Cited by 375Metabolism, Diabetes, and CancerDiabetes, Cardiovascular Risks, and LipoproteinsAdipokines, Inflammation, and Metabolic Diseases

The DOI matches its Crossref record; 19 of the 19 references it cites were found in a registry or an index.

Characterization of signal transduction and glucose transport in skeletal muscle from type 2 diabetic patients

Open access

Krook, A, Björnholm, M, Galuska, D, Jiang, X J, Fahlman, R, Myers, M G, Wallberg-Henriksson, H, Zierath, J R·2000·Diabetes

DOI 10.2337/diabetes.49.2.284

Open this paper in CoChat — free account Open PDF

Abstract

We characterized metabolic and mitogenic signaling pathways in isolated skeletal muscle from well-matched type 2 diabetic and control subjects. Time course studies of the insulin receptor, insulin receptor substrate (IRS)-1/2, and phosphatidylinositol (PI) 3-kinase revealed that signal transduction through this pathway was engaged between 4 and 40 min. Insulin-stimulated (0.6-60 nmol/l) tyrosine phosphorylation of the insulin receptor beta-subunit, mitogen-activated protein (MAP) kinase phosphorylation, and glycogen synthase activity were not altered in type 2 diabetic subjects. In contrast, insulin-stimulated tyrosine phosphorylation of IRS-1 and anti-phosphotyrosine-associated PI 3-kinase activity were reduced 40-55% in type 2 diabetic subjects at high insulin concentrations (2.4 and 60 nmol/l, respectively). Impaired glucose transport activity was noted at all insulin concentrations (0.6-60 nmol/l). Aberrant protein expression cannot account for these insulin-signaling defects because expression of insulin receptor, IRS-1, IRS-2, MAP kinase, or glycogen synthase was similar between type 2 diabetic and control subjects. In skeletal muscle from type 2 diabetic subjects, IRS-1 phosphorylation, PI 3-kinase activity, and glucose transport activity were impaired, whereas insulin receptor tyrosine phosphorylation, MAP kinase phosphorylation, and glycogen synthase activity were normal. Impaired insulin signal transduction in skeletal muscle from type 2 diabetic patients may partly account for reduced insulin-stimulated glucose transport; however, additional defects are likely to play a role.

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

Crossref · 10.2337/diabetes.49.2.284

Cites

19 of 19 references verified0 citation errors · 0 not checkable

Statistics

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?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Structure of the insulin receptor substrate IRS-1 defines a unique signal transduction protein
Sun, X. J., Rothenberg, P., Kahn, C. R., Backer, J. M., Araki, E., Wilden, P. A., Cahill, D. A., Goldstein, B. J., & White, M. F. (1991) · Nature · doi:10.1038/352073a0 · Cited by 1,574
A rapid filter paper assay for UDPglucose-glycogen glucosyltransferase, including an improved biosynthesis of UDP-14C-glucose
Thomas, J. A., Schlender, K. K., & Larner, J. (1968) · Analytical Biochemistry · doi:10.1016/0003-2697(68)90127-9 · Cited by 1,198
Effects of insulin on peripheral and splanchnic glucose metabolism in noninsulin-dependent (type II) diabetes mellitus.
DeFronzo, R. A., Gunnarsson, R., Björkman, O., Olsson, M., & Wahren, J. (1985) · Journal of Clinical Investigation · doi:10.1172/jci111938 · Cited by 1,167
Insulin receptor phosphorylation, insulin receptor substrate-1 phosphorylation, and phosphatidylinositol 3-kinase activity are decreased in intact skeletal muscle strips from obese subjects.
Goodyear, L. J., Giorgino, F., Sherman, L., Carey, J., Smith, R. J., & Dohm, G. L. (1995) · Journal of Clinical Investigation · doi:10.1172/jci117909 · Cited by 527
Evidence for defects in the trafficking and translocation of GLUT4 glucose transporters in skeletal muscle as a cause of human insulin resistance
Garvey, W. T., Maianu, L., Zhu, J. H., Brechtel-Hook, G., Wallace, P., & Baron, A. D. (1998) · Journal of Clinical Investigation · doi:10.1172/jci1557 · Cited by 459
A microfluorometric method for the determination of free fatty acids in plasma
Miles, J., Glasscock, R., Aikens, J., Gerich, J. E., & Haymond, M. W. (1983) · Journal of Lipid Research · doi:10.1016/s0022-2275(20)38029-9 · Cited by 329
31P nuclear magnetic resonance measurements of muscle glucose-6-phosphate. Evidence for reduced insulin-dependent muscle glucose transport or phosphorylation activity in non-insulin-dependent diabetes mellitus.
Rothman, D. L., Shulman, R. G., & Shulman, G. I. (1992) · Journal of Clinical Investigation · doi:10.1172/jci115686 · Cited by 327
Decreased insulin activation of glycogen synthase in skeletal muscles in young nonobese Caucasian first-degree relatives of patients with non-insulin-dependent diabetes mellitus
Vaag, A., Henriksen, J. E., & Beck-Nielsen, H. (1992) · Journal of Clinical Investigation · doi:10.1172/jci115656 · Cited by 299
An in vitro human muscle preparation suitable for metabolic studies. Decreased insulin stimulation of glucose transport in muscle from morbidly obese and diabetic subjects.
Dohm, G. L., Tapscott, E. B., Pories, W. J., Dabbs, D. J., Flickinger, E. G., Meelheim, D., Fushiki, T., Atkinson, S., Elton, C. W., & Caro, J. F. (1988) · Journal of Clinical Investigation · doi:10.1172/jci113622 · Cited by 296
The effect of non-insulin-dependent diabetes mellitus and obesity on glucose transport and phosphorylation in skeletal muscle.
Kelley, D. E., Mintun, M. A., Watkins, S. C., Simoneau, J. A., Jadali, F., Fredrickson, A., Beattie, J., & Thériault, R. (1996) · Journal of Clinical Investigation · doi:10.1172/jci118724 · Cited by 228

Show all 19 references

Sorted by citations

From the Triumvirate to the Ominous Octet: A New Paradigm for the Treatment of Type 2 Diabetes Mellitus.
DeFronzo, R. A. (2009) · Diabetes · doi:10.2337/db09-9028 · Cited by 3,016
Mechanisms of Insulin Action and Insulin Resistance
Petersen, M. C., & Shulman, G. I. (2018) · Physiological Reviews · doi:10.1152/physrev.00063.2017 · Cited by 3,028
Type 2 diabetes mellitus
DeFronzo, R. A., Ferrannini, E., Groop, L., Henry, R. R., Herman, W. H., Holst, J. J., Hu, F. B., Kahn, C. R., Raz, I., Shulman, G. I., et al. (2015) · Nature Reviews Disease Primers · doi:10.1038/nrdp.2015.19 · Cited by 2,611
Skeletal Muscle Insulin Resistance Is the Primary Defect in Type 2 Diabetes
DeFronzo, R. A., & Tripathy, D. (2009) · Diabetes Care · doi:10.2337/dc09-s302 · Cited by 2,102
“Maintaining the integrity of the IRS-1/PI-3 kinase/Akt pathway is essential for normal insulinmediated glucose uptake in skeletal muscle (26).”
Background
Pathogenesis of type 2 diabetes mellitus
DeFronzo, R. A. (2004) · Medical Clinics of North America · doi:10.1016/j.mcna.2004.04.013 · Cited by 1,342
Signaling Pathways in Skeletal Muscle Remodeling
Bassel‐Duby, R., & Olson, E. N. (2006) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.75.103004.142622 · Cited by 823
Pathogenesis of insulin resistance in skeletal muscle
Abdul-Ghani, M. A., & DeFronzo, R. A. (2010) · Journal of Biomedicine and Biotechnology · doi:10.1155/2010/476279 · Cited by 670
Ceramide Content Is Increased in Skeletal Muscle From Obese Insulin-Resistant Humans
Adams, J. M., Pratipanawatr, T., Berria, R., Wang, E. L., DeFronzo, R. A., Sullards, M. C., & Mandarino, L. J. (2004) · Diabetes · doi:10.2337/diabetes.53.1.25 · Cited by 677
Strength training increases insulin-mediated glucose uptake, GLUT4 content, and insulin signaling in skeletal muscle in patients with type 2 diabetes
Holten, M. K., Zacho, M., Gaster, M., Juel, C., Wojtaszewski, J. F. P., & Dela, F. (2004) · Diabetes · doi:10.2337/diabetes.53.2.294 · Cited by 615
Engineered In Vitro Disease Models
Benam, K. H., Dauth, S., Hassell, B., Herland, A., Jain, A., Jang, K.-J., Karalis, K., Kim, H. J., MacQueen, L., Mahmoodian, R., et al. (2015) · Annual Review of Pathology: Mechanisms of Disease · doi:10.1146/annurev-pathol-012414-040418 · Cited by 554
Invited Review: Effects of acute exercise and exercise training on insulin resistance
Henriksen, E. J. (2002) · Journal of Applied Physiology · doi:10.1152/japplphysiol.01219.2001 · Cited by 535
Insulin action and insulin resistance in human skeletal muscle
Zierath, J. R., Krook, A., & Wallberg-Henriksson, H. (2000) · Diabetologia · doi:10.1007/s001250051457 · Cited by 367
Self-citation
Exercise as a therapeutic intervention for the prevention and treatment of insulin resistance
Hawley, J. A. (2004) · Diabetes/Metabolism Research and Reviews · doi:10.1002/dmrr.505 · Cited by 344
Cholesterol Depletion Disrupts Caveolae and Insulin Receptor Signaling for Metabolic Control via Insulin Receptor Substrate-1, but Not for Mitogen-activated Protein Kinase Control
Parpal, S., Karlsson, M., Thorn, H., & Strålfors, P. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m007454200 · Cited by 339
Recent Advances in Our Understanding of Insulin Action and Insulin Resistance
Roith, D. L., & Zick, Y. (2001) · Diabetes Care · doi:10.2337/diacare.24.3.588 · Cited by 347
Defects in insulin receptor signaling in vivo in the polycystic ovary syndrome (PCOS)
Dunaif, A., Wu, X., Lee, A., & Diamanti-Kandarakis, E. (2001) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.2001.281.2.e392 · Cited by 337
Insulin resistance in spontaneously hypertensive rats is associated with endothelial dysfunction characterized by imbalance between NO and ET-1 production
Potenza, M. A., Marasciulo, F. L., Chieppa, D. M., Brigiani, G. S., Formoso, G., Quon, M. J., & Montagnani, M. (2005) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00092.2005 · Cited by 314
Reduced activation of phosphatidylinositol-3 kinase and increased serine 636 phosphorylation of insulin receptor substrate-1 in primary culture of skeletal muscle cells from patients with type 2 diabetes
Bouzakri, K., Roques, M., Gual, P., Espinosa, S., Guebre-Egziabher, F., Riou, J.-P., Laville, M., Le Marchand-Brustel, Y., Tanti, J.-F., & Vidal, H. (2003) · Diabetes · doi:10.2337/diabetes.52.6.1319 · Cited by 305
Skeletal muscle tissue engineering: methods to form skeletal myotubes and their applications
Ostrovidov, S., Hosseini, V., Ahadian, S., Fujie, T., Parthiban, S. P., Ramalingam, M., Bae, H., Kaji, H., & Khademhosseini, A. (2014) · Tissue Engineering Part B: Reviews · doi:10.1089/ten.teb.2013.0534 · Cited by 302
Insulin-Stimulated Phosphorylation of the Akt Substrate AS160 Is Impaired in Skeletal Muscle of Type 2 Diabetic Subjects
Karlsson, H., Zierath, J. R., Kane, S., Krook, A., Lienhard, G. E., & Wallberg‐Henriksson, H. (2005) · Diabetes · doi:10.2337/diabetes.54.6.1692 · Cited by 299
Self-citation
Current Concepts in the Polycystic Ovary Syndrome
Dunaif, A. E., & Thomas, A. (2001) · Annual Review of Medicine · doi:10.1146/annurev.med.52.1.401 · Cited by 303
Low birthweight is associated with specific changes in muscle insulin-signalling protein expression
Ozanne, S. E., Jensen, C. B., Tingey, K., Storgaard, H., Madsbad, S., & Vaag, A. A. (2005) · Diabetologia · doi:10.1007/s00125-005-1669-7 · Cited by 290
Pathophysiology of insulin resistance
Sesti, G. (2006) · Best Practice & Research Clinical Endocrinology & Metabolism · doi:10.1016/j.beem.2006.09.007 · Cited by 297
Modulation of insulin action
Pirola, L., Johnston, A., & OBBERGHEN, E. V. (2004) · Diabetologia · doi:10.1007/s00125-003-1313-3 · Cited by 286
Insulin resistance in the skeletal muscle of women with PCOS involves intrinsic and acquired defects in insulin signaling
Corbould, A., Kim, Y.-B., Youngren, J. F., Pender, C., Kahn, B. B., Lee, A., & Dunaif, A. (2005) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00361.2004 · Cited by 283
Adipose tissue and its role in organ crosstalk
Romacho, T., Elsen, M., Röhrborn, D., & Eckel, J. (2014) · Acta Physiologica · doi:10.1111/apha.12246 · Cited by 292
Signalling aspects of insulin resistance in skeletal muscle
Schmitz‐Peiffer, C. (2000) · Cellular Signalling · doi:10.1016/s0898-6568(00)00110-8 · Cited by 269
Regulation by Insulin of Gene Expression in Human Skeletal Muscle and Adipose Tissue
Ducluzeau, P., Peretti, N., Laville, M., Andréelli, F., Véga, N., Riou, J. P., & Vidal, H. (2001) · Diabetes · doi:10.2337/diabetes.50.5.1134 · Cited by 263
S-Nitrosylation-dependent Inactivation of Akt/Protein Kinase B in Insulin Resistance
Yasukawa, T., Tokunaga, E., Ota, H., Sugita, H., Martyn, J. A. J., & Kaneki, M. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m411871200 · Cited by 265
Proteomics analysis of human skeletal muscle reveals novel abnormalities in obesity and type 2 diabetes
Hwang, H., Bowen, B. P., Lefort, N., Flynn, C. R., De Filippis, E. A., Roberts, C., Smoke, C. C., Meyer, C., Højlund, K., Yi, Z., et al. (2010) · Diabetes · doi:10.2337/db09-0214 · Cited by 255
Alterations of insulin signaling in type 2 diabetes: A review of the current evidence from humans
Fröjdö, S., Vidal, H., & Pirola, L. (2008) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2008.10.019 · Cited by 247
Programming of glucose-insulin metabolism in adult sheep after maternal undernutrition
Gardner, D. S., Tingey, K., van Bon, B. W. M., Ozanne, S. E., Wilson, V., Dandrea, J., Keisler, D. H., Stephenson, T. J., & Symonds, M. E. (2005) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00120.2005 · Cited by 241
5-Amino-Imidazole Carboxamide Riboside Increases Glucose Transport and Cell-Surface GLUT4 Content in Skeletal Muscle From Subjects With Type 2 Diabetes
Koistinen, H. A., Galuska, D., Chibalin, A., Yang, J., Zierath, J. R., Holman, G. D., & Wallberg‐Henriksson, H. (2003) · Diabetes · doi:10.2337/diabetes.52.5.1066 · Cited by 232
Self-citation
Downregulation of Diacylglycerol Kinase Delta Contributes to Hyperglycemia-Induced Insulin Resistance
Chibalin, A. V., Leng, Y., Vieira, E., Krook, A., Björnholm, M., Long, Y. C., Kotova, O., Zhong, Z., Sakane, F., Steiler, T., et al. (2008) · Cell · doi:10.1016/j.cell.2007.12.035 · Cited by 232
Self-citation
Early growth restriction leads to down regulation of protein kinase C zeta and insulin resistance in skeletal muscle
Ozanne, S. E., Olsen, G., Hansen, L., Tingey, K., NAVÉ, B. T., Wang, C., Hartil, K., Petry, C. J., Buckley, A., & Mosthaf, L. (2003) · Journal of Endocrinology · doi:10.1677/joe.0.1770235 · Cited by 230
Exercise training increases insulin-stimulated glucose disposal and GLUT4 (SLC2A4) protein content in patients with type 2 diabetes
O’Gorman, D. J., Karlsson, H. K. R., McQuaid, S., Yousif, O., Rahman, Y., Gasparro, D., Glund, S., Chibalin, A. V., Zierath, J. R., & Nolan, J. J. (2006) · Diabetologia · doi:10.1007/s00125-006-0457-3 · Cited by 226
Self-citation
Enhanced Basal Activation of Mitogen-Activated Protein Kinases in Adipocytes From Type 2 Diabetes
Carlson, C. J., Koterski, S., Sciotti, R. J., Poccard, G. B., & Rondinone, C. M. (2003) · Diabetes · doi:10.2337/diabetes.52.3.634 · Cited by 230
Invited Review: Exercise training-induced changes in insulin signaling in skeletal muscle
Zierath, J. R. (2002) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00126.2002 · Cited by 215
Self-citation
siRNA-based gene silencing reveals specialized roles of IRS-1/Akt2 and IRS-2/Akt1 in glucose and lipid metabolism in human skeletal muscle
Bouzakri, K., Zachrisson, A., Al‐Khalili, L., Zhang, B. B., Koistinen, H. A., Krook, A., & Zierath, J. R. (2006) · Cell Metabolism · doi:10.1016/j.cmet.2006.04.008 · Cited by 222
Self-citation
n-3 long chain polyunsaturated fatty acids: a nutritional tool to prevent insulin resistance associated to type 2 diabetes and obesity?
Delarue, J., Foll, C. L., Corporeau, C., & Lucas, D. (2004) · annales de biologie animale biochimie biophysique · doi:10.1051/rnd:2004033 · Cited by 205
Long-term effects of nutritional programming of the embryo and fetus: mechanisms and critical windows
Symonds, M. E., Stephenson, T. J., Gardner, D. S., & Budge, H. (2006) · Reproduction Fertility and Development · doi:10.1071/rd06130 · Cited by 211
Untitled work
(2006) · doi:10.1016/j.tem.2006.01.005 · Cited by 256
PTP1B and TCPTP – nonredundant phosphatases in insulin signaling and glucose homeostasis
Tiganis, T. (2012) · FEBS Journal · doi:10.1111/j.1742-4658.2012.08563.x · Cited by 209
Altered miR-29 Expression in Type 2 Diabetes Influences Glucose and Lipid Metabolism in Skeletal Muscle
Massart, J., Sjögren, R. J. O., Lundell, L. S., Mudry, J. M., Franck, N., O’Gorman, D. J., Egan, B., Zierath, J. R., & Krook, A. (2017) · Diabetes · doi:10.2337/db17-0141 · Cited by 201
Self-citation
Impaired microvascular perfusion: a consequence of vascular dysfunction and a potential cause of insulin resistance in muscle
Clark, M. G. (2008) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.90477.2008 · Cited by 195
Muscle and adipose tissue insulin resistance: malady without mechanism?
Fazakerley, D. J., Krycer, J. R., Kearney, A. L., HOCKING, S. L., & James, D. E. (2018) · Journal of Lipid Research · doi:10.1194/jlr.r087510 · Cited by 188
Differential Contribution of Insulin Receptor Substrates 1 Versus 2 to Insulin Signaling and Glucose Uptake in L6 Myotubes
Huang, C., Thirone, A. C. P., Huang, X., & Klip, A. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m412317200 · Cited by 181
Diabetes Reduces Basal Retinal Insulin Receptor Signaling
Reiter, C. E. N., Wu, X., Sandirasegarane, L., Nakamura, M., Gilbert, K. A., Singh, R. S., Fort, P. E., Antonetti, D. A., & Gardner, T. W. (2006) · Diabetes · doi:10.2337/diabetes.55.04.06.db05-0744 · Cited by 174
Mitogen‐activated protein kinase signal transduction in skeletal muscle: effects of exercise and muscle contraction
Widegren, U., Ryder, J. W., & Zierath, J. R. (2001) · Acta Physiologica Scandinavica · doi:10.1046/j.1365-201x.2001.00855.x · Cited by 178
Self-citation
Randomized clinical trial to compare the effects of preoperative oral carbohydrate versus placebo on insulin resistance after colorectal surgery
Wang, Z. G., Wang, Q., Wang, W.-Z., & Qin, H. (2010) · British journal of surgery · doi:10.1002/bjs.6963 · Cited by 175
Increased collagen content in insulin-resistant skeletal muscle
Berria, R., Wang, L., Richardson, D. K., Finlayson, J., Belfort, R., Pratipanawatr, T., De Filippis, E. A., Kashyap, S., & Mandarino, L. J. (2006) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00202.2005 · Cited by 171
Defective Signaling Through Akt-2 and -3 But Not Akt-1 in Insulin-Resistant Human Skeletal Muscle
Brozinick, J. T., Roberts, B. R., & Dohm, G. L. (2003) · Diabetes · doi:10.2337/diabetes.52.4.935 · Cited by 164
Enhanced Mitogenic Signaling in Skeletal Muscle of Women With Polycystic Ovary Syndrome
Corbould, A. M., Zhao, H., Mirzoeva, S., Aird, F., & Dunaif, A. E. (2006) · Diabetes · doi:10.2337/diabetes.55.03.06.db05-0453 · Cited by 166
Insulin signaling and glucose transport in insulin resistant human skeletal muscle
Karlsson, H. K. R., & Zierath, J. R. (2007) · Cell Biochemistry and Biophysics · doi:10.1007/s12013-007-0030-9 · Cited by 159
Self-citation
Colistin and rifampicin in the treatment of multidrug-resistant Acinetobacter baumannii infections
Bassetti, M., Repetto, E. C., Righi, E., Boni, S., Diverio, M., Molinari, M. P., Mussap, M., Artioli, S., Ansaldi, F., Durando, P., et al. (2007) · Journal of Antimicrobial Chemotherapy · doi:10.1093/jac/dkm509 · Cited by 162
Coronary Vasomotor Abnormalities in Insulin-Resistant Individuals
Quiñones, M. J., Hernandez‐Pampaloni, M., Schelbert, H., Bulnes‐Enriquez, I., Jimenez, X., Hernandez, G., Rosa, R. D. L., Chon, Y., Yang, H., Nicholas, S. B., et al. (2004) · Annals of Internal Medicine · doi:10.7326/0003-4819-140-9-200405040-00009 · Cited by 163
Insulin-Stimulated Protein Kinase C λ/ζ Activity Is Reduced in Skeletal Muscle of Humans With Obesity and Type 2 Diabetes
Kim, Y., Kotani, K., Ciaraldi, T. P., Henry, R. R., & Kahn, B. B. (2003) · Diabetes · doi:10.2337/diabetes.52.8.1935 · Cited by 159
Intracellular mechanisms underlying increases in glucose uptake in response to insulin or exercise in skeletal muscle
Ryder, J. W., Chibalin, A., & Zierath, J. R. (2001) · Acta Physiologica Scandinavica · doi:10.1046/j.1365-201x.2001.00827.x · Cited by 158
Self-citation
Systemic and mitochondrial adaptive responses to moderate exercise in rodents
Boveris, A., & Navarro, A. (2007) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2007.08.015 · Cited by 154
Proline-rich Akt substrate of 40 kDa (PRAS40): A novel downstream target of PI3k/Akt signaling pathway
Wang, H., Zhang, Q., Wen, Q. J., Zheng, Y., Lazarovici, P., Jiang, H., Lin, J., & Zheng, W. (2011) · Cellular Signalling · doi:10.1016/j.cellsig.2011.08.010 · Cited by 156
Sending the Signal: Molecular Mechanisms Regulating Glucose Uptake
Krook, A., Wallberg‐Henriksson, H., & Zierath, J. R. (2004) · Medicine & Science in Sports & Exercise · doi:10.1249/01.mss.0000132387.25853.3b · Cited by 152
Self-citation
Akt activation: A potential strategy to ameliorate insulin resistance
Zhang, Z., Liu, H., & Liu, J. (2017) · Diabetes Research and Clinical Practice · doi:10.1016/j.diabres.2017.10.004 · Cited by 143
Human placental exosomes in gestational diabetes mellitus carry a specific set of miRNAs associated with skeletal muscle insulin sensitivity
Nair, S., Jayabalan, N., Guanzon, D., Palma, C., Scholz‐Romero, K., Elfeky, O. W. M., Zuñiga, F. A., Ormazábal, V., Diaz, E., Rice, G. E., et al. (2018) · Clinical Science · doi:10.1042/cs20180487 · Cited by 146
Mechanisms for greater insulin-stimulated glucose uptake in normal and insulin-resistant skeletal muscle after acute exercise
Cartee, G. D. (2015) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00416.2015 · Cited by 146
For Debate: Fetal and early postnatal growth restriction lead to diabetes, the metabolic syndrome and renal failure*
Ozanne, S. E., & Hales, C. N. (2003) · Diabetologia · doi:10.1007/s00125-003-1131-7 · Cited by 137
Exercise training and the antioxidant α-lipoic acid in the treatment of insulin resistance and type 2 diabetes
Henriksen, E. J. (2006) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2005.04.002 · Cited by 136
The Role of Membrane Glycoprotein Plasma Cell Antigen 1/Ectonucleotide Pyrophosphatase Phosphodiesterase 1 in the Pathogenesis of Insulin Resistance and Related Abnormalities
Goldfine, I. D., Maddux, B. A., YOUNGREN, J. F., Reaven, G. M., Accili, D., Trischitta, V., Vigneri, R., & Frittitta, L. (2008) · Endocrine Reviews · doi:10.1210/er.2007-0004 · Cited by 137
Mitochondrial Dysfunction in Type 2 Diabetes and Obesity
Højlund, K., Mogensen, M., Sahlin, K., & Beck-Nielsen, H. (2008) · Endocrinology and Metabolism Clinics of North America · doi:10.1016/j.ecl.2008.06.006 · Cited by 135
Skeletal Muscle Reprogramming by Activation of Calcineurin Improves Insulin Action on Metabolic Pathways
Ryder, J. W., Bassel‐Duby, R., Olson, E. N., & Zierath, J. R. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m304510200 · Cited by 135
Self-citation
Modulation of metabolic control by angiotensin converting enzyme (ACE) inhibition
Henriksen, E. J., & Jacob, S. (2003) · Journal of Cellular Physiology · doi:10.1002/jcp.10294 · Cited by 132
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
In Vivo Actions of Peroxisome Proliferator–Activated Receptors
Eldor, R., DeFronzo, R. A., & Abdul‐Ghani, M. A. (2013) · Diabetes Care · doi:10.2337/dcs13-2003 · Cited by 128
Retinol‐binding protein‐4 attenuates insulin‐induced phosphorylation of IRS1 and ERK1/2 in primary human adipocytes
Öst, A., Danielsson, A., Lidén, M., Eriksson, U., Nyström, F. H., & Strålfors, P. (2007) · The FASEB Journal · doi:10.1096/fj.07-8173com · Cited by 126
Improvement of insulin sensitivity by antagonism of the renin-angiotensin system
Henriksen, E. J. (2007) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00147.2007 · Cited by 127
Interplay between impaired calcium regulation and insulin signaling abnormalities in diabetic cardiomyopathy.
Lebeche, D., Davidoff, A. J., & Hajjar, R. J. (2008) · Nature Clinical Practice Cardiovascular Medicine · doi:10.1038/ncpcardio1347 · Cited by 122
Exercise in the Metabolic Syndrome
Golbidi, S., Mesdaghinia, A., & Laher, I. (2012) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2012/349710 · Cited by 127
Regulation of glucose transport in human skeletal muscle
Koistinen, H. A., & Zierath, J. R. (2002) · Annals of Medicine · doi:10.1080/078538902321012351 · Cited by 124
Self-citation
Protein Kinase C and Lipid‐Induced Insulin Resistance in Skeletal Muscle
Schmitz‐Peiffer, C. (2002) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2002.tb04272.x · Cited by 124
Skeletal muscle insulin resistance in normoglycemic subjects with a strong family history of type 2 diabetes is associated with decreased insulin-stimulated insulin receptor substrate-1 tyrosine phosphorylation
Pratipanawatr, W., Pratipanawatr, T., Cusi, K., Berria, R., Adams, J. M., Jenkinson, C. P., Maezono, K., DeFronzo, R. A., & Mandarino, L. J. (2001) · Diabetes · doi:10.2337/diabetes.50.11.2572 · Cited by 118
Initial steps of insulin signaling and glucose transport are defective in the type 2 diabetic rat heart
Desrois, M. (2003) · Cardiovascular Research · doi:10.1016/j.cardiores.2003.11.021 · Cited by 118
Enhanced Skeletal Muscle for Effective Glucose Homeostasis
Yang, J. (2014) · Progress in molecular biology and translational science · doi:10.1016/b978-0-12-800101-1.00005-3 · Cited by 122
PPAR-α activation protects the type 2 diabetic myocardium against ischemia-reperfusion injury: involvement of the PI3-Kinase/Akt and NO pathway
Bulhak, A., Jung, C., Östenson, C., Lundberg, J. O., Sjöquist, P.-O. B., & Pernow, J. (2009) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00394.2008 · Cited by 116
Immunocytochemical Detection of Phosphatidylinositol 3-kinase Activation by Insulin and Leptin
Niswender, K. D., Gallis, B. M., Blevins, J. E., Corson, M. A., Schwartz, M. W., & Baskin, D. G. (2003) · Journal of Histochemistry & Cytochemistry · doi:10.1177/002215540305100302 · Cited by 115
Dietary Flavonoids in the Prevention of T2D: An Overview
Alkhalidy, H., Wang, Y., & Liu, D. (2018) · Nutrients · doi:10.3390/nu10040438 · Cited by 123
Absence of functional insulin receptor substrate-3 ( IRS-3 ) gene in humans
rnholm, M. B. X. F., He, A., Attersand, A., Lake, S., Liu, S., Lienhard, G. E., Taylor, S. I., Arner, P., & Zierath, J. R. (2002) · Diabetologia · doi:10.1007/s00125-002-0945-z · Cited by 116
Self-citation
Electrical pulse stimulation of cultured skeletal muscle cells as a model for in vitro exercise – possibilities and limitations
Nikolić, N., Görgens, S. W., Thoresen, G. H., Aas, V., Eckel, J., & Eckardt, K. (2016) · Acta Physiologica · doi:10.1111/apha.12830 · Cited by 122
Phosphoinositide 3-Kinase-mediated Reduction of Insulin Receptor Substrate-1/2 Protein Expression via Different Mechanisms Contributes to the Insulin-induced Desensitization of Its Signaling Pathways in L6 Muscle Cells
Pirola, L., Bonnafous, S., Johnston, A., Chaussade, C., Portis, F., & OBBERGHEN, E. V. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m208984200 · Cited by 110
Fat Oxidation, Fitness and Skeletal Muscle Expression of Oxidative/Lipid Metabolism Genes in South Asians: Implications for Insulin Resistance?
Hall, L. M. L., Moran, C. N., Milne, G. R., Wilson, J., MacFarlane, N. G., Forouhi, N. G., Hariharan, N., Salt, I. P., Sattar, N., & Gill, J. M. R. (2010) · PLoS ONE · doi:10.1371/journal.pone.0014197 · Cited by 106
Burn injury impairs insulin-stimulated Akt/PKB activation in skeletal muscle
Sugita, H., Kaneki, M., Sugita, M., Yasukawa, T., Yasuhara, S., & Martyn, J. A. J. (2004) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00321.2004 · Cited by 110
A review on the molecular mechanisms involved in insulin resistance induced by organophosphorus pesticides
Lasram, M. M., Dhouib, I. B., Annabi, A. B., Fazâa, S. E., & Gharbi, N. (2014) · Toxicology · doi:10.1016/j.tox.2014.04.009 · Cited by 108
Isoform-specific defects of insulin stimulation of Akt/protein kinase B (PKB) in skeletal muscle cells from type 2 diabetic patients
Cozzone, D., Fröjdö, S., Disse, E., Debard, C., Laville, M., Pirola, L., & Vidal, H. (2008) · Diabetologia · doi:10.1007/s00125-007-0913-8 · Cited by 111
Altered skeletal muscle insulin signaling and mitochondrial complex II-III linked activity in adult offspring of obese mice
Shelley, P., Martin‐Gronert, M. S., Rowlerson, A. M., Poston, L., Heales, S., Hargreaves, I. P., McConnell, J. M. L., Ozanne, S. E., & Fernandez‐Twinn, D. S. (2009) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00146.2009 · Cited by 110
Aberrant p38 mitogen-activated protein kinase signalling in skeletal muscle from Type 2 diabetic patients
Koistinen, H. A., Chibalin, A., & Zierath, J. R. (2003) · Diabetologia · doi:10.1007/s00125-003-1196-3 · Cited by 108
Self-citation
Increased SRF transcriptional activity in human and mouse skeletal muscle is a signature of insulin resistance
Jin, W., Goldfine, A. B., Boes, T., Henry, R. R., Ciaraldi, T. P., Kim, E. Y., Şanlı, M. E., Fitzpatrick, C., Sen, A., Shah, A. M., et al. (2011) · Journal of Clinical Investigation · doi:10.1172/jci41940 · Cited by 107
Tissue‐specific insulin signaling in the regulation of metabolism and aging
Zhang, J., & Liu, F. (2014) · IUBMB Life · doi:10.1002/iub.1293 · Cited by 105
Protein Kinase D1 Stimulates MEF2 Activity in Skeletal Muscle and Enhances Muscle Performance
Kim, M.-S., Fielitz, J., McAnally, J., Shelton, J. M., Lemon, D. D., McKinsey, T. A., Richardson, J. A., Bassel‐Duby, R., & Olson, E. N. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.00189-08 · Cited by 104
Potential new treatments for type 2 diabetes
Bailey, C. J. (2000) · Trends in Pharmacological Sciences · doi:10.1016/s0165-6147(00)01506-6 · Cited by 102
Genetic and nutrient determinants of the metabolic syndrome
Phillips, C. M., López‐Miranda, J., Pérez‐Jiménez, F., McManus, R., & Roche, H. M. (2006) · Current Opinion in Cardiology · doi:10.1097/01.hco.0000221579.25878.11 · Cited by 99
Characterization of a Protein Kinase B Inhibitor In Vitro and in Insulin-Treated Liver Cells
Logie, L., Ruiz‐Alcaraz, A. J., Keane, M. P., Woods, Y. L., Bain, J., Márquez, R., Alessi, D. R., & Sutherland, C. D. (2007) · Diabetes · doi:10.2337/db07-0343 · Cited by 100
Maternal nutritional programming of fetal adipose tissue development: Long‐term consequences for later obesity
Budge, H., Gnanalingham, M. G., Gardner, D. S., Mostyn, A., Stephenson, T. J., & Symonds, M. E. (2005) · Birth Defects Research Part C Embryo Today Reviews · doi:10.1002/bdrc.20044 · Cited by 95

Authors: Krook, A., Björnholm, M., Galuska, D., Jiang, X. J., Fahlman, R., Myers, M. G., Wallberg-Henriksson, H., & Zierath, J. R.
Affiliations: Karolinska University Hospital (SE)
Department of Clinical Physiology, Karolinska Hospital, Stockholm, Sweden.
ORCID: Krook, A
Björnholm, M
Jiang, X J
Myers, M G
Zierath, J R
Venue: Diabetes
Publisher: American Diabetes Association
Published: 2000-02-01
Volume: 49
Issue: 2
Pages: 284-292
ISSN: 0012-1797 (ISSN-L)
1939-327X
DOI: 10.2337/diabetes.49.2.284
OpenAlex: W2124948826
Cited by: 375
References: 19
Citations by year: 2026: 4 · 2025: 7 · 2024: 10 · 2023: 5 · 2022: 5 · 2021: 13 · 2020: 7 · 2019: 6 · 2018: 20 · 2017: 11 · 2016: 11 · 2015: 13 · 2014: 15 · 2013: 12 · 2012: 13
FWCI: 8.55
Type: journal article
Language: en
Open access: bronze
doi.org
Locations: Diabetes (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Diabetes, Cardiovascular Risks, and Lipoproteins
Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Adipokines, Inflammation, and Metabolic Diseases
Keywords: type 2 diabetes, skeletal muscle, insulin signaling, insulin receptor, IRS-1, insulin receptor substrate 2, phosphatidylinositol 3-kinase, glucose transport, mitogen-activated protein kinase, glycogen synthase, tyrosine phosphorylation, insulin resistance
MeSH terms: Biological Transport, Diabetes Mellitus, Type 2, Glucose, Glycogen Synthase, Humans, Insulin, Male, Middle Aged, Phosphoproteins, Phosphorylation, Receptor, Insulin, Time Factors, Tyrosine, Signal Transduction, Muscle, Skeletal, Phosphotyrosine, Phosphatidylinositol 3-Kinases, Mitogen-Activated Protein Kinases, 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

Characterization of signal transduction and glucose transport in skeletal muscle from type 2 diabetic patients

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Self-check

Citations

Cites

Cited by

Related

Metadata

Record

About these checks