Chemistry and Biochemistry of Type 2 Diabetes

The Effect of Intensive Treatment of Diabetes on the Development and Progression of Long-Term Complications in Insulin-Dependent Diabetes Mellitus

(1993) · New England Journal of Medicine · doi:10.1056/nejm199309303291401 · Cited by 24,667

Intensive blood-glucose control with sulphonylureas or insulin compared with conventional treatment and risk of complications in patients with type 2 diabetes (UKPDS 33)

(1998) · The Lancet · doi:10.1016/s0140-6736(98)07019-6 · Cited by 20,023

Positional cloning of the mouse obese gene and its human homologue

Zhang, Y., Proenca, R., Maffei, M., Barone, M., Leopold, L., & Friedman, J. M. (1994) · Nature · doi:10.1038/372425a0 · Cited by 13,419

Effect of intensive blood-glucose control with metformin on complications in overweight patients with type 2 diabetes (UKPDS 34)

(1998) · The Lancet · doi:10.1016/s0140-6736(98)07037-8 · Cited by 8,247

Adipose Expression of Tumor Necrosis Factor-α: Direct Role in Obesity-Linked Insulin Resistance

Hotamisligil, G. S., Shargill, N. S., & Spiegelman, B. M. (1993) · Science · doi:10.1126/science.7678183 · Cited by 7,518

Tight blood pressure control and risk of macrovascular and microvascular complications in type 2 diabetes: UKPDS 38

(1998) · BMJ · doi:10.1136/bmj.317.7160.703 · Cited by 6,683

Role of AMP-Activated Protein Kinase in Mechanism of Metformin Action

Zhou, G., Myers, R., Li, Y., Chen, Y., Shen, X., Fenyk-Melody, J., Wu, M., Ventre, J., Doebber, T., Fujii, N., et al. (2001) · Journal of Clinical Investigation · doi:10.1172/jci13505 · Cited by 5,652

The effect of angiotensin-converting-enzyme inhibition on diabetic nephropathy

Lewis, E. J., Hunsicker, L. G., Bain, R. P., & Rohde, R. D. (1993) · New England Journal of Medicine · doi:10.1056/nejm199311113292004 · Cited by 5,394

The glucose fatty-acid cycle. Its role in insulin sensitivity and the metabolic disturbances of diabetes mellitus

Randle, P. J., Garland, P. B., Hales, C. N., & Newsholme, E. A. (1963) · The Lancet · doi:10.1016/s0140-6736(63)91500-9 · Cited by 5,093

The fat-derived hormone adiponectin reverses insulin resistance associated with both lipoatrophy and obesity

Yamauchi, T., Kamon, J., Waki, H., Terauchi, Y., Kubota, N., Hara, K., Mori, Y., Ide, T., Murakami, K., Tsuboyama-Kasaoka, N., et al. (2001) · Nature Medicine · doi:10.1038/90984 · Cited by 4,915

Paradoxical Decrease of an Adipose-Specific Protein, Adiponectin, in Obesity

Arita, Y., Kihara, S., Ouchi, N., Takahashi, M., Maeda, K., Miyagawa, J.-I., Hotta, K., Shimomura, I., Nakamura, T., Miyaoka, K., et al. (1999) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1999.0255 · Cited by 4,856

Tight blood pressure control and risk of macrovascular and microvascular complications in type 2 diabetes: UKPDS 38

Stearne, M. R., Palmer, S. L., Hammersley, M. S., Franklin, S. L., Spivey, R. S., Lévy, J., Tidy, C. R., Bell, N. J., Steemson, J., Barrow, B. A., et al. (1998) · UCL Discovery (University College London) · Cited by 4,802

The hormone resistin links obesity to diabetes

Steppan, C. M., Bailey, S. T., Bhat, S., Brown, E. J., Banerjee, R. R., Wright, C. M., Patel, H. R., Ahima, R. S., & Lazar, M. A. (2001) · Nature · doi:10.1038/35053000 · Cited by 4,755

Effects of diet and exercise in preventing NIDDM in people with impaired glucose tolerance: the Da Qing IGT and Diabetes Study

Pan, X.-R., Li, G.-W., Hu, Y.-H., Wang, J.-X., Yang, W.-Y., An, Z.-X., Hu, Z.-X., Juan-Lin, Xiao, J.-Z., Cao, H.-B., et al. (1997) · Diabetes Care · doi:10.2337/diacare.20.4.537 · Cited by 4,320

Hypoadiponectinemia in Obesity and Type 2 Diabetes: Close Association with Insulin Resistance and Hyperinsulinemia

Weyer, C., Funahashi, T., Tanaka, S., Hotta, K., Matsuzawa, Y., Pratley, R. E., & Tataranni, P. A. (2001) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jcem.86.5.7463 · Cited by 3,541

Identification and expression cloning of a leptin receptor, OB-R.

Tartaglia, L. A., Dembski, M., Weng, X., Deng, N., Culpepper, J., Devos, R., Richards, G. J., Campfield, L. A., Clark, F. T., Deeds, J., et al. (1995) · Cell · doi:10.1016/0092-8674(95)90151-5 · Cited by 3,496

Rab proteins as membrane organizers

Zerial, M., & McBride, H. (2001) · Nature Reviews Molecular Cell Biology · doi:10.1038/35052055 · Cited by 3,381

A central role for JNK in obesity and insulin resistance

Hirosumi, J., Tuncman, G., Chang, L., Görgün, C. Z., Uysal, K. T., Maeda, K., Karin, M., & Hotamisligil, G. S. (2002) · Nature · doi:10.1038/nature01137 · Cited by 3,359

A Novel Serum Protein Similar to C1q, Produced Exclusively in Adipocytes

Scherer, P. E., Williams, S., Fogliano, M., Baldini, G., & Lodish, H. F. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.45.26746 · Cited by 3,237

Cloning of adiponectin receptors that mediate antidiabetic metabolic effects

Yamauchi, T., Kamon, J., Ito, Y., Tsuchida, A., Yokomizo, T., Kita, S., Sugiyama, T., Miyagishi, M., Hara, K., Tsunoda, M., et al. (2003) · Nature · doi:10.1038/nature01705 · Cited by 3,176

Plasma Concentrations of a Novel, Adipose-Specific Protein, Adiponectin, in Type 2 Diabetic Patients

Hotta, K., Funahashi, T., Arita, Y., Takahashi, M., Matsuda, M., Okamoto, Y., Iwahashi, H., Kuriyama, H., Ouchi, N., Maeda, K., et al. (2000) · Arteriosclerosis, Thrombosis, and Vascular Biology · doi:10.1161/01.atv.20.6.1595 · Cited by 3,133

Intensive insulin therapy prevents the progression of diabetic microvascular complications in Japanese patients with non-insulin-dependent diabetes mellitus: a randomized prospective 6-year study.

Ohkubo, Y., Kishikawa, H., Araki, E., Miyata, T., Isami, S., Motoyoshi, S., Kojima, Y., Furuyoshi, N., & Shichiri, M. (1995) · Diabetes Research and Clinical Practice · doi:10.1016/0168-8227(95)01064-k · Cited by 3,079

Targeted disruption of the melanocortin-4 receptor results in obesity in mice

Huszar, D., Lynch, C. A., Fairchild-Huntress, V., Dunmore, J. H., Fang, Q., Berkemeier, L. R., Gu, W., Kesterson, R. A., Boston, B. A., Cone, R. D., et al. (1997) · Cell · doi:10.1016/s0092-8674(00)81865-6 · Cited by 3,030

Diabetes and Atherosclerosis: Epidemiology, Pathophysiology, and Management

Beckman, J. A., Creager, M. A., & Libby, P. (2002) · JAMA · doi:10.1001/jama.287.19.2570 · Cited by 2,724

Prevalence of diabetes, impaired fasting glucose, and impaired glucose tolerance in U.S. adults. The Third National Health and Nutrition Examination Survey, 1988–1994

Harris, M. I., Flegal, K. M., Cowie, C. C., Eberhardt, M. S., Goldstein, D. E., Little, R. R., Wiedmeyer, H.-M., & Byrd-Holt, D. D. (1998) · Diabetes Care · doi:10.2337/diacare.21.4.518 · Cited by 2,703

The adipocyte-secreted protein Acrp30 enhances hepatic insulin action

Berg, A. H., Combs, T. P., Du, X., Brownlee, M., & Scherer, P. E. (2001) · Nature Medicine · doi:10.1038/90992 · Cited by 2,526

Human insulin receptor and its relationship to the tyrosine kinase family of oncogenes

Ullrich, A., Bell, J. R., Chen, E. Y., Herrera, R., Petruzzelli, L. M., Dull, T. J., Gray, A., Coussens, L., Liao, Y.-C., Tsubokawa, M., et al. (1985) · Nature · doi:10.1038/313756a0 · Cited by 2,251

AdipoQ Is a Novel Adipose-specific Gene Dysregulated in Obesity

Hu, E., Liang, P., & Spiegelman, B. M. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.18.10697 · Cited by 2,238

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

Increased Insulin Sensitivity and Obesity Resistance in Mice Lacking the Protein Tyrosine Phosphatase-1B Gene

Elchebly, M., Payette, P., Michaliszyn, E., Cromlish, W., Collins, S., Loy, A. L., Normandin, D., Cheng, A., Himms-Hagen, J., Chan, C.-C., et al. (1999) · Science · doi:10.1126/science.283.5407.1544 · Cited by 2,210

Diet-induced insulin resistance in mice lacking adiponectin/ACRP30

Maeda, N., Shimomura, I., Kishida, K., Nishizawa, H., Matsuda, M., Nagaretani, H., Furuyama, N., Kondo, H., Takahashi, M., Arita, Y., et al. (2002) · Nature Medicine · doi:10.1038/nm724 · Cited by 2,088

Leptin stimulates fatty-acid oxidation by activating AMP-activated protein kinase

Minokoshi, Y., Kim, Y.-B., Peroni, O. D., Fryer, L. G. D., Müller, C., Carling, D., & Kahn, B. B. (2002) · Nature · doi:10.1038/415339a · Cited by 2,053

The protein kinase encoded by the Akt proto-oncogene is a target of the PDGF-activated phosphatidylinositol 3-kinase

Franke, T. F., Yang, S.-I., Chan, T. O., Datta, K., Kazlauskas, A., Morrison, D. K., Kaplan, D. R., & Tsichlis, P. N. (1995) · Cell · doi:10.1016/0092-8674(95)90534-0 · Cited by 2,006

Proteolytic cleavage product of 30-kDa adipocyte complement-related protein increases fatty acid oxidation in muscle and causes weight loss in mice

Fruebis, J., Tsao, T., Javorschi, S., Ebbets-Reed, D., Erickson, M., Yen, F. T., Bihain, B. E., & Lodish, H. F. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.041591798 · Cited by 1,985

Role of melanocortinergic neurons in feeding and the agouti obesity syndrome

Fan, W., Boston, B. A., Kesterson, R. A., Hruby, V. J., & Cone, R. D. (1997) · Nature · doi:10.1038/385165a0 · Cited by 1,902

ERKs: A family of protein-serine/threonine kinases that are activated and tyrosine phosphorylated in response to insulin and NGF

Boulton, T. G., Nye, S. H., Robbins, D. J., Ip, N. Y., Radzlejewska, E., Morgenbesser, S. D., DePinho, R. A., Panayotatos, N., Cobb, M. H., & Yancopoulos, G. D. (1991) · Cell · doi:10.1016/0092-8674(91)90098-j · Cited by 1,897

Reversal of Obesity- and Diet-Induced Insulin Resistance with Salicylates or Targeted Disruption of Ikkβ

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

Control of hepatic gluconeogenesis through the transcriptional coactivator PGC-1

Yoon, J. C., Puigserver, P., Chen, G., Donovan, J., Wu, Z., Rhee, J., Adelmant, G., Stafford, J., Kahn, C. R., Granner, D. K., et al. (2001) · Nature · doi:10.1038/35093050 · Cited by 1,821

Disruption of IRS-2 causes type 2 diabetes in mice

Withers, D. J., Gutierrez, J. S., Towery, H., Burks, D. J., Ren, J.-M., Previs, S., Zhang, Y., Bernal, D., Pons, S., Shulman, G. I., et al. (1998) · Nature · doi:10.1038/36116 · Cited by 1,775

A transgenic model of visceral obesity and the metabolic syndrome

Masuzaki, H., Paterson, J., Shinyama, H., Morton, N. M., Mullins, J. J., Seckl, J. R., & Flier, J. S. (2001) · Science · doi:10.1126/science.1066285 · Cited by 1,766

Physical activity and reduced occurrence of non–insulin-dependent diabetes mellitus

Helmrich, S. P., Ragland, D. R., Leung, R. W., & Paffenbarger, R. S. (1991) · New England Journal of Medicine · doi:10.1056/nejm199107183250302 · Cited by 1,634

The anti-inflammatory agents aspirin and salicylate inhibit the activity of IκB kinase-β

Yin, M.-J., Yamamoto, Y., & Gaynor, R. B. (1998) · Nature · doi:10.1038/23948 · Cited by 1,590

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

Retinopathy and Nephropathy in Patients with Type 1 Diabetes Four Years after a Trial of Intensive Therapy

(2000) · New England Journal of Medicine · doi:10.1056/nejm200002103420603 · Cited by 1,534

Gabapentin for the Symptomatic Treatment of Painful Neuropathy in Patients With Diabetes Mellitus<SUBTITLE>A Randomized Controlled Trial</SUBTITLE>

Backonja, M. (1998) · JAMA · doi:10.1001/jama.280.21.1831 · Cited by 1,533

Efficacy of atenolol and captopril in reducing risk of macrovascular and microvascular complications in type 2 diabetes: UKPDS 39

(1998) · BMJ · doi:10.1136/bmj.317.7160.713 · Cited by 1,502

The c-Jun NH2-terminal kinase promotes insulin resistance during association with insulin receptor substrate-1 and phosphorylation of Ser307

Aguirre, V., Uchida, T., Yenush, L., Davis, R., & White, M. F. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.12.9047 · Cited by 1,487

The human insulin receptor cDNA: The structural basis for hormone-activated transmembrane signalling

Ebina, Y., Ellis, L., Jarnagin, K., Edery, M., Graf, L., Clauser, E., Ou, J.-H., Masiarz, F., Kan, Y. W., Goldfine, I. D., et al. (1985) · Cell · doi:10.1016/0092-8674(85)90334-4 · Cited by 1,477

Efficacy of atenolol and captopril in reducing risk of macrovascular and microvascular complications in type 2 diabetes: UKPDS 39

Stearne, M. R., Palmer, S. L., Hammersley, M. S., Franklin, S. L., Spivey, R. S., Lévy, J., Tidy, C. R., Bell, N. J., Steemson, J., Barrow, B. A., et al. (1998) · UCL Discovery (University College London) · Cited by 1,406

Obese and diabetes: Two mutant genes causing diabetes-obesity syndromes in mice

Coleman, D. L. (1978) · Diabetologia · doi:10.1007/bf00429772 · Cited by 1,307

Effect of 6-week course of glucagon-like peptide 1 on glycaemic control, insulin sensitivity, and β-cell function in type 2 diabetes: a parallel-group study

Zander, M., Madsbad, S., Madsen, J. L., & Holst, J. J. (2002) · The Lancet · doi:10.1016/s0140-6736(02)07952-7 · Cited by 1,297

Expression of a Constitutively Active Akt Ser/Thr Kinase in 3T3-L1 Adipocytes Stimulates Glucose Uptake and Glucose Transporter 4 Translocation

Kohn, A. D., Summers, S. A., Birnbaum, M. J., & Roth, R. A. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.49.31372 · Cited by 1,284

Adipose-selective targeting of the GLUT4 gene impairs insulin action in muscle and liver

Abel, E. D., Peroni, O., Kim, J. K., Kim, Y.-B., Boss, O., Hadro, E., Minnemann, T., Shulman, G. I., & Kahn, B. B. (2001) · Nature · doi:10.1038/35055575 · Cited by 1,253

Alternative pathway of insulin signalling in mice with targeted disruption of the IRS-1 gene

Araki, E., Lipes, M. A., Patti, M.-E., Brüning, J. C., Haag III, B., Johnson, R. S., & Kahn, C. R. (1994) · Nature · doi:10.1038/372186a0 · Cited by 1,252

Diet-Induced Type II Diabetes in C57BL/6J Mice

Surwit, R. S., Kuhn, C. M., Cochrane, C., McCubbin, J. A., & Feinglos, M. N. (1988) · Diabetes · doi:10.2337/diab.37.9.1163 · Cited by 1,208

The Effect of Long-Term Intensified Insulin Treatment on the Development of Microvascular Complications of Diabetes Mellitus

Reichard, P., Nilsson, B.-Y., & Rosenqvist, U. (1993) · New England Journal of Medicine · doi:10.1056/nejm199307293290502 · Cited by 1,202

Tumor necrosis factor alpha inhibits signaling from the insulin receptor.

Hotamisligil, G. S., Murray, D. L., Choy, L. N., & Spiegelman, B. M. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.11.4854 · Cited by 1,199

A Muscle-Specific Insulin Receptor Knockout Exhibits Features of the Metabolic Syndrome of NIDDM without Altering Glucose Tolerance

Brüning, J. C., Michael, M. D., Winnay, J. N., Hayashi, T., Hörsch, D., Accili, D., Goodyear, L. J., & Kahn, C. R. (1998) · Molecular Cell · doi:10.1016/s1097-2765(00)80155-0 · Cited by 1,182

Metabolic effects of metformin in non-insulin-dependent diabetes mellitus

Stumvoll, M., Nurjhan, N., Perriello, G., Dailey, G., & Gerich, J. E. (1995) · New England Journal of Medicine · doi:10.1056/nejm199508313330903 · Cited by 1,148

Insulin resistance differentially affects the PI 3-kinase- and MAP kinase-mediated signaling in human muscle

Cusi, K., Maezono, K., Osman, A., Pendergrass, M., Patti, M. E., Pratipanawatr, T., DeFronzo, R. A., Kahn, C. R., & Mandarino, L. J. (2000) · Journal of Clinical Investigation · doi:10.1172/jci7535 · Cited by 1,139

Effects of Desipramine, Amitriptyline, and Fluoxetine on Pain in Diabetic Neuropathy

Max, M. B., Lynch, S. A., Muir, J., Shoaf, S. E., Smoller, B., & Dubner, R. (1992) · New England Journal of Medicine · doi:10.1056/nejm199205073261904 · Cited by 1,117

Chronic intracerebroventricular infusion of insulin reduces food intake and body weight of baboons

Woods, S. C., Lotter, E. C., McKay, L. D., & Porte, D. (1979) · Nature · doi:10.1038/282503a0 · Cited by 1,114

OBESE, A NEW MUTATION IN THE HOUSE MOUSE*

INGALLS, A. M., DICKIE, M. M., & SNELL, G. D. (1950) · Journal of Heredity · doi:10.1093/oxfordjournals.jhered.a106073 · Cited by 1,090

Potential mechanism of insulin action on glucose transport in the isolated rat adipose cell. Apparent translocation of intracellular transport systems to the plasma membrane.

Cushman, S. W., & Wardzala, L. J. (1980) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)85561-8 · Cited by 1,086

Insulin resistance and growth retardation in mice lacking insulin receptor substrate-1

Tamemoto, H., Kadowaki, T., Tobe, K., Yagi, T., Sakura, H., Hayakawa, T., Terauchi, Y., Ueki, K., Kaburagi, Y., Satoh, S., et al. (1994) · Nature · doi:10.1038/372182a0 · Cited by 1,083

Agouti protein is an antagonist of the melanocyte-stimulating-hormone receptor

Lu, D., Willard, D., Patel, I. R., Kadwell, S., Overton, L., Kost, T., Luther, M., Chen, W., Woychik, R. P., Wilkison, W. O., et al. (1994) · Nature · doi:10.1038/371799a0 · Cited by 1,076

Phenotypes of Mouse diabetes and Rat fatty Due to Mutations in the OB (Leptin) Receptor

Chua, S. C., Chung, W. K., Wu-Peng, X. S., Zhang, Y., Liu, S.-M., Tartaglia, L., & Leibel, R. L. (1996) · Science · doi:10.1126/science.271.5251.994 · Cited by 1,075

PKB/Akt

Lawlor, M. A., & Alessi, D. R. (2001) · Journal of Cell Science · doi:10.1242/jcs.114.16.2903 · Cited by 1,071

Phosphatidylinositol 3-kinase activation is required for insulin stimulation of pp70 S6 kinase, DNA synthesis, and glucose transporter translocation.

Cheatham, B., Vlahos, C. J., Cheatham, L., Wang, L., Blenis, J., & Kahn, C. R. (1994) · Molecular and Cellular Biology · doi:10.1128/mcb.14.7.4902 · Cited by 1,068

Biochemical Adaptations to Endurance Exercise in Muscle

Holloszy, J. O., & Booth, F. W. (1976) · Annual Review of Physiology · doi:10.1146/annurev.ph.38.030176.001421 · Cited by 1,053

Mechanism by which metformin reduces glucose production in type 2 diabetes.

Hundal, R. S., Krssak, M., Dufour, S., Laurent, D., Lebon, V, Chandramouli, V, Inzucchi, S. E., Schumann, W. C., Petersen, K. F., Landau, B. R., et al. (2000) · Diabetes · doi:10.2337/diabetes.49.12.2063 · Cited by 1,052

Discovery of a metabolic pathway mediating glucose-induced desensitization of the glucose transport system. Role of hexosamine biosynthesis in the induction of insulin resistance.

Marshall, S., Bacote, V, & Traxinger, R. R. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)67706-9 · Cited by 1,047

A selective peroxisome proliferator-activated receptor δ agonist promotes reverse cholesterol transport

Oliver, W. R., Shenk, J. L., Snaith, M. R., Russell, C. S., Plunket, K. D., Bodkin, N. L., Lewis, M. C., Winegar, D. A., Sznaidman, M. L., Lambert, M. H., et al. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.091021198 · Cited by 1,046

Evidence that insulin causes translocation of glucose transport activity to the plasma membrane from an intracellular storage site.

Suzuki, K., & Kono, T. (1980) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.77.5.2542 · Cited by 1,034

Isolation and characterization of exendin-4, an exendin-3 analogue, from Heloderma suspectum venom. Further evidence for an exendin receptor on dispersed acini from guinea pig pancreas.

Eng, J., Kleinman, W. A., Singh, L., Singh, G., & Raufman, J. P. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)42531-8 · Cited by 1,000

Enhanced muscle fat oxidation and glucose transport by ACRP30 globular domain: Acetyl-CoA carboxylase inhibition and AMP-activated protein kinase activation

Tomas, E., Tsao, T.-S., Saha, A. K., Murrey, H. E., Zhang, C. C., Itani, S. I., Lodish, H. F., & Ruderman, N. B. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.222657499 · Cited by 973

Activation of the zeta isozyme of protein kinase C by phosphatidylinositol 3,4,5-trisphosphate.

Nakanishi, H., Brewer, K. A., & Exton, J. H. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)54107-7 · Cited by 965

Inhibition of gastric inhibitory polypeptide signaling prevents obesity

Miyawaki, K., Yamada, Y., Ban, N., Ihara, Y., Tsukiyama, K., Zhou, H., Fujimoto, S., Oku, A., Tsuda, K., Toyokuni, S., et al. (2002) · Nature Medicine · doi:10.1038/nm727 · Cited by 963

Akt1/PKBα Is Required for Normal Growth but Dispensable for Maintenance of Glucose Homeostasis in Mice

Cho, H., Thorvaldsen, J. L., Chu, Q., Feng, F., & Birnbaum, M. J. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.c100462200 · Cited by 959

Essential role of phosphatidylinositol 3-kinase in insulin-induced glucose transport and antilipolysis in rat adipocytes. Studies with a selective inhibitor wortmannin.

Okada, T., Kawano, Y., Sakakibara, T., Hazeki, O., & Ui, M. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)41901-6 · Cited by 918

Expression cloning of the pancreatic beta cell receptor for the gluco-incretin hormone glucagon-like peptide 1.

Thorens, B. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.18.8641 · Cited by 906

Glucagon-like peptide I stimulates insulin gene expression and increases cyclic AMP levels in a rat islet cell line.

Drucker, D. J., Philippe, J., Mojsov, S., Chick, W. L., & Habener, J. F. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.10.3434 · Cited by 903

Molecular cloning and characterization of an insulin-regulatable glucose transporter

James, D. E., Strube, M., & Muecdler, M. (1989) · Nature · doi:10.1038/338083a0 · Cited by 903

Fructose-induced insulin resistance and hypertension in rats.

Hwang, I. S., Ho, H., Hoffman, B. B., & Reaven, G. M. (1987) · Hypertension · doi:10.1161/01.hyp.10.5.512 · Cited by 889

Reduced Postprandial Concentrations of Intact Biologically Active Glucagon-Like Peptide 1 in Type 2 Diabetic Patients

Vilsbøll, T., Krarup, T., Deacon, C. F., Madsbad, S., & Holst, J. J. (2001) · Diabetes · doi:10.2337/diabetes.50.3.609 · Cited by 884

11β-Hydroxysteroid dehydrogenase type 1 knockout mice show attenuated glucocorticoid-inducible responses and resist hyperglycemia on obesity or stress

Kotelevtsev, Y., Holmes, M. C., Burchell, A., Houston, P. M., Schmoll, D., Jamieson, P., Best, R., Brown, R., Edwards, C. R. W., Seckl, J. R., et al. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.26.14924 · Cited by 858

AMP‐activated protein kinase phosphorylation of endothelial NO synthase

Chen, Z.-P., Mitchelhill, K. I., Michell, B. J., Stapleton, D., Rodriguez-Crespo, I., Witters, L. A., Power, D. A., Ortiz de Montellano, P. R., & Kemp, B. E. (1999) · FEBS Letters · doi:10.1016/s0014-5793(98)01705-0 · Cited by 835

Degradation of glucagon-like peptide-1 by human plasma in vitro yields an N-terminally truncated peptide that is a major endogenous metabolite in vivo.

Deacon, C. F., Johnsen, A. H., & Holst, J. J. (1995) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jcem.80.3.7883856 · Cited by 792

Serine Phosphorylation of Insulin Receptor Substrate 1 by Inhibitor κB Kinase Complex

Gao, Z., Hwang, D., Bataille, F., Lefevre, M., York, D., Quon, M. J., & Ye, J. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m209459200 · Cited by 778

Effect of fenofibrate on progression of coronary-artery disease in type 2 diabetes: the Diabetes Atherosclerosis Intervention Study, a randomised study

(2001) · The Lancet · doi:10.1016/s0140-6736(00)04209-4 · Cited by 768

Targeted disruption of the glucose transporter 4 selectively in muscle causes insulin resistance and glucose intolerance

Zisman, A., Peroni, O. D., Abel, E. D., Michael, M. D., Mauvais-Jarvis, F., Lowell, B. B., Wojtaszewski, J. F. P., Hirshman, M. F., Virkamaki, A., Goodyear, L. J., et al. (2000) · Nature Medicine · doi:10.1038/78693 · Cited by 743

Effect of fenofibrate on progression of coronary-artery disease in type 2 diabetes: the Diabetes Atherosclerosis Intervention Study, a randomised study

Steiner, G. A. (2001) · Cited by 732

Preliminary Report on Effects of Photocoagulation Therapy

(1976) · American Journal of Ophthalmology · doi:10.1016/0002-9394(76)90292-0 · Cited by 723

Decreasing hypothalamic insulin receptors causes hyperphagia and insulin resistance in rats

Obici, S., Feng, Z., Karkanias, G., Baskin, D. G., & Rossetti, L. (2002) · Nature Neuroscience · doi:10.1038/nn0602-861 · Cited by 719

5' AMP-activated protein kinase activation causes GLUT4 translocation in skeletal muscle.

Kurth-Kraczek, E. J., Hirshman, M. F., Goodyear, L. J., & Winder, W. W. (1999) · Diabetes · doi:10.2337/diabetes.48.8.1667 · Cited by 713

Activation of AMP-activated protein kinase increases mitochondrial enzymes in skeletal muscle

Winder, W. W., Holmes, B. F., Rubink, D. S., Jensen, E. B., Chen, M., & Holloszy, J. O. (2000) · Journal of Applied Physiology · doi:10.1152/jappl.2000.88.6.2219 · Cited by 709

Potent Derivatives of Glucagon-like Peptide-1 with Pharmacokinetic Properties Suitable for Once Daily Administration

Knudsen, L. B., Nielsen, P. F., Huusfeldt, P. O., Johansen, N. L., Madsen, K., Pedersen, F. Z., Thøgersen, H., Wilken, M., & Agersø, H. (2000) · Journal of Medicinal Chemistry · doi:10.1021/jm9909645 · Cited by 700

Waging war on modern chronic diseases: primary prevention through exercise biology

Booth, F. W., Gordon, S. E., Carlson, C. J., & Hamilton, M. T. (2000) · Journal of Applied Physiology · doi:10.1152/jappl.2000.88.2.774 · Cited by 693

Untitled work

(1997) · Diabetes reviews · Cited by 671

Insulin-regulatable tissues express a unique insulin-sensitive glucose transport protein

James, D. E., Brown, R., Navarro, J., & Pilch, P. F. (1988) · Nature · doi:10.1038/333183a0 · Cited by 666

CAP defines a second signalling pathway required for insulin-stimulated glucose transport

Baumann, C. A., Ribon, V., Kanzaki, M., Thurmond, D. C., Mora, S., Shigematsu, S., Bickel, P. E., Pessin, J. E., & Saltiel, A. R. (2000) · Nature · doi:10.1038/35025089 · Cited by 661

The crystal structure of a complement-1q family protein suggests an evolutionary link to tumor necrosis factor

Shapiro, L., & Scherer, P. E. (1998) · Current Biology · doi:10.1016/s0960-9822(98)70133-2 · Cited by 655

Pioglitazone hydrochloride monotherapy improves glycemic control in the treatment of patients with type 2 diabetes: a 6-month randomized placebo-controlled dose-response study. The Pioglitazone 001 Study Group.

Aronoff, S., Rosenblatt, S., Braithwaite, S., Egan, J. W., Mathisen, A. L., & Schneider, R. L. (2000) · Diabetes Care · doi:10.2337/diacare.23.11.1605 · Cited by 629

Insulin-stimulated GLUT4 translocation requires the CAP-dependent activation of TC10

Chiang, S.-H., Baumann, C. A., Kanzaki, M., Thurmond, D. C., Watson, R. T., Neudauer, C. L., Macara, I. G., Pessin, J. E., & Saltiel, A. R. (2001) · Nature · doi:10.1038/35073608 · Cited by 611

Effects of Glucagon-Like Peptide 1 on Counterregulatory Hormone Responses, Cognitive Functions, and Insulin Secretion during Hyperinsulinemic, Stepped Hypoglycemic Clamp Experiments in Healthy Volunteers

Nauck, M. A., Heimesaat, M. M., Behle, K., Holst, J. J., Nauck, M. S., Ritzel, R., Hüfner, M., & Schmiegel, W. H. (2002) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jcem.87.3.8355 · Cited by 605

Identification of a novel gene encoding an insulin-responsive glucose transporter protein

Birnbaum, M. J. (1989) · Cell · doi:10.1016/0092-8674(89)90968-9 · Cited by 598

Biguanides and NIDDM

Bailey, C. J. (1992) · Diabetes Care · doi:10.2337/diacare.15.6.755 · Cited by 593

Nephropathy in Patients with Type 2 Diabetes

Remuzzi, G., Schieppati, A., & Ruggenenti, P. (2002) · New England Journal of Medicine · doi:10.1056/nejmcp011773 · Cited by 587

The pathway to signal achievement

Egan, S. E., & Weinberg, R. A. (1993) · Nature · doi:10.1038/365781a0 · Cited by 559

Activation of protein kinase C family members by the novel polyphosphoinositides PtdIns-3,4-P2 and PtdIns-3,4,5-P3.

Toker, A., Meyer, M., Reddy, K. K., Falck, J. R., Aneja, R., Aneja, S., Parra, A., Burns, D. J., Ballas, L. M., & Cantley, L. C. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)31643-0 · Cited by 553

Tumor necrosis factor-alpha suppresses insulin-induced tyrosine phosphorylation of insulin receptor and its substrates.

Feinstein, R., Kanety, H., Papa, M. Z., Lunenfeld, B., & Karasik, A. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)74276-8 · Cited by 549

A Molecular Basis for Insulin Resistance

Paz, K., Hemi, R., LeRoith, D., Karasik, A., Elhanany, E., Kanety, H., & Zick, Y. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.47.29911 · Cited by 549

Development of a Novel Polygenic Model of NIDDM in Mice Heterozygous for IR and IRS-1 Null Alleles

Brüning, J. C., Winnay, J., Bonner-Weir, S., Taylor, S. I., Accili, D., & Kahn, C. R. (1997) · Cell · doi:10.1016/s0092-8674(00)81896-6 · Cited by 547

Tumor necrosis factor impairs insulin action on peripheral glucose disposal and hepatic glucose output.

Lang, C. H., Dobrescu, C., & Bagby, G. J. (1992) · Endocrinology · doi:10.1210/endo.130.1.1727716 · Cited by 535

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

A Method to Identify Serine Kinase Substrates

Kane, S., Sano, H., Liu, S. C. H., Asara, J. M., Lane, W. S., Garner, C. C., & Lienhard, G. E. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.c200198200 · Cited by 526

Efficacy of Metformin in Type II Diabetes

Garber, A. J., Duncan, T. G., Goodman, A. M., Mills, D. J., & Rohlf, J. L. (1997) · The American Journal of Medicine · doi:10.1016/s0002-9343(97)00254-4 · Cited by 519

Rosiglitazone Monotherapy Is Effective in Patients with Type 2 Diabetes

Lebovitz, H. E., Dole, J., Patwardhan, R., Rappaport, E. B., & Freed, M. I. (2001) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.86.1.280 · Cited by 518

Randomised placebo-controlled trial of lisinopril in normotensive patients with insulin-dependent diabetes and normoalbuminuria or microalbuminuria

Chaturvedi, N. (1997) · The Lancet · doi:10.1016/s0140-6736(96)10244-0 · Cited by 518

Additive insulinotropic effects of exogenous synthetic human gastric inhibitory polypeptide and glucagon-like peptide-1-(7-36) amide infused at near-physiological insulinotropic hormone and glucose concentrations

Nauck, M. A. (1993) · Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.76.4.912 · Cited by 506

Gastric emptying, glucose responses, and insulin secretion after a liquid test meal: effects of exogenous glucagon-like peptide-1 (GLP-1)-(7-36) amide in type 2 (noninsulin-dependent) diabetic patients.

Willms, B., Werner, J., Holst, J. J., Orskov, C., Creutzfeldt, W., & Nauck, M. A. (1996) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jcem.81.1.8550773 · Cited by 502

Tissue-specific insulin resistance in mice with mutations in the insulin receptor, IRS-1, and IRS-2

Kido, Y., Burks, D. J., Withers, D., Bruning, J. C., Kahn, C. R., White, M. F., & Accili, D. (2000) · Journal of Clinical Investigation · doi:10.1172/jci7917 · Cited by 492

Cloning and characterization of the major insulin-responsive glucose transporter expressed in human skeletal muscle and other insulin-responsive tissues

Fukumoto, H., Kayano, T., Buse, J. B., Edwards, Y., Pilch, P. F., Bell, G. I., & Seino, S. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)83106-4 · Cited by 474

AMP-activated protein kinase, super metabolic regulator

Kemp, B. E., Stapleton, D., Campbell, D. J., Chen, Z.-P., Murthy, S., Walter, M., Gupta, A., Adams, J. J., Katsis, F., van Denderen, B., et al. (2003) · Biochemical Society Transactions · doi:10.1042/bst0310162 · Cited by 473

Cardiac and adipose tissue abnormalities but not diabetes in mice deficient in GLUT4

Katz, E. B., Stenbit, A. E., Hatton, K., DePinhot, R., & Charron, M. J. (1995) · Nature · doi:10.1038/377151a0 · Cited by 471

Insulin Stimulates Phosphorylation of the Forkhead Transcription Factor FKHR on Serine 253 through a Wortmannin-sensitive Pathway

Nakae, J., Park, B.-C., & Accili, D. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.23.15982 · Cited by 470

Akt, a Pleckstrin Homology Domain Containing Kinase, Is Activated Primarily by Phosphorylation

Kohn, A. D., Takeuchi, F., & Roth, R. A. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.36.21920 · Cited by 467

Evidence That the Angiotensin IV (AT4) Receptor Is the Enzyme Insulin-regulated Aminopeptidase

Albiston, A. L., McDowall, S. G., Matsacos, D., Sim, P., Clune, E., Mustafa, T., Lee, J., Mendelsohn, F. A. O., Simpson, R. J., Connolly, L. M., et al. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.c100512200 · Cited by 461

Discovery of a Small Molecule Insulin Mimetic with Antidiabetic Activity in Mice

Zhang, B., Salituro, G., Szalkowski, D., Li, Z., Zhang, Y., Royo, I., Vilella, D., Dı́ez, M. T., Pelaez, F., Ruby, C., et al. (1999) · Science · doi:10.1126/science.284.5416.974 · Cited by 456

Glucose-lowering and insulin-sensitizing actions of exendin-4: studies in obese diabetic (ob/ob, db/db) mice, diabetic fatty Zucker rats, and diabetic rhesus monkeys (Macaca mulatta).

Young, A. A., Gedulin, B. R., Bhavsar, S., Bodkin, N., Jodka, C., Hansen, B., & Denaro, M. (1999) · Diabetes · doi:10.2337/diabetes.48.5.1026 · Cited by 440

The Efficacy of Acarbose in the Treatment of Patients with Non–Insulin-Dependent Diabetes Mellitus: A Multicenter, Controlled Clinical Trial

Chiasson, J.-L., Josse, R. G., Hunt, J. A., Palmason, C., Rodger, N. W., Ross, S. A., Ryan, E. A., Tan, M. H., & Wolever*, T. M. S. (1994) · Annals of Internal Medicine · doi:10.7326/0003-4819-121-12-199412150-00004 · Cited by 436

Minireview: The Glucagon-Like Peptides

Drucker, D. J. (2001) · Endocrinology · doi:10.1210/en.142.2.521 · Cited by 421

Inhibition of Dipeptidyl Peptidase IV Improves Metabolic Control Over a 4-Week Study Period in Type 2 Diabetes

Ahrén, B., Simonsson, E., Larsson, H., Landin-Olsson, M., Torgeirsson, H., Jansson, P.-A., Sandqvist, M., Båvenholm, P., Efendic, S., Eriksson, J. W., et al. (2002) · Diabetes Care · doi:10.2337/diacare.25.5.869 · Cited by 421

Acute exercise induces GLUT4 translocation in skeletal muscle of normal human subjects and subjects with type 2 diabetes

Kennedy, J. W., Hirshman, M. F., Gervino, E. V., Ocel, J. V., Forse, R. A., Hoenig, S. J., Aronson, D., Goodyear, L. J., & Horton, E. S. (1999) · Diabetes · doi:10.2337/diabetes.48.5.1192 · Cited by 415

Exercise induces rapid increases in GLUT4 expression, glucose transport capacity, and insulin-stimulated glycogen storage in muscle.

Ren, J. M., Semenkovich, C. F., Gulve, E. A., Gao, J., & Holloszy, J. O. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)36636-x · Cited by 415

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., Jacobson, P., Frost, L., et al. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.142298199 · Cited by 414

Insulin action on glucose transport and plasma membrane GLUT4 content in skeletal muscle from patients with NIDDM

Zierath, J. R., He, L., Gumà, A., Wahlström, E. O., Klip, A., & Wallberg-Henriksson, H. (1996) · Diabetologia · doi:10.1007/bf02658504 · Cited by 402

Mitogen-activated Protein Kinase Kinase Inhibition Does Not Block the Stimulation of Glucose Utilization by Insulin

Lazar, D. F., Wiese, R. J., Brady, M. J., Mastick, C. C., Waters, S. B., Yamauchi, K., Pessin, J. E., Cuatrecasas, P., & Saltiel, A. R. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.35.20801 · Cited by 396

Contraction-induced Changes in Acetyl-CoA Carboxylase and 5′-AMP-activated Kinase in Skeletal Muscle

Vavvas, D., Apazidis, A., Saha, A. K., Gamble, J., Patel, A., Kemp, B. E., Witters, L. A., & Ruderman, N. B. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.20.13255 · Cited by 395

A glucose transport protein expressed predominately in insulin-responsive tissues.

Charron, M. J., Brosius, F. C., Alper, S. L., & Lodish, H. F. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.8.2535 · Cited by 390

Use of Enalapril To Attenuate Decline in Renal Function in Normotensive, Normoalbuminuric Patients with Type 2 Diabetes Mellitus: A Randomized, Controlled Trial

Ravid, M., Brosh, D., Levi, Z., Bar-Dayan, Y., Ravid, D., & Rachmani, R. (1998) · Annals of Internal Medicine · doi:10.7326/0003-4819-128-12_part_1-199806150-00004 · Cited by 389

The identification of ATP-citrate lyase as a protein kinase B (Akt) substrate in primary adipocytes

Berwick, D. C., Hers, I., Heesom, K. J., Moule, S. K., & Tavareá, J. M. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m204681200 · Cited by 383

AMP-activated protein kinase (AMPK) is activated in muscle of subjects with type 2 diabetes during exercise

Musi, N., Fujii, N., Hirshman, M. F., Ekberg, I., Fröberg, S., Ljungqvist, O., Thorell, A., & Goodyear, L. J. (2001) · Diabetes · doi:10.2337/diabetes.50.5.921 · Cited by 371

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

The blooming of the French lilac

Witters, L. A. (2001) · Journal of Clinical Investigation · doi:10.1172/jci14178 · Cited by 367

Requirement of Atypical Protein Kinase Cλ for Insulin Stimulation of Glucose Uptake but Not for Akt Activation in 3T3-L1 Adipocytes

Kotani, K., Ogawa, W., Matsumoto, M., Kitamura, T., Sakaue, H., Hino, Y., Miyake, K., Sano, W., Akimoto, K., Ohno, S., et al. (1998) · Molecular and Cellular Biology · doi:10.1128/mcb.18.12.6971 · Cited by 360

Insulin stimulates the kinase activity of RAC-PK, a pleckstrin homology domain containing ser/thr kinase.

Kohn, A. D., Kovacina, K. S., & Roth, R. A. (1995) · The EMBO Journal · doi:10.1002/j.1460-2075.1995.tb00103.x · Cited by 355

Dietary Obesity in Rats: Body Weight and Body Fat Accretion in Seven Strains of Rats

Schemmel, R., Mickelsen, O., & Gill, J. L. (1970) · The Journal of Nutrition · doi:10.1093/jn/100.9.1041 · Cited by 352

Antidiabetic thiazolidinediones inhibit leptin (ob) gene expression in 3T3-L1 adipocytes.

Kallen, C. B., & Lazar, M. A. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.12.5793 · Cited by 337

Overexpression of glutamine:fructose-6-phosphate amidotransferase in transgenic mice leads to insulin resistance.

Hebert, L. F., Daniels, M. C., Zhou, J., Crook, E. D., Turner, R. L., Simmons, S. T., Neidigh, J. L., Zhu, J. S., Baron, A. D., & McClain, D. A. (1996) · Journal of Clinical Investigation · doi:10.1172/jci118876 · Cited by 335

Hexosamines and Insulin Resistance

McClain, D. A., & Crook, E. D. (1996) · Diabetes · doi:10.2337/diab.45.8.1003 · Cited by 334

Effects of weight loss on mechanisms of hyperglycemia in obese non-insulin-dependent diabetes mellitus

Henry, R. R., Wallace, P., & Olefsky, J. M. (1986) · Diabetes · doi:10.2337/diab.35.9.990 · Cited by 325

Role of the glucosamine pathway in fat-induced insulin resistance.

Hawkins, M., Barzilai, N., Liu, R., Hu, M., Chen, W., & Rossetti, L. (1997) · Journal of Clinical Investigation · doi:10.1172/jci119390 · Cited by 325

Cloning and Characterization of a Novel Insulin-regulated Membrane Aminopeptidase from Glut4 Vesicles

Keller, S. R., Scott, H. M., Mastick, C. C., Aebersold, R., & Lienhard, G. E. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.40.23612 · Cited by 325

Postchallenge Glucose Concentration and Coronary Heart Disease in Men of Japanese Ancestry: Honolulu Heart Program

Donahue, R. P., Abbott, R. D., Reed, D. M., & Yano, K. (1987) · Diabetes · doi:10.2337/diab.36.6.689 · Cited by 316

Alterations in the Expression and Cellular Localization of Protein Kinase C Isozymes ε and θ Are Associated With Insulin Resistance in Skeletal Muscle of the High-Fat–Fed Rat

Schmitz-Peiffer, C., Browne, C. L., Oakes, N. D., Watkinson, A., Chisholm, D. J., Kraegen, E. W., & Biden, T. J. (1997) · Diabetes · doi:10.2337/diab.46.2.169 · Cited by 314

The Effects of Wortmannin on Rat Skeletal Muscle

Yeh, J.-I., Gulve, E. A., Rameh, L., & Birnbaum, M. J. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.5.2107 · Cited by 314

The Antihyperglycaemic Effect of Metformin: Therapeutic and Cellular Mechanisms

Wiernsperger, N. F., & Bailey, C. J. (1999) · Drugs · doi:10.2165/00003495-199958001-00009 · Cited by 312

The Finnish Diabetes Prevention Study

Uusitupa, M., Louheranta, A., Lindström, J., Valle, T., Sundvall, J., Eriksson, J., & Tuomilehto, J. (2000) · British Journal of Nutrition · doi:10.1017/s0007114500001070 · Cited by 306

Once- and Twice-Daily Dosing With Rosiglitazone Improves Glycemic Control in Patients With Type 2 Diabetes

Phillips, L. S., Grunberger, G., Miller, E., Patwardhan, R., Rappaport, E. B., Salzman, A., & the Rosiglitazone Clinical Trials Study Group (2001) · Diabetes Care · doi:10.2337/diacare.24.2.308 · Cited by 302

Exercise training increases lipid metabolism gene expression in human skeletal muscle

Tunstall, R. J., Mehan, K. A., Wadley, G. D., Collier, G. R., Bonen, A., Hargreaves, M., & Cameron-Smith, D. (2002) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00475.2001 · Cited by 292

Increased β-Oxidation but No Insulin Resistance or Glucose Intolerance in Mice Lacking Adiponectin

Ma, K., Cabrero, A., Saha, P. K., Kojima, H., Li, L., Chang, B. H.-J., Paul, A., & Chan, L. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.c200362200 · Cited by 287

Effect of intensive diabetes treatment on nerve conduction in the diabetes control and complications trial

DCCT Research Group, B. N. (1995) · Annals of Neurology · doi:10.1002/ana.410380607 · Cited by 283

Acarbose: A Preliminary Review of its Pharmacodynamic and Pharmacokinetic Properties, and Therapeutic Potential

Clissold, S. P., & Edwards, C. (1988) · Drugs · doi:10.2165/00003495-198835030-00003 · Cited by 282

Pharmacokinetics, Pharmacodynamics, Safety, and Tolerability of a Single-Dose of NN2211, a Long-Acting Glucagon-Like Peptide 1 Derivative, in Healthy Male Subjects

Elbrønd, B., Jakobsen, G., Larsen, S., Agersø, H., Jensen, L. B., Rolan, P., Sturis, J., Hatorp, V., & Zdravkovic, M. (2002) · Diabetes Care · doi:10.2337/diacare.25.8.1398 · Cited by 279

Carbenoxolone increases hepatic insulin sensitivity in man: a novel role for 11-oxosteroid reductase in enhancing glucocorticoid receptor activation

Walker, B. R. (1995) · Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.80.11.3155 · Cited by 277

Evidence from transgenic mice that glucose transport is rate-limiting for glycogen deposition and glycolysis in skeletal muscle

Ren, J. M., Marshall, B. A., Gulve, E. A., Gao, J., Johnson, D. W., Holloszy, J. O., & Mueckler, M. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)85395-4 · Cited by 274

Sodium salicylate induces apoptosis via p38 mitogen-activated protein kinase but inhibits tumor necrosis factor-induced c-Jun N-terminal kinase/stress-activated protein kinase activation

Schwenger, P., Bellosta, P., Vietor, I., Basilico, C., Skolnik, E. Y., & Vilček, J. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.7.2869 · Cited by 274

EGF or PDGF receptors activate atypical PKClambda through phosphatidylinositol 3-kinase.

Akimoto, K., Takahashi, R., Moriya, S., Nishioka, N., Takayanagi, J., Kimura, K., Fukui, Y., Osada, S.-I., Mizuno, K., Hirai, S.-I., et al. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb00414.x · Cited by 273

Near-normalisation of diurnal glucose concentrations by continuous administration of glucagon-like peptide-1 (GLP-1) in subjects with NIDDM

Rachman, J., Barrow, B. A., Levy, J. C., & Turner, R. C. (1997) · Diabetologia · doi:10.1007/s001250050664 · Cited by 269

Improved Glucose Tolerance in Zucker Fatty Rats by Oral Administration of the Dipeptidyl Peptidase IV Inhibitor Isoleucine Thiazolidide

Pederson, R. A., White, H. A., Schlenzig, D., Pauly, R. P., McIntosh, C. H. S., & Demuth, H.-U. (1998) · Diabetes · doi:10.2337/diab.47.8.1253 · Cited by 267

GIF biology and fat metabolism

Yip, R. G. C., & Wolfe, M. M. (1999) · Life Sciences · doi:10.1016/s0024-3205(99)00314-8 · Cited by 266

In vivo glucosamine infusion induces insulin resistance in normoglycemic but not in hyperglycemic conscious rats.

Rossetti, L., Hawkins, M., Chen, W., Gindi, J., & Barzilai, N. (1995) · Journal of Clinical Investigation · doi:10.1172/jci118013 · Cited by 264

Bedtime Administration of NN2211, a Long-Acting GLP-1 Derivative, Substantially Reduces Fasting and Postprandial Glycemia in Type 2 Diabetes

Juhl, C. B., Hollingdal, M., Sturis, J., Jakobsen, G., Agersø, H., Veldhuis, J., Pørksen, N., & Schmitz, O. (2002) · Diabetes · doi:10.2337/diabetes.51.2.424 · Cited by 264

Selective inhibition of 11β-hydroxysteroid dehydrogenase type 1 decreases blood glucose concentrations in hyperglycaemic mice

P., A., L., E., N., E., M., F., G., K., C., L., Y., R.-N., B., Ö., & L., A. (2002) · Diabetologia · doi:10.1007/s00125-002-0959-6 · Cited by 259

The Insulinotropic Effect of Acute Exendin-4 Administered to Humans: Comparison of Nondiabetic State to Type 2 Diabetes

Egan, J. M. (2002) · Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.87.3.1282 · Cited by 256

Mouse models of insulin resistance

Hribal, M. L., Oriente, F., & Accili, D. (2002) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00561.2001 · Cited by 252

Insights into insulin resistance and type 2 diabetes from knockout mouse models

Kadowaki, T. (2000) · Journal of Clinical Investigation · doi:10.1172/jci10830 · Cited by 249

Insulin Increases the Association of Akt-2 with Glut4-containing Vesicles

Calera, M. R., Martinez, C., Liu, H., Jack, A. K. E., Birnbaum, M. J., & Pilch, P. F. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.13.7201 · Cited by 245

Insulinotropic actions of exendin-4 and glucagon-like peptide-1 in vivo and in vitro

Parkes, D. G., Pittner, R., Jodka, C., Smith, P., & Young, A. (2001) · Metabolism · doi:10.1053/meta.2001.22519 · Cited by 241

Glucosamine induces insulin resistance in vivo by affecting GLUT 4 translocation in skeletal muscle. Implications for glucose toxicity.

Baron, A. D., Zhu, J. S., Zhu, J. H., Weldon, H., Maianu, L., & Garvey, W. T. (1995) · Journal of Clinical Investigation · doi:10.1172/jci118349 · Cited by 241

Activated Phosphatidylinositol 3-Kinase Is Sufficient to Mediate Actin Rearrangement and GLUT4 Translocation in 3T3-L1 Adipocytes

Martin, S. S., Haruta, T., Morris, A. J., Klippel, A., Williams, L. T., & Olefsky, J. M. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.30.17605 · Cited by 238

Therapeutic potential of dipeptidyl peptidase IV inhibitors for the treatment of type 2 diabetes

Drucker, D. (2003) · Expert Opinion on Investigational Drugs · doi:10.1517/13543784.12.1.87 · Cited by 237

Long-Term Treatment With the Dipeptidyl Peptidase IV Inhibitor P32/98 Causes Sustained Improvements in Glucose Tolerance, Insulin Sensitivity, Hyperinsulinemia, and β-Cell Glucose Responsiveness in VDF (fa/fa) Zucker Rats

Pospisilik, J. A., Stafford, S. G., Demuth, H.-U., Brownsey, R., Parkhouse, W., Finegood, D. T., McIntosh, C. H. S., & Pederson, R. A. (2002) · Diabetes · doi:10.2337/diabetes.51.4.943 · Cited by 232

Dormancy of Inhibitory Interneurons in a Model of Temporal Lobe Epilepsy

Bekenstein, J. W., & Lothman, E. W. (1993) · Science · doi:10.1126/science.8093417 · Cited by 231

Adult human chondrocytes cultured in alginate form a matrix similar to native human articular cartilage

Hauselmann, H. J., Masuda, K., Hunziker, E. B., Neidhart, M., Mok, S. S., Michel, B. A., & Thonar, E. J. (1996) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.1996.271.3.c742 · Cited by 230

Reduced Insulinotropic Effect of Gastric Inhibitory Polypeptide in First-Degree Relatives of Patients With Type 2 Diabetes

Meier, J. J., Hücking, K., Holst, J. J., Deacon, C. F., Schmiegel, W. H., & Nauck, M. A. (2001) · Diabetes · doi:10.2337/diabetes.50.11.2497 · Cited by 230

Mice lacking insulin receptor substrate 4 exhibit mild defects in growth, reproduction, and glucose homeostasis

Fantin, V. R., Wang, Q., Lienhard, G. E., & Keller, S. R. (2000) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.2000.278.1.e127 · Cited by 225

Regulation of glucose transport into skeletal muscle.

Holloszy, J., & Hansen, P. (1996) · Reviews of Physiology, Biochemistry and Pharmacology · doi:10.1007/3-540-61343-9_8 · Cited by 220

Evidence for Involvement of Protein Kinase C (PKC)-ζ and Noninvolvement of Diacylglycerol-Sensitive PKCs in Insulin-Stimulated Glucose Transport in L6 Myotubes*

Bandyopadhyay, G., Standaert, M. L., Galloway, L., Moscat, J., & Farese, R. V. (1997) · Endocrinology · doi:10.1210/endo.138.11.5473 · Cited by 218

Insulin-stimulated phosphatidylinositol 3-kinase. Association with a 185-kDa tyrosine-phosphorylated protein (IRS-1) and localization in a low density membrane vesicle.

Kelly, K. L., & Ruderman, N. B. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)53622-x · Cited by 216

Glucose Transport Is Rate Limiting for Skeletal Muscle Glucose Metabolism in Normal and STZ-Induced Diabetic Rats

Ziel, F. H., Venkatesan, N., & Davidson, M. B. (1988) · Diabetes · doi:10.2337/diab.37.7.885 · Cited by 215

Molecular cloning of rat obese cDNA and augmented gene expression in genetically obese Zucker fatty (fa/fa) rats.

Ogawa, Y., Masuzaki, H., Isse, N., Okazaki, T., Mori, K., Shigemoto, M., Satoh, N., Tamura, N., Hosoda, K., & Yoshimasa, Y. (1995) · Journal of Clinical Investigation · doi:10.1172/jci118204 · Cited by 215

The glucose transporter (GLUT-4) and vesicle-associated membrane protein-2 (VAMP-2) are segregated from recycling endosomes in insulin-sensitive cells.

Martin, S., Tellam, J., Livingstone, C., Slot, J. W., Gould, G. W., & James, D. E. (1996) · The Journal of cell biology · doi:10.1083/jcb.134.3.625 · Cited by 214

A Novel, Multifunctional c-Cbl Binding Protein in Insulin Receptor Signaling in 3T3-L1 Adipocytes

Ribon, V., Printen, J. A., Hoffman, N. G., Kay, B. K., & Saltiel, A. R. (1998) · Molecular and Cellular Biology · doi:10.1128/mcb.18.2.872 · Cited by 214

GENETICS OF NON-INSULIN-DEPENDENT (TYPE-II) DIABETES MELLITUS

Kahn, M. D., Vicent, M. D., & Doria, M. D. (1996) · Annual Review of Medicine · doi:10.1146/annurev.med.47.1.509 · Cited by 213

Minireview: Tissue-Specific Versus Generalized Gene Targeting of the igf1 and igf1r Genes and Their Roles in Insulin-Like Growth Factor Physiology

Butler, A. A. (2001) · Endocrinology · doi:10.1210/en.142.5.1685 · Cited by 211

Pharmacokinetic, insulinotropic, and glucagonostatic properties of GLP-1 [7?36 amide] after subcutaneous injection in healthy volunteers. Dose-response-relationships

Ritzel, R., �rskov, C., Holst, J. J., & Nauck, M. A. (1995) · Diabetologia · doi:10.1007/bf00401846 · Cited by 210

Insulin Activates Protein Kinases C-ζ and C-λ by an Autophosphorylation-dependent Mechanism and Stimulates Their Translocation to GLUT4 Vesicles and Other Membrane Fractions in Rat Adipocytes

Standaert, M. L., Bandyopadhyay, G., Perez, L., Price, D., Galloway, L., Poklepovic, A., Sajan, M. P., Cenni, V., Sirri, A., Moscat, J., et al. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.36.25308 · Cited by 210

Differential Signaling by Insulin Receptor Substrate 1 (IRS-1) and IRS-2 in IRS-1-Deficient Cells

Brüning, J. C., Winnay, J., Cheatham, B., & Kahn, C. R. (1997) · Molecular and Cellular Biology · doi:10.1128/mcb.17.3.1513 · Cited by 210

Impaired cardiac contractile function in ventricular myocytes from leptin-deficient ob/ob obese mice

Dong, F., Zhang, X., Yang, X., Esberg, L. B., Yang, H., Zhang, Z., Culver, B., & Ren, J. (2006) · Journal of Endocrinology · doi:10.1677/joe.1.06241 · Cited by 155

Exercise and Glycemic Control in Diabetes: Benefits, Challenges, and Adjustments to Pharmacotherapy

Gulve, E. A. (2008) · Physical Therapy · doi:10.2522/ptj.20080114 · Cited by 120