The DOI matches its Crossref record; 43 of the 44 references it cites were found in a registry or an index.
SOCS-1 and SOCS-3 Block Insulin Signaling by Ubiquitin-mediated Degradation of IRS1 and IRS2
Open accessAbstract
Inflammation associates with peripheral insulin resistance, which dysregulates nutrient homeostasis and leads to diabetes. Inflammation induces the expression of SOCS proteins. We show that SOCS1 or SOCS3 targeted IRS1 and IRS2, two critical signaling molecules for insulin action, for ubiquitin-mediated degradation. SOCS1 or SOCS3 bound both recombinant and endogenous IRS1 and IRS2 and promoted their ubiquitination and subsequent degradation in multiple cell types. Mutations in the conserved SOCS box of SOCS1 abrogated its interaction with the elongin BC ubiquitin-ligase complex without affecting its binding to IRS1 or IRS2. The SOCS1 mutants also failed to promote the ubiquitination and degradation of either IRS1 or IRS2. Adenoviral-mediated expression of SOCS1 in mouse liver dramatically reduced hepatic IRS1 and IRS2 protein levels and caused glucose intolerance; by contrast, expression of the SOCS1 mutants had no effect. Thus, SOCS-mediated degradation of IRS proteins, presumably via the elongin BC ubiquitin-ligase, might be a general mechanism of inflammation-induced insulin resistance, providing a target for therapy.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“obesity-related insulin resistance could result from a diminution in insulin receptor substrate-1 (IRS-1) in animals, secondary to an increase in suppressor of cytokine signaling 3 (SOCS-3), which binds to IRS-1 and leads to its ubiquitylation and proteolysis in experimental animals [5]”
From Bariatric surgery: remission of inflammation, cardiometabolic benefits, and common adverse effects (2020) · cites this paper as [5]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Obesity and insulin resistance
Kahn, B. B., & Flier, J. S. (2000) · Journal of Clinical Investigation · doi:10.1172/jci10842 · Cited by 3,345
Role of Brain Insulin Receptor in Control of Body Weight and Reproduction
Brüning, J. C., Gautam, D., Burks, D. J., Gillette, J., Schubert, M., Orban, P. C., Klein, R., Krone, W., Müller-Wieland, D., & Kahn, C. R. (2000) · Science · doi:10.1126/science.289.5487.2122 · Cited by 2,235
Yuan, M., Konstantopoulos, N., Lee, J., Hansen, L., Li, Z.-W., Karin, M., & Shoelson, S. E. (2001) · Science · doi:10.1126/science.1061620 · Cited by 1,884
Disruption of IRS-2 causes type 2 diabetes in mice
Withers, D. J., Gutierrez, J. S., Towery, H. H., Burks, D. J., Ren, J., Previs, S. F., Zhang, Y., Bernal, D., Pons, S., Shulman, G. I., et al. (1998) · Nature · doi:10.1038/36116 · Cited by 1,775
Insulin resistance and cardiovascular disease
Ginsberg, H. N. (2000) · Journal of Clinical Investigation · doi:10.1172/jci10762 · Cited by 1,372
Aguirre, V., Werner, E. D., Giraud, J., Lee, Y. H., Shoelson, S. E., & White, M. F. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m101521200 · Cited by 1,010
Shimomura, I., Matsuda, M., Hammer, R. E., Bashmakov, Y. K., Brown, M. S., & Goldstein, J. L. (2000) · Molecular Cell · doi:10.1016/s1097-2765(05)00010-9 · Cited by 860
SOCS Proteins: Negative Regulators of Cytokine Signaling
Krebs, D. L., & Hilton, D. J. (2001) · Stem Cells · doi:10.1634/stemcells.19-5-378 · Cited by 826
New Perspectives into the Molecular Pathogenesis and Treatment of Type 2 Diabetes
Saltiel, A. R. (2001) · Cell · doi:10.1016/s0092-8674(01)00239-2 · Cited by 688
Zhang, J., Farley, A., Nicholson, S. E., Willson, T. A., Zugaro, L. M., Simpson, R. J., Moritz, R. L., Cary, D., Richardson, R. T., Hausmann, G., et al. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.5.2071 · Cited by 626
Flagged first, then by citations
1 of the 44 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
Items 101–200 of 899
Jojima, T., Tomotsune, T., Iijima, T., Akimoto, K., Suzuki, K., & Aso, Y. (2016) · Diabetology & Metabolic Syndrome · doi:10.1186/s13098-016-0169-x · Cited by 205
Rieusset, J., Bouzakri, K., Chevillotte, E., Ricard, N., Jacquet, D., Bastard, J.-P., Laville, M., & Vidal, H. (2004) · Diabetes · doi:10.2337/diabetes.53.9.2232 · Cited by 200
Resistin- and Obesity-associated Metabolic Diseases
Lazar, M. A. (2007) · Hormone and Metabolic Research · doi:10.1055/s-2007-985897 · Cited by 201
Glycaemic control in type 2 diabetes: Targets and new therapies
Tahrani, A. A., Piya, M. K., Kennedy, A., & Barnett, A. H. (2009) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2009.11.001 · Cited by 190
Nakao, R., Hirasaka, K., Goto, J., Ishidoh, K., Yamada, C., Ohno, A., Okumura, Y., Nonaka, I., Yasutomo, K., Baldwin, K. M., et al. (2009) · Molecular and Cellular Biology · doi:10.1128/mcb.01347-08 · Cited by 194
Regulation of the O-Linked β-N-Acetylglucosamine Transferase by Insulin Signaling
Whelan, S. A., Lane, M. D., & Hart, G. W. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m800677200 · Cited by 186
AgRP/NPY and POMC neurons in the arcuate nucleus and their potential role in treatment of obesity
Vohra, M. S., Benchoula, K., Serpell, C. J., & Wong, E. H. (2021) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2021.174611 · Cited by 199
SOCS proteins in development and disease.
Trengove, M. C., & Ward, A. C. (2013) · Europe PMC (PubMed Central) · Cited by 185
Negative Regulation of Growth Hormone Receptor Signaling
Flores‐Morales, A., Greenhalgh, C. J., Norstedt, G., & Rico-Bautista, E. (2005) · Molecular Endocrinology · doi:10.1210/me.2005-0170 · Cited by 184
Effects of growth hormone on glucose metabolism and insulin resistance in human
Kim, S.-H., & Park, M.-J. (2017) · Annals of Pediatric Endocrinology & Metabolism · doi:10.6065/apem.2017.22.3.145 · Cited by 181
Impaired insulin signalling and allostatic load in Alzheimer disease
Felice, F. G. D., Gonçalves, R. A., & Ferreira, S. T. (2022) · Nature reviews. Neuroscience · doi:10.1038/s41583-022-00558-9 · Cited by 183
Kapitulnik, J., & Maines, M. D. (2009) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2008.12.003 · Cited by 178
The ubiquitin system, disease, and drug discovery
Petroski, M. D. (2008) · BMC Biochemistry · doi:10.1186/1471-2091-9-s1-s7 · Cited by 184
Interleukin-6 does/does not have a beneficial role in insulin sensitivity and glucose homeostasis
Pedersen, B. K., & Febbraio, M. A. (2006) · Journal of Applied Physiology · doi:10.1152/japplphysiol.01208.2006 · Cited by 181
Mechanisms of chronic JAK-STAT3-SOCS3 signaling in obesity
Wunderlich, C. M., Hövelmeyer, N., & Wunderlich, F. T. (2013) · JAK-STAT · doi:10.4161/jkst.23878 · Cited by 176
The many faces of the SOCS box
Piessevaux, J., Lavens, D., Peelman, F., & Tavernier, J. H. (2008) · Cytokine & Growth Factor Reviews · doi:10.1016/j.cytogfr.2008.08.006 · Cited by 183
Duan, C., Li, M., & Rui, L. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m408495200 · Cited by 177
The interaction of metabolic factors with HCV infection: Does it matter?
Bugianesi, E., Salomone, F., & Negro, F. (2012) · Journal of Hepatology · doi:10.1016/s0168-8278(12)60007-5 · Cited by 176
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
Insulin Resistance and Cancer: In Search for a Causal Link
CHIEFARI, E. D., Mirabelli, M., Vignera, S. L., Tanyolaç, S., FOTI, D. P., Aversa, A., & Brunetti, A. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222011137 · Cited by 180
Dominici, F. P., Argentino, D. P., Muñoz, M. C., Miquet, J. G., Sotelo, A. I., & Turyn, D. (2005) · Growth Hormone & IGF Research · doi:10.1016/j.ghir.2005.07.001 · Cited by 169
Insulin Resistance in Patients with Chronic Kidney Disease
Liao, M.-T., Sung, C., Hung, K.-C., Wu, C., Lo, L., & Lu, K. (2012) · BioMed Research International · doi:10.1155/2012/691369 · Cited by 180
Inhibition of IKKɛ and TBK1 Improves Glucose Control in a Subset of Patients with Type 2 Diabetes
Oral, E. A., Reilly, S. M., Gomez, A. V., Meral, R., Butz, L., Ajluni, N., Chenevert, T. L., Korytnaya, E., Neidert, A., HENCH, R. P., et al. (2017) · Cell Metabolism · doi:10.1016/j.cmet.2017.06.006 · Cited by 165
White, M. F. (2006) · Canadian Journal of Physiology and Pharmacology · doi:10.1139/y06-008 · Cited by 164
Dandona, P., Ghanim, H., Chaudhuri, A., Dhindsa, S., & Kim, S. S. (2010) · Experimental & Molecular Medicine · doi:10.3858/emm.2010.42.4.033 · Cited by 166
Negative regulation of cytokine signaling and immune responses by SOCS proteins.
Yoshimura, A., Nishinakamura, H., Matsumura, Y., & Hanada, T. (2005) · Arthritis Research · doi:10.1186/ar1741 · Cited by 165
The ubiquitin–proteasome system in kidney physiology and disease
Meyer‐Schwesinger, C. (2019) · Nature Reviews Nephrology · doi:10.1038/s41581-019-0148-1 · Cited by 164
Hypothalamic inflammation: a double‐edged sword to nutritional diseases
Cai, D., & Liu, T. (2011) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2011.06388.x · Cited by 162
Ko, H. J., Zhang, Z., Jung, D. Y., Jun, J. Y., Ma, Z., Jones, K. E., Chan, S. Y., & Kim, J. K. (2009) · Diabetes · doi:10.2337/db08-1361 · Cited by 160
Lerner‐Marmarosh, N., Shen, J. Y., Torno, M. D., Kravets, A., Hu, Z., & Maines, M. D. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0502173102 · Cited by 157
Cellular Stresses and Stress Responses in the Pathogenesis of Insulin Resistance
Onyango, A. N. (2018) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2018/4321714 · Cited by 168
Sands, W. A., Woolson, H. D., Milne, G. R., Rutherford, C. L., & Palmer, T. M. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.00207-06 · Cited by 156
Identification of MUP1 as a Regulator for Glucose and Lipid Metabolism in Mice
Zhou, Y., Jiang, L., & Rui, L. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m900754200 · Cited by 154
Insulin resistance, adiponectin, cytokines in NASH: Which is the best target to treat?
Larter, C. Z., & Farrell, G. C. (2005) · Journal of Hepatology · doi:10.1016/j.jhep.2005.11.030 · Cited by 155
The SCF-Fbxo40 Complex Induces IRS1 Ubiquitination in Skeletal Muscle, Limiting IGF1 Signaling
Shi, J., Luo, L., Eash, J. K., Ibebunjo, C., & Glass, D. J. (2011) · Developmental Cell · doi:10.1016/j.devcel.2011.09.011 · Cited by 153
A human multi-lineage hepatic organoid model for liver fibrosis
Guan, Y., Enejder, A., Wang, M., Fang, Z., Cui, L., Chen, S.-Y., Wang, J., Tan, Y., Wu, M., Chen, X., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-26410-9 · Cited by 149
Suppressors of Cytokine Signaling 4 and 5 Regulate Epidermal Growth Factor Receptor Signaling
Kario, E., Marmor, M. D., Adamsky, K., Citri, A., Amit, I., Amariglio, N., Rechavi, G., & Yarden, Y. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m408575200 · Cited by 149
Deletion of Skeletal Muscle SOCS3 Prevents Insulin Resistance in Obesity
Jørgensen, S. B., O’Neill, H. M., Sylow, L., Honeyman, J. E., Hewitt, K. A., Palanivel, R., Fullerton, M. D., Öberg, L., Balendran, A., Galić, S., et al. (2012) · Diabetes · doi:10.2337/db12-0443 · Cited by 152
Epigenetic associations of type 2 diabetes and BMI in an Arab population
Al‐Muftah, W., Al-Shafai, M. N., Zaghlool, S. B., Visconti, A., Tsai, P.-C., Kumar, P., Spector, T. D., Bell, J. T., Falchi, M., & Suhre, K. (2016) · Clinical Epigenetics · doi:10.1186/s13148-016-0177-6 · Cited by 148
SOCS2 Can Enhance Interleukin-2 (IL-2) and IL-3 Signaling by Accelerating SOCS3 Degradation
Tannahill, G. M., Elliott, J., Barry, A. C., Hibbert, L., Cacalano, N. A., & Johnston, J. A. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.20.9115-9126.2005 · Cited by 148
Metabolic Syndrome and Robustness Tradeoffs
Kitano, H., Oda, K., Kimura, T., Matsuoka, Y., CSETE, M. E., Doyle, J. C., & Muramatsu, M. (2004) · Diabetes · doi:10.2337/diabetes.53.suppl_3.s6 · Cited by 148
Babon, J. J., Sabo, J. K., Zhang, J., Nicola, N. A., & Norton, R. S. (2009) · Journal of Molecular Biology · doi:10.1016/j.jmb.2009.01.024 · Cited by 146
SOCS proteins causing trouble in insulin action
Lebrun, P., & OBBERGHEN, E. V. (2007) · Acta Physiologica · doi:10.1111/j.1748-1716.2007.01782.x · Cited by 142
Benomar, Y., Naour, N., Aubourg, A., Bailleux, V., Gertler, A., Djiane, J., Guerre-Millo, M., & Taouis, M. (2006) · Endocrinology · doi:10.1210/en.2005-1464 · Cited by 142
Briaud, I., Dickson, L. M., Lingohr, M. K., McCuaig, J., Lawrence, J., & Rhodes, C. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m412179200 · Cited by 131
Improved glucose homeostasis and enhanced insulin signalling in Grb14‐deficient mice
Cooney, G. J., Lyons, R. J., Crew, A. J., Jensen, T. E., Molero, J. C., Mitchell, C. J., Biden, T. J., Ormandy, C. J., James, D. E., & Daly, R. J. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600082 · Cited by 132
Innate Immune Cells in the Adipose Tissue in Health and Metabolic Disease
Michailidou, Z., Gomez-Salazar, M. A., & Alexaki, V. I. (2021) · Journal of Innate Immunity · doi:10.1159/000515117 · Cited by 143
Winer, S., & Winer, D. A. (2012) · Immunology and Cell Biology · doi:10.1038/icb.2011.110 · Cited by 141
Yadav, A. K., Kalita, A., Dhillon, S., & Banerjee, K. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m501316200 · Cited by 139
Mechanisms regulating phosphoinositide 3‐kinase signalling in insulin‐sensitive tissues
Shepherd, P. R. (2005) · Acta Physiologica Scandinavica · doi:10.1111/j.1365-201x.2004.01382.x · Cited by 132
Miao, T., Wu, D., Zhang, Y., Bo, X., Subang, M. C., Wang, P., & Richardson, P. M. (2006) · Journal of Neuroscience · doi:10.1523/jneurosci.2160-06.2006 · Cited by 131
Interleukin-1 beta targeted therapy for type 2 diabetes
Maedler, K., Dharmadhikari, G., Schumann, D., & Størling, J. (2009) · Expert Opinion on Biological Therapy · doi:10.1517/14712590903136688 · Cited by 132
Chronic kidney disease-induced muscle atrophy: Molecular mechanisms and promising therapies
Wang, K., Liu, Q., Tang, M., Qi, G., Qiu, C., Huang, Y. H., Yu, W., Wang, W., Sun, H., Ni, X., et al. (2022) · Biochemical Pharmacology · doi:10.1016/j.bcp.2022.115407 · Cited by 145
Regulation of the immune system by SOCS family adaptor proteins
Ilangumaran, S., Ramanathan, S., & Rottapel, R. K. (2004) · Seminars in Immunology · doi:10.1016/j.smim.2004.08.015 · Cited by 128
Bullock, A. N., Rodríguez, M. C., Debreczeni, J. E., Songyang, Z., & Knapp, S. (2007) · Structure · doi:10.1016/j.str.2007.09.016 · Cited by 131
Disruption of the SH2-B Gene Causes Age-Dependent Insulin Resistance and Glucose Intolerance
Duan, C., Yang, H., White, M. F., & Rui, L. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.17.7435-7443.2004 · Cited by 127
Morino, K., Neschen, S., Bilz, S., Sono, S., Tsirigotis, D., Reznick, R. M., Moore, I., Nagai, Y., Samuel, V., Sebastian, D., et al. (2008) · Diabetes · doi:10.2337/db06-0454 · Cited by 125
Self-citationMashili, F. L., Chibalin, A., Krook, A., & Zierath, J. R. (2012) · Diabetes · doi:10.2337/db12-0337 · Cited by 128
Viral Exploitation of Host SOCS Protein Functions
Akhtar, L. N., & Benveniste, E. N. (2010) · Journal of Virology · doi:10.1128/jvi.01857-10 · Cited by 123
Leptin Impairs Insulin Signaling in Rat Adipocytes
Pérez, C., Fernández‐Galaz, C., Fernández‐Agulló, T., Arribas, C., Andrés, A., Ros, M., & Carrascosa, J. M. (2004) · Diabetes · doi:10.2337/diabetes.53.2.347 · Cited by 132
Siddiqui, J. A., Pothuraju, R., Jain, M., Batra, S. K., & Nasser, M. W. (2020) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2020.188359 · Cited by 126
Molecular mechanisms of insulin receptor substrate protein‐mediated modulation of insulin signalling
Johnston, A., Pirola, L., & OBBERGHEN, E. V. (2003) · FEBS Letters · doi:10.1016/s0014-5793(03)00438-1 · Cited by 123
IL-22-mediated liver cell regeneration is abrogated by SOCS-1/3 overexpression in vitro
Brand, S., Dambacher, J., Beigel, F., Zitzmann, K., Heeg, M. H. J., Weiß, T. S., Prüfer, T., Olszak, T., Steib, C. J., Storr, M., et al. (2007) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00239.2006 · Cited by 126
Engineering the IL ‐4/ IL ‐13 axis for targeted immune modulation
Bernstein, Z. J., Shenoy, A., Chen, A. Y.-C., Heller, N. M., & Spangler, J. B. (2023) · Immunological Reviews · doi:10.1111/imr.13230 · Cited by 127
Growth, growth factors and diabetes
Chiarelli, F., Giannini, C., & Mohn, A. (2004) · European Journal of Endocrinology · doi:10.1530/eje.0.151u109 · Cited by 125
The SOCS box—Adapting proteins for ubiquitination and proteasomal degradation
Linossi, E. M., & Nicholson, S. E. (2012) · IUBMB Life · doi:10.1002/iub.1011 · Cited by 122
Fuentes, L., Rőszer, T., & Ricote, M. (2010) · Mediators of Inflammation · doi:10.1155/2010/219583 · Cited by 122
Ishii, M., Maeda, A., Tani, S., & Akagawa, M. (2014) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2014.12.009 · Cited by 118
Tyrosine Phosphorylation Disrupts Elongin Interaction and Accelerates SOCS3 Degradation
Haan, S., FERGUSON, P. W., Sommer, U., Hiremath, M. M., McVicar, D. W., Heinrich, P. C., Johnston, J. A., & Cacalano, N. A. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m303170200 · Cited by 119
ASB proteins interact with Cullin5 and Rbx2 to form E3 ubiquitin ligase complexes
Kohroki, J., Nishiyama, T., Nakamura, T., & Masuho, Y. (2005) · FEBS Letters · doi:10.1016/j.febslet.2005.11.016 · Cited by 117
Shi, H., Cave, B. J., Inouye, K., Bjørbæk, C., & Flier, J. S. (2006) · Diabetes · doi:10.2337/diabetes.55.03.06.db05-0841 · Cited by 117
Functional Cross-modulation between SOCS Proteins Can Stimulate Cytokine Signaling
Piessevaux, J., Lavens, D., Montoye, T., Wauman, J., Catteeuw, D., Vandekerckhove, J. S., Belsham, D. D., Peelman, F., & Tavernier, J. H. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m600776200 · Cited by 116
Borniger, J. C., Walker, W. H., Surbhi, Emmer, K. M., Zhang, N., Zalenski, A. A., Muscarella, S. L., Fitzgerald, J. A., Smith, A. N., Braam, C. J., et al. (2018) · Cell Metabolism · doi:10.1016/j.cmet.2018.04.021 · Cited by 114
The multi‐faceted cross‐talk between the insulin and angiotensin II signaling systems
Velloso, L. A., Folli, F. B., Perego, L., & Saad, M. J. A. (2006) · Diabetes/Metabolism Research and Reviews · doi:10.1002/dmrr.611 · Cited by 113
The role of ubiquitin–proteasome system in ageing
Lőw, P. (2011) · General and Comparative Endocrinology · doi:10.1016/j.ygcen.2011.02.005 · Cited by 114
SOCS1: a potent and multifaceted regulator of cytokines and cell‐mediated inflammation
Davey, G. M., Heath, W. R., & Starr, R. (2005) · Tissue Antigens · doi:10.1111/j.1399-0039.2005.00532.x · Cited by 119
Molecular mechanisms of insulin resistance in chronic kidney disease
Thomas, S. S., Zhang, L., & Mitch, W. E. (2015) · Kidney International · doi:10.1038/ki.2015.305 · Cited by 121
The dual function of hepatic SOCS3 in insulin resistance in vivo
Torisu, T., Sato, N., Yoshiga, D., Kobayashi, T., Yoshioka, T., Mori, H., Iida, M., & Yoshimura, A. (2007) · Genes to Cells · doi:10.1111/j.1365-2443.2007.01044.x · Cited by 118
Zhou, H., Miki, R., Eeva, M., Fike, F. M., Seligson, D. B., Yang, L., Yoshimura, A., Teitell, M. A., Jamieson, C., & Cacalano, N. A. (2007) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-06-2303 · Cited by 109
He, J., Usui, I., Ishizuka, K., Kanatani, Y., Hiratani, K., Iwata, M., Bukhari, A., Haruta, T., Sasaoka, T., & Kobayashi, M. (2005) · Molecular Endocrinology · doi:10.1210/me.2005-0107 · Cited by 111
Out of Control: The Role of the Ubiquitin Proteasome System in Skeletal Muscle during Inflammation
Haberecht-Müller, S., Krüger, E., & Fielitz, J. (2021) · Biomolecules · doi:10.3390/biom11091327 · Cited by 108
MiR-155 Enhances Insulin Sensitivity by Coordinated Regulation of Multiple Genes in Mice
Lin, X., Qin, Y., Jia, J.-S., Lin, T., Lin, X., Chen, L., Zeng, H., Han, Y., Wu, L., Huang, S., et al. (2016) · PLoS Genetics · doi:10.1371/journal.pgen.1006308 · Cited by 107
Salminen, A., Kaarniranta, K., & Kauppinen, A. (2021) · Inflammation Research · doi:10.1007/s00011-021-01498-3 · Cited by 115
Collino, M., Aragno, M., Castiglia, S., Miglio, G., Tomasinelli, C. E., Boccuzzi, G., Thiemermann, C., & Fantozzi, R. (2010) · British Journal of Pharmacology · doi:10.1111/j.1476-5381.2010.00671.x · Cited by 107
RetractedDeletion of SOCS7 leads to enhanced insulin action and enlarged islets of Langerhans
Banks, A. S., Li, J., McKeag, L., Hribal, M. L., Kashiwada, M., Accili, D., & Rothman, P. B. (2005) · Journal of Clinical Investigation · doi:10.1172/jci23853 · Cited by 104
Hepatitis C, insulin resistance and diabetes: clinical and pathogenic data
Serfaty, L., & Capeau, J. (2009) · Liver International · doi:10.1111/j.1478-3231.2008.01952.x · Cited by 108
Acute insulin resistance following injury
Li, L., & Messina, J. L. (2009) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2009.06.004 · Cited by 109
SOCS Proteins as Regulators of Inflammatory Responses Induced by Bacterial Infections: A Review
Duncan, S. A., Baganizi, D. R., Sahu, R., Singh, S. R., & Dennis, V. A. (2017) · Frontiers in Microbiology · doi:10.3389/fmicb.2017.02431 · Cited by 104
Biobaku, F., Ghanim, H., Batra, M., & Dandona, P. (2019) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2018-01833 · Cited by 104
The SOCS Box Domain of SOCS3: Structure and Interaction with the ElonginBC-Cullin5 Ubiquitin Ligase
Babon, J. J., Sabo, J. K., Soetopo, A., Yao, S., Bailey, M. F., Zhang, J., Nicola, N. A., & Norton, R. S. (2008) · Journal of Molecular Biology · doi:10.1016/j.jmb.2008.06.038 · Cited by 107
Antonova, Y., Arik, A. J., Moore, W., Riehle, M. A., & Brown, M. R. (2011) · Elsevier eBooks · doi:10.1016/b978-0-12-384749-2.10002-0 · Cited by 107
Sachithanandan, N., Fam, B. C., Fynch, S., Dzamko, N. L., Watt, M. J., Wormald, S., Honeyman, J. E., Galić, S., Proietto, J., Andrikopoulos, S., et al. (2010) · Hepatology · doi:10.1002/hep.23861 · Cited by 107
SOCS3 as a future target to treat metabolic disorders
Pedroso, J. A. B., Ramos-Lobo, A. M., & Donato, J. (2018) · HORMONES · doi:10.1007/s42000-018-0078-5 · Cited by 106
Negative Regulation of Cytokine and TLR Signalings by SOCS and Others
Naka, T., Fujimoto, M., Tsutsui, H., & Yoshimura, A. (2005) · Advances in immunology · doi:10.1016/s0065-2776(05)87003-8 · Cited by 101
Himpe, E., & Kooijman, R. (2009) · BioFactors · doi:10.1002/biof.20 · Cited by 101
Genomic aspects of NAFLD pathogenesis
Naik, A., Košir, R., & Rozman, D. (2013) · Genomics · doi:10.1016/j.ygeno.2013.03.007 · Cited by 108
The Emerging Role of the COP9 Signalosome in Cancer
Richardson, K. S., & Zundel, W. (2005) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-05-0233 · Cited by 101
The role of cullin 5-containing ubiquitin ligases
Okumura, F., Akiko, J.-O., Nakatsukasa, K., & Kamura, T. (2016) · Cell Division · doi:10.1186/s13008-016-0016-3 · Cited by 99
Giraud, J., Leshan, R. L., Lee, Y.-H., & White, M. F. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m308631200 · Cited by 100
Role of NK and NKT cells in the immunopathogenesis of HCV-induced hepatitis
Ahmad, A., & Álvarez, F. (2004) · Journal of Leukocyte Biology · doi:10.1189/jlb.0304197 · Cited by 100
Metadata
- Authors
- Rui, L., Yuan, M., Frantz, D., Shoelson, S., & White, M. F.
- Affiliations
- Joslin Diabetes Center (US)
- Corresponding author
- White, Morris F.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2002-11
- Volume
- 277
- Issue
- 44
- Pages
- 42394-42398
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2069711307
- Cited by
- 904
- References
- 44
- Citations by year
- 2026: 14 · 2025: 18 · 2024: 18 · 2023: 25 · 2022: 35 · 2021: 39 · 2020: 27 · 2019: 29 · 2018: 42 · 2017: 33 · 2016: 48 · 2015: 27 · 2014: 50 · 2013: 51 · 2012: 57
- FWCI
- 30.83
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health
- Topics
- Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Adipokines, Inflammation, and Metabolic Diseases
- Life Sciences › Immunology and Microbiology › Immunology › Cytokine Signaling Pathways and Interactions
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Keywords
- SOCS1, SOCS3, IRS-1, insulin receptor substrate 2, insulin signaling, ubiquitin-mediated proteolysis, SOCS box, inflammation, insulin resistance, impaired glucose tolerance, liver, diabetes mellitus
- MeSH terms
- Suppressor of Cytokine Signaling 1 Protein, Suppressor of Cytokine Signaling 3 Protein, Elongin, Animals, Carrier Proteins, Glucose, Homeostasis, Humans, Insulin Resistance, Male, Mice, Inbred C57BL, Phosphoproteins, Proteins, Repressor Proteins, Transcription Factors, Ubiquitin, Intracellular Signaling Peptides and Proteins, Suppressor of Cytokine Signaling Proteins, Mice, Insulin Receptor Substrate Proteins
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review