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

NRF2 Regulation Processes as a Source of Potential Drug Targets against Neurodegenerative Diseases

Cores, Á., Piquero, M., Villacampa, M., Leon, R. M., & Menéndez, J. C. (2020) · Biomolecules · doi:10.3390/biom10060904 · Cited by 86

Whole Cigarette Smoke Increased the Expression of TLRs, HBDs, and Proinflammory Cytokines by Human Gingival Epithelial Cells through Different Signaling Pathways

Semlali, A., Witoled, C., Alanazi, M. M., & Rouabhia, M. (2012) · PLoS ONE · doi:10.1371/journal.pone.0052614 · Cited by 80

Extracellular signal‐regulated kinase 1/2 signaling promotes oligodendrocyte myelination in vitro

Xiao, J., Ferner, A. H., Wong, A. W., Denham, M., Kilpatrick, T. J., & Murray, S. S. (2012) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2012.07871.x · Cited by 84

Involvement of JNK-AP-1 and ERK-NF-κB signaling in tension-stimulated expression of Type I collagen and MMP-1 in human periodontal ligament fibroblasts

Kook, S., Jang, Y., & Lee, J. (2011) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00348.2011 · Cited by 82

PTPH1 Dephosphorylates and Cooperates with p38γ MAPK to Increase Ras Oncogenesis through PDZ-Mediated Interaction

Hou, S.-W., Zhi, H.-Y., Pohl, N. M., Loesch, M., Qi, X.-M., Li, R.-S., Basir, Z., & Chen, G. (2010) · Cancer Research · doi:10.1158/0008-5472.can-09-3229 · Cited by 81

Natural feed contaminant zearalenone decreases the expressions of important pro- and anti-inflammatory mediators and mitogen-activated protein kinase/NF-κB signalling molecules in pigs

Pistol, G. C., Gras, M. A., Marin, D. E., Israel-Roming, F., Stancu, M., & Țăranu, I. (2013) · British Journal Of Nutrition · doi:10.1017/s0007114513002675 · Cited by 80

Structural basis of p38α regulation by hematopoietic tyrosine phosphatase

Francis, D. M., Różycki, B., Koveal, D., Hummer, G., Page, R., & Peti, W. (2011) · Nature Chemical Biology · doi:10.1038/nchembio.707 · Cited by 79

Crucial requirement of ERK/MAPK signaling in respiratory tract development

Boucherat, O., Nadeau, V., Bérubé‐Simard, F., Charron, J., & Jeannotte, L. (2014) · Development · doi:10.1242/dev.110254 · Cited by 79

Mitogen-activated protein kinases and Hedgehog-GLI signaling in cancer: A crosstalk providing therapeutic opportunities?

Rovida, E., & Stecca, B. A. (2015) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2015.08.003 · Cited by 78

β1 integrin/Fak/Src signaling in intestinal epithelial crypt cell survival: integration of complex regulatory mechanisms

Bouchard, V., Harnois, C., Demers, M., Thibodeau, S., Laquerre, V., Gauthier, R., Vézina, A., Noël, D., Fujita, N., Tsuruo, T., et al. (2008) · APOPTOSIS · doi:10.1007/s10495-008-0192-y · Cited by 79

MST Kinases Monitor Actin Cytoskeletal Integrity and Signal via c-Jun N-Terminal Kinase Stress-Activated Kinase To Regulate p21Waf1/Cip1 Stability

Densham, R. M., O’Neill, E. E., Munro, J., König, I., Anderson, K. I., Kölch, W., & Olson, M. F. (2009) · Molecular and Cellular Biology · doi:10.1128/mcb.00116-09 · Cited by 84

A Retrograde Neuronal Survival Response: Target-Derived Neurotrophins Regulate MEF2D and bcl-w

Pazyra‐Murphy, M. F., Hans, A., Courchesne, S. L., Karch, C., Cosker, K., Heerssen, H. M., Watson, F. L., Kim, T.-K., Greenberg, M. E., & Segal, R. A. (2009) · Journal of Neuroscience · doi:10.1523/jneurosci.0233-09.2009 · Cited by 79

Hydrogen-rich saline protects against liver injury in rats with obstructive jaundice

Liu, Q., Shen, W.-F., Sun, H.-Y., Fan, D.-F., Nakao, A., Cai, J.-M., Yan, G., Zhou, W.-P., Shen, R.-X., Yang, J.-M., et al. (2010) · Liver International · doi:10.1111/j.1478-3231.2010.02254.x · Cited by 79

Current Molecular Markers of Melanoma and Treatment Targets

Yang, K., Oak, A. S. W., Slominski, R. M., Brożyna, A. A., & Slominski, A. T. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21103535 · Cited by 80

Mitofusin 2 ameliorates hypoxia-induced apoptosis via mitochondrial function and signaling pathways

Peng, C., Rao, W., Zhang, L., Wang, K., Hui, H., Wang, L., Su, N., Luo, P., Hao, Y., Tu, Y., et al. (2015) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2015.09.011 · Cited by 78

Sulfur mustard analog induces oxidative stress and activates signaling cascades in the skin of SKH-1 hairless mice

Pal, A., Tewari‐Singh, N., Gu, M., Agarwal, C., Huang, J., Day, B. J., White, C. W., & Agarwal, R. (2009) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.09.011 · Cited by 78

JNK phosphorylation, induced during dengue virus infection, is important for viral infection and requires the presence of cholesterol

Ceballos‐Olvera, I., Chávez-Salinas, S., Medina, F., Ludert, J. E., & del Angel, R. M. (2009) · Virology · doi:10.1016/j.virol.2009.10.019 · Cited by 78

Oscillation of p38 activity controls efficient pro-inflammatory gene expression

Tomida, T., Takekawa, M., & Saito, H. (2015) · Nature Communications · doi:10.1038/ncomms9350 · Cited by 80

The osteogenic differentiation of PDLSCs is mediated through MEK/ERK and p38 MAPK signalling under hypoxia

Wu, Y., Yang, Y., Yang, P., Gu, Y., Zhao, Z., Tan, L., Zhao, L., Tang, T., & Li, Y. (2013) · Archives of Oral Biology · doi:10.1016/j.archoralbio.2013.03.011 · Cited by 77

The Role of Extracellular Signal-Related Kinase During Abdominal Aortic Aneurysm Formation

Ghosh, A., DiMusto, P. D., Ehrlichman, L. K., Sadiq, O., McEvoy, B., Futchko, J. S., Henke, P. K., Eliason, J. L., & Upchurch, G. R. (2012) · Journal of the American College of Surgeons · doi:10.1016/j.jamcollsurg.2012.06.414 · Cited by 77

Protein Targets of Reactive Metabolites of Thiobenzamide in Rat Liver in Vivo

Ikehata, K., Duzhak, T. G., Galeva, N. A., Ji, T., Koen, Y. M., & Hanzlik, R. P. (2008) · Chemical Research in Toxicology · doi:10.1021/tx800093k · Cited by 76

Experimental Stroke-Induced Changes in the Bone Marrow Reveal Complex Regulation of Leukocyte Responses

Dénes, Á., McColl, B. W., Leow‐Dyke, S., Chapman, K. Z., Humphreys, N. E., Grencis, R. K., Allan, S. M., & Rothwell, N. J. (2010) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1038/jcbfm.2010.198 · Cited by 76

Apoptosis commitment and activation of mitochondrial Bax during anoikis is regulated by p38MAPK

Owens, T. W., Valentijn, A., Upton, J.-P., Keeble, J. A., Zhang, L., Lindsay, J., Zouq, N. K., & Gilmore, A. P. (2009) · Cell Death and Differentiation · doi:10.1038/cdd.2009.102 · Cited by 77

Sertraline, an antidepressant, induces apoptosis in hepatic cells through the mitogen-activated protein kinase pathway

Chen, S., Xuan, J., Wan, L., Lin, H., Couch, L., Mei, N., Dobrovolsky, V. N., & Guo, L. (2014) · Toxicological Sciences · doi:10.1093/toxsci/kft254 · Cited by 75

The Nuclear Translocation of Mitogen-Activated Protein Kinases: Molecular Mechanisms and Use as Novel Therapeutic Target

Flores, K., Yadav, S. S., Katz, A. A., & Seger, R. (2018) · Neuroendocrinology · doi:10.1159/000494085 · Cited by 75

SMYD3: a regulator of epigenetic and signaling pathways in cancer

Bernard, B., Nigam, N., Burkitt, K., & Saloura, V. (2021) · Clinical Epigenetics · doi:10.1186/s13148-021-01021-9 · Cited by 76

Structure and RAF family kinase isoform selectivity of type II RAF inhibitors tovorafenib and naporafenib

Tkacik, E., Li, K., Pino, G. L. G., Ha, B. H., Viñals, J., Park, E., Beyett, T. S., & Eck, M. J. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2023.104634 · Cited by 72

Regulating cell morphogenesis: The drosophila jun N‐terminal kinase pathway

Ríos‐Barrera, L. D., & Riesgo‐Escovar, J. R. (2012) · genesis · doi:10.1002/dvg.22354 · Cited by 75

Dual-Specificity Phosphatase 14 (DUSP14/MKP6) Negatively Regulates TCR Signaling by Inhibiting TAB1 Activation

Yang, C., Li, J., Chiu, L., Lan, J., Chen, D., Chuang, H., Huang, C., & Tan, T. (2014) · The Journal of Immunology · doi:10.4049/jimmunol.1300989 · Cited by 78

Copper induces hepatic inflammatory responses by activation of MAPKs and NF-κB signalling pathways in the mouse

Liu, H., Guo, H., Deng, H., Cui, H., Fang, J. S., Zuo, Z., Deng, J., Li, Y., Wang, X., & Zhao, L. (2020) · Ecotoxicology and Environmental Safety · doi:10.1016/j.ecoenv.2020.110806 · Cited by 74

When Good Kinases Go Rogue: GSK3, p38 MAPK and CDKs as Therapeutic Targets for Alzheimer’s and Huntington’s Disease

D’Mello, S. R. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22115911 · Cited by 80

Dexamethasone prevents alteration of tight junction-associated proteins and barrier function in porcine choroid plexus epithelial cells after infection with Streptococcus suis in vitro

Tenenbaum, T., Matalon, D., Adam, R., Seibt, A., Friedrich, C., Schwerk, C., Galla, H., & Schroten, H. (2008) · Brain Research · doi:10.1016/j.brainres.2008.06.118 · Cited by 74

p38δ Mitogen-Activated Protein Kinase Is Essential for Skin Tumor Development in Mice

Schindler, E. M., Hindes, A. E., Gribben, E. L., Burns, C. J., Yin, Y., Lin, M., Owen, R. J., Longmore, G. D., Kissling, G. E., Arthur, J. S. C., et al. (2009) · Cancer Research · doi:10.1158/0008-5472.can-08-4455 · Cited by 75

Resveratrol, an antioxidant, protects spinal cord injury in rats by suppressing MAPK pathway

Fu, S., Lv, R., Wang, L., Hou, H., Liu, H., & Shao, S. (2016) · Saudi Journal of Biological Sciences · doi:10.1016/j.sjbs.2016.10.019 · Cited by 74

Specificity models in MAPK cascade signaling

Ma, Y., & Nicolet, J. (2023) · FEBS Open Bio · doi:10.1002/2211-5463.13619 · Cited by 76

Fucoidan’s Molecular Targets: A Comprehensive Review of Its Unique and Multiple Targets Accounting for Promising Bioactivities Supported by In Silico Studies

Zayed, A., Al-Saedi, D. A., Mensah, E. O., Kanwugu, O. N., Adadi, P., & Ulber, R. (2023) · Marine Drugs · doi:10.3390/md22010029 · Cited by 78

Uncovering mechanisms of bistability in biological systems

Pomerening, J. R. (2008) · Current Opinion in Biotechnology · doi:10.1016/j.copbio.2008.06.009 · Cited by 74

LncRNA H19 promotes the committed differentiation of stem cells from apical papilla via miR-141/SPAG9 pathway

Li, Z., Yan, M., Yu, Y., Wang, Y., Lei, G., Pan, Y., Li, N., Gobin, R., & Yu, J. (2019) · Cell Death and Disease · doi:10.1038/s41419-019-1337-3 · Cited by 72

Microtubule depolymerization and phosphorylation of c-Jun N-terminal kinase-1 and p38 were involved in gambogic acid induced cell cycle arrest and apoptosis in human breast carcinoma MCF-7 cells

Chen, J., Gu, H.-Y., Lu, N., Yang, Y., Liu, W., Qi, Q., Rong, J., Wang, X.-T., You, Q., & Guo, Q. (2008) · Life Sciences · doi:10.1016/j.lfs.2008.05.003 · Cited by 73

Opioidergic regulation of astroglial/neuronal proliferation: where are we now?

Sargeant, T. J., Miller, J. H., & Day, D. J. (2008) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2008.05671.x · Cited by 69

Mitogen‐Activated Protein Kinase Phosphatase 1 as an Inflammatory Factor and Drug Target

Korhonen, R., & Moilanen, E. (2013) · Basic & Clinical Pharmacology & Toxicology · doi:10.1111/bcpt.12141 · Cited by 73

Effects of salubrinal on cadmium-induced apoptosis in HK-2 human renal proximal tubular cells

Komoike, Y., Inamura, H., & Matsuoka, M. (2011) · Archives of Toxicology · doi:10.1007/s00204-011-0742-x · Cited by 71

Oncogenic Ras abrogates MEK SUMOylation that suppresses the ERK pathway and cell transformation

Kubota, Y., O'Grady, P., Saito, H., & Takekawa, M. (2011) · Nature Cell Biology · doi:10.1038/ncb2169 · Cited by 70

Aflatoxin B1 disrupts the androgen biosynthetic pathway in rat Leydig cells

Adedara, I. A., Nanjappa, M. K., Farombi, E. O., & Akingbemi, B. T. (2013) · Food and Chemical Toxicology · doi:10.1016/j.fct.2013.12.027 · Cited by 73

The Role of MAPK in Drug-Induced Kidney Injury

Cassidy, H., Radford, R., Slyne, J., O’Connell, S., Slattery, C., Ryan, M. P., & McMorrow, T. (2012) · Journal of Signal Transduction · doi:10.1155/2012/463617 · Cited by 71

Mono-2-ethylhexylphthalate (MEHP) induces TNF-α release and macrophage differentiation through different signalling pathways in RAW264.7 cells

Bølling, A. K., Øvrevik, J., Samuelsen, J. T., Holme, J. A., Rakkestad, K. E., Mathisen, G. H., Paulsen, R. E., Korsnes, M. S., & Becher, R. (2011) · Toxicology Letters · doi:10.1016/j.toxlet.2011.11.016 · Cited by 68

Carbon Source Metabolism and Its Regulation in Cancer Cells

Yin, C., Qie, S., & Sang, N. (2012) · Critical Reviews in Eukaryotic Gene Expression · doi:10.1615/critreveukargeneexpr.v22.i1.20 · Cited by 67

Activation loop phosphorylation of the atypical MAP kinases ERK3 and ERK4 is required for binding, activation and cytoplasmic relocalization of MK5

Déléris, P., Rousseau, J., Coulombe, P., Rodier, G., Tanguay, P., & Meloche, S. (2008) · Journal of Cellular Physiology · doi:10.1002/jcp.21560 · Cited by 69

Posttranslational Modifications of the Retinoblastoma Tumor Suppressor Protein as Determinants of Function

MacDonald, J. I., & Dick, F. A. (2012) · Genes & Cancer · doi:10.1177/1947601912473305 · Cited by 71

Modulating p38 MAPK signaling by proteostasis mechanisms supports tissue integrity during growth and aging

Yuan, W., Weaver, Y. M., Earnest, S., Taylor, C. A., Cobb, M. H., & Weaver, B. P. (2023) · Nature Communications · doi:10.1038/s41467-023-40317-7 · Cited by 56

A review of signal pathway induced by virulent protein CagA of Helicobacter pylori

Wang, H., Zhao, M., Shi, F., Zheng, S., Xiong, L., & Zheng, L. (2023) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2023.1062803 · Cited by 68

JAK2 and MPL protein levels determine TPO-induced megakaryocyte proliferation vs differentiation

Besancenot, R., Roos‐Weil, D., Tonetti, C., Abdelouahab, H., Lacout, C., Pasquier, F., Willekens, C., Rameau, P., Lécluse, Y., Micol, J., et al. (2014) · Blood · doi:10.1182/blood-2014-03-559815 · Cited by 68

Targeting MAPK (Ras/ERK) and PI3K/Akt pathways in pituitary tumorigenesis

Çakır, M., & Grossman, A. B. (2009) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728220903170675 · Cited by 69

Mitogen-activated protein kinase p38 and MK2, MK3 and MK5: Ménage à trois or ménage à quatre?

Shiryaev, A., & Moens, U. L. (2010) · Cellular Signalling · doi:10.1016/j.cellsig.2010.03.002 · Cited by 64

Vitamin D3-driven signals for myeloid cell differentiation—Implications for differentiation therapy

Hughes, P., Marcinkowska, E., Gocek, E., Studzinski, G. P., & Brown, G. (2009) · Leukemia Research · doi:10.1016/j.leukres.2009.09.010 · Cited by 67

ERK Mutations and Amplification Confer Resistance to ERK-Inhibitor Therapy

Jaiswal, B. S., Durinck, S., Stawiski, E. W., Yin, J., Wang, W., Lin, E., Moffat, J. G., Martin, S. E., Modrusan, Z. D., & Seshagiri, S. (2018) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-17-3674 · Cited by 69

Resveratrol alleviates diabetes-induced testicular dysfunction by inhibiting oxidative stress and c-Jun N-terminal kinase signaling in rats

Faid, I., Al‐Hussaini, H., & Kilarkaje, N. (2015) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2015.10.012 · Cited by 66

Prevention of premature senescence requires JNK regulation of Bcl-2 and reactive oxygen species

Lee, J. J., Lee, J. H., Ko, Y. G., Hong, S., & Js, L. (2009) · Oncogene · doi:10.1038/onc.2009.355 · Cited by 67

An evolutionary perspective on the kinome of malaria parasites

Talevich, E., Tobin, A. B., Kannan, N., & Doerig, C. (2012) · Philosophical Transactions of the Royal Society B Biological Sciences · doi:10.1098/rstb.2012.0014 · Cited by 70

The emerging role of substance P/neurokinin-1 receptor signaling pathways in growth and development of tumor cells

Javid, H., Mohammadi, F., Zahiri, E., & Hashemy, S. I. (2019) · Journal of Physiology and Biochemistry · doi:10.1007/s13105-019-00697-1 · Cited by 64

Targeting Phosphatases and Kinases: How to Checkmate Cancer

Turdo, A., D’Accardo, C., Glaviano, A., Porcelli, G., Colarossi, C., Colarossi, L., Mare, M., Faldetta, N., Modica, C., Pistone, G., et al. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.690306 · Cited by 66

Resistance to CDK4/6 inhibition: Mechanisms and strategies to overcome a therapeutic problem in the treatment of hormone receptor-positive metastatic breast cancer

Papadimitriou, M., Pazaiti, A., Iliakopoulos, K., Markouli, M., Michalaki, V., & PAPADIMITRIOU, C. A. (2022) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2022.119346 · Cited by 68

Massive gene amplification drives paediatric hepatocellular carcinoma caused by bile salt export pump deficiency

Iannelli, F., Collino, A., Sinha, S., Radaelli, E., Nicoli, P., D’Antiga, L., Sonzogni, A., Faivre, J., Buendia, M. A., Sturm, E., et al. (2014) · Nature Communications · doi:10.1038/ncomms4850 · Cited by 68

MAPK phosphatase-1 facilitates the loss of oxidative myofibers associated with obesity in mice

Flach, R. J. R., Le, A. M., Zhang, L., Kahn, M., Samuel, V. T., Shulman, G. I., & Bennett, A. M. (2009) · Journal of Clinical Investigation · doi:10.1172/jci39054 · Cited by 65

Interleukin 1/Toll-like Receptor-induced Autophosphorylation Activates Interleukin 1 Receptor-associated Kinase 4 and Controls Cytokine Induction in a Cell Type-specific Manner

Cushing, L., Stochaj, W. R., Siegel, M. M., Czerwiński, R., Dower, K., Wright, Q. G., Hirschfield, M., Casanova, J., Pïcard, C., Puel, A., et al. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.544809 · Cited by 64

Smad linker region phosphorylation in the regulation of extracellular matrix synthesis

Burch, M. L., Zheng, W., & Little, P. J. (2010) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-010-0514-4 · Cited by 65

ERK1/2/COX-2/PGE2 signaling pathway mediates GPR91-dependent VEGF release in streptozotocin-induced diabetes.

Li, T., Hu, J., Du, S., Chen, Y., Wang, S., & Wu, Q. E. (2014) · PubMed Central · Cited by 65

Effects of Mesenchymal Stem Cell Derivatives on Hematopoiesis and Hematopoietic Stem Cells

Aqmasheh, S., Shamsasenjan, K., Akbarzadehlaleh, P., Sarvar, D. P., & Timari, H. (2017) · Advanced Pharmaceutical Bulletin · doi:10.15171/apb.2017.021 · Cited by 65

Astragalin heptaacetate-induced cell death in human leukemia cells is dependent on caspases and activates the MAPK pathway

Burmistrova, O., Quintana, J., Dı́az, J. G., & Estévez, F. (2011) · Cancer Letters · doi:10.1016/j.canlet.2011.05.018 · Cited by 63

Peroxisome proliferator-activated receptor-gamma (PPAR-gamma) ligands as potential therapeutic agents to treat arthritis.

Giaginis, C., Giagini, A., & Theocharis, S. (2009) · Pharmacological Research · doi:10.1016/j.phrs.2009.02.005 · Cited by 62

Influence of long-term caloric restriction on myocardial and cardiomyocyte contractile function and autophagy in mice

Han, X., Turdi, S., Hu, N., Guo, R., Zhang, Y., & Ren, J. (2012) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2011.11.002 · Cited by 56

Signalling pathways and the regulation of SUMO modification

Guo, B., Yang, S., Witty, J., & Sharrocks, A. D. (2007) · Biochemical Society Transactions · doi:10.1042/bst0351414 · Cited by 67

Oxidative stress-induced inhibition of adrenal steroidogenesis requires participation of p38 mitogen-activated protein kinase signaling pathway

Abidi, P., Zhang, H., Zaidi, S. K., Shen, W., Leers‐Sucheta, S., Cortez, Y., Han, J., & Azhar, S. (2008) · Journal of Endocrinology · doi:10.1677/joe-07-0570 · Cited by 64

Differential neuroendocrine and immune responses to acute psychosocial stress in women with type 1 bipolar disorder

Wieck, A., Grassi-Oliveira, R., do Prado, C. H., Rizzo, L. B., de Oliveira, A. S., Kommers-Molina, J., Viola, T. W., Teixeira, A. L., & Bauer, M. E. (2013) · Brain, Behavior, and Immunity · doi:10.1016/j.bbi.2013.07.005 · Cited by 63

Vemurafenib: an evidence-based review of its clinical utility in the treatment of metastatic melanoma

Joseph, R. W., Swaika, A., & Crozier, J. A. (2014) · Drug Design Development and Therapy · doi:10.2147/dddt.s31143 · Cited by 66

Paving the way for targeting RSK in cancer

Roméo, Y., & Roux, P. P. (2010) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728222.2010.531014 · Cited by 62

Emerging biological functions of the vaccinia-related kinase (VRK) family.

Klerkx, E. P. F., Lazo, P. A., & Askjaer, P. (2009) · PubMed · doi:10.14670/hh-24.749 · Cited by 62

Molecular profiling of signalling pathways in formalin-fixed and paraffin-embedded cancer tissues

Berg, D., Hipp, S., Malinowsky, K., Böllner, C., & Becker, K. (2009) · European Journal of Cancer · doi:10.1016/j.ejca.2009.10.016 · Cited by 62

UVB Radiation Induces Apoptosis in Keratinocytes by Activating a Pathway Linked to “BLT2-Reactive Oxygen Species”

Ryu, H.-C., Kim, C.-M., Kim, J., Chung, J., & Kim, J. (2010) · Journal of Investigative Dermatology · doi:10.1038/jid.2009.436 · Cited by 62

Acute Oxidative Stress Can Reverse Insulin Resistance by Inactivation of Cytoplasmic JNK

Berdichevsky, A., Guarente, L., & Bose, A. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.093633 · Cited by 62

Time Courses of Changes in Phospho- and Total- MAP Kinases in the Cochlea after Intense Noise Exposure

Maeda, Y., Fukushima, K., Omichi, R., Kariya, S., & Nishizaki, K. (2013) · PLoS ONE · doi:10.1371/journal.pone.0058775 · Cited by 62

PKC-δ and -η, MEKK-1, MEK-6, MEK-3, and p38-δ Are Essential Mediators of the Response of Normal Human Epidermal Keratinocytes to Differentiating Agents

Adhikary, G., Chew, Y. C., Reece, E. A., & Eckert, R. L. (2010) · Journal of Investigative Dermatology · doi:10.1038/jid.2010.108 · Cited by 62

Tpl2 Kinase Is Upregulated in Adipose Tissue in Obesity and May Mediate Interleukin-1β and Tumor Necrosis Factor-α Effects on Extracellular Signal–Regulated Kinase Activation and Lipolysis

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