Mitogen activated protein kinases: a role in inflammatory bowel disease?

Association of NOD2 leucine-rich repeat variants with susceptibility to Crohn's disease

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Unravelling the pathogenesis of inflammatory bowel disease

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A protein kinase involved in the regulation of inflammatory cytokine biosynthesis

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A Genome-Wide Association Study Identifies <i>IL23R</i> as an Inflammatory Bowel Disease Gene

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Blockade of interleukin 6 trans signaling suppresses T-cell resistance against apoptosis in chronic intestinal inflammation: evidence in Crohn disease and experimental colitis in vivo

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Enhanced Th1 activity and development of chronic enterocolitis in mice devoid of Stat3 in macrophages and neutrophils

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The genetics and immunopathogenesis of inflammatory bowel disease

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NF‐κB in inflammatory bowel disease

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MAP Kinases

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MAPKAP kinase 2 is essential for LPS-induced TNF-α biosynthesis

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Defective T Cell Differentiation in the Absence of Jnk1

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Targeting dual-specificity phosphatases: Manipulating MAP kinase signalling and immune responses

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MAPKs and their relevance to arthritis and inflammation

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TNF: A master switch for inflammation to cancer

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MAPK signalling: ERK5 versus ERK1/2

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The p38 MAP kinase pathway as a therapeutic target in inflammatory disease

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p38 Mitogen-Activated Protein Kinase Is Activated and Linked to TNF-α Signaling in Inflammatory Bowel Disease

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Inhibition of stress-activated MAP kinases induces clinical improvement in moderate to severe Crohn's disease

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Lipopolysaccharide activation of the MEK-ERK1/2 pathway in human monocytic cells mediates tissue factor and tumor necrosis factor α expression by inducing Elk-1 phosphorylation and Egr-1 expression

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Activator protein 1 (Fos/Jun) functions in inflammatory bone and skin disease

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

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Requirement for Ras/Rac1-Mediated p38 and c-Jun N-Terminal Kinase Signaling in Stat3 Transcriptional Activity Induced by the Src Oncoprotein

Turkson, J., Bowman, T. L., Adnane, J., Zhang, Y., Djeu, J. Y., Sekharam, M., Frank, D. A., Holzman, L. B., Wu, J., Sebti, S. M., et al. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.11.7519 · Cited by 256 · see citing works

Anti-Inflammatory Effects of a p38 Mitogen-Activated Protein Kinase Inhibitor During Human Endotoxemia

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p38 Pathway Kinases as Anti-inflammatory Drug Targets

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The Mitogen-Activated Protein Kinase (MAPK)-Activated Protein Kinases MK2 and MK3 Cooperate in Stimulation of Tumor Necrosis Factor Biosynthesis and Stabilization of p38 MAPK

Ronkina, N., Kotlyarov, A., Dittrich‐Breiholz, O., Kracht, M., Hitti, E., Milarski, K. L., Askew, R., Marušić, S., Lin, L.-L., Gaestel, M., et al. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.01456-06 · Cited by 217 · see citing works

Inhibition of p38 MAP kinase‐and RICK/NF‐κB‐signaling suppresses inflammatory bowel disease

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Oral p38 Mitogen-Activated Protein Kinase Inhibition With BIRB 796 for Active Crohn’s Disease: A Randomized, Double-Blind, Placebo-Controlled Trial

Schreiber, S., Feagan, B. G., D’Haens, G., Colombel, J., Geboes, K. J., Yurcov, M., Va, I., Головенко, О. В., Bernstein, C. N., Ludwig, D., et al. (2006) · Clinical Gastroenterology and Hepatology · doi:10.1016/j.cgh.2005.11.013 · Cited by 186 · see citing works

Combinations of ERK and p38 MAPK Inhibitors Ablate Tumor Necrosis Factor-α (TNF-α) mRNA Induction

Rutault, K., Hazzalin, C. A., & Mahadevan, L. C. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m005486200 · Cited by 177 · see citing works

Intestinal Epithelial Cell Differentiation Involves Activation of p38 Mitogen-activated Protein Kinase That Regulates the Homeobox Transcription Factor CDX2

Houde, M., Laprise, P., Jean, D., Blais, M., Asselin, C., & Rivard, N. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m100236200 · Cited by 155 · see citing works

AIP1 mediates TNF-α–induced ASK1 activation by facilitating dissociation of ASK1 from its inhibitor 14-3-3

Zhang, R., He, X., Liu, W., Lü, M., Hsieh, J., & Wang, M. (2003) · Journal of Clinical Investigation · doi:10.1172/jci17790 · Cited by 152 · see citing works

MKP-7, a Novel Mitogen-activated Protein Kinase Phosphatase, Functions as a Shuttle Protein

Masuda, K., Shima, H., Watanabe, M., & Kikuchi, K. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m104600200 · Cited by 151 · see citing works

A Functional Role for Interleukin-21 in Promoting the Synthesis of the T-Cell Chemoattractant, MIP-3α, by Gut Epithelial Cells

Caruso, R., Fina, D., Peluso, I., Stolfi, C., Fantini, M. C., Gioia, V., Caprioli, F., Blanco, G. D. V., Paoluzi, O. A., MacDonald, T. T., et al. (2006) · Gastroenterology · doi:10.1053/j.gastro.2006.09.053 · Cited by 150 · see citing works

Inhibition of RICK/Nuclear Factor-κB and p38 Signaling Attenuates the Inflammatory Response in a Murine Model of Crohn Disease

Hollenbach, E., Vieth, M. W., Roessner, A., Neumann, M., Malfertheiner, P., & Naumann, M. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m500966200 · Cited by 149 · see citing works

Role of the JNK signal transduction pathway in inflammatory bowel disease

Roy, P. K., Rashid, F., Bragg, J. D., Ibdah, J. A., Hepatology, D. O. G. A., Columbia, Missouri, & States, U. (2008) · World Journal of Gastroenterology · doi:10.3748/wjg.14.200 · Cited by 145 · see citing works

Genome-wide Association Scanning Highlights Two Autophagy Genes,ATG16L1andIRGM, as Being Significantly Associated with Crohn’s Disease

Massey, D. C. O., & Parkes, M. (2007) · Autophagy · doi:10.4161/auto.5075 · Cited by 141 · see citing works

Both Nuclear-Cytoplasmic Shuttling of the Dual Specificity Phosphatase MKP-3 and Its Ability to Anchor MAP Kinase in the Cytoplasm Are Mediated by a Conserved Nuclear Export Signal

Karlsson, M. E., Mathers, J. E., Dickinson, R. J., Mandl, M., & Keyse, S. M. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m406720200 · Cited by 132 · see citing works

Role of STAT3 in inflammatory bowel disease

Sugimoto, K. (2008) · World Journal of Gastroenterology · doi:10.3748/wjg.14.5110 · Cited by 130 · see citing works

Rdp58 Is a Novel and Potentially Effective Oral Therapy for Ulcerative Colitis

Travis, S. P. L., Yap, L. M., Hawkey, C., Warren, B. F., Lazarov, M. E., Fong, T., & Tesi, R. J. (2005) · Inflammatory Bowel Diseases · doi:10.1097/01.mib.0000172807.26748.16 · Cited by 121 · see citing works

Crohn's disease: beyond antagonists of tumour necrosis factor

Peyrin‐Biroulet, L., Desreumaux, P., Sandborn, W. J., & Colombel, J. (2008) · The Lancet · doi:10.1016/s0140-6736(08)60995-2 · Cited by 109 · see citing works

Dichotomal role of inhibition of p38 MAPK with SB 203580 in experimental colitis

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The specific JNK inhibitor SP600125 targets tumour necrosis factor‐α production and epithelial cell apoptosis in acute murine colitis

Assi, K., Pillai, R., Gómez‐Muñoz, A., Owen, D., & Salh, B. S. (2006) · Immunology · doi:10.1111/j.1365-2567.2006.02349.x · Cited by 108 · see citing works

Effect of glucocorticoids on rectal transport in normal subjects and patients with ulcerative colitis.

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Intracellular IL-1Ra type 1 inhibits IL-1-induced IL-6 and IL-8 production in Caco-2 intestinal epithelial cells through inhibition of p38 mitogen-activated protein kinase and NF-κB pathways

Garat, C. (2003) · Cytokine · doi:10.1016/s1043-4666(03)00182-0 · Cited by 92 · see citing works

The IRAK-1-BCL10-MALT1-TRAF6-TAK1 Cascade Mediates Signaling to NF-κB from Toll-like Receptor 4

Dong, W., Liu, Y., Jinhong, P., Chen, L., Zou, T., Xiao, H., Liu, Z., Li, W., Bu, Y., & Qi, Y. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m513057200 · Cited by 92 · see citing works

Molecular effects of recombinant human interleukin-11 in the HLA-B27 rat model of inflammatory bowel disease.

Peterson, R. L., Wang, L., Albert, L. M., Keith, J. C., & Dorner, A. J. (1998) · PubMed · Cited by 91 · see citing works

ERK5 Activation Inhibits Inflammatory Responses via Peroxisome Proliferator-activated Receptor δ (PPARδ) Stimulation

Woo, C.-H., Massett, M. P., Shishido, T., Itoh, S., Ding, B., McClain, C., Che, W., Vulapalli, R., Chen, Y., & Abe, J. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m602369200 · Cited by 89 · see citing works

Nrf1 in a complex with fosB, c-jun, junD and ATF2 forms the AP1 component at the TNF promoter in stimulated mast cells

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Altered TAB1:IκB Kinase Interaction Promotes Transforming Growth Factor β–Mediated Nuclear Factor-κB Activation during Breast Cancer Progression

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Altered ENaC Expression Leads to Impaired Sodium Absorption in the Noninflamed Intestine in Crohn's Disease

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MNK kinases regulate multiple TLR pathways and innate proinflammatory cytokines in macrophages

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Epithelial: Lamina Propria Lymphocyte Interactions Promote Epithelial Cell Differentiation

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Scaffold Proteins in Mammalian MAP Kinase Cascades

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Pro-inflammatory signaling by Jun-N-terminal kinase in inflammatory bowel disease

Mitsuyama, K., Suzuki, A., Tomiyasu, N., Tsuruta, O., Kitazaki, S., Takeda, T., Satoh, Y., Bennett, B. L., Toyonaga, A., & Sata, M. (2006) · International Journal of Molecular Medicine · doi:10.3892/ijmm.17.3.449 · Cited by 71 · see citing works

Regulation of PRAK Subcellular Location by p38 MAP Kinases

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Inflammatory bowel disease: Genetic and epidemiologic considerations

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Streptococcus pneumoniae induced c-Jun-N-terminal kinase- and AP-1 -dependent IL-8 release by lung epithelial BEAS-2B cells

Schmeck, B., Moog, K., Zahlten, J., van Laak, V., N’Guessan, P. D., Opitz, B., Rosseau, S., Suttorp, N., & Hippenstiel, S. (2006) · Respiratory Research · doi:10.1186/1465-9921-7-98 · Cited by 65 · see citing works

ERK5/BMK1 Is Indispensable for Optimal Colony-Stimulating Factor 1 (CSF-1)-Induced Proliferation in Macrophages in a Src-Dependent Fashion

Rovida, E., Spinelli, E., Sdelci, S., Barbetti, V., Morandi, A., Giuntoli, S., & Sbarba, P. D. (2008) · The Journal of Immunology · doi:10.4049/jimmunol.180.6.4166 · Cited by 63 · see citing works

Compartmentalised MAPK Pathways

Brown, M. D., & Sacks, D. B. (2008) · Handbook of experimental pharmacology · doi:10.1007/978-3-540-72843-6_9 · Cited by 58 · see citing works

Dextran sulfate sodium enhances interleukin-1β release via activation of p38 MAPK and ERK1/2 pathways in murine peritoneal macrophages

Kwon, K. H., Ohigashi, H., & Murakami, A. (2007) · Life Sciences · doi:10.1016/j.lfs.2007.05.022 · Cited by 55 · see citing works

MAPK phosphatases as novel targets for rheumatoid arthritis

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PEROXISOME PROLIFERATOR-ACTIVATED RECEPTOR-α MODULATES THE ANTI-INFLAMMATORY EFFECT OF GLUCOCORTICOIDS IN A MODEL OF INFLAMMATORY BOWEL DISEASE IN MICE

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Specific Inhibition of c-Raf Activity by Semapimod Induces Clinical Remission in Severe Crohn’s Disease

Löwenberg, M., Verhaar, A. P., van den Blink, B., ten Kate, F. J. W., van Deventer, S. J. H., Peppelenbosch, M. P., & Hommes, D. W. (2005) · The Journal of Immunology · doi:10.4049/jimmunol.175.4.2293 · Cited by 46 · see citing works

Regulation of RELM/FIZZ isoform expression byCdx2in response to innate and adaptive immune stimulation in the intestine

Wang, M., Shin, M. E., Knight, P. A., Artis, D., Silberg, D. G., Suh, E. R., & Wu, G. D. (2004) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00442.2004 · Cited by 44 · see citing works

HETEs enhance IL-1-mediated COX-2 expression via augmentation of message stability in human colonic myofibroblasts

Mari, J. F. D., Saada, J. I., Mifflin, R. C., Valentich, J. D., & Powell, D. W. (2007) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00117.2007 · Cited by 43 · see citing works

Inhibitors of c-jun-N-Terminal Kinase (JNK)

LoGrasso, P. V., & Kamenecka, T. M. (2008) · Mini-Reviews in Medicinal Chemistry · doi:10.2174/138955708784912120 · Cited by 40 · see citing works

Interleukins 2 and 15 Regulate Ets1 Expression via ERK1/2 and MNK1 in Human Natural Killer Cells

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Genetic Deletion of JNK1 and JNK2 Aggravates the DSS-Induced Colitis in Mice

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Regulation of c-fos, c-jun and c-myc Gene Expression by Angiotensin II in Primary Cultured Rat Astrocytes: Role of ERK1/2 MAP Kinases

Delaney, J., Chiarello, R., Villar, D., Kandalam, U., Castejon, A. M., & Clark, M. A. (2007) · Neurochemical Research · doi:10.1007/s11064-007-9474-y · Cited by 33 · see citing works

Mechanisms of Disease: transcription factors in inflammatory arthritis

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State-of-the-art of irritable bowel syndrome and inflammatory bowel disease research in 2008

McFarland, L. V. (2008) · World Journal of Gastroenterology · doi:10.3748/wjg.14.2625 · Cited by 31 · see citing works

Rational Design and Development of RDP58

Iyer, S., Lahana, R., & Buelow, R. (2002) · Current Pharmaceutical Design · doi:10.2174/1381612023393170 · Cited by 29 · see citing works

No Evidence for an Involvement of the P38 and JNK Mitogen-Activated Protein in Inflammatory Bowel Diseases

Malamut, G., Cabane, C., Dubuquoy, L., Body–Malapel, M., Dérijard, B., Gay, J., Tamboli, C., Colombel, J., & Desreumaux, P. (2006) · Digestive Diseases and Sciences · doi:10.1007/s10620-006-9116-2 · Cited by 24 · see citing works

Differential Regulation of the Antiapoptotic Action of B-Cell Lymphoma 2 (Bcl-2) and B-Cell Lymphoma Extra Long (Bcl-xL) by c-Jun N-Terminal Protein Kinase (JNK) 1-Involved Pathway in Neuroglioma Cells

Jeong, H., Choi, H.-Y., Choi, T.-W., Kim, B., Kim, J., Lee, E.-R., & Cho, S. (2008) · Biological and Pharmaceutical Bulletin · doi:10.1248/bpb.31.1686 · Cited by 23 · see citing works

743 Rdea119, a Potent and Highly Selective MEK Inhibitor Ameliorates Murine Colitis

Miampamba, M. (2008) · Gastroenterology · doi:10.1016/s0016-5085(08)60502-8 · Cited by 5 · see citing works

Protein kinases: mechanisms and downstream targets in inflammation-mediated obesity and insulin resistance

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Involvement of MAPK/NF-κB Signaling in the Activation of the Cholinergic Anti-Inflammatory Pathway in Experimental Colitis by Chronic Vagus Nerve Stimulation

Sun, P., Zhou, K., Wang, S., Li, P., Chen, S., Lin, G., Zhao, Y., & Wang, T. (2013) · PLoS ONE · doi:10.1371/journal.pone.0069424 · Cited by 208 · see citing works

Intracellular signaling pathways of inflammation modulated by dietary flavonoids: The most recent evidence

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γ-Glutamyl cysteine and γ-glutamyl valine inhibit TNF-α signaling in intestinal epithelial cells and reduce inflammation in a mouse model of colitis via allosteric activation of the calcium-sensing receptor

Zhang, H., Kovacs-Nolan, J., Kodera, T., Eto, Y., & Mine, Y. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2014.12.023 · Cited by 186 · see citing works

MAP kinases in inflammatory bowel disease

Coskun, M., Olsen, J., Seidelin, J. B., & Nielsen, O. H. (2010) · Clinica Chimica Acta · doi:10.1016/j.cca.2010.12.020 · Cited by 173 · see citing works

Modulation of Intestinal Epithelial Permeability by Plasma from Patients with Crohn’s Disease in a Three-dimensional Cell Culture Model

Xu, P., Elamin, E. E., Elizalde, M., Bours, P. H. A., Pierik, M. J., Masclee, A., & Jonkers, D. M. A. E. (2019) · Scientific Reports · doi:10.1038/s41598-018-38322-8 · Cited by 168 · see citing works

Curcumin, an active component of turmeric in the prevention and treatment of ulcerative colitis: preclinical and clinical observations

Baliga, M. S., Joseph, N., Venkataranganna, M. V., Saxena, A., Ponemone, V., & Fayad, R. (2012) · Food & Function · doi:10.1039/c2fo30097d · Cited by 162 · see citing works

Macrophage-based nanotherapeutic strategies in ulcerative colitis

Zhang, J., Zhao, Y., Hou, T., Zeng, H., Kalambhe, D., Wang, B., Shen, X., & Huang, Y. (2020) · Journal of Controlled Release · doi:10.1016/j.jconrel.2020.01.047 · Cited by 160 · see citing works

Phytochemicals and inflammatory bowel disease: a review

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