Differential regulation and properties of MAPKs

Mitogen-Activated Protein Kinase Pathways Mediated by ERK, JNK, and p38 Protein Kinases

Johnson, G. L., & Lapadat, R. (2002) · Science · doi:10.1126/science.1072682 · Cited by 4,295

Mammalian Mitogen-Activated Protein Kinase Signal Transduction Pathways Activated by Stress and Inflammation

Kyriakis, J. M., & Avruch, J. (2001) · Physiological Reviews · doi:10.1152/physrev.2001.81.2.807 · Cited by 3,400

A central role for JNK in obesity and insulin resistance

Hirosumi, J., Tuncman, G., Chang, L., Görgün, C. Z., Uysal, K. T., Maeda, K., Karin, M., & Hotamisligil, G. S. (2002) · Nature · doi:10.1038/nature01137 · Cited by 3,359

A protein kinase involved in the regulation of inflammatory cytokine biosynthesis

Lee, J. C., Laydon, J. T., McDonnell, P., Gallagher, T. F., Kumar, S., Green, D., McNulty, D. E., Blumenthal, M. J., Keys, J., vatter, S. W. L., et al. (1994) · Nature · doi:10.1038/372739a0 · Cited by 3,266

Protein Tyrosine Phosphatases in the Human Genome

Alonso, A., Sasin, J., Bottini, N., Friedberg, I., Friedberg, I., Osterman, A., Godzik, A., Hunter, T., Dixon, J., & Mustelin, T. (2004) · Cell · doi:10.1016/j.cell.2004.05.018 · Cited by 1,886

Identification of an oncoprotein- and UV-responsive protein kinase that binds and potentiates the c-Jun activation domain.

Hibi, M., Lin, A., Smeal, T., Minden, A., & Karin, M. (1993) · Genes & Development · doi:10.1101/gad.7.11.2135 · Cited by 1,886

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

Rapamycin decreases tau phosphorylation at Ser214 through regulation of cAMP-dependent kinase.

Liu, Y., Su, Y., Wang, J., Sun, S., Wang, T., Qiao, X., Run, X., Li, H., & Liang, Z. (2013) · Neurochemistry International · doi:10.1016/j.neuint.2013.01.014 · Cited by 64

Global Transcriptional Changes Following Statin Treatment in Breast Cancer

Bjarnadóttir, Ó., Kimbung, S., Johansson, I., Veerla, S., Jönsson, M., Bendahl, P., Grabau, D., Hedenfalk, I., & Borgquist, S. (2015) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-14-1403 · Cited by 59

Molecular and Cellular Mechanisms of Hexavalent Chromium-Induced Lung Cancer: An Updated Perspective

Urbano, A. M., Ferreira, L. M. R., & Alpoim, M. C. (2012) · Current Drug Metabolism · doi:10.2174/138920012799320464 · Cited by 59

Vibrational spectroscopy in sensing radiobiological effects: analyses of targeted and non-targeted effects in human keratinocytes

Meade, A. D., Howe, O. L., Unterreiner, V., Sockalingum, G. D., Byrne, H. J., & Lyng, F. M. (2015) · Faraday Discussions · doi:10.1039/c5fd00208g · Cited by 57

P38K and JNK pathways are induced by amyloid-β in astrocyte: Implication of MAPK pathways in astrogliosis in Alzheimer's disease

Saha, P., Guha, S., & Biswas, S. C. (2020) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2020.103551 · Cited by 57

Challenges in tendon–bone healing: emphasizing inflammatory modulation mechanisms and treatment

Jiang, F., Zhao, H., Zhang, P., Bi, Y., Zhang, H., Sun, S., Yao, Y., Zhu, X., Yang, F., Liu, Y., et al. (2024) · Frontiers in Endocrinology · doi:10.3389/fendo.2024.1485876 · Cited by 61

SOX4 is a direct target gene of FRA-2 and induces expression of HDAC8 in adult T-cell leukemia/lymphoma

Higuchi, T., Nakayama, T., Arao, T., Nishio, K., & Yoshie, O. (2013) · Blood · doi:10.1182/blood-2012-07-441022 · Cited by 58

The yeast mitogen-activated protein kinase Slt2 is involved in the cellular response to genotoxic stress

Soriano-Carot, M., Bañó, M. C., & Igual, J. C. (2012) · Cell Division · doi:10.1186/1747-1028-7-1 · Cited by 59

Deoxynivalenol Induces p38 Interaction with the Ribosome in Monocytes and Macrophages

Bae, H. K., & Pestka, J. J. (2008) · Toxicological Sciences · doi:10.1093/toxsci/kfn102 · Cited by 57

Protein Farnesylation–Dependent Raf/Extracellular Signal–Related Kinase Signaling Links to Cytoskeletal Remodeling to Facilitate Glucose-Induced Insulin Secretion in Pancreatic β-Cells

Kowluru, A., Veluthakal, R., Rhodes, C. J., Kamath, V. G., Syed, I., & Koch, B. J. (2010) · Diabetes · doi:10.2337/db09-1334 · Cited by 57

Epidermal CFTR Suppresses MAPK/NF-κB to Promote Cutaneous Wound Healing

Chen, J., Chen, Y., Chen, Y., Yang, Z., You, B. R., Ruan, Y. C., & Peng, Y. (2016) · Cellular Physiology and Biochemistry · doi:10.1159/000447919 · Cited by 58

Bioactive phytochemicals that regulate the cellular processes involved in diabetic nephropathy

Parveen, A., Jin, M., & Kim, S. Y. (2017) · Phytomedicine · doi:10.1016/j.phymed.2017.12.018 · Cited by 57

Crosstalk between oxidative stress-induced apoptotic and autophagic signaling pathways in Zn(II) phthalocyanine photodynamic therapy of melanoma

Valli, F., Vior, M. C. G., Roguin, L. P., & Marino, J. (2020) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2020.01.018 · Cited by 57

A Distinct Interaction Mode Revealed by the Crystal Structure of the Kinase p38α with the MAPK Binding Domain of the Phosphatase MKP5

Zhang, Y.-Y., Wu, J.-W., & Wang, Z.-X. (2011) · Science Signaling · doi:10.1126/scisignal.2002241 · Cited by 52

Anti-Photoaging Effect of Hydrolysates from Pacific Whiting Skin via MAPK/AP-1, NF-κB, TGF-β/Smad, and Nrf-2/HO-1 Signaling Pathway in UVB-Induced Human Dermal Fibroblasts

Han, S., Ballinger, E. A., Choung, S., & Kwon, J. Y. (2022) · Marine Drugs · doi:10.3390/md20050308 · Cited by 59

Effects of vascular endothelial cells on osteogenic differentiation of noncontact co‐cultured periodontal ligament stem cells under hypoxia

Wu, Y., Cao, H., Yang, Y., Zhou, Y., Gu, Y., Zhao, X., Zhang, Y., Zhao, Z., Zhang, L., & Yin, J. (2012) · Journal of Periodontal Research · doi:10.1111/j.1600-0765.2012.01503.x · Cited by 56

MEK/ERK activation plays a decisive role in yellow fever virus replication: Implication as an antiviral therapeutic target

Albarnaz, J. D., de Oliveira, L. C., Torres, A. A., Palhares, R. M., Casteluber, M. C. D. F., Rodrigues, C. M., Cardozo, P. L., Souza, A. M. R. D., Pacca, C. C., Ferreira, P. C. P., et al. (2014) · Antiviral Research · doi:10.1016/j.antiviral.2014.09.004 · Cited by 56

Canonical and Kinase Activity-Independent Mechanisms for Extracellular Signal-Regulated Kinase 5 (ERK5) Nuclear Translocation Require Dissociation of Hsp90 from the ERK5-Cdc37 Complex

Erazo, T., Moreno, A., Ruiz‐Babot, G., Rodríguez-Asiain, A., Morrice, N. A., Espadamala, J., Bayascas, J. R., Gómez, N., & Lizcano, J. M. (2013) · Molecular and Cellular Biology · doi:10.1128/mcb.01246-12 · Cited by 56

Induction of Apoptosis in Human Leukemia Cells by Grape Seed Extract Occurs via Activation of c-Jun NH2-Terminal Kinase

Gao, N., Budhraja, A., Cheng, S., Yao, H., Zhang, Z., & Shi, X. (2008) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-08-1447 · Cited by 56

Activation of p38 MAPK by feline infectious peritonitis virus regulates pro-inflammatory cytokine production in primary blood-derived feline mononuclear cells

Regan, A. D., Cohen, R. D., & Whittaker, G. R. (2008) · Virology · doi:10.1016/j.virol.2008.11.006 · Cited by 56

Impairment of learning and memory induced by perinatal exposure to BPA is associated with ERα-mediated alterations of synaptic plasticity and PKC/ERK/CREB signaling pathway in offspring rats

Wu, D., Wu, F., Lin, R., Meng, Y., Wei, W., Sun, Q., & Jia, L. (2020) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2020.04.023 · Cited by 55

Redox proteomics combined with proximity labeling enables monitoring of localized cysteine oxidation in cells

Kisty, E. A., Falco, J. A., & Weerapana, E. (2023) · Cell chemical biology · doi:10.1016/j.chembiol.2023.02.006 · Cited by 55

Inactivation of p38 MAPK during liver regeneration

Campbell, J. S., Argast, G. M., Yuen, S. Y., Hayes, B. J., & Fausto, N. (2010) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2010.08.002 · Cited by 59

A conserved motif in JNK/p38-specific MAPK phosphatases as a determinant for JNK1 recognition and inactivation

Liu, X., Zhang, C., Lu, C., Lin, S., Wu, J., & Wang, Z. (2016) · Nature Communications · doi:10.1038/ncomms10879 · Cited by 58

Long-Term Neuroprotective Effects of NT-4–Engineered Mesenchymal Stem Cells Injected Intravitreally in a Mouse Model of Acute Retinal Injury

Machalińska, A., Kawa, M. P., Pius‐Sadowska, E., Stępniewski, J., Nowak, W. N., Rogińska, D., Kaczyńska, K., Baumert, B., Wiszniewska, B., Józkowicz, A., et al. (2013) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.13-12221 · Cited by 55

Signaling Pathways Implicated in the Stimulation of β-Cell Proliferation by Extracellular Matrix

Parnaud, G., Hammar, E. B., Ribaux, P., Donath, M. Y., Berney, T., & Halban, P. A. (2009) · Molecular Endocrinology · doi:10.1210/me.2009-0008 · Cited by 56

Basal c-Jun NH2-terminal protein kinase activity is essential for survival and proliferation of T-cell acute lymphoblastic leukemia cells

Cui, J., Wang, Q., Wang, J., Lv, M., Zhu, N., Li, Y., Feng, J., Shen, B., & Zhang, J. (2009) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-09-0408 · Cited by 54

A-Kinase Anchoring Protein (AKAP)-Lbc Anchors a PKN-based Signaling Complex Involved in α1-Adrenergic Receptor-induced p38 Activation

Cariolato, L., Cavin, S., & Diviani, D. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.185645 · Cited by 54

Targeting BRAF in melanoma: Biological and clinical challenges

Mandalà, M., & Voit, C. A. (2013) · Critical Reviews in Oncology/Hematology · doi:10.1016/j.critrevonc.2013.01.003 · Cited by 56

MAPK signaling in cisplatin-induced death: predominant role of ERK1 over ERK2 in human hepatocellular carcinoma cells

Guégan, J., Ezan, F., Théret, N., Langouët, S., & Baffet, G. (2012) · Carcinogenesis · doi:10.1093/carcin/bgs317 · Cited by 57

High‐power, red‐light‐emitting diode irradiation enhances proliferation, osteogenic differentiation, and mineralization of human periodontal ligament stem cells via ERK signaling pathway

Yamauchi, N., Taguchi, Y., Kato, H., & Umeda, M. (2018) · Journal of Periodontology · doi:10.1002/jper.17-0365 · Cited by 54

Immunotoxicological effects of insecticides in exposed fishes

Yang, C., Lim, W., & Song, G. (2021) · Comparative Biochemistry and Physiology Part C Toxicology & Pharmacology · doi:10.1016/j.cbpc.2021.109064 · Cited by 53

A guide to ERK dynamics, part 1: mechanisms and models

Ram, A. R., Murphy, D. A., DeCuzzi, N. L., Patankar, M., Hu, J., Pargett, M., & Albeck, J. G. (2023) · Biochemical Journal · doi:10.1042/bcj20230276 · Cited by 54

Role of oxidation‐triggered activation of JNK and p38 MAPK in black tea polyphenols induced apoptotic death of A375 cells

Bhattacharya, U., Halder, B., Mukhopadhyay, S., & Giri, A. K. (2009) · Cancer Science · doi:10.1111/j.1349-7006.2009.01251.x · Cited by 55

Loss of Mitogen-activated Protein Kinase Phosphatase-1 Protects from Hepatic Steatosis by Repression of Cell Death-inducing DNA Fragmentation Factor A (DFFA)-like Effector C (CIDEC)/Fat-specific Protein 27

Flach, R. J. R., Hui, Q., Zhang, L., & Bennett, A. M. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.210237 · Cited by 54

Working Without Kinase Activity: Phosphotransfer-Independent Functions of Extracellular Signal–Regulated Kinases

Rodríguez, J., & Crespo, P. (2011) · Science Signaling · doi:10.1126/scisignal.2002324 · Cited by 56

Protective effects of asiatic acid against D-galactosamine/lipopolysaccharide-induced hepatotoxicity in hepatocytes and kupffer cells co-cultured system via redox-regulated leukotriene C4 synthase expression pathway

Ma, K., Zhang, Y., Zhu, D., & Lou, Y. (2008) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2008.11.054 · Cited by 53

High-frequency low-level diode laser irradiation promotes proliferation and migration of primary cultured human gingival epithelial cells

Ejiri, K., Aoki, A., Yamaguchi, Y., Ohshima, M., & Izumi, Y. (2013) · Lasers in Medical Science · doi:10.1007/s10103-013-1292-7 · Cited by 52

Integrative genomic profiling reveals conserved genetic mechanisms for tumorigenesis in common entities of non‐Hodgkin's lymphoma

Green, M. R., Aya‐Bonilla, C., Gandhi, M. K., Lea, R. A., Wellwood, J., Wood, P., Marlton, P. V., & Griffiths, L. R. (2011) · Genes Chromosomes and Cancer · doi:10.1002/gcc.20856 · Cited by 53

F-Box Only Protein 31 (FBXO31) Negatively Regulates p38 Mitogen-activated Protein Kinase (MAPK) Signaling by Mediating Lysine 48-linked Ubiquitination and Degradation of Mitogen-activated Protein Kinase Kinase 6 (MKK6)

Liu, J., Han, L., Li, B., Yang, J., Huen, M. S. Y., Pan, X., Tsao, S. W., & Cheung, A. L. M. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.560342 · Cited by 52

Oleuropein Induced Apoptosis in HeLa Cells via a Mitochondrial Apoptotic Cascade Associated With Activation of the c-Jun NH2-Terminal Kinase

Yao, J. J., Wu, J., Yang, X., Yang, J., Zhang, Y., & Du, L. (2014) · Journal of Pharmacological Sciences · doi:10.1254/jphs.14012fp · Cited by 54

Partner exchange: protein–protein interactions in the Raf pathway

Wimmer, R., & Baccarini, M. (2010) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2010.06.001 · Cited by 57

Role of cytochrome P450–mediated arachidonic acid metabolites in the pathogenesis of cardiac hypertrophy

Alsaad, A. M. S., Zordoky, B. N. M., Tse, M. M. Y., & El‐Kadi, A. O. S. (2013) · Drug Metabolism Reviews · doi:10.3109/03602532.2012.754460 · Cited by 53

Preventing Phosphorylation of Sterol Regulatory Element-Binding Protein 1a by MAP-Kinases Protects Mice from Fatty Liver and Visceral Obesity

Kotzka, J., Knebel, B., Haas, J., Kremer, L., Jacob, S., Hartwig, S., Nitzgen, U., & Müller‐Wieland, D. (2012) · PLoS ONE · doi:10.1371/journal.pone.0032609 · Cited by 50

Astragalin-induced cell death is caspase-dependent and enhances the susceptibility of lung cancer cells to tumor necrosis factor by inhibiting the NF-κB pathway

Chen, M., Cai, F., Zha, D., Wang, X., Zhang, W., He, Y., Huang, Q., Zhuang, H., & Hua, Z. (2017) · Oncotarget · doi:10.18632/oncotarget.15264 · Cited by 51

The Mechanisms of Bushen-Yizhi Formula as a Therapeutic Agent against Alzheimer’s Disease

Cai, H., Luo, Y., Yan, X., Ding, P., Huang, Y., Fang, S., Zhang, R., Chen, Y., Guo, Z., Fang, J., et al. (2018) · Scientific Reports · doi:10.1038/s41598-018-21468-w · Cited by 50

Pre-Treatment with Curcumin Ameliorates Cisplatin-Induced Kidney Damage by Suppressing Kidney Inflammation and Apoptosis in Rats

Soetikno, V., Sari, S. D. P., Maknun, L. U., Sumbung, N. K., Rahmi, D. N. I., Pandhita, B. A. W., Louisa, M., & Estuningtyas, A. (2018) · Drug Research · doi:10.1055/a-0641-5148 · Cited by 51

Cell division cycle associated 5 promotes colorectal cancer progression by activating the ERK signaling pathway

Shen, A., Liu, L., Chen, H., Qi, F., Huang, Y., Lin, J., Sferra, T. J., Sankararaman, S., Wei, L., Chu, J., et al. (2019) · Oncogenesis · doi:10.1038/s41389-019-0123-5 · Cited by 52

The role of traditional Chinese medicine in the treatment of atherosclerosis through the regulation of macrophage activity

Jian, X., Liu, Y., Zhao, Z., Zhao, L., Wang, D., & Liu, Q. (2019) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2019.109375 · Cited by 51

Structural Mechanisms of Allostery and Autoinhibition in JNK Family Kinases

Laughlin, J. D., Nwachukwu, J. C., Figuera-Losada, M., Cherry, L., Nettles, K. W., & LoGrasso, P. V. (2012) · Structure · doi:10.1016/j.str.2012.09.021 · Cited by 50

Roles of p38 MAPK signalling in intervertebral disc degeneration

Shi, Z., Zhu, L., Song, Z., Liu, T.-J., & Hao, D. (2023) · Cell Proliferation · doi:10.1111/cpr.13438 · Cited by 50

Multisite phosphorylation of c-Jun at threonine 91/93/95 triggers the onset of c-Jun pro-apoptotic activity in cerebellar granule neurons

Edamakanti, C. R., Albanito, L., Marco, P. D., Aiello, D., Maggiolini, M., Napoli, A., & Musti, A. M. (2013) · Cell Death and Disease · doi:10.1038/cddis.2013.381 · Cited by 50

MAVS-MKK7-JNK2 Defines a Novel Apoptotic Signaling Pathway during Viral Infection

Huang, Y., Liu, H., Li, S., Tang, Y., Wei, B., Yu, H., & Wang, C. (2014) · PLoS Pathogens · doi:10.1371/journal.ppat.1004020 · Cited by 49

A RING to rule them all? Insights into the Map3k1 PHD motif provide a new mechanistic understanding into the diverse roles of Map3k1

Suddason, T., & Gallagher, E. D. (2015) · Cell Death and Differentiation · doi:10.1038/cdd.2014.239 · Cited by 51

Anti-citrullinated Protein Antibodies Activated ERK1/2 and JNK Mitogen-activated Protein Kinases via Binding to Surface-expressed Citrullinated GRP78 on Mononuclear Cells

Lu, M., Lai, N., Yin, W., Yu, H.-C., Huang, H., Tung, C., Huang, K., & Yu, C. (2012) · Journal of Clinical Immunology · doi:10.1007/s10875-012-9841-6 · Cited by 51

MAPKs and NF-κB differentially regulate cytokine expression in the diaphragm in response to resistive breathing: the role of oxidative stress.

Sigala, I., Zacharatos, P., Toumpanakis, D., Michailidou, T., Noussia, O., Theocharis, S., Roussos, C., Papapetropoulos, A., & Vassilakopoulos, T. (2011) · American Journal of Physiology. Regulatory Integrative and Comparative Physiology · doi:10.1152/ajpregu.00376.2010 · Cited by 56

Chromatin-tethered MAPKs

Klein, A. M., Zaganjor, E., & Cobb, M. H. (2013) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2013.01.002 · Cited by 50

Allosteric enhancement of MAP kinase p38α's activity and substrate selectivity by docking interactions

Tokunaga, Y., Takeuchi, K., Takahashi, H. K., & Shimada, I. (2014) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2861 · Cited by 50

Gonadotropes and Gonadotropin-Releasing Hormone Signaling

McArdle, C. A., & Roberson, M. S. (2014) · Elsevier eBooks · doi:10.1016/b978-0-12-397175-3.00010-7 · Cited by 52

Flow-induced mechanotransduction in skeletal cells

Alfieri, R. R., Vassalli, M., & Viti, F. (2019) · Biophysical Reviews · doi:10.1007/s12551-019-00596-1 · Cited by 51

p38α- and DYRK1A-dependent phosphorylation of caspase-9 at an inhibitory site in response to hyperosmotic stress

Seifert, A., & Clarke, P. R. (2009) · Cellular Signalling · doi:10.1016/j.cellsig.2009.06.009 · Cited by 50

A Novel N-Terminal Domain May Dictate the Glucose Response of Mondo Proteins

McFerrin, L. G., & Atchley, W. R. (2012) · PLoS ONE · doi:10.1371/journal.pone.0034803 · Cited by 50

Diosmetin Induces Human Osteoblastic Differentiation Through the Protein Kinase C/p38 and Extracellular Signal-Regulated Kinase 1/2 Pathway

Hsu, Y., & Kuo, P. (2008) · Journal of Bone and Mineral Research · doi:10.1359/jbmr.080219 · Cited by 50

FGF2: A Key Regulator Augmenting Tendon-to-Bone Healing and Cartilage Repair

Zhang, J., Liu, Z., Li, Y., You, Q., Yang, J., Jin, Y. H., Zou, G., Tang, J., Ge, Z., & Liu, Y. (2020) · Regenerative Medicine · doi:10.2217/rme-2019-0080 · Cited by 49

Regulation of Mitogen-Activated Protein Kinase Signaling Pathways by the Ubiquitin-Proteasome System and Its Pharmacological Potential

Mathien, S., Tesnière, C., & Meloche, S. (2021) · Pharmacological Reviews · doi:10.1124/pharmrev.120.000170 · Cited by 51

Mark4 promotes adipogenesis and triggers apoptosis in 3T3‐L1 adipocytes by activating JNK1 and inhibiting p38MAPK pathways

Feng, M., Liang, T., Gan, L., Liu, Z., & Sun, C. (2014) · Biology of the Cell · doi:10.1111/boc.201400004 · Cited by 49

Role of B-RafV600E in differentiated thyroid cancer and preclinical validation of compounds against B-RafV600E

Nucera, C., Goldfarb, M. R., Hodin, R. A., & Parangi, S. (2009) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2009.01.003 · Cited by 51

Ginsenoside Rg3 induces apoptosis in the U87MG human glioblastoma cell line through the MEK signaling pathway and reactive oxygen species

Choi, Y. J., Lee, H. J., Kang, D. W., Han, I. H., Choi, B. K., & Cho, W. H. (2013) · Oncology Reports · doi:10.3892/or.2013.2555 · Cited by 49

Extracellularly Signal-Regulated Kinase Activity in the Human Endometrium: Possible Roles in the Pathogenesis of Endometriosis

Murk, W. K., Atabekoğlu, C. S., Çakmak, H., Heper, A. O., Ensarı, A., Kayisli, U. A., & Arici, A. M. (2008) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2007-2051 · Cited by 49

Differential genetic interactions of yeast stress response MAPK pathways

Martı́n, H., Shales, M., Fernández-Piñar, P., Wei, P., Molina, M., Fiedler, D., Shokat, K. M., Beltrão, P., Lim, W. A., & Krogan, N. J. (2015) · Molecular Systems Biology · doi:10.15252/msb.20145606 · Cited by 52

Sef Downregulation by Ras Causes MEK1/2 to Become Aberrantly Nuclear Localized Leading to Polyploidy and Neoplastic Transformation

Duhamel, S., Hébert, J., Gaboury, L. A., Bouchard, A., Simon, R., Sauter, G., Basik, M., & Meloche, S. (2012) · Cancer Research · doi:10.1158/0008-5472.can-11-2126 · Cited by 51

A Hydroxylated Metabolite of Flame-Retardant PBDE-47 Decreases the Survival, Proliferation, and Neuronal Differentiation of Primary Cultured Adult Neural Stem Cells and Interferes with Signaling of ERK5 MAP Kinase and Neurotrophin 3

Li, T., Wang, W., Pan, Y.-W., Xu, L., & Xia, Z. (2013) · Toxicological Sciences · doi:10.1093/toxsci/kft083 · Cited by 49

c-Jun N-Terminal Kinase Inhibitors as Potential Leads for New Therapeutics for Alzheimer’s Diseases

Rehfeldt, S. C. H., Majolo, F., Goettert, M. I., & Laufer, S. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21249677 · Cited by 47

The MAPK signaling pathway mediates the GPR91-dependent release of VEGF from RGC-5 cells

HU, J., LI, T., DU, S., CHEN, Y., WANG, S., XIONG, F., & WU, Q. (2015) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2015.2195 · Cited by 48

MAPK pathway involved in epidermal terminal differentiation of normal human epidermal keratinocytes

Meng, X., Qiu, L., Song, H., & Dang, N. (2018) · Open Medicine · doi:10.1515/med-2018-0029 · Cited by 48

Restoring KLF5 in Esophageal Squamous Cell Cancer Cells Activates the JNK Pathway Leading to Apoptosis and Reduced Cell Survival

Tarapore, R. S., Yang, Y., & Katz, J. P. (2013) · Neoplasia · doi:10.1593/neo.122126 · Cited by 51

Examining Docking Interactions on ERK2 with Modular Peptide Substrates

Lee, S., Warthaka, M., Yan, C., Kaoud, T. S., Ren, P. Y., & Dalby, K. N. (2011) · Biochemistry · doi:10.1021/bi201103b · Cited by 50

The MEKK1 PHD ubiquitinates TAB1 to activate MAPKs in response to cytokines

Charlaftis, N., Suddason, T., Wu, X., Anwar, S., Karin, M., & Gallagher, E. D. (2014) · The EMBO Journal · doi:10.15252/embj.201488351 · Cited by 48

The many faces of p38 mitogen-activated protein kinase in progenitor/stem cell differentiation

Oeztuerk-Winder, F., & Ventura, J. (2012) · Biochemical Journal · doi:10.1042/bj20120401 · Cited by 48

The role of p38 MAPK pathway in p53 compromised state and telomere mediated DNA damage response

Roy, S., Roy, S., Rana, A., Akhter, Y., Hande, M. P., & Banerjee, B. (2018) · Mutation Research/Genetic Toxicology and Environmental Mutagenesis · doi:10.1016/j.mrgentox.2018.05.018 · Cited by 48

CDK4/6 and MAPK—Crosstalk as Opportunity for Cancer Treatment

Scheiblecker, L., Kollmann, K., & Sexl, V. (2020) · Pharmaceuticals · doi:10.3390/ph13120418 · Cited by 48

Anti-inflammatory and antioxidant effects of Chaetoglobosin Vb in LPS-induced RAW264.7 cells: Achieved via the MAPK and NF-κB signaling pathways

Zhang, H., Guo, Q., Liang, Z., Wang, M., Wang, B., Sun‐Waterhouse, D., Waterhouse, G. I. N., Wang, J., Ma, C., & Kang, W. (2020) · Food and Chemical Toxicology · doi:10.1016/j.fct.2020.111915 · Cited by 48

Signaling to Cardiac Hypertrophy: Insights from Human and Mouse RASopathies

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