Improving Obesity and Insulin Resistance by Targeting Skeletal Muscle MKP-1

Heart Disease and Stroke Statistics—2015 Update: A Report From the American Heart Association

Mozaffarian, D., Benjamin, E. J., Go, A. S., Arnett, D. K., Blaha, M. J., Cushman, M., de Ferranti, S., Després, J.-P., Fullerton, H. J., Howard, V. J., et al. (2015) · Circulation · doi:10.1161/cir.0000000000000152 · Cited by 5,797 · see citing works

Fiber Types in Mammalian Skeletal Muscles

Schiaffino, S., & Reggiani, C. (2011) · Physiological Reviews · doi:10.1152/physrev.00031.2010 · Cited by 3,022 · see citing works

Muscles, exercise and obesity: skeletal muscle as a secretory organ

Pedersen, B. K., & Febbraio, M. A. (2012) · Nature Reviews Endocrinology · doi:10.1038/nrendo.2012.49 · Cited by 2,909 · see citing works

Impaired Mitochondrial Activity in the Insulin-Resistant Offspring of Patients with Type 2 Diabetes

Petersen, K. F., Dufour, S., Befroy, D., Garcia, R., & Shulman, G. I. (2004) · New England Journal of Medicine · doi:10.1056/nejmoa031314 · Cited by 2,193 · see citing works

Peroxisome Proliferator-Activated Receptor-γ Coactivator 1α (PGC-1α): Transcriptional Coactivator and Metabolic Regulator

Puigserver, P., & Spiegelman, B. M. (2003) · Endocrine Reviews · doi:10.1210/er.2002-0012 · Cited by 2,076 · see citing works

Molecular Basis of Cardioprotection

Heusch, G. (2015) · Circulation Research · doi:10.1161/circresaha.116.305348 · Cited by 811 · see citing works

Exercise Stimulates Pgc-1α Transcription in Skeletal Muscle through Activation of the p38 MAPK Pathway

Akimoto, T., Pohnert, S. C., Li, P., Zhang, M., Gumbs, C., Rosenberg, P. B., Williams, R. S., & Yan, Z. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m408862200 · Cited by 714 · see citing works

Skeletal muscle inflammation and insulin resistance in obesity

Wu, H., & Ballantyne, C. M. (2017) · Journal of Clinical Investigation · doi:10.1172/jci88880 · Cited by 695 · see citing works

Obesity Epidemiology Worldwide

Arroyo, C., & Mincey, K. D. (2016) · Gastroenterology Clinics of North America · doi:10.1016/j.gtc.2016.07.012 · Cited by 588 · see citing works

Severe muscle depletion in patients on the liver transplant wait list: Its prevalence and independent prognostic value

Tandon, P., Ney, M., Irwin, I., Ma, M. M., Gramlich, L. M., Bain, V. G., Esfandiari, N., Baracos, V. E., Montaño‐Loza, A. J., & Myers, R. P. (2012) · Liver Transplantation · doi:10.1002/lt.23495 · Cited by 580 · see citing works

Dual‐specificity MAP kinase phosphatases (MKPs): Shaping the outcome of MAP kinase signalling

Caunt, C. J., & Keyse, S. M. (2013) · The FEBS Journal · doi:10.1111/j.1742-4658.2012.08716.x · Cited by 535 · see citing works

Skeletal Muscle Fiber Type: Influence on Contractile and Metabolic Properties

Zierath, J. R., & Hawley, J. A. (2004) · PLoS Biology · doi:10.1371/journal.pbio.0020348 · Cited by 518 · see citing works

Targeting cancer with kinase inhibitors

Gross, S. D., Rahal, R., Stransky, N., Lengauer, C., & Hoeflich, K. P. (2015) · Journal of Clinical Investigation · doi:10.1172/jci76094 · Cited by 442 · see citing works

JNK at the crossroad of obesity, insulin resistance, and cell stress response

Solinas, G., & Becattini, B. (2016) · Molecular Metabolism · doi:10.1016/j.molmet.2016.12.001 · Cited by 431 · see citing works

PTP1B antisense oligonucleotide lowers PTP1B protein, normalizes blood glucose, and improves insulin sensitivity in diabetic mice

Zinker, B. A., Rondinone, C. M., Trevillyan, J. M., Gum, R. J., Clampit, J. E., Waring, J. F., Xie, N., Wilcox, D. M., Jacobson, P. B., Frost, L., et al. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.142298199 · Cited by 416 · see citing works

New insights into PGC ‐1 coactivators: redefining their role in the regulation of mitochondrial function and beyond

Villena, J. A. (2014) · FEBS Journal · doi:10.1111/febs.13175 · Cited by 404 · see citing works

Altered Fiber Distribution and Fiber-Specific Glycolytic and Oxidative Enzyme Activity in Skeletal Muscle of Patients With Type 2 Diabetes

Oberbach, A., Bossenz, Y., Lehmann, S., Niebauer, J., Adams, V., Paschke, R., Schön, M. R., Blüher, M., & Punkt, K. (2006) · Diabetes Care · doi:10.2337/diacare.29.04.06.dc05-1854 · Cited by 385 · see citing works

Targeting the disordered C terminus of PTP1B with an allosteric inhibitor

Krishnan, N., Koveal, D., Miller, D. H., Xue, B., Akshinthala, S. D., Kragelj, J., Jensen, M. R., Gauss, C., Page, R., Blackledge, M. J., et al. (2014) · Nature Chemical Biology · doi:10.1038/nchembio.1528 · Cited by 378 · see citing works

Sarcopenia in cirrhosis: from pathogenesis to interventions

Ebadi, M., Bhanji, R. A., Mazurak, V. C., & Montaño‐Loza, A. J. (2019) · Journal of Gastroenterology · doi:10.1007/s00535-019-01605-6 · Cited by 298 · see citing works

Phosphorylation of Tyrosine 182 of p38 Mitogen-activated Protein Kinase Correlates with the Protection of Preconditioning in the Rabbit Heart

Weinbrenner, C., Liu, G.-S., Cohen, M. V., & Downey, J. M. (1997) · Journal of Molecular and Cellular Cardiology · doi:10.1006/jmcc.1997.0473 · Cited by 262 · see citing works

Insulin Prevents Cardiomyocytes From Oxidative Stress–Induced Apoptosis Through Activation of PI3 Kinase/ Akt

Aikawa, R., Nawano, M., Gu, Y., Katagiri, H., Asano, T., Zhu, W., Nagai, R., & Komuro, I. (2000) · Circulation · doi:10.1161/01.cir.102.23.2873 · Cited by 227 · see citing works

Slow-Twitch Fiber Proportion in Skeletal Muscle Correlates With Insulin Responsiveness

Stuart, C. A., McCurry, M. P., Marino, A., South, M. A., Howell, M. E. A., Layne, A. S., Ramsey, M. W., & Stone, M. H. (2013) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2012-3876 · Cited by 221 · see citing works

Sarcopenia is associated with severe liver fibrosis in patients with non-alcoholic fatty liver disease

Petta, S., Ciminnisi, S., Marco, V. D., Cabibi, D., Cammà, C., Licata, A., Marchesini, G., & Craxı̀, A. (2016) · Alimentary Pharmacology & Therapeutics · doi:10.1111/apt.13889 · Cited by 217 · see citing works

The effects of obesity on skeletal muscle contractile function

Tallis, J. A., James, R. S., & Seebacher, F. (2018) · Journal of Experimental Biology · doi:10.1242/jeb.163840 · Cited by 214 · see citing works

Mice lacking MAP kinase phosphatase-1 have enhanced MAP kinase activity and resistance to diet-induced obesity

Wu, J., Flach, R. J. R., Anderson, E. J., Hong, E., Lee, M., Choi, C. S., Neufer, P. D., Shulman, G. I., Kim, J. K., & Bennett, A. M. (2006) · Cell Metabolism · doi:10.1016/j.cmet.2006.05.010 · Cited by 212 · see citing works

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

Nandipati, K. C., Subramanian, S., & Agrawal, D. K. (2016) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-016-2878-8 · Cited by 210 · see citing works

Targeting Tyrosine Phosphatases: Time to End the Stigma

Stanford, S. M., & Bottini, N. (2017) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2017.03.004 · Cited by 190 · see citing works

Stimulation of Glucose Transport by AMP-activated Protein Kinase via Activation of p38 Mitogen-activated Protein Kinase

Xi, X., Han, J., & Zhang, J. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m102824200 · Cited by 182 · see citing works

Impact of Skeletal Muscle Mass on Metabolic Health

Kim, G., & Kim, J. H. (2020) · Endocrinology and Metabolism · doi:10.3803/enm.2020.35.1.1 · Cited by 171 · see citing works

cJun NH2-terminal kinase 1 (JNK1): Roles in metabolic regulation of insulin resistance

Sabio, G., & Davis, R. J. (2010) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2010.04.004 · Cited by 170 · see citing works

Dual-specificity MAP kinase phosphatases in health and disease

Seternes, O. M., Kidger, A. M., & Keyse, S. M. (2018) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2018.09.002 · Cited by 148 · see citing works

Role of Muscle c-Jun NH2-Terminal Kinase 1 in Obesity-Induced Insulin Resistance

Sabio, G., Kennedy, N. J., Cavanagh, J., Jung, D. Y., Ko, H. J., Ong, H., Barrett, T., Kim, J. K., & Davis, R. J. (2009) · Molecular and Cellular Biology · doi:10.1128/mcb.01162-09 · Cited by 144 · see citing works

Mitochondria as a Target for Mitigating Sarcopenia

Coen, P. M., Musci, R., Hinkley, J., & Miller, B. F. (2019) · Frontiers in Physiology · doi:10.3389/fphys.2018.01883 · Cited by 140 · see citing works

Inhibition of the JNK/MAPK signaling pathway by myogenesis-associated miRNAs is required for skeletal muscle development

Xie, S., Li, J., Chen, H.-F., Tan, Y.-Y., Liu, S., Zhang, Y., Xu, H. M., Yang, J., Liu, S., Zheng, L., et al. (2018) · Cell Death and Differentiation · doi:10.1038/s41418-018-0063-1 · Cited by 125 · see citing works

The roles of c‐Jun NH2‐terminal kinases (JNKs) in obesity and insulin resistance

Pál, M., Febbraio, M. A., & Lancaster, G. I. (2015) · The Journal of Physiology · doi:10.1113/jp271457 · Cited by 114 · see citing works

Relationship of sarcopenia with steatohepatitis and advanced liver fibrosis in non-alcoholic fatty liver disease: a meta-analysis

Yu, R., Shi, Q., Liu, L., & Chen, L. (2018) · BMC Gastroenterology · doi:10.1186/s12876-018-0776-0 · Cited by 94 · see citing works

Functions and Regulatory Mechanisms of lncRNAs in Skeletal Myogenesis, Muscle Disease and Meat Production

Wang, S., Jin, J., Xu, Z., & Zuo, B. (2019) · Cells · doi:10.3390/cells8091107 · Cited by 88 · see citing works

Skeletal Muscle–Specific Deletion of MKP-1 Reveals a p38 MAPK/JNK/Akt Signaling Node That Regulates Obesity-Induced Insulin Resistance

Lawan, A., Min, K., Zhang, L., Canfrán‐Duque, A., Jurczak, M. J., Camporez, J. P., Nie, Y., Gavin, T. P., Shulman, G. I., Fernandez-Hernando, C. F., et al. (2018) · Diabetes · doi:10.2337/db17-0826 · Cited by 86 · see citing works

Sarcolab pilot study into skeletal muscle’s adaptation to long-term spaceflight

Rittweger, J., Albracht, K., Flück, M., Ruoss, S., Brocca, L., Longa, E., Moriggi, M., Seynnes, O., Giulio, I. D., Tenori, L., et al. (2018) · npj Microgravity · doi:10.1038/s41526-018-0052-1 · Cited by 85 · see citing works

Hepatic Mitogen-Activated Protein Kinase Phosphatase 1 Selectively Regulates Glucose Metabolism and Energy Homeostasis

Lawan, A., Zhang, L., Gatzke, F., Min, K., Jurczak, M. J., Al‐Mutairi, M., Richter, P., Camporez, J. P., Couvillon, A. D., Pesta, D. H., et al. (2014) · Molecular and Cellular Biology · doi:10.1128/mcb.00503-14 · Cited by 84 · see citing works

Tissue-selective therapy of cancer

Blagosklonny, M. V. (2003) · British Journal of Cancer · doi:10.1038/sj.bjc.6601256 · Cited by 83 · see citing works

Modulation of skeletal muscle fiber type by mitogen‐activated protein kinase signaling

Shi, H., Scheffler, J. M., Pleitner, J. M., Zeng, C., Park, S., Hannon, K., Grant, A. L., & Gerrard, D. E. (2008) · The FASEB Journal · doi:10.1096/fj.07-097600 · Cited by 82 · see citing works

Sarcopenia in Cirrhosis: Looking Beyond the Skeletal Muscle Loss to See the Systemic Disease

Bhanji, R. A., Montaño‐Loza, A. J., & Watt, K. D. S. (2019) · Hepatology · doi:10.1002/hep.30686 · Cited by 82 · see citing works

Diversity and specificity of the mitogen-activated protein kinase phosphatase-1 functions

Lawan, A., Shi, H., Gatzke, F., & Bennett, A. M. (2012) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-012-1041-2 · Cited by 81 · see citing works

Stress kinases in the modulation of metabolism and energy balance

Manieri, E., & Sabio, G. (2015) · Journal of Molecular Endocrinology · doi:10.1530/jme-15-0146 · Cited by 80 · see citing works

Mitogen-Activated Protein Kinase (MAPK) and Obesity-Related Cancer

Donohoe, F., Wilkinson, M., Baxter, E., & Brennan, D. J. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21041241 · Cited by 79 · see citing works

Myocardial injury and protection related to cardiopulmonary bypass

Hert, S. G. D., & Moerman, A. (2015) · Best practice & research. Clinical anaesthesiology · doi:10.1016/j.bpa.2015.03.002 · Cited by 73 · see citing works

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 · see citing works

MAP kinase phosphatase DUSP1 is overexpressed in obese humans and modulated by physical exercise

Khadir, A., Tiss, A., Abubaker, J. A., Abu‐Farha, M., Al‐Khairi, I., Cherian, P., John, J., Kavalakatt, S., Warsame, S., Madhoun, A. S. A., et al. (2014) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00577.2013 · Cited by 60 · see citing works

p38 MAPK activation upregulates proinflammatory pathways in skeletal muscle cells from insulin-resistant type 2 diabetic patients

Brown, A. E., Palsgaard, J., Borup, R., Avery, P. J., Gunn, D. A., MEYTS, P. D., Yeaman, S. J., & Walker, M. (2014) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00115.2014 · Cited by 52 · see citing works

MAP kinase phosphatase‐1 deficiency impairs skeletal muscle regeneration and exacerbates muscular dystrophy

Shi, H., Boadu, E., Mercan, F., Le, A. M., Flach, R. J. R., Zhang, L., Tyner, K. J., Olwin, B. B., & Bennett, A. M. (2010) · The FASEB Journal · doi:10.1096/fj.09-150045 · Cited by 49 · see citing works

Shp2 protein tyrosine phosphatase inhibitor activity of estramustine phosphate and its triterpenoid analogs

Scott, L. M., Chen, L., Daniel, K. G., Brooks, W. H., Guida, W. C., Lawrence, H. R., Sebti, S. M., Lawrence, N. J., & Wu, J. (2010) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2010.11.117 · Cited by 48 · see citing works

Insulin resistance affects the cytoprotective effect of insulin in cardiomyocytes through an impairment of MAPK phosphatase-1 expression

Morisco, C., Marrone, C., Trimarco, V., Crispo, S., Monti, M. G., Sadoshima, J., & Trimarco, B. (2007) · Cardiovascular Research · doi:10.1016/j.cardiores.2007.07.012 · Cited by 45 · see citing works

PTP1B antisense-treated mice show regulation of genes involved in lipogenesis in liver and fat

Waring, J. F., Ciurlionis, R., Clampit, J. E., Morgan, S. J., Gum, R. J., Jolly, R. A., Kroeger, P., Frost, L., Trevillyan, J. M., Zinker, B. A., et al. (2003) · Molecular and Cellular Endocrinology · doi:10.1016/s0303-7207(03)00008-x · Cited by 44 · see citing works

Inhibition of cellular Shp2 activity by a methyl ester analog of SPI-112

Chen, L., Pernazza, D., Scott, L. M., Lawrence, H. R., Ren, Y., Luo, Y., Wu, X., Sung, S., Guida, W. C., Sebti, S. M., et al. (2010) · Biochemical Pharmacology · doi:10.1016/j.bcp.2010.05.019 · Cited by 43 · see citing works

Targeting Mitogen-Activated Protein Kinase Phosphatase-1 (MKP-1): Structure-Based Design of MKP-1 Inhibitors and Upregulators

Doddareddy, M. R., Rawling, T., & Ammit, A. J. (2012) · Current Medicinal Chemistry · doi:10.2174/092986712803414196 · Cited by 38 · see citing works

Recovery from 6‐month spaceflight at the International Space Station: muscle‐related stress into a proinflammatory setting

Capri, M., Morsiani, C., Santoro, A., Moriggi, M., Conte, M., Martucci, M., Bellavista, E., Fabbri, C., Giampieri, E., Albracht, K., et al. (2019) · The FASEB Journal · doi:10.1096/fj.201801625r · Cited by 36 · see citing works

Dexamethasone-induced cardioprotection: A role for the phosphatase MKP-1?

Fan, W.-J., Genade, S., Genis, A., Huisamen, B., & Lochner, A. (2009) · Life Sciences · doi:10.1016/j.lfs.2009.03.014 · Cited by 28 · see citing works

Mitogen-activated protein kinase phosphatase-1 – a potential therapeutic target in metabolic disease

Flach, R. J. R., & Bennett, A. M. (2010) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728222.2010.528395 · Cited by 25 · see citing works

An allosteric site on MKP5 reveals a strategy for small-molecule inhibition

Gannam, Z. T. K., Min, K., Shillingford, S. R., Zhang, L., Herrington, J. B., Abriola, L., Gareiss, P. C., Pantouris, G., Tzouvelekis, A., Kaminski, N., et al. (2020) · Science Signaling · doi:10.1126/scisignal.aba3043 · Cited by 21 · see citing works

Mitogen-activated protein kinase phosphatase-1: function and regulation in bone and related tissues

Broome, D. T., & Datta, N. S. (2016) · Connective Tissue Research · doi:10.3109/03008207.2015.1125480 · Cited by 14 · see citing works

Crystal structure of the human dual specificity phosphatase 1 catalytic domain

Gumpena, R., Lountos, G. T., Raran‐Kurussi, S., Tropea, J. E., Cherry, S., & Waugh, D. S. (2017) · Protein Science · doi:10.1002/pro.3328 · Cited by 13 · see citing works

Special Issue: Protein Phosphatases: From Molecules to Networks

Tonks, N. K. (2012) · FEBS Journal · doi:10.1111/febs.12098 · Cited by 12 · see citing works

Parathyroid hormone-related peptide protects cardiomyocytes from oxidative stress-induced cell death: First evidence of a novel endocrine–cardiovascular interaction

Datta, N. S., Chukkapalli, S., Vengalil, N., Zhan, E., Przyklenk, K., & Lasley, R. D. (2015) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2015.10.130 · Cited by 9 · see citing works

Restructuring a State Nutrition Education and Obesity Prevention Program: Implications of a Local Health Department Model for SNAP-Ed

Wu, H., Backman, D. R., & Kizer, K. W. (2016) · Journal of Public Health Management and Practice · doi:10.1097/phh.0000000000000457 · Cited by 9 · see citing works

The Role of MKP-1 in Insulin-Induced Cardioprotection

Webster, I., Smith, A., Lochner, A., & Huisamen, B. (2017) · Cardiovascular Drugs and Therapy · doi:10.1007/s10557-017-6731-4 · Cited by 8 · see citing works

Tissue-Specific Delivery of Oligonucleotides

Xia, X., Pollock, N., Zhou, J., & Rossi, J. J. (2019) · Methods in molecular biology · doi:10.1007/978-1-4939-9670-4_2 · Cited by 7 · see citing works

Reactive Oxygen Species, Toxicity, Oxidative Stress, and Antioxidants: Chronic Diseases and Aging

Jomova, K., Raptova, R., Alomar, S. Y., Alwasel, S. H., Nepovimova, E., Kuca, K., & Valko, M. (2023) · Archives of Toxicology · doi:10.1007/s00204-023-03562-9 · Cited by 2,638 · see citing works

MAPK phosphatase 1 inhibition of p38α within lung myofibroblasts is essential for spontaneous fibrosis resolution

Fortier, S. M., Walker, N., Penke, L. R. K., Baas, J. D., Shen, Q., Speth, J. M., Huang, S. K., Zemans, R. L., Bennett, A. M., & Peters-Golden, M. L. (2024) · Journal of Clinical Investigation · doi:10.1172/jci172826 · Cited by 37 · see citing works

Mitogen-Activated Protein Kinase Phosphatases: No Longer Undruggable?

Shillingford, S. R., & Bennett, A. M. (2023) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-051921-121923 · Cited by 22 · see citing works

Protein Tyrosine Phosphatases in Metabolism: A New Frontier for Therapeutics

Bennett, A. M., & Tiganis, T. (2024) · Annual Review of Physiology · doi:10.1146/annurev-physiol-022724-105540 · Cited by 12 · see citing works

p38α MAPK Regulation of Energy Metabolism in Skeletal Muscle Offers a Therapeutic Path for Type 2 Diabetes

Bengal, E., & Aviram, S. (2025) · Cells · doi:10.3390/cells14161277 · Cited by 10 · see citing works

Fasting-Induced Upregulation of MKP-1 Modulates the Hepatic Response to Feeding

Sellers, J., Brooks, A., Fernando, S., Westenberger, G., Junkins, S., Smith, S., Min, K., & Lawan, A. (2021) · Nutrients · doi:10.3390/nu13113941 · Cited by 10 · see citing works

MAP kinase phosphatases in metabolic diseases

Hota, A., & Bennett, A. M. (2025) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2025.05.002 · Cited by 7 · see citing works

Oxidative Stress and Pathophysiology of Chronic Disease

Balaji, S., Pandian, M. S., Ganesamoorthy, R., Parameswari, R., & Babujanarthanam, R. (2026) · Springer eBooks · doi:10.1007/978-981-96-9670-3_3

Skeletal Muscle–Specific Deletion of MKP-1 Reveals a p38 MAPK/JNK/Akt Signaling Node That Regulates Obesity-Induced Insulin Resistance

Lawan, A., Min, K., Zhang, L., Canfrán‐Duque, A., Jurczak, M. J., Camporez, J. P., Nie, Y., Gavin, T. P., Shulman, G. I., Fernandez-Hernando, C. F., et al. (2018) · Diabetes · doi:10.2337/db17-0826 · Cited by 86 · see citing works

Metabolic Impact of MKP-2 Upregulation in Obesity Promotes Insulin Resistance and Fatty Liver Disease

Fernando, S., Sellers, J., Smith, S., Bhogoju, S., Junkins, S., Welch, M., Willoughby, O. S., Ghimire, N., Secunda, C., Barmanova, M., et al. (2022) · Nutrients · doi:10.3390/nu14122475 · Cited by 20 · see citing works

MKP‐2 Deficiency Improves Insulin Sensitivity and Protects Against Fatty Liver Disease

Lawan, A. (2022) · The FASEB Journal · doi:10.1096/fasebj.2022.36.s1.l8125

Treatment of Obese Insulin-Resistant Mice With an Allosteric MAPKAPK2/3 Inhibitor Lowers Blood Glucose and Improves Insulin Sensitivity

Özcan, L., Xu, X., Deng, S., Ghorpade, D. S., Thomas, T. A., Cremers, S., Hubbard, B. K., Serrano‐Wu, M. H., Gaestel, M., Landry, D. W., et al. (2015) · Diabetes · doi:10.2337/db14-1945 · Cited by 35 · see citing works

Insulin Resistance and Improvements in Signal Transduction

Musi, N., & Goodyear, L. J. (2006) · Endocrine · doi:10.1385/endo:29:1:73 · Cited by 103 · see citing works