Phosphatase‐mediated crosstalk between MAPK signaling pathways in the regulation of cell survival

Mutations of the BRAF gene in human cancer

Davies, H., Bignell, G. R., Cox, C., Stephens, P., Edkins, S., Clegg, S., Teague, J., Woffendin, H., Garnett, M. J., Bottomley, W., et al. (2002) · Nature · doi:10.1038/nature00766 · Cited by 10,674

Opposing Effects of ERK and JNK-p38 MAP Kinases on Apoptosis

Xia, Z., Dickens, M., Raingeaud, J., Davis, R. J., & Greenberg, M. E. (1995) · Science · doi:10.1126/science.270.5240.1326 · Cited by 5,273

Signal transduction by the JNK group of MAP kinases

Davis, R. J. (2000) · Cell · doi:10.1016/s0092-8674(00)00116-1 · Cited by 4,237

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

AP-1 as a regulator of cell life and death

Shaulian, E., & Karin, M. (2002) · Nature Cell Biology · doi:10.1038/ncb0502-e131 · Cited by 2,961 · cited 1×

Protein kinases and phosphatases: The Yin and Yang of protein phosphorylation and signaling

Hunter, T. R. (1995) · Cell · doi:10.1016/0092-8674(95)90405-0 · Cited by 2,961

Targeting the Raf-MEK-ERK mitogen-activated protein kinase cascade for the treatment of cancer

Roberts, P. J., & Der, C. J. (2007) · Oncogene · doi:10.1038/sj.onc.1210422 · Cited by 2,788

ERK and p38 MAPK-Activated Protein Kinases: a Family of Protein Kinases with Diverse Biological Functions

Roux, P. P., & Blenis, J. (2004) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.68.2.320-344.2004 · Cited by 2,540

Pro-inflammatory Cytokines and Environmental Stress Cause p38 Mitogen-activated Protein Kinase Activation by Dual Phosphorylation on Tyrosine and Threonine

Raingeaud, J., Gupta, S., Rogers, J. S., Dickens, M., Han, J., Ulevitch, R. J., & Davis, R. J. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.13.7420 · Cited by 2,244

Anisomycin induces glioma cell death via down-regulation of PP2A catalytic subunit in vitro

Li, J., Huang, J., Li, M., Zhang, H., Xing, B., Chen, G., Wei, D., Gu, P., & Hu, W. (2012) · Acta Pharmacologica Sinica · doi:10.1038/aps.2012.46 · Cited by 35

Ultrasonic Bioreactor as a Platform for Studying Cellular Response

Subramanian, A., Turner, J. A., Budhiraja, G., Thakurta, S. G., Whitney, N. P., & Nudurupati, S. S. (2012) · Tissue Engineering Part C Methods · doi:10.1089/ten.tec.2012.0199 · Cited by 34

Driven to Death: Inhibition of Farnesylation Increases Ras Activity and Promotes Growth Arrest and Cell Death

Geryk-Hall, M., Yang, Y., & Hughes, D. P. M. (2010) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-09-0833 · Cited by 34

Evaluation of long-term biocompatibility and osteogenic differentiation of graphene nanosheet doped calcium phosphate-chitosan AZ91D composites

Zhao, M., Dai, Y., Li, X., Yang, L., Zhang, Y., Wu, H., Wen, Z., & Dai, C. (2018) · Materials Science and Engineering C · doi:10.1016/j.msec.2018.04.082 · Cited by 36

Inhibition of Myocardial Cell Apoptosis Is Important Mechanism for Ginsenoside in the Limitation of Myocardial Ischemia/Reperfusion Injury

Chen, Z., Wu, J., Li, S., Liu, C., & Ren, Y. (2022) · Frontiers in Pharmacology · doi:10.3389/fphar.2022.806216 · Cited by 34

Mitigation of radiation-induced hematopoietic injury via regulation of cellular MAPK/phosphatase levels and increasing hematopoietic stem cells

Patwardhan, R. S., Sharma, D., Checker, R., & Sandur, S. K. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.11.004 · Cited by 34

Unfertilized Xenopus Eggs Die by Bad-Dependent Apoptosis under the Control of Cdk1 and JNK

Pasquier, D. D., Dupré, A., & Jessus, C. (2011) · PLoS ONE · doi:10.1371/journal.pone.0023672 · Cited by 34

S100A8/A9 Stimulates Keratinocyte Proliferation in the Development of Squamous Cell Carcinoma of the Skin via the Receptor for Advanced Glycation-End Products

Iotzova-Weiss, G., Dziunycz, P., Freiberger, S. N., Läuchli, S., Hafner, J., Vogl, T., French, L. E., & Hofbauer, G. F. L. (2015) · PLoS ONE · doi:10.1371/journal.pone.0120971 · Cited by 34

Silymarin Attenuates Airway Inflammation Induced by Cigarette Smoke in Mice

Li, D., Xu, D., Wang, T., Shen, Y., Guo, S., Zhang, X., Guo, L., Li, X., Liu, L., & Wen, F. (2014) · Inflammation · doi:10.1007/s10753-014-9996-9 · Cited by 34

The genome-wide identification of mitogen-activated protein kinase kinase (MKK) genes in Yesso scallop Patinopecten yessoensis and their expression responses to bacteria challenges

Zou, J., Wang, R., Li, R., Kong, Y., Wang, J., Ning, X., Zhang, L., Wang, S., Hu, X., & Bao, Z. (2015) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2015.06.006 · Cited by 34

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Gao, F., Zhao, Y., Shi, X., Qiao, D., Pei, C., & Kong, X. (2024) · Reviews in Aquaculture · doi:10.1111/raq.12895 · Cited by 34

Resveratrol as an adjunct therapy in cyclophosphamide‐treated MCF‐7 cells and breast tumor explants

Singh, N., Nigam, M., Ranjan, V., Zaidi, D., Garg, V. K., Sharma, S., Chaturvedi, R., Shankar, R., Kumar, S., Sharma, R., et al. (2011) · Cancer Science · doi:10.1111/j.1349-7006.2011.01893.x · Cited by 33

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Gao, J., Yan, Q., Liu, S., & Yang, X. (2014) · PLoS ONE · doi:10.1371/journal.pone.0102590 · Cited by 33

Short and long access to cocaine self-administration activates tyrosine phosphatase STEP and attenuates GluN expression but differentially regulates GluA expression in the prefrontal cortex

Sun, W., Zelek-Molik, A., & McGinty, J. F. (2013) · Psychopharmacology · doi:10.1007/s00213-013-3118-5 · Cited by 34

Deep-Sequencing Analysis of the Mouse Transcriptome Response to Infection with Brucella melitensis Strains of Differing Virulence

Wang, F., Hu, S., Liu, W., Qiao, Z., Gao, Y., & Bu, Z. (2011) · PLoS ONE · doi:10.1371/journal.pone.0028485 · Cited by 33

Triggering of p38 MAPK and JNK Signaling is Important for Oleanolic Acid‐Induced Apoptosis via the Mitochondrial Death Pathway in Hypertrophic Scar Fibroblasts

Chen, J., Zhang, L., Zhang, H., Su, L., & Qin, L. (2014) · Phytotherapy Research · doi:10.1002/ptr.5150 · Cited by 33

Functional heterogeneity of osteocytes in FGF23 production: the possible involvement of DMP1 as a direct negative regulator

Lee, J., Yamaguchi, A., & Iimura, T. (2014) · BoneKEy Reports · doi:10.1038/bonekey.2014.38 · Cited by 33

Orexin A upregulates the protein expression of OX1R and enhances the proliferation of SGC-7901 gastric cancer cells through the ERK signaling pathway

Liu, Y., Zhao, Y., JU, S., & Guo, L. (2014) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2014.2038 · Cited by 33

A chemical biology approach identifies AMPK as a modulator of melanoma oncogene MITF

Borgdorff, V., Rix, U., Winter, G. E., Gridling, M., Müller, A. C., Breitwieser, F. P., Wagner, C., Colinge, J., Bennett, K. L., Superti‐Furga, G., et al. (2013) · Oncogene · doi:10.1038/onc.2013.185 · Cited by 32

Isolation and Characterization of Chondroitin Sulfates from Sturgeon (Acipenser sinensis) and Their Effects on Growth of Fibroblasts

Im, A., Park, Y., & Kim, Y. S. (2010) · Biological and Pharmaceutical Bulletin · doi:10.1248/bpb.33.1268 · Cited by 32

Lack of REDD1 reduces whole body glucose and insulin tolerance, and impairs skeletal muscle insulin signaling

Dungan, C. M., Wright, D. C., & Williamson, D. L. (2014) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2014.10.032 · Cited by 35

Fruiting-Body Development in Ascomycetes

Pöggeler, S., Nowrousian, M., Teichert, I., Beier, A., & Kück, U. (2018) · Springer eBooks · doi:10.1007/978-3-319-71740-1_1 · Cited by 37

Microcystin‐LR induces cytotoxicity and affects carp immune cells by impairment of their phagocytosis and the organization of the cytoskeleton

Rymuszka, A. (2012) · Journal of Applied Toxicology · doi:10.1002/jat.2791 · Cited by 32

Peroxynitrite-induced p38 MAPK pro-apoptotic signaling in enterocytes

Guner, Y. S., Ochoa, C. J., Wang, J., Zhang, X., Steinhauser, S., Stephenson, L., Grishin, A., & Upperman, J. S. (2009) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2009.04.091 · Cited by 32

Kinases and phosphatases in ischaemic preconditioning: a re-evaluation

Fan, W. J., van Vuuren, D., Genade, S., & Lochner, A. (2010) · Basic Research in Cardiology · doi:10.1007/s00395-010-0086-3 · Cited by 32

Dual specificity phosphatase 6 as a predictor of invasiveness in papillary thyroid cancer

Lee, J. U., Huang, S., Lee, M. H., Lee, S. E., Ryu, M. J., Kim, S. J., Kim, Y. K., Kim, S. Y., Joung, K. H., Kim, J., et al. (2012) · European Journal of Endocrinology · doi:10.1530/eje-12-0010 · Cited by 34

Mitogen-Activated Protein Kinase: A Potent Signaling Protein that Combats Biotic and Abiotic Stress in Plants

Khan, A. R., Shah, S. T., Basıt, A., Mohamed, H. I., & Li, Y. (2024) · Journal of Plant Growth Regulation · doi:10.1007/s00344-024-11239-5 · Cited by 33

Hepatic response to oxidative injury in long‐lived Ames dwarf mice

Sun, L. Y., Bokov, A. F., Richardson, A. G., & Miller, R. A. (2010) · The FASEB Journal · doi:10.1096/fj.10-164376 · Cited by 31

Overexpression of Transforming Growth Factor β1 in Malignant Prostate Cells is Partly Caused by a Runaway of TGF-β1 Auto-induction Mediated Through a Defective Recruitment of Protein Phosphatase 2A by TGF-β Type I Receptor

Yu, N., Kozlowski, J. M., Park, I. I., Chen, L., Zhang, Q., Xu, D., Doll, J. A., Crawford, S. E., Brendler, C. B., & Lee, C. (2010) · Urology · doi:10.1016/j.urology.2010.03.061 · Cited by 31

NPM1 Silencing Reduces Tumour Growth and MAPK Signalling in Prostate Cancer Cells

Loubeau, G., Boudra, R., Maquaire, S., Lours-Calet, C., Beaudoin, C., Verrelle, P., & Morel, L. (2014) · PLoS ONE · doi:10.1371/journal.pone.0096293 · Cited by 31

Regulation of JNK activity in the apoptotic response of intestinal epithelial cells

Ray, R. M., Jin, S. K., Bavaria, M. N., & Johnson, L. R. (2011) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00405.2010 · Cited by 31

The ERK 1 / 2 Inhibitor U0126 Attenuates Diabetes-Induced Upregulation of MMP-9 and Biomarkers of Inflammation in the Retina

Mohammad, G., Siddiquei, M. M., Nawaz, M. I., & El‐Asrar, A. M. A. (2013) · Journal of Diabetes Research · doi:10.1155/2013/658548 · Cited by 31

Increased activity of mitogen activated protein kinase pathway in flotillin-2 knockout mouse model

Banning, A., Regenbrecht, C. R. A., & Tikkanen, R. (2013) · Cellular Signalling · doi:10.1016/j.cellsig.2013.11.001 · Cited by 31

Prohibitin-1 deficiency promotes inflammation and increases sensitivity to liver injury

Sánchez‐Quiles, V., Segura, V., Bigaud, E., He, B., O’Malley, B. W., Santamaría, E., Prìeto, J., & Corrales, F. J. (2012) · Journal of Proteomics · doi:10.1016/j.jprot.2012.08.009 · Cited by 30

Opposing effects of ERK and p38‐JNK MAP kinase pathways on formation of prions in GT1‐1 cells

Nordström, E. K., Fisone, G., & Kristensson, K. (2008) · The FASEB Journal · doi:10.1096/fj.08-115360 · Cited by 31

The PP2C Alphabet Is a Negative Regulator of Stress-Activated Protein Kinase Signaling in Drosophila

Baril, C., Sahmi, M., Ashton‐Beaucage, D., Stronach, B. E., & Therrien, M. (2008) · Genetics · doi:10.1534/genetics.108.096461 · Cited by 32

Molecular insight into the viral biology and clinical features of trichodysplasia spinulosa

Wu, J. H., Nguyen, H. P., Rady, P. L., & Tyring, S. K. (2015) · British Journal of Dermatology · doi:10.1111/bjd.14239 · Cited by 31

Combined targeting of Arf1 and Ras potentiates anticancer activity for prostate cancer therapeutics

Lang, L., Shay, C., Zhao, X., & Teng, Y. (2017) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-017-0583-4 · Cited by 31

Bufalin inhibits gefitinib resistant NCI-H460 human lung cancer cell migration and invasion in vitro

Huang, A., Yang, M., Hsiao, Y.-T., Lin, T.-S., Ma, Y., Peng, S., Hsia, T., Cheng, Y., Kuo, C., & Chung, J. (2016) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2016.11.004 · Cited by 30

Inflammatory but not mitogenic contexts prime synovial fibroblasts for compensatory signaling responses to p38 inhibition

Jones, D. S., Jenney, A., Joughin, B. A., Sorger, P. K., & Lauffenburger, D. A. (2018) · Science Signaling · doi:10.1126/scisignal.aal1601 · Cited by 30

Amoebiasis in the Tropics: Epidemiology and Pathogenesis

Samie, A., ElBakri, A. M. K., & AbuOdeh, R. (2012) · InTech eBooks · doi:10.5772/26810 · Cited by 30

Molecular mechanisms underlying the pro-inflammatory synergistic effect of tumor necrosis factor α and interferon γ in human microvascular endothelium

Lombardi, A., Cantini, G., Mello, T., Francalanci, M., Gelmini, S., Cosmi, L., Santarlasci, V., Degl’Innocenti, S., Luciani, P., Deledda, C., et al. (2009) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2009.07.004 · Cited by 30

Manganese modulation of MAPK pathways: effects on upstream mitogen activated protein kinase kinases and mitogen activated kinase phosphatase‐1 in microglial cells

Crittenden, P. L., & Filipov, N. M. (2010) · Journal of Applied Toxicology · doi:10.1002/jat.1552 · Cited by 30

PIK3CA mutations are frequently observed in BRCAX but not BRCA2-associated male breast cancer

Deb, S., Do, H., Byrne, D. J., Jene, N., kConFab Investigators, Dobrovic, A., & Fox, S. B. (2013) · Breast Cancer Research · doi:10.1186/bcr3463 · Cited by 30

DNA damage dependent activation of checkpoint kinase-1 and mitogen-activated protein kinase-p38 are required in malabaricone C-induced mitochondrial cell death

Tyagi, M., Bhattacharyya, R., Bauri, A. K., Patro, B. S., & Chattopadhyay, S. (2013) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2013.11.020 · Cited by 30

Caecal transcriptome analysis of colonized and non‐colonized chickens within two genetic lines that differ in caecal colonization by Campylobacter jejuni

Li, X. Y., Swaggerty, C. L., Kogut, M. H., Chiang, H., Wang, Y., Genovese, K. J., He, H., Pevzner, I. Y., & Zhou, H. J. (2011) · Animal Genetics · doi:10.1111/j.1365-2052.2010.02168.x · Cited by 30

Sphingosine kinase inhibitors decrease viability and induce cell death in natural killer-large granular lymphocyte leukemia

LeBlanc, F., Liu, X., Hengst, J. A., Fox, T. E., Calvert, V. S., Petricoin, E. F., Yun, J. K., Feith, D. J., & Loughran, T. P. (2015) · Cancer Biology & Therapy · doi:10.1080/15384047.2015.1078949 · Cited by 31

Nitric oxide and calcium signaling regulate myocardial tumor necrosis factor-α expression and cardiac function in sepsisThis article is one of a selection of papers published in this special issue on Calcium Signaling.

Zhang, T., & Feng, Q. (2010) · Canadian Journal of Physiology and Pharmacology · doi:10.1139/y09-097 · Cited by 30

MDA-7/IL-24 inhibits Nrf2-mediated antioxidant response through activation of p38 pathway and inhibition of ERK pathway involved in cancer cell apoptosis

Tian, H., Zhang, D., Gao, Z., Li, H., Zhang, B., Zhang, Q., Li, L., Cheng, Q., Pei, D., & Zheng, J. (2014) · Cancer Gene Therapy · doi:10.1038/cgt.2014.45 · Cited by 29

Kaempferol induces chondrogenesis in ATDC5 cells through activation of ERK/BMP-2 signaling pathway

Nepal, M. K., Li, L., Cho, H. K., Park, J. K., & Soh, Y. (2013) · Food and Chemical Toxicology · doi:10.1016/j.fct.2013.08.034 · Cited by 29

TAK1 regulates hepatic lipid homeostasis through SREBP

Morioka, S., Sai, K., Omori, E., Ikeda, Y., Matsumoto, K., & Ninomiya‐Tsuji, J. (2016) · Oncogene · doi:10.1038/onc.2015.453 · Cited by 31

p38 MAPK Activity Is Required to Prevent Hyperactivation of NLRP3 Inflammasome

Shin, J. N., Rao, L., Sha, Y., Fattah, E. A., Hyser, J. M., & Eissa, N. T. (2021) · The Journal of Immunology · doi:10.4049/jimmunol.2000416 · Cited by 32

Galectin-9 accelerates transforming growth factor β3-induced differentiation of human mesenchymal stem cells to chondrocytes

Arikawa, T., Matsukawa, A., Watanabe, K., Sakata, K.-M., Seki, M., Nagayama, M., Takeshita, K., Ito, K., Niki, T., Oomizu, S., et al. (2009) · Bone · doi:10.1016/j.bone.2009.01.365 · Cited by 29

p16 INK4A inhibits the pro-metastatic potentials of osteosarcoma cells through targeting the ERK pathway and TGF-β1

Silva, G. P. D. L., & Aboussekhra, A. (2015) · Molecular Carcinogenesis · doi:10.1002/mc.22299 · Cited by 31

Inhibition of the TNF-α^|^ndash;Induced Serine Phosphorylation of IRS-1 at 636/639 by AICAR

Shibata, T., Takaguri, A., Ichihara, K., & Satoh, K. (2013) · Journal of Pharmacological Sciences · doi:10.1254/jphs.12270fp · Cited by 28

Deciphering the mechanistic impact of acupuncture on the neurovascular unit in acute ischemic stroke: Insights from basic research in a narrative review

Jiang, H., Zhang, C., Lin, M., Yin, Y., Deng, S., Liu, W., Zhuo, B., Tian, G., Du, Y., & Meng, Z. (2024) · Ageing Research Reviews · doi:10.1016/j.arr.2024.102536 · Cited by 32

Reprogramming the oncogenic response: SET protein as a potential therapeutic target in cancer

Hung, M., & Chen, K. (2017) · Expert Opinion on Therapeutic Targets · doi:10.1080/14728222.2017.1336226 · Cited by 29

An improved Erk biosensor detects oscillatory Erk dynamics driven by mitotic erasure during early development

Wilcockson, S. G., Guglielmi, L., Rodriguez, P. A., Amoyel, M., & Hill, C. S. (2023) · Developmental Cell · doi:10.1016/j.devcel.2023.08.021 · Cited by 28

Sorafenib and pemetrexed toxicity in cancer cells is mediated via SRC-ERK signaling

Bareford, M. D., Hamed, H. A., Allegood, J. C., Cruickshanks, N. A., Poklepovic, A. S., Park, M. A., Öğretmen, B., Spiegel, S., Grant, S., & Dent, P. (2012) · Cancer Biology & Therapy · doi:10.4161/cbt.20562 · Cited by 28

Astragaloside IV Attenuates Glutamate-Induced Neurotoxicity in PC12 Cells through Raf-MEK-ERK Pathway

Yue, R., Li, X., Chen, B., Zhao, J., He, W., Hu, Y., Xing, Y., Gao, N., Wu, G., Jin, H., et al. (2015) · PLoS ONE · doi:10.1371/journal.pone.0126603 · Cited by 28

MAP Kinase cross talks in oxidative stress‐induced impairment of insulin secretion. Involvement in the protective activity of quercetin

Youl, E., Magous, R., Cros, G. H., & Oiry, C. (2014) · Fundamental and Clinical Pharmacology · doi:10.1111/fcp.12078 · Cited by 28

A Novel Class of Hsp90 C-Terminal Modulators Have Pre-Clinical Efficacy in Prostate Tumor Cells Without Induction of a Heat Shock Response

Armstrong, H., Koay, Y. C., Irani, S., Das, R., Nassar, Z. D., BioResource, T. A. P. C., Selth, L. A., Centenera, M. M., McAlpine, S. R., & Butler, L. M. (2016) · The Prostate · doi:10.1002/pros.23239 · Cited by 28

Cytisine induces endoplasmic reticulum stress caused by calcium overload in HepG2 cells

Yu, L., Jiang, B., Chen, Z., Wang, X., Shang, D., Zhang, X., Sun, Y., Yang, J., & Yu-bin, J. (2018) · Oncology Reports · doi:10.3892/or.2018.6200 · Cited by 28

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Peris, I., Romero-Murillo, S., Vicente, C., Narla, G., & Odero, M. D. (2023) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2023.188953 · Cited by 30

Plasticity of the MAPK Signaling Network in Response to Mechanical Stress

Pereira, A. M., Tudor, C., Pouille, P., Shekhar, S., Kanger, J. S., Subramaniam, V., & Martı́n-Blanco, E. (2014) · PLoS ONE · doi:10.1371/journal.pone.0101963 · Cited by 27

Tristetraprolin and Its Role in Regulation of Airway Inflammation

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Expression of a Homeostatic Regulator, Wip1 (Wild-type p53-induced Phosphatase), Is Temporally Induced by c-Jun and p53 in Response to UV Irradiation

Song, J., Han, H., Sabapathy, K., Lee, B., Yu, E., & Choi, J. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.070003 · Cited by 28

Nitric oxide-donating aspirin inhibits the growth of pancreatic cancer cells through redox-dependent signaling

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Moderate aerobic exercise training decreases middle-aged induced pathologic cardiac hypertrophy by improving Klotho expression, MAPK signaling pathway, and oxidative stress status in Wistar rats.

Baghaiee, B., Karimi, P., Siahkouhian, M., & Pescatello, L. S. (2018) · Europe PMC (PubMed Central) · doi:10.22038/ijbms.2018.29615.7148 · Cited by 27

Microporous density-mediated response of MSCs on 3D trimodal macro/micro/nano-porous scaffolds via fibronectin/integrin and FAK/MAPK signaling pathways

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Isoproterenol-induced beta-2 adrenergic receptor activation negatively regulates interleukin-2 signaling

Ruiz-Medina, B. E., Cadena-Medina, D. A., Esparza, E., Arrieta, A. J., & Kirken, R. A. (2018) · Biochemical Journal · doi:10.1042/bcj20180503 · Cited by 26

Neuroprotective effects of diarylpropionitrile against β-amyloid peptide-induced neurotoxicity in rat cultured cortical neurons

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Critical role of farnesoid X receptor for hepatocellular carcinoma cell proliferation

Fujino, T., Takeuchi, A., Maruko-Ohtake, A., Ohtake, Y., Satoh, J., Kobayashi, T., Tanaka, T., Ito, H., Sakamaki, R., Kashimura, R., et al. (2012) · The Journal of Biochemistry · doi:10.1093/jb/mvs101 · Cited by 26

p38α regulates SERCA2a function

Kaikkonen, L., Magga, J. M., Ronkainen, V., Koivisto, E., Perjés, Á., Chuprun, J. K., Vinge, L. E., Kilpiö, T., Aro, J., Ulvila, J., et al. (2013) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2013.12.005 · Cited by 26

A peptide from Porphyra yezoensis stimulates the proliferation of IEC-6 cells by activating the insulin-like growth factor I receptor signaling pathway

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Recruitment of protein phosphatase 2A to dorsal ruffles by platelet-derived growth factor in smooth muscle cells: Dephosphorylation of Hsp27

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Selective Activation of Intracellular Signalling Pathways in Dendritic Cells for Cancer Immunotherapy

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Microcystin-LR induces a wide variety of biochemical changes in the A549 human non-small cell lung cancer cell line: Roles for protein phosphatase 2A and its substrates

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β-d-glucan from Antrodia Camphorata ameliorates LPS-induced inflammation and ROS production in human hepatocytes

Chen, Q., Tang, H., Zha, Z., Yin, H., Wang, Y., Wang, Y., Li, H., & Yue, L. (2017) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2017.05.191 · Cited by 27

Edaravone is a candidate agent for spinal muscular atrophy: In vitro analysis using a human induced pluripotent stem cells-derived disease model

Ando, S., Funato, M., Ohuchi, K., Kameyama, T., Inagaki, S., Seki, J., Kawase, C., Tsuruma, K., Shimazawa, M., Kaneko, H., et al. (2017) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2017.08.005 · Cited by 27

The ubiquitin ligase HERC1 regulates cell migration via RAF-dependent regulation of MKK3/p38 signaling

Pedrazza, L., Schneider, T., Bartrons, R., Ventura, F., & Rosa, J. L. (2020) · Scientific Reports · doi:10.1038/s41598-020-57756-7 · Cited by 26

The Cell Cycle Checkpoint System MAST(L)-ENSA/ARPP19-PP2A is Targeted by cAMP/PKA and cGMP/PKG in Anucleate Human Platelets

Kumm, E. J., Pagel, O., Gambaryan, S. P., Walter, U., Zahedi, R. P., Smolenski, A., & Jurk, K. (2020) · Cells · doi:10.3390/cells9020472 · Cited by 27

Squamocin modulates histone H3 phosphorylation levels and induces G1 phase arrest and apoptosis in cancer cells

Lee, C. C., Lin, Y., Chang, W.-H., Lin, P., Wu, Y., & Chang, J. G. (2011) · BMC Cancer · doi:10.1186/1471-2407-11-58 · Cited by 26

Anti-Proliferation Activity of Fucoidan in MKN45 Gastric Cancer Cells and Downregulation of Phosphorylated ASK1, a Cell Cycle-Regulated Kinase.

Yoshimoto, M., Higaki, K., Nanba, E., & Ikeguchi, M. (2015) · PubMed Central · Cited by 25

Presenting a New Standard Drug Model for Turmeric and Its Prized Extract, Curcumin

Cavaleri, F. (2018) · International Journal of Inflammation · doi:10.1155/2018/5023429 · Cited by 26

Alisol B 23-Acetate Ameliorates Lipopolysaccharide-Induced Cardiac Dysfunction by Suppressing Toll-Like Receptor 4 (TLR4)/NADPH Oxidase 2 (NOX2) Signaling Pathway

Wang, B., Chen, L., Dai, L., Fang, W., & Wang, H. (2019) · Medical Science Monitor · doi:10.12659/msm.918252 · Cited by 25

BAFF activates Erk1/2 promoting cell proliferation and survival by Ca2+-CaMKII-dependent inhibition of PP2A in normal and neoplastic B-lymphoid cells

Liang, D., Zeng, Q., Xu, Z., Zhang, H., Gui, L., Xu, C., Chen, S., Zhang, S., Huang, S., & Chen, L. (2013) · Biochemical Pharmacology · doi:10.1016/j.bcp.2013.11.006 · Cited by 25

Cochlear protection from acoustic injury by inhibitors of p38 mitogen-activated protein kinase and sequestosome 1 stress protein

Tabuchi, K., Oikawa, K., Hoshino, T., Nishimura, B., Hayashi, K., Yanagawa, T., Warabi, E., Ishii, T., Tanaka, S., & Hara, A. (2009) · Neuroscience · doi:10.1016/j.neuroscience.2009.12.038 · Cited by 25

Evaluation of antimycobacterium activity of the essential oils of cumin (Cuminum cyminum), clove (Eugenia caryophyllata), cinnamon (Cinnamomum verum), laurel (Laurus nobilis) and anis (Pimpinella anisum) against Mycobacterium tuberculosis

Andrade-Ochoa, S., Fabiola, C.-V., Nevárez‐Moorillón, G. V., Rivera-Chavira, B. E., & Hernández-Ochoa, L. R. (2013) · Advances in Biological Chemistry · doi:10.4236/abc.2013.35052 · Cited by 25

DUSP1 Maintains IRF1 and Leads to Increased Expression of IRF1-dependent Genes

Shah, S., King, E. M., Mostafa, M., Altonsy, M. O., & Newton, R. C. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.728964 · Cited by 25

Mathematical modelling unveils the essential role of cellular phosphatases in the inhibition of RAF-MEK-ERK signalling by sorafenib in hepatocellular carcinoma cells

Saidak, Z., Giacobbi, A., Louandre, C., Sauzay, C., Mammeri, Y., & Galmiche, A. (2017) · Cancer Letters · doi:10.1016/j.canlet.2017.01.038 · Cited by 25

P2X7 Nucleotide and EGF Receptors Exert Dual Modulation of the Dual-Specificity Phosphatase 6 (MKP-3) in Granule Neurons and Astrocytes, Contributing to Negative Feedback on ERK Signaling

Queipo, M. J., Gil‐Redondo, J. C., Morente, V., Ortega, F., Miras‐Portugal, M. T., Delicado, E. G., & Pérez‐Sen, R. (2018) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2017.00448 · Cited by 25

OspF directly attenuates the activity of extracellular signal-regulated kinase during invasion by Shigella flexneri in human dendritic cells

Kim, D. W., Chu, H., Joo, D. H., Jang, M. S., Choi, J. H., Park, S., Choi, Y.-J., Han, S. H., & Yun, C. (2008) · Molecular Immunology · doi:10.1016/j.molimm.2008.02.013 · Cited by 25

Inhibition of gap-junctional intercellular communication and activation of mitogen-activated protein kinases by cyanobacterial extracts – Indications of novel tumor-promoting cyanotoxins?

Bláha, L., Babica, P., Hilscherová, K., & Upham, B. L. (2009) · Toxicon · doi:10.1016/j.toxicon.2009.07.009 · Cited by 25

L-DOPA modulates cell viability through the ERK-c-Jun system in PC12 and dopaminergic neuronal cells

Park, K. H., Shin, K. S., Zhao, T., Park, H. J., Lee, K. E., & Lee, M. K. (2015) · Neuropharmacology · doi:10.1016/j.neuropharm.2015.09.006 · Cited by 24

Hirudin promotes angiogenesis by modulating the cross-talk between p38 MAPK and ERK in rat ischemic skin flap tissue

Pan, X., Peng, L., Han, Z.-Q., Yin, G., Song, Y.-K., & Huang, J. (2015) · Tissue and Cell · doi:10.1016/j.tice.2015.04.001 · Cited by 24

Endosulfan upregulates AP-1 binding and ARE-mediated transcription via ERK1/2 and p38 activation in HepG2 cells

Song, M. O., Lee, C.-H., Yang, H. O., & Freedman, J. H. (2011) · Toxicology · doi:10.1016/j.tox.2011.11.013 · Cited by 24

Phosphatase Specificity and Pathway Insulation in Signaling Networks

Rowland, M. A., Harrison, B., & Deeds, E. J. (2015) · Biophysical Journal · doi:10.1016/j.bpj.2014.12.011 · Cited by 24

Autocrine transforming growth factor β signaling regulates extracellular signal-regulated kinase 1/2 phosphorylation via modulation of protein phosphatase 2A expression in scleroderma fibroblasts

Samuel, G. H., Bujor, A. M., Nakerakanti, S. S., Hant, F. N., & Trojanowska, M. E. (2010) · Fibrogenesis & Tissue Repair · doi:10.1186/1755-1536-3-25 · Cited by 24

The FASEB Journal • Review Phosphatase-mediated crosstalk between MAPK signaling pathways in the regulation of cell survival

Junttila, M. R., Li, S.-P., & Westermarck, J. (2014)

Signal transduction mediated by mitogen-activated protein kinases and apoptisis of tumor cells

Ji, Yubin, Y., Sun, Shengnan, Zou, Xiang, ■., antineoplastic, Harbin, on, Postdoctoral, et al. (2008) · Shenyang Yaoke Daxue xuebao

Mitogen-activated protein kinases in apoptosis regulation

Wada, T., & Penninger, J. M. (2004) · Oncogene · doi:10.1038/sj.onc.1207556 · Cited by 1,432

Opposing Effects of ERK and JNK-p38 MAP Kinases on Apoptosis

Xia, Z., Dickens, M., Raingeaud, J., Davis, R. J., & Greenberg, M. E. (1995) · Science · doi:10.1126/science.270.5240.1326 · Cited by 5,273

Crosstalk and Signaling Switches in Mitogen-Activated Protein Kinase Cascades

Fey, D., Croucher, D. R., Kölch, W., & Kholodenko, B. Ν. (2012) · Frontiers in Physiology · doi:10.3389/fphys.2012.00355 · Cited by 171