-Espinosa, D. A. (2018) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2018.04.001 · Cited by 16

Nature of the Pre-Chemistry Ensemble in Mitogen-Activated Protein Kinases

Ghose, R. (2018) · Journal of Molecular Biology · doi:10.1016/j.jmb.2018.12.007 · Cited by 15

Identification of atypical mitogen-activated protein kinase MAPK4 as a novel regulator in acute lung injury

Mao, L., Zhou, Y., Chen, L., Hu, L. T., Liu, S., Zheng, W., Zhao, J., Guo, M., Chen, C., He, Z., et al. (2020) · Cell & Bioscience · doi:10.1186/s13578-020-00484-2 · Cited by 16

Profiling MAP kinase cysteines for targeted covalent inhibitor design

Liu, R., Verma, N., Henderson, J. A., Zhan, S., & Shen, J. (2021) · RSC Medicinal Chemistry · doi:10.1039/d1md00277e · Cited by 16

Administration of antenatal glucocorticoids and postnatal surfactant ameliorates respiratory distress syndrome–associated neonatal lethality in Erk3−/− mouse pups

Guamán, M. C., Sbrana, E., Shope, C. D., Showalter, L., Hu, M., Meloche, S., & Aagaard, K. M. (2014) · Pediatric Research · doi:10.1038/pr.2014.54 · Cited by 16

Visualization of the spatial and temporal dynamics of MAPK signaling using fluorescence imaging techniques

Tomida, T. (2014) · The Journal of Physiological Sciences · doi:10.1007/s12576-014-0332-9 · Cited by 17

Erythrocyte mitogen-activated protein kinases mediate hemolytic events under osmotic and oxidative stress and in hemolytic diseases

Hazegh, K. E., Fang, F., Kelly, K. K., Sinchar, D. J., Wang, L., Zuchelkowski, B. E., Ufelle, A. C., Esparza, O., Davizon‐Castillo, P., Page, G. P., et al. (2022) · Cellular Signalling · doi:10.1016/j.cellsig.2022.110450 · Cited by 15

A Novel Protein Kinase from the Ciliate Euplotes raikovi with Close Structural Identity to the Mammalian Intestinal and Male-Germ Cell Kinases: Characterization and Functional Implications in the Autocrine Pheromone Signaling Loop

Vallesi, A., Pretoro, B. D., Ballarini, P., Apone, F., & Luporini, P. (2010) · Protist · doi:10.1016/j.protis.2009.12.002 · Cited by 15

The relationship between KRAS gene mutations and HLA class I antigen downregulation in the metastasis of non-small cell lung cancer

He, X., Song, F.-J., Liu, X., Wang, Z., Li, X., Liu, F., Chen, G., & Jiang, W. (2013) · Journal of International Medical Research · doi:10.1177/0300060513489801 · Cited by 15

Tcf7l1 Acts as a Suppressor for the Self-Renewal of Liver Cancer Stem Cells and Is Regulated by IGF/MEK/ERK Signaling Independent of β-Catenin

Shan, J., Shen, J., Wu, M. C., Zhou, H., Feng, J., Yao, C., Yang, Z., Ma, Q., Luo, Y., Wang, Y., et al. (2019) · Stem Cells · doi:10.1002/stem.3063 · Cited by 14

Biochemical, cellular and structural characterization of novel and selective ERK3 inhibitors

Grädler, U., Busch, M., Leuthner, B., Raba, M., Burgdorf, L. T., Lehmann, M., Linde, N., & Esdar, C. (2020) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2020.127551 · Cited by 15

Experimental evidence of MAP kinase gene expression on the response of intestinal anti-inflammatory drugs

Quaglio, A. E. V., Castilho, A. C. S., & Stasi, L. C. D. (2015) · Life Sciences · doi:10.1016/j.lfs.2015.06.012 · Cited by 15

Special Issue: MAPK Signaling Cascades in Human Health and Diseases

Seger, R. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms252011226 · Cited by 14

The atypical MAPK ERK 3 controls positive selection of thymocytes

Sirois, J., Daudelin, J., Boulet, S., Marquis, M., Meloche, S., & Labrecque, N. (2014) · Immunology · doi:10.1111/imm.12433 · Cited by 14

The Catalytic Activity of the Mitogen-Activated Protein Kinase Extracellular Signal-Regulated Kinase 3 Is Required To Sustain CD4+ CD8+ Thymocyte Survival

Marquis, M., Daudelin, J., Boulet, S., Sirois, J., Crain, K., Mathien, S., Turgeon, B., Rousseau, J., Meloche, S., & Labrecque, N. (2014) · Molecular and Cellular Biology · doi:10.1128/mcb.01701-13 · Cited by 14

Structure Prediction and Validation of the ERK8 Kinase Domain

Strambi, A., Mori, M., Rossi, M., Colecchia, D., Manetti, F., Carlomagno, F., Botta, M., & Chiariello, M. (2013) · PLoS ONE · doi:10.1371/journal.pone.0052011 · Cited by 14

Coordinated control of adiposity and growth by anti-anabolic kinase ERK7

Hasygar, K., Deniz, O., Liu, Y., Gullmets, J., Hynynen, R., Ruhanen, H., Kokki, K., Käkelä, R., & Hietakangas, V. (2020) · EMBO Reports · doi:10.15252/embr.201949602 · Cited by 14

Papel de las proteínas quinasas activadas por mitógenos (MAPK) en el carcinoma de células renales esporádico

Sánchez, A. S. S., Bachs, J. M. G., Serrano‐Oviedo, L., Cha, S. H. N., & Sánchez‐Prieto, R. (2012) · Actas Urológicas Españolas · doi:10.1016/j.acuro.2011.07.013 · Cited by 14

Gut instinct: harnessing the power of probiotics to tame pathogenic signaling pathways in ulcerative colitis

Hsu, C., Mustafa, M. A., Omar, T. M., Taher, S. G., Ubaid, M., Gilmanova, N. S., Abdulraheem, M. N., Saadh, M. J., Athab, A. H., Mirzaei, R., et al. (2024) · Frontiers in Medicine · doi:10.3389/fmed.2024.1396789 · Cited by 14

Redox‐sensitive signaling pathways in renal cell carcinoma

Cruz‐Gregorio, A., Aranda‐Rivera, A. K., Pedraza‐Chaverrí, J., Solano, J. D., & Ibarra‐Rubio, M. E. (2021) · BioFactors · doi:10.1002/biof.1784 · Cited by 12

Regulation of MAPK Signaling Pathways by the Large HERC Ubiquitin Ligases

Sala-Gaston, J., Costa‑Sastre, L., Pedrazza, L., Martinez-Martinez, A., Ventura, F., & Rosa, J. L. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24054906 · Cited by 13

L290P/V mutations increase ERK3’s cytoplasmic localization and migration/invasion-promoting capability in cancer cells

Alsaran, H., Elkhadragy, L., Shakya, A., & Long, W. (2017) · Scientific Reports · doi:10.1038/s41598-017-15135-9 · Cited by 13

Changes of vitamin D receptors (VDR) and MAPK activation in cytoplasmic and nuclear fractions following exposure to cigarette smoke with or without filter in rats

Okrit, F., Chantranuwatana, P., Werawatganon, D., Chayanupatkul, M., & Sanguanrungsirikul, S. (2021) · Heliyon · doi:10.1016/j.heliyon.2021.e05927 · Cited by 15

ERK3 is transcriptionally upregulated by ∆Np63α and mediates the role of ∆Np63α in suppressing cell migration in non-melanoma skin cancers

Alshammari, E. S., Aljagthmi, A. A., Stacy, A. J., Bottomley, M., Shamma, H. N., Kadakia, M., & Long, W. (2021) · BMC Cancer · doi:10.1186/s12885-021-07866-w · Cited by 13

Anti-inflammatory effect of Piper longum L. fruit methanolic extract on lipopolysaccharide-treated RAW 264.7 murine macrophages

Phan, U. T. T., Nguyen, H. D., Nguyen, T. K. O., Tran, T. H., Hương, L. T., & Tran, T. T. P. (2024) · Heliyon · doi:10.1016/j.heliyon.2024.e26174 · Cited by 17

Extracellular-signal regulated kinase 8 of Trypanosoma brucei uniquely phosphorylates its proliferating cell nuclear antigen homolog and reveals exploitable properties

Valenciano, A. L., Knudsen, G. M., & Mackey, Z. B. (2016) · Cell Cycle · doi:10.1080/15384101.2016.1222340 · Cited by 12

Modulation of Bovine Endometrial Cell Receptors and Signaling Pathways as a Nanotherapeutic Exploration against Dairy Cow Postpartum Endometritis

Oladejo, A. O., Li, Y.-J., Wu, X.-H., Imam, B. H., Yang, J., Ma, X., Yan, Z.-T., & Wang, S.-Y. (2021) · Animals · doi:10.3390/ani11061516 · Cited by 12

Pyrido[2,3-d]pyrimidine-2,4(1H,3H)-dione derivatives as RAF-MEK-ERK pathway signaling pathway blockers: Synthesis, cytotoxic activity, mechanistic investigation and structure-activity relationships

Xie, Q., Shen, Y., Meng, Y., Liang, J., Xu, J., Liang, S., Liu, X., Wang, Y., & Hu, C. (2022) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2022.114579 · Cited by 11

MAPK4 predicts poor prognosis and facilitates the proliferation and migration of glioma through the AKT / mTOR pathway

Ren, J., Zheng, S., Zhang, L., Liu, J., Cao, H., Wu, S., Xu, Y., & Sun, J. (2023) · Cancer Medicine · doi:10.1002/cam4.5859 · Cited by 11

Paraquat-Induced Oxidative Stress and Lung Inflammation

Tyagi, N., & Singh, R. (2019) · Springer eBooks · doi:10.1007/978-981-32-9366-3_11 · Cited by 11

Evolution of mitogen-activated protein kinase family and their immune function in Apostichopus japonicus

Wu, Y., Zhao, X., Xiang, Y., Guo, M. H., & Li, C. (2022) · Developmental & Comparative Immunology · doi:10.1016/j.dci.2022.104586 · Cited by 11

MAPK family genes' influences on myogenesis in cattle: Genome-wide analysis and identification

Li, B., Wang, J., Raza, S. H. A., Wang, S., Liang, C., Zhang, W., Yu, S., Shah, M. A., Abdulmonem, W. A., Alharbi, Y. M., et al. (2023) · Research in Veterinary Science · doi:10.1016/j.rvsc.2023.04.024 · Cited by 11

MAPK4 silencing together with a PARP1 inhibitor as a combination therapy in triple‑negative breast cancer cells

Zeng, X., Jiang, S., Ruan, S., Guo, Z., Guo, J., Liu, M., Ye, C., & Dong, J. (2021) · Molecular Medicine Reports · doi:10.3892/mmr.2021.12187 · Cited by 11

EhMAPK, the Mitogen-Activated Protein Kinase from Entamoeba histolytica Is Associated with Cell Survival

Ghosh, A. S., Ray, D., Dutta, S., & Raha, S. (2010) · PLoS ONE · doi:10.1371/journal.pone.0013291 · Cited by 11

Inhibiting TRIM8 alleviates adipocyte inflammation and insulin resistance by regulating the DUSP14/MAPKs pathway

Zhu, M., Pu, J., Zhang, T., Shao, H., Su, R., & Tang, C. (2024) · Adipocyte · doi:10.1080/21623945.2024.2381262 · Cited by 10

Accelerating rejection-based simulation of biochemical reactions with bounded acceptance probability

Thanh, V. H., Priami, C., & Zunino, R. (2016) · The Journal of Chemical Physics · doi:10.1063/1.4953559 · Cited by 10

Role of mitogen-activated protein kinase (MAPK) in the sporadic renal cell carcinoma

Sánchez, A. S. S., Bachs, J. M. G., Serrano‐Oviedo, L., Cha, S. H. N., & Sánchez‐Prieto, R. (2012) · Actas Urológicas Españolas (English Edition) · doi:10.1016/j.acuroe.2012.04.009 · Cited by 10

Identification and functional analysis of a stress-responsive MAPK15 in Entamoeba invadens

Singh, T., Agarwal, T., & Ghosh, S. K. (2018) · Molecular and Biochemical Parasitology · doi:10.1016/j.molbiopara.2018.05.002 · Cited by 9

Crystal Structure and Inhibitor Identifications Reveal Targeting Opportunity for the Atypical MAPK Kinase ERK3

Schröder, M., Filippakopoulos, P., Schwalm, M. P., Alamillo‐Ferrer, C., Drewry, D. H., Knapp, S., & Chaikuad, A. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21217953 · Cited by 8

Genome-wide evolution of MAPKs family and their expression in response to bacterial infection in seahorse Hippocampus erectus

Wang, K., Wang, X., Zou, Q., Jiang, H., Zhang, R., Tian, Y., Zhang, L., & Lin, Q. (2021) · Journal of Oceanology and Limnology · doi:10.1007/s00343-020-0332-y · Cited by 9

In silico identification and characterization of the MAPK family members of unicellular model eukaryote Tetrahymena thermophila

Yıldız, M. T., & Arslanyolu, M. (2014) · European Journal of Protistology · doi:10.1016/j.ejop.2014.08.005 · Cited by 9

Linear motif specificity in signaling through p38α and ERK2 mitogen–activated protein kinases

Robles, J. T., Lou, H. J., Shi, G., Pan, P. L., & Turk, B. E. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2316599120 · Cited by 9

Mitogen-Activated Protein Kinases (MAPK) in Cancer

Cuenda, A. (2018) · Elsevier eBooks · doi:10.1016/b978-0-12-801238-3.64980-2 · Cited by 8

The non-linearity of RAF-MEK signaling in dendritic cells

Riegel, K., & Rajalingam, K. (2020) · Cell Cycle · doi:10.1080/15384101.2020.1795990 · Cited by 8

Allicin regulates Treg/Th17 balance in mice with collagen‐induced arthritis by increasing the expression of MEKK2 protein

Zhang, Y., & Gong, Y. (2021) · Food Science & Nutrition · doi:10.1002/fsn3.2034 · Cited by 8

Exploration of the shared pathways and common biomarker PAN3 in ankylosing spondylitis and ulcerative colitis using integrated bioinformatics analysis

Zhang, M., Zhou, J., Wang, H., Le, H., Wang, J., Yang, X., & Zhong, X. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1089622 · Cited by 8

Silencing MAP3K1 expression inhibits the proliferation of goat hair follicle stem cells

Ma, J., Wang, J., Feng, Y., Zhang, L., Hu, H., Wang, Q., Chu, C., Qu, J., Wang, Y., & Li, Y. (2021) · In Vitro Cellular & Developmental Biology - Animal · doi:10.1007/s11626-021-00557-7 · Cited by 7

An atypical MAPK regulates translocation of a GATA transcription factor in response to chemoattractant stimulation

Hadwiger, J. A., Cai, H., Aranda, R. G., & Fatima, S. (2022) · Journal of Cell Science · doi:10.1242/jcs.260148 · Cited by 7

Phosphoproteomic analysis identifies supervillin as an ERK3 substrate regulating cytokinesis and cell ploidy

Javary, J., Goupil, E., Soulez, M., Kanshin, E., Bouchard, A., Seternes, O. M., Thibault, P., Labbé, J., & Meloche, S. (2022) · Journal of Cellular Physiology · doi:10.1002/jcp.30938 · Cited by 7

Atypical MAP kinases – new insights and directions from amoeba

Hadwiger, J. A., Aranda, R. G., & Fatima, S. (2023) · Journal of Cell Science · doi:10.1242/jcs.261447 · Cited by 7

Mitogen-Activated Protein Kinase Family

Teramoto, H., & Gutkind, J. S. (2013) · Encyclopedia of Biological Chemistry · doi:10.1016/b978-0-12-378630-2.00362-5 · Cited by 7

Mitogen-Activated Protein (MAP) Kinase Pathways: Regulation and Physiological Functions*

Pearson, G. W., Robinson, F. L., Gibson, T. B., Xu, B.-E., Karandikar, M. S., Berman, K. S., & Cobb, M. H. (2001) · Endocrine Reviews · doi:10.1210/edrv.22.2.0428 · Cited by 4,111

Protein Function | Mitogen-Activated Protein Kinase Family

Teramoto, H., & Gutkind, J. S. (2013) · Elsevier eBooks · doi:10.1016/b978-0-12-819460-7.00594-6

Activation and function of the MAPKs and their substrates, the MAPK-activated protein kinases

Cargnello, M., & Roux, P. P. (2011) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00031-10 · Cited by 3,274

Atypical MAPK s in cancer

Dahm, K., Vijayarangakannan, P., Wollscheid, H.-P., Schild, H., & Rajalingam, K. (2024) · FEBS Journal · doi:10.1111/febs.17283 · Cited by 11