Adiponectin Activates AMP-Activated Protein Kinase in Muscle Cells via APPL1/LKB1-Dependent and Phospholipase C/Ca2+/Ca2+/Calmodulin-Dependent Protein Kinase Kinase-Dependent Pathways

Adiponectin stimulates glucose utilization and fatty-acid oxidation by activating AMP-activated protein kinase

Yamauchi, T., Kamon, J., Minokoshi, Y., Ito, Y., Waki, H., Uchida, S., Yamashita, S., Noda, M., Kita, S., Ueki, K., et al. (2002) · Nature Medicine · doi:10.1038/nm788 · Cited by 4,238 · see citing works

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

Scherer, P. E., Williams, S. P., Fogliano, M., Baldini, G., & Lodish, H. F. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.45.26746 · Cited by 3,238 · see citing works

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 · see citing works

de la Chapelle, A.

Beighton, P., & Beighton, G. (1997) · Springer eBooks · doi:10.1007/978-1-4471-0925-9_118 · Cited by 3,165 · see citing works

Adiponectin and Adiponectin Receptors

Kadowaki, T., & Yamauchi, T. (2005) · Endocrine Reviews · doi:10.1210/er.2005-0005 · Cited by 2,634 · see citing works

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.98.4.2005 · Cited by 1,987 · see citing works

A serine/threonine kinase gene defective in Peutz–Jeghers syndrome

Hemminki, A., Markie, D., Tomlinson, I. P. M., Avizienyte, E., Roth, S., Loukola, A., Bignell, G. R., Warren, W., Aminoff, M., Höglund, P., et al. (1998) · Nature · doi:10.1038/34432 · Cited by 1,652 · see citing works

Calmodulin-dependent protein kinase kinase-β is an alternative upstream kinase for AMP-activated protein kinase

Hawley, S. A., Pan, D. A., Mustard, K. J., Ross, L., Bain, J., Edelman, A. M., Frenguelli, B. G., & Hardie, D. G. (2005) · Cell Metabolism · doi:10.1016/j.cmet.2005.05.009 · Cited by 1,589 · see citing works

Ca2+/calmodulin-dependent protein kinase kinase-β acts upstream of AMP-activated protein kinase in mammalian cells

Woods, A., Dickerson, K., Heath, R. B., Hong, S. P., Momcilovic, M., Johnstone, S. R., Carlson, M., & Carling, D. (2005) · Cell Metabolism · doi:10.1016/j.cmet.2005.06.005 · Cited by 1,382 · see citing works

Characterization of the AMP-activated Protein Kinase Kinase from Rat Liver and Identification of Threonine 172 as the Major Site at Which It Phosphorylates AMP-activated Protein Kinase

Hawley, S. A., Davison, M., Woods, A., Davies, S. P., Beri, R. K., Carling, D., & Hardie, D. G. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.44.27879 · Cited by 1,264 · see citing works

AMP-Activated Protein Kinase in Metabolic Control and Insulin Signaling

Towler, M. C., & Hardie, D. G. (2007) · Circulation Research · doi:10.1161/01.res.0000256090.42690.05 · Cited by 1,248 · see citing works

The Ca2+/Calmodulin-dependent Protein Kinase Kinases Are AMP-activated Protein Kinase Kinases

Hurley, R. L., Anderson, K. A., Franzone, J. M., Kemp, B. E., Means, A. R., & Witters, L. A. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m503824200 · Cited by 1,004 · see citing works

Globular adiponectin protected ob/ob mice from diabetes and ApoE-deficient mice from atherosclerosis

Yamauchi, T., Kamon, J., Waki, H., Imai, Y., Shimozawa, N., Hioki, K., Uchida, S., Ito, Y., Takakuwa, K., Matsui, J., et al. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m209033200 · Cited by 911 · see citing works

LKB1-Dependent Signaling Pathways

Alessi, D. R., Sakamoto, K., & Bayascas, J. R. (2006) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.75.103004.142702 · Cited by 783 · see citing works

CBS domains form energy-sensing modules whose binding of adenosine ligands is disrupted by disease mutations

Scott, J. W., Hawley, S. A., Green, K. A., Anis, M., Stewart, G., Scullion, G. A., Norman, D. G., & Hardie, D. G. (2004) · Journal of Clinical Investigation · doi:10.1172/jci19874 · Cited by 754 · see citing works

APPL1 binds to adiponectin receptors and mediates adiponectin signalling and function

Mao, X., Kikani, C. K., Riojas, R. A., Langlais, P. R., Wang, L., Ramos, F. J., Fang, Q., Christ-Roberts, C. Y., Hong, J., Kim, R. Y., et al. (2006) · Nature Cell Biology · doi:10.1038/ncb1404 · Cited by 661 · see citing works

Investigating the mechanism for AMP activation of the AMP-activated protein kinase cascade

Sanders, M. J., Grondin, P., Hegarty, B. D., Snowden, M. A., & Carling, D. (2007) · Biochemical Journal · doi:10.1042/bj20061520 · Cited by 660 · see citing works

Deficiency of LKB1 in skeletal muscle prevents AMPK activation and glucose uptake during contraction

Sakamoto, K., McCarthy, A., Smith, D. P., Green, K. A., Hardie, D. G., Ashworth, A., & Alessi, D. R. (2005) · The EMBO Journal · doi:10.1038/sj.emboj.7600667 · Cited by 538 · see citing works

APPL Proteins Link Rab5 to Nuclear Signal Transduction via an Endosomal Compartment

Miączyńska, M., Christoforidis, S., Giner, A., Shevchenko, A., Uttenweiler‐Joseph, S., Habermann, B. H., Wilm, M. S., Parton, R. G., & Zerial, M. (2004) · Cell · doi:10.1016/s0092-8674(04)00117-5 · Cited by 536 · see citing works

Dissecting the Role of 5′-AMP for Allosteric Stimulation, Activation, and Deactivation of AMP-activated Protein Kinase

Suter, M., Riek, U., Tuerk, R. D., Schlattner, U., Wallimann, T., & Neumann, D. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m606357200 · Cited by 473 · see citing works

MO25α/β interact with STRADα/β enhancing their ability to bind, activate and localize LKB1 in the cytoplasm

Boudeau, J., Baas, A. F., Deák, M., MORRICE, N. A., Kieloch, A., Schutkowski, M., Prescott, A. R., Clevers, H. C., & Alessi, D. R. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg490 · Cited by 456 · see citing works

5′-AMP Activates the AMP-activated Protein Kinase Cascade, and Ca2+/Calmodulin Activates the Calmodulin-dependent Protein Kinase I Cascade, via Three Independent Mechanisms

Hawley, S. A., Selbert, M. A., Goldstein, E. G., Edelman, A. M., Carling, D., & Hardie, D. G. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.45.27186 · Cited by 441 · see citing works

AMP-activated protein kinase: greater AMP dependence, and preferential nuclear localization, of complexes containing the α2 isoform

Salt, I. P., Celler, J. W., Hawley, S. A., Prescott, A. R., Woods, A., Carling, D., & Hardie, D. G. (1998) · Biochemical Journal · doi:10.1042/bj3340177 · Cited by 437 · see citing works

Activation of the tumour suppressor kinase LKB1 by the STE20‐like pseudokinase STRAD

Baas, A. F., Boudeau, J., Sapkota, G. P., Smit, L., Medema, R. H., Morrice, N. A., Alessi, D. R., & Clevers, H. C. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg292 · Cited by 385 · see citing works

Generation of globular fragment of adiponectin by leukocyte elastase secreted by monocytic cell line THP-1

Waki, H., Yamauchi, T., Kamon, J., Kita, S., Ito, Y., Hada, Y., Uchida, S., Tsuchida, A., Takekawa, S., & Kadowaki, T. (2005) · Endocrinology · doi:10.1210/en.2004-1096 · Cited by 319 · see citing works

Growth suppression by Lkb1 is mediated by a G 1 cell cycle arrest

Tiainen, M., Ylikorkala, A., & Mäkelä, T. P. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.16.9248 · Cited by 302 · see citing works

Activity of LKB1 and AMPK-related kinases in skeletal muscle: effects of contraction, phenformin, and AICAR

Sakamoto, K., Göransson, O., Hardie, D. G., & Alessi, D. R. (2004) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00074.2004 · Cited by 299 · see citing works

APPL1: role in adiponectin signaling and beyond

Deepa, S. S., & Dong, L. (2008) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.90731.2008 · Cited by 287 · see citing works

Identification of the Immunophilins Capable of Mediating Inhibition of Signal Transduction by Cyclosporin A and FK506: Roles of Calcineurin Binding and Cellular Location

Bram, R. J., Hung, D. T., Martin, P. K., Schreiber, S. L., & Crabtree, G. R. (1993) · Molecular and Cellular Biology · doi:10.1128/mcb.13.8.4760 · Cited by 276 · see citing works

Phosphorylation of LKB1 at Serine 428 by Protein Kinase C-ζ Is Required for Metformin-Enhanced Activation of the AMP-Activated Protein Kinase in Endothelial Cells

Xie, Z., Dong, Y., Scholz, R., Neumann, D., & Zou, M.-H. (2008) · Circulation · doi:10.1161/circulationaha.107.744490 · Cited by 273 · see citing works

Components of a Calmodulin-dependent Protein Kinase Cascade

Anderson, K. A., Means, R. L., Huang, Q.-H., Kemp, B. E., Goldstein, E. G., Selbert, M. A., Edelman, A. M., Fremeau, R. T., & Means, A. R. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.48.31880 · Cited by 253 · see citing works

AMP-activated protein kinase in skeletal muscle: From structure and localization to its role as a master regulator of cellular metabolism

Witczak, C. A., Sharoff, C. G., & Goodyear, L. J. (2008) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-008-8244-6 · Cited by 250 · see citing works

Characterization of a Ca2+/Calmodulin-dependent Protein Kinase Cascade

Tokumitsu, H., Enslen, H., & Soderling, T. R. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.33.19320 · Cited by 229 · see citing works

Possible CaMKK-dependent regulation of AMPK phosphorylation and glucose uptake at the onset of mild tetanic skeletal muscle contraction

Jensen, T. E., Rose, A. J., Jørgensen, S. B., Brandt, N., Schjerling, P., Wojtaszewski, J. F. P., & Richter, E. A. (2007) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00456.2006 · Cited by 214 · see citing works

Identification of a chromosome 3p14.3-21.1 gene, APPL, encoding an adaptor molecule that interacts with the oncoprotein-serine/threonine kinase AKT2

Mitsuuchi, Y., Johnson, S. W., Sonoda, G., Tanno, S., Golemis, E. A., & Testa, J. R. (1999) · Oncogene · doi:10.1038/sj.onc.1203080 · Cited by 202 · see citing works

Growth arrest by the LKB1 tumor suppressor: induction of p21WAF1/CIP1

Tiainen, M. (2002) · Human Molecular Genetics · doi:10.1093/hmg/11.13.1497 · Cited by 200 · see citing works

Activation of Protein Kinase Cζ by Peroxynitrite Regulates LKB1-dependent AMP-activated Protein Kinase in Cultured Endothelial Cells

Xie, Z., Dong, Y., Zhang, M., Cui, M.-Z., Cohen, R. A., Riek, U., Neumann, D., Schlattner, U., & Zou, M.-H. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m511178200 · Cited by 172 · see citing works

Increased Frequency of Calcium Waves in Xenopus laevis Oocytes that Express a Calcium-ATPase

Camacho, P., & Lechleiter, J. D. (1993) · Science · doi:10.1126/science.8385800 · Cited by 167 · see citing works

Analysis of the LKB1-STRAD-MO25 complex

Boudeau, J., Scott, J. W., Resta, N., Deák, M., Kieloch, A., Komander, D., Hardie, D. G., Prescott, A. R., van Aalten, D. M. F., & Alessi, D. R. (2004) · Journal of Cell Science · doi:10.1242/jcs.01571 · Cited by 161 · see citing works

Ca2+/Calmodulin-Dependent Protein Kinase Kinase-α Regulates Skeletal Muscle Glucose Uptake Independent of AMP-Activated Protein Kinase and Akt Activation

Witczak, C. A., FUJII, N. L., Hirshman, M. F., & Goodyear, L. J. (2007) · Diabetes · doi:10.2337/db06-1230 · Cited by 122 · see citing works

High molecular weight adiponectin activates AMPK and suppresses cytokine‐induced NF‐κB activation in vascular endothelial cells

Hattori, Y., Nakano, Y., Hattori, S., Tomizawa, A., Inukai, K., & Kasai, K. (2008) · FEBS Letters · doi:10.1016/j.febslet.2008.04.037 · Cited by 119 · see citing works

Normal hypertrophy accompanied by phosphoryation and activation of AMP‐activated protein kinase α1 following overload in LKB1 knockout mice

McGee, S. L., Mustard, K. J., Hardie, D. G., & Baar, K. (2008) · The Journal of Physiology · doi:10.1113/jphysiol.2007.143685 · Cited by 105 · see citing works

Identification and characterization of four novel phosphorylation sites (Ser31, Ser325, Thr336 and Thr366) on LKB1/STK11, the protein kinase mutated in Peutz‒Jeghers cancer syndrome

Sapkota, G. P., Boudeau, J., Deák, M., Kieloch, A., MORRICE, N. A., & Alessi, D. R. (2002) · Biochemical Journal · doi:10.1042/0264-6021:3620481 · Cited by 97 · see citing works

Multiple Ca2+-Calmodulin-dependent Protein Kinase Kinases from Rat Brain

Edelman, A. M., Mitchelhill, K. I., Selbert, M. A., Anderson, K. A., Hook, S. S., Stapleton, D., Goldstein, E. G., Means, A. R., & Kemp, B. E. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.18.10806 · Cited by 95 · see citing works

Primary Structure, Tissue Distribution, and Expression of Mouse Phosphoinositide-dependent Protein Kinase-1, a Protein Kinase That Phosphorylates and Activates Protein Kinase Cζ

Dong, L., Zhang, R.-B., Langlais, P. R., He, H., Clark, M. C., Zhu, L. X., & Liu, F. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.12.8117 · Cited by 94 · see citing works

APPL1, APPL2, Akt2 and FOXO1a interact with FSHR in a potential signaling complex

Nechamen, C. A., Thomas, R. M., & Dias, J. A. (2006) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2006.08.014 · Cited by 92 · see citing works

LIP1, a cytoplasmic protein functionally linked to the Peutz-Jeghers syndrome kinase LKB1

Smith, D. P. (2001) · Human Molecular Genetics · doi:10.1093/hmg/10.25.2869 · Cited by 89 · see citing works

The Mouse Peutz-Jeghers Syndrome Gene Lkbl Encodes a Nuclear Protein Kinase

Smith, D. P., Spicer, J. F., Smith, A. L., Swift, S., & Ashworth, A. (1999) · Human Molecular Genetics · doi:10.1093/hmg/8.8.1479 · Cited by 85 · see citing works

Nuclear translocation of 3′-phosphoinositide-dependent protein kinase 1 (PDK-1): A potential regulatory mechanism for PDK-1 function

Lim, M. A., Kikani, C. K., Wick, M. J., & Dong, L. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2335486100 · Cited by 84 · see citing works

Oxytocin stimulates glucose uptake in skeletal muscle cells through the calcium–CaMKK–AMPK pathway

Lee, E. S., Uhm, K.-O., Lee, Y. M., Kwon, J., Park, S.-H., & Soo, K. H. (2008) · Regulatory Peptides · doi:10.1016/j.regpep.2008.05.001 · Cited by 76 · see citing works

The AMP-activated protein kinase: more than an energy sensor

Hue, L., & Rider, M. H. (2007) · Essays in Biochemistry · doi:10.1042/bse0430121 · Cited by 74 · see citing works

C-terminal Phosphorylation of LKB1 Is Not Required for Regulation of AMP-activated Protein Kinase, BRSK1, BRSK2, or Cell Cycle Arrest

Fogarty, S., & Hardie, D. G. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m806152200 · Cited by 61 · see citing works

Thyroid Hormone Activates Adenosine 5′-Monophosphate-Activated Protein Kinase via Intracellular Calcium Mobilization and Activation of Calcium/Calmodulin-Dependent Protein Kinase Kinase-β

Yamauchi, M., Kambe, F., Cao, X., Lu, X., Kozaki, Y., Oiso, Y., & Seo, H. (2008) · Molecular Endocrinology · doi:10.1210/me.2007-0249 · Cited by 61 · see citing works

Identification and characterization of four novel phosphorylation sites (Ser31, Ser325, Thr336 and Thr366) on LKB1/STK11, the protein kinase mutated in Peutz–Jeghers cancer syndrome

Sapkota, G. P., Boudeau, J., Deák, M., et al. (2002) · Biochemical Journal · doi:10.1042/bj3620481 · Cited by 60 · see citing works

LKB1, an upstream AMPK kinase, regulates glucose and lipid metabolism in cultured liver and muscle cells

Imai, K., Inukai, K., Ikegami, Y., Awata, T., & Katayama, S. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2006.10.056 · Cited by 53 · see citing works

How is AMPK activity regulated in skeletal muscles during exercise?

Jørgensen, S. B. (2008) · Frontiers in bioscience · doi:10.2741/3102 · Cited by 44 · see citing works

Localization of the mRNAs for two isoforms of Ca2+/calmodulin-dependent protein kinase kinases in the adult rat brain

Sakagami, H., Saito, S., Kitani, T., Okuno, S., Fujisawa, H., & Kondo, H. (1998) · Molecular Brain Research · doi:10.1016/s0169-328x(97)00362-8 · Cited by 40 · see citing works

The Adiponectin Signaling Pathway as a Novel Pharmacological Target

Mao, X., Hong, J., & Dong, L. (2006) · Mini-Reviews in Medicinal Chemistry · doi:10.2174/138955706778992978 · Cited by 32 · see citing works

Cloning of mouse Ca2+/calmodulin-dependent protein kinase kinase beta (CaMKKβ) and characterization of CaMKKβ and CaMKKα distribution in the adult mouse brain

Vinet, J., Carra, S., Blom, J. M. C., Harvey, M., Brunello, N., Barden, N., & Tascedda, F. (2003) · Molecular Brain Research · doi:10.1016/s0169-328x(02)00698-8 · Cited by 24 · see citing works

Globular adiponectin stimulates glucose transport in type 2 diabetic muscle

Kuoppamaa, H., Skrobuk, P., Sihvo, M., Hiukka, A., Chibalin, A., Zierath, J. R., & Koistinen, H. A. (2008) · Diabetes/Metabolism Research and Reviews · doi:10.1002/dmrr.883 · Cited by 23 · see citing works

Adipose tissue in control of metabolism

Luo, L., & Liu, M. (2016) · Journal of Endocrinology · doi:10.1530/joe-16-0211 · Cited by 708 · see citing works

The Role of Adiponectin in Cancer: A Review of Current Evidence

Dalamaga, Μ., Diakopoulos, K. N., & Mantzoros, C. S. (2012) · Endocrine Reviews · doi:10.1210/er.2011-1015 · Cited by 639 · see citing works

Adiponectin regulation and function

Fang, H., & Judd, R. L. (2018) · Comprehensive physiology · doi:10.1002/cphy.c170046 · Cited by 631 · see citing works

Adiponectin, the past two decades

Wang, Z. V., & Scherer, P. E. (2016) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjw011 · Cited by 609 · see citing works

Adiponectin signaling and function in insulin target tissues

Ruan, H., & Dong, L. Q. (2016) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjw014 · Cited by 395 · see citing works

Metabolic Messengers: adiponectin

Straub, L. G., & Scherer, P. E. (2019) · Nature Metabolism · doi:10.1038/s42255-019-0041-z · Cited by 352 · see citing works

Adiponectin: Structure, Physiological Functions, Role in Diseases, and Effects of Nutrition

Khoramipour, K., Chamari, K., hekmatikar, A. A., Ziyaiyan, A., Taherkhani, S., Elguindy, N. M., & Bragazzi, N. L. (2021) · Nutrients · doi:10.3390/nu13041180 · Cited by 339 · see citing works

Adiponectin and cardiovascular health: an update

Hui, X. H., Lam, K. S., Vanhoutte, P. M., & Xu, A. (2011) · British Journal of Pharmacology · doi:10.1111/j.1476-5381.2011.01395.x · Cited by 287 · see citing works

Metabolic function of the CTRP family of hormones

Seldin, M. M., Tan, S. Y., & Wong, G. W. (2013) · Reviews in Endocrine and Metabolic Disorders · doi:10.1007/s11154-013-9255-7 · Cited by 244 · see citing works

Adiponectin: a versatile player of innate immunity

Luo, Y., & Liu, M. (2016) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjw012 · Cited by 244 · see citing works

Adipokines, Hepatokines and Myokines: Focus on Their Role and Molecular Mechanisms in Adipose Tissue Inflammation

Ren, Y., Zhao, H., Yin, C., Lan, X., Wu, L., Du, X., Griffiths, H. R., & Gao, D. (2022) · Frontiers in Endocrinology · doi:10.3389/fendo.2022.873699 · Cited by 260 · see citing works

Food Timing, Circadian Rhythm and Chrononutrition: A Systematic Review of Time-Restricted Eating’s Effects on Human Health

Adafer, R., Messaadi, W., Meddahi, M., Patey, A., Haderbache, A., Bayen, S., & Messaadi, N. (2020) · Nutrients · doi:10.3390/nu12123770 · Cited by 233 · see citing works

The Adiponectin Receptor Agonist AdipoRon Ameliorates Diabetic Nephropathy in a Model of Type 2 Diabetes

Kim, Y., Lim, J. H., Kim, M. Y., Kim, E. N., Yoon, H. E., Shin, S. J., Choi, B. S., Kim, Y.-S., Chang, Y. S., & Park, C. W. (2018) · Journal of the American Society of Nephrology · doi:10.1681/asn.2017060627 · Cited by 229 · see citing works

Adiponectin: Anti-inflammatory and cardioprotective effects

Villarreal-Molina, M. T., & Antuna-Puente, B. (2012) · Biochimie · doi:10.1016/j.biochi.2012.06.030 · Cited by 197 · see citing works

Adiponectin suppresses gluconeogenic gene expression in mouse hepatocytes independent of LKB1-AMPK signaling

Miller, R., Chu, Q., Lay, J. E. L., Scherer, P. E., Ahima, R. S., Kaestner, K. H., Foretz, M., Viollet, B., & Birnbaum, M. J. (2011) · Journal of Clinical Investigation · doi:10.1172/jci45942 · Cited by 178 · see citing works

Impaired mitochondrial biogenesis due to dysfunctional adiponectin-AMPK-PGC-1α signaling contributing to increased vulnerability in diabetic heart

Yan, W., Zhang, H., Liu, P., Wang, H., Liu, J., Gao, C., Liu, Y., Lian, K., Yang, L., Sun, L., et al. (2013) · Basic Research in Cardiology · doi:10.1007/s00395-013-0329-1 · Cited by 169 · see citing works

Time-restricted feeding improves markers of cardiometabolic health in physically active college-age men: a 4-week randomized pre-post pilot study

McAllister, M. J., Pigg, B., Rentería, L. I., & Waldman, H. S. (2019) · Nutrition Research · doi:10.1016/j.nutres.2019.12.001 · Cited by 152 · see citing works

Regulation of adiponectin multimerization, signaling and function

Liu, M., & Liu, F. (2014) · Best Practice & Research Clinical Endocrinology & Metabolism · doi:10.1016/j.beem.2013.06.003 · Cited by 152 · see citing works

Adiponectin signaling in the liver

Combs, T. P., & Marliss, E. B. (2013) · Reviews in Endocrine and Metabolic Disorders · doi:10.1007/s11154-013-9280-6 · Cited by 149 · see citing works

Perivascular adipose tissue-derived adiponectin activates BKCa channels to induce anticontractile responses

Lynch, F. M., Withers, S., Yao, Z., Werner, M. E., Edwards, G., Weston, A. H., & Heagerty, A. M. (2013) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00697.2012 · Cited by 135 · see citing works

APPL1 Potentiates Insulin Sensitivity by Facilitating the Binding of IRS1/2 to the Insulin Receptor

Ryu, J., Galan-Davila, A. K., Xin, X., Dong, F., Abdul-Ghani, M. A., Zhou, L., Wang, C., Li, C., Holmes, B. M., Sloane, L. B., et al. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.04.006 · Cited by 128 · see citing works

Adiponectin and adipocyte fatty acid binding protein in the pathogenesis of cardiovascular disease

Xu, A., & Vanhoutte, P. M. (2011) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00765.2011 · Cited by 128 · see citing works

Tissue differences in the exosomal/small extracellular vesicle proteome and their potential as indicators of altered tissue metabolism

García-Martín, R., Brandão, B. B., Thomou, T., Altındiş, E., & Kahn, C. R. (2022) · Cell Reports · doi:10.1016/j.celrep.2021.110277 · Cited by 124 · see citing works

Adiponectin—Consideration for its Role in Skeletal Muscle Health

Krause, M. P., Milne, K. J., & Hawke, T. J. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20071528 · Cited by 121 · see citing works

PGC-1 coactivators in the cardiovascular system

Patten, I. S., & Arany, Z. P. (2011) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2011.09.007 · Cited by 119 · see citing works

Signaling mechanisms underlying the insulin-sensitizing effects of adiponectin

Cheng, K. K. Y., Lam, K. S. L., Wang, B., & Xu, A. (2013) · Best Practice & Research Clinical Endocrinology & Metabolism · doi:10.1016/j.beem.2013.06.006 · Cited by 116 · see citing works

FGF21 activates AMPK signaling: impact on metabolic regulation and the aging process

Salminen, A., Kauppinen, A., & Kaarniranta, K. (2016) · Journal of Molecular Medicine · doi:10.1007/s00109-016-1477-1 · Cited by 117 · see citing works

An APPL1-AMPK signaling axis mediates beneficial metabolic effects of adiponectin in the heart

Fang, X., Palanivel, R., Cresser, J., Schram, K., Ganguly, R., Thong, F. S. L., Tuinei, J., Xu, A., Abel, E. D., & Sweeney, G. (2010) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00086.2010 · Cited by 117 · see citing works

Adiponectin Regulation and Function

Fang, H., & Judd, R. L. (2018) · Comprehensive physiology · doi:10.1002/j.2040-4603.2018.tb00036.x · Cited by 116 · see citing works

Role of adiponectin system in insulin resistance

Caselli, C. (2014) · Molecular Genetics and Metabolism · doi:10.1016/j.ymgme.2014.09.003 · Cited by 110 · see citing works

Honokiol activates AMP-activated protein kinase in breast cancer cells via an LKB1-dependent pathway and inhibits breast carcinogenesis

Nagalingam, A., Arbiser, J. L., Bonner, M. Y., Saxena, N. K., & Sharma, D. (2012) · Breast Cancer Research · doi:10.1186/bcr3128 · Cited by 105 · see citing works

Positive Feedback Regulation Between Adiponectin and T-Cadherin Impacts Adiponectin Levels in Tissue and Plasma of Male Mice

Matsuda, K., Fujishima, Y., Maeda, N., Mori, T., Hirata, A., Sekimoto, R., Tsushima, Y., Masuda, S., Yamaoka, M., Inoue, K., et al. (2014) · Endocrinology · doi:10.1210/en.2014-1618 · Cited by 104 · see citing works

Muscle transcriptomic profiles in pigs with divergent phenotypes for fatness traits

Cánovas, Á., Quintanilla, R., Amills, M., & Pena, R. (2010) · BMC Genomics · doi:10.1186/1471-2164-11-372 · Cited by 102 · see citing works

Molecular mechanisms of signal transduction via adiponectin and adiponectin receptors

Heiker, J. T., Kosel, D., & Beck‐Sickinger, A. G. (2010) · Biological Chemistry · doi:10.1515/bc.2010.104 · Cited by 103 · see citing works

Adiponectin and Its Receptors in Diabetic Kidney Disease: Molecular Mechanisms and Clinical Potential

Zha, D., Wu, X., & Gao, P. H. (2017) · Endocrinology · doi:10.1210/en.2016-1765 · Cited by 100 · see citing works

AMPK and the Endocrine Control of Metabolism

Townsend, L. K., & Steinberg, G. R. (2023) · Endocrine Reviews · doi:10.1210/endrev/bnad012 · Cited by 107 · see citing works

APPL1 mediates adiponectin-stimulated p38 MAPK activation by scaffolding the TAK1-MKK3-p38 MAPK pathway

Xin, X., Zhou, L., Reyes, C. M., Liu, F., & Dong, L. (2010) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00427.2010 · Cited by 100 · see citing works

Emerging role of AMP-activated protein kinase in endocrine control of metabolism in the liver

Hasenour, C. M., Berglund, E. D., & Wasserman, D. H. (2012) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2012.06.018 · Cited by 98 · see citing works

Adiponectin Action: A Combination of Endocrine and Autocrine/Paracrine Effects

Dadson, K., Liu, Y., & Sweeney, G. (2011) · Frontiers in Endocrinology · doi:10.3389/fendo.2011.00062 · Cited by 97 · see citing works

Green tea extract activates AMPK and ameliorates white adipose tissue metabolic dysfunction induced by obesity

Rocha, A. L. S., Bolin, A. P., Cardoso, C. A. L., & Otton, R. (2015) · European Journal of Nutrition · doi:10.1007/s00394-015-1033-8 · Cited by 96 · see citing works

Glial Cells as Therapeutic Approaches in Brain Ischemia-Reperfusion Injury

Hernández, I. H., Villa-González, M., Martín-López, G., Soto, M. S., & Pérez-Álvarez, M. J. (2021) · Cells · doi:10.3390/cells10071639 · Cited by 94 · see citing works

5'-Monophosphate-activated protein kinase (AMPK) improves autophagic activity in diabetes and diabetic complications

Yao, F., Zhang, M., & Chen, L. (2015) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2015.07.009 · Cited by 93 · see citing works

Prenatal Androgenization of Female Mice Programs an Increase in Firing Activity of Gonadotropin-Releasing Hormone (GnRH) Neurons That Is Reversed by Metformin Treatment in Adulthood

Roland, A. V., & Moenter, S. M. (2010) · Endocrinology · doi:10.1210/en.2010-0823 · Cited by 92 · see citing works

Adiponectin receptor binding proteins – recent advances in elucidating adiponectin signalling pathways

Buechler, C., Wanninger, J., & Neumeier, M. (2010) · FEBS Letters · doi:10.1016/j.febslet.2010.09.035 · Cited by 92 · see citing works

Activation of AMP-Activated Protein Kinase and Stimulation of Energy Metabolism by Acetic Acid in L6 Myotube Cells

Maruta, H., Yoshimura, Y., Araki, A., Kimoto, M., Takahashi, Y., & Yamashita, H. (2016) · PLoS ONE · doi:10.1371/journal.pone.0158055 · Cited by 89 · see citing works

Disulfide-bond A oxidoreductase-like protein protects against ectopic fat deposition and lipid-related kidney damage in diabetic nephropathy

Chen, X., Han, Y., Gao, P., Yang, M., Xiao, L., Xiong, X., Zhao, H., Tang, C., Chen, G., Zhu, X., et al. (2019) · Kidney International · doi:10.1016/j.kint.2018.10.038 · Cited by 90 · see citing works

Bariatric surgery and bone disease: from clinical perspective to molecular insights

Folli, F. B., Sabowitz, B., Schwesinger, W. H., Fanti, P., Guardado‐Mendoza, R., & Muscogiuri, G. (2012) · International Journal of Obesity · doi:10.1038/ijo.2012.115 · Cited by 87 · see citing works

Apelin and insulin resistance: Another arrow for the quiver?

Xu, S., Tsao, P. S., & Yue, P. (2011) · Journal of Diabetes · doi:10.1111/j.1753-0407.2011.00132.x · Cited by 83 · see citing works

Adiponectin attenuates neuronal apoptosis induced by hypoxia-ischemia via the activation of AdipoR1/APPL1/LKB1/AMPK pathway in neonatal rats

Xu, N., Zhang, Y., Doycheva, D. M., Ding, Y. P., Zhang, Y., Tang, J., Guo, H., & Zhang, J. H. (2018) · Neuropharmacology · doi:10.1016/j.neuropharm.2018.02.024 · Cited by 82 · see citing works

Globular Adiponectin, Acting via AdipoR1/APPL1, Protects H9c2 Cells from Hypoxia/Reoxygenation-Induced Apoptosis

Park, M. S., Youn, B., Zheng, X., Wu, D., Xu, A., & Sweeney, G. (2011) · PLoS ONE · doi:10.1371/journal.pone.0019143 · Cited by 82 · see citing works

Role of adiponectin and some other factors linking type 2 diabetes mellitus and obesity

Chakraborti, C. K. (2015) · World Journal of Diabetes · doi:10.4239/wjd.v6.i15.1296 · Cited by 81 · see citing works

Mechanism and Role of High Density Lipoprotein-induced Activation of AMP-activated Protein Kinase in Endothelial Cells

Kimura, T., Tomura, H., Sato, K., Ito, M., Matsuoka, I., Im, D., Kuwabara, A., Mogi, C., Itoh, H., Kurose, H., et al. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.043869 · Cited by 81 · see citing works

Inhibitory effect of ethanol on AMPK phosphorylation is mediated in part through elevated ceramide levels

Liangpunsakul, S., Sozio, M. S., Shin, E., Zhao, Z., Xu, Y., Ross, R. A., Zeng, Y., & Crabb, D. W. (2010) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00482.2009 · Cited by 79 · see citing works

Protective effects of adiponectin against renal ischemia‐reperfusion injury via prostacyclin‐PPARα‐Heme oxygenase‐1 signaling pathway

Cheng, C., Lian, W., Chen, S., Lai, P., Li, H., Lan, Y., Cheng, W. T., & Lin, H. (2011) · Journal of Cellular Physiology · doi:10.1002/jcp.22726 · Cited by 76 · see citing works

Adiponectin and Its Isoforms in Pathophysiology

van Andel, M., Heijboer, A. C., & Drent, M. L. (2018) · Advances in clinical chemistry · doi:10.1016/bs.acc.2018.02.007 · Cited by 77 · see citing works

Adiponectin and Its Mimics on Skeletal Muscle: Insulin Sensitizers, Fat Burners, Exercise Mimickers, Muscling Pills … or Everything Together?

Abou-Samra, M., Selvais, C. M., Dubuisson, N., & Brichard, S. M. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21072620 · Cited by 72 · see citing works

New Insights into AMPK, as a Potential Therapeutic Target in Metabolic Dysfunction-Associated Steatotic Liver Disease and Hepatic Fibrosis

An, H., Jang, Y., Choi, J.-I., Hur, J., Kim, S., & Kwon, Y. (2024) · Biomolecules & Therapeutics · doi:10.4062/biomolther.2024.188 · Cited by 72 · see citing works

Adiponectin Receptors Form Homomers and Heteromers Exhibiting Distinct Ligand Binding and Intracellular Signaling Properties

Almabouada, F., Díaz‐Ruiz, A., Rabanal‐Ruiz, Y., Peinado, J. R., Vázquez‐Martínez, R., & Malagón, M. M. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.404624 · Cited by 70 · see citing works

Examining the Potential of Developing and Implementing Use of Adiponectin-Targeted Therapeutics for Metabolic and Cardiovascular Diseases

Liu, Y., Vu, V., & Sweeney, G. (2019) · Frontiers in Endocrinology · doi:10.3389/fendo.2019.00842 · Cited by 69 · see citing works

APPL1 Mediates Adiponectin-Induced LKB1 Cytosolic Localization Through the PP2A-PKCζ Signaling Pathway

Deepa, S. S., Zhou, L., Ryu, J., Wang, C., Mao, X., Cai, L., Zhang, N., Musi, N., DeFronzo, R. A., Liu, F., et al. (2011) · Molecular Endocrinology · doi:10.1210/me.2011-0082 · Cited by 68 · see citing works

Bone marrow adipose tissue as an endocrine organ: close to the bone?

Sulston, R. J., & Cawthorn, W. P. (2016) · Hormone Molecular Biology and Clinical Investigation · doi:10.1515/hmbci-2016-0012 · Cited by 67 · see citing works

Overexpression of the Adiponectin Receptor AdipoR1 in Rat Skeletal Muscle Amplifies Local Insulin Sensitivity

Patel, S. A., Hoehn, K. L., Lawrence, R., Sawbridge, L., Talbot, N. A., Tomsig, J. L., Turner, N. A., Cooney, G. J., Whitehead, J. P., Kraegen, E. W., et al. (2012) · Endocrinology · doi:10.1210/en.2012-1368 · Cited by 66 · see citing works

The Role of Adipokines in the Pathogenesis of Psoriasis

Kiełbowski, K., Bakinowska, E., Ostrowski, P., Pala, B., Gromowska, E., Gurazda, K., Dec, P., Modrzejewski, A., & Pawlik, A. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24076390 · Cited by 63 · see citing works

Back to the heart: The protective role of adiponectin

Caselli, C., D’Amico, A., Cabiati, M., Prescimone, T., Ry, S. D., & Giannessi, D. (2014) · Pharmacological Research · doi:10.1016/j.phrs.2014.03.003 · Cited by 61 · see citing works

APPLs: More than just adiponectin receptor binding proteins

Liu, Z., Xiao, T., Peng, X., Li, G., & Hu, F. (2017) · Cellular Signalling · doi:10.1016/j.cellsig.2017.01.018 · Cited by 58 · see citing works

Role of Perivascular Adipose Tissue-Derived Adiponectin in Vascular Homeostasis

Sówka, A., & Dobrzyń, P. (2021) · Cells · doi:10.3390/cells10061485 · Cited by 62 · see citing works

The role of adiponectin in obesity-associated female-specific carcinogenesis

Nagaraju, G. P., Rajitha, B., Aliya, S., Kotipatruni, R. P., Santharam, M. A., Hammond, A. L., Park, D., Chigurupati, S., Alam, A., & Pattnaik, S. (2016) · Cytokine & Growth Factor Reviews · doi:10.1016/j.cytogfr.2016.03.014 · Cited by 58 · see citing works

Vascular Actions of Adipokines

Xu, A., Wang, Y., Lam, K. S. L., & Vanhoutte, P. M. (2010) · Advances in pharmacology · doi:10.1016/b978-0-12-385061-4.00008-8 · Cited by 57 · see citing works

Adiponectin affects vascular smooth muscle cell proliferation and apoptosis through modulation of the mitofusin-2-mediated Ras-Raf-Erk1/2 signaling pathway

Zhang, W., Shu, C., Li, Q., Li, M., & Li, X. (2015) · Molecular Medicine Reports · doi:10.3892/mmr.2015.3899 · Cited by 57 · see citing works

Adiponectin signaling and its role in bone metabolism

Pal China, S., Sanyal, S., & Chattopadhyay, N. (2018) · Cytokine · doi:10.1016/j.cyto.2018.06.012 · Cited by 53 · see citing works

AMPK as a mediator of tissue preservation: time for a shift in dogma?

Langer, H. T., Rohm, M., Goncalves, M. D., & Sylow, L. (2024) · Nature Reviews Endocrinology · doi:10.1038/s41574-024-00992-y · Cited by 51 · see citing works

Adiponectin Mediated APPL1-AMPK Signaling Induces Cell Migration, MMP Activation, and Collagen Remodeling in Cardiac Fibroblasts

Dadson, K., Chasiotis, H., Wannaiampikul, S., Tungtrongchitr, R., Xu, A., & Sweeney, G. (2013) · Journal of Cellular Biochemistry · doi:10.1002/jcb.24722 · Cited by 51 · see citing works

Adiponectin in health and diseases: from metabolic syndrome to tissue regeneration

Chiarugi, P., & Fiaschi, T. (2009) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728220903530712 · Cited by 52 · see citing works

The adiponectin signalling pathway - A therapeutic target for the cardiac complications of type 2 diabetes?

Sharma, A., Mah, M., Ritchie, R. H., & Blasio, M. J. D. (2021) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2021.108008 · Cited by 50 · see citing works

AdipoR1/APPL1 Potentiates the Protective Effects of Globular Adiponectin on Angiotensin II-Induced Cardiac Hypertrophy and Fibrosis in Neonatal Rat Atrial Myocytes and Fibroblasts

Cao, T., Gao, Z. L., Gu, L., Chen, M., Yang, B., Cao, K., Huang, H., & Li, M. (2014) · PLoS ONE · doi:10.1371/journal.pone.0103793 · Cited by 47 · see citing works

The role of adiponectin signaling in metabolic syndrome and cancer

Scheid, M. P., & Sweeney, G. (2013) · Reviews in Endocrine and Metabolic Disorders · doi:10.1007/s11154-013-9265-5 · Cited by 47 · see citing works

Does LKB1 Mediate Activation of Hepatic AMP-Protein Kinase (AMPK) and Sirtuin1 (SIRT1) After Roux-en-Y Gastric Bypass in Obese Rats?

Peng, Y., Rideout, D. A., Rakita, S., Gower, W. R., You, M., & Murr, M. M. (2009) · Journal of Gastrointestinal Surgery · doi:10.1007/s11605-009-1102-5 · Cited by 46 · see citing works

Emerging roles for the FSH receptor adapter protein APPL1 and overlap of a putative 14-3-3τ interaction domain with a canonical G-protein interaction site

Dias, J. A., Mahale, S. D., Nechamen, C. A., Davydenko, O., Thomas, R. M., & Ulloa‐Aguirre, A. (2010) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2010.05.009 · Cited by 42 · see citing works

The adaptor protein APPL1 increases glycogen accumulation in rat skeletal muscle through activation of the PI3-kinase signalling pathway

Cleasby, M. E., Lau, Q., Polkinghorne, E., Patel, S. A., Leslie, S. J., Turner, N. A., Cooney, G. J., Xu, A., & Kraegen, E. W. (2011) · Journal of Endocrinology · doi:10.1530/joe-11-0039 · Cited by 42 · see citing works

White to beige conversion in PDE3B KO adipose tissue through activation of AMPK signaling and mitochondrial function

Chung, Y. W., Ahmad, F., Tang, Y., Hockman, S. C., Kee, H. J., Berger, K., Guirguis, E., Choi, Y. H., Schimel, D., Aponte, A. M., et al. (2017) · Scientific Reports · doi:10.1038/srep40445 · Cited by 43 · see citing works

A collagen domain–derived short adiponectin peptide activates APPL1 and AMPK signaling pathways and improves glucose and fatty acid metabolisms

Sayeed, M., Gautam, S., Verma, D. P., Afshan, T., Kumari, T., Srivastava, A. K., & Ghosh, J. K. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.001801 · Cited by 42 · see citing works

Exercise-Induced Muscle–Fat Crosstalk: Molecular Mediators and Their Pharmacological Modulation for the Maintenance of Metabolic Flexibility in Aging

Tero-Vescan, A., Degens, H., Matsakas, A., Ștefănescu, R., Ősz, B. E., & Slevin, M. (2025) · Pharmaceuticals · doi:10.3390/ph18081222 · Cited by 44 · see citing works

Pioglitazone Reduces Hepatocellular Carcinoma Development in Two Rodent Models of Cirrhosis

Li, S., Ghoshal, S., Sojoodi, M., Arora, G., Masia, R., Erstad, D. J., Lanuti, M. D., Hoshida, Y., Baumert, T. F., Tanabe, K. K., et al. (2018) · Journal of Gastrointestinal Surgery · doi:10.1007/s11605-018-4004-6 · Cited by 41 · see citing works

Globular Adiponectin Inhibits Ethanol-Induced Reactive Oxygen Species Production through Modulation of NADPH Oxidase in Macrophages: Involvement of Liver Kinase B1/AMP-Activated Protein Kinase Pathway

Kim, M. J., Nagy, L. E., & Park, P. (2014) · Molecular Pharmacology · doi:10.1124/mol.114.093039 · Cited by 40 · see citing works

Targeting Neurovascular Interaction in Retinal Disorders

Fu, Z., Sun, Y., Cakir, B., Tomita, Y., Huang, S., Wang, Z., Liu, C., Cho, S. S., Britton, W. R., Kern, T. S., et al. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21041503 · Cited by 41 · see citing works

Shared signaling pathways and targeted therapy by natural bioactive compounds for obesity and type 2 diabetes

Tian, S., Zhao, H., & Song, H. (2022) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408398.2022.2148090 · Cited by 39 · see citing works

An Explanation for the Adiponectin Paradox

Kalkman, H. O. (2021) · Pharmaceuticals · doi:10.3390/ph14121266 · Cited by 39 · see citing works

A Novel Mechanism for Vascular Insulin Resistance in Normotensive Young SHRs

Xing, W., Yan, W., Liu, P., Ji, L., Li, Y., Sun, L., Tao, L., Zhang, H., & Gao, F. (2013) · Hypertension · doi:10.1161/hypertensionaha.111.00728 · Cited by 39 · see citing works

APPL1 transgenic mice are protected from high-fat diet-induced cardiac dysfunction

Park, M. S., Wu, D., Park, T., Choi, C., Li, R., Cheng, K. K. Y., Xu, A., & Sweeney, G. (2013) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00257.2013 · Cited by 38 · see citing works

Characteristics of Obesity and Its Related Disorders in China

Jia, W., Wang, C., Jiang, S., & Pan, J. (2010) · Biomedical and Environmental Sciences · doi:10.1016/s0895-3988(10)60025-6 · Cited by 38 · see citing works

High molecular weight adiponectin reduces glucolipotoxicity-induced inflammation and improves lipid metabolism and insulin sensitivity via APPL1-AMPK-GLUT4 regulation in 3T3-L1 adipocytes

Pandey, G. K., Vadivel, S., Raghavan, S., Mohan, V., Balasubramanyam, M., & Gokulakrishnan, K. (2019) · Atherosclerosis · doi:10.1016/j.atherosclerosis.2019.07.011 · Cited by 38 · see citing works

Aerobic Exercise Alleviates Abnormal Autophagy in Brain Cells of APP/PS1 Mice by Upregulating AdipoR1 Levels

Jian, Y., Yuan, S., Yang, J., Lei, Y., Li, X., & Liu, W. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23179921 · Cited by 36 · see citing works

Adiponectin for the treatment of diabetic nephropathy

Lee, J. Y., Yang, J. W., Han, B. G., Choi, S. O., & Kim, J. S. (2019) · The Korean Journal of Internal Medicine · doi:10.3904/kjim.2019.109 · Cited by 37 · see citing works

Nicotinamide Mononucleotide Combined With Lactobacillus fermentum TKSN041 Reduces the Photoaging Damage in Murine Skin by Activating AMPK Signaling Pathway

Zhou, X., Du, H.-H., Ni, L., Ran, J., Hu, J. P., Yu, J., & Zhao, X. (2021) · Frontiers in Pharmacology · doi:10.3389/fphar.2021.643089 · Cited by 36 · see citing works

Reduced vascular responsiveness to adiponectin in hyperlipidemic rats—mechanisms and significance

Li, R., Xu, M., Wang, X., Wang, Y., Lau, W. B., Yuan, Y., Yi, W., Wei, X., Lopez, B. L., Christopher, T. A., et al. (2010) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2010.03.002 · Cited by 36 · see citing works

Adiponectin Enhances Intercellular Adhesion Molecule-1 Expression and Promotes Monocyte Adhesion in Human Synovial Fibroblasts

Chen, H., Tsou, H., Chen, J., Shih, J. M.-K., Chen, Y., & Tang, C. (2014) · PLoS ONE · doi:10.1371/journal.pone.0092741 · Cited by 36 · see citing works

Globular adiponectin induces LKB1/AMPK-dependent glucose uptake via actin cytoskeleton remodeling

Vu, V. P., Bui, P., Eguchi, M., Xu, A., & Sweeney, G. (2013) · Journal of Molecular Endocrinology · doi:10.1530/jme-13-0059 · Cited by 34 · see citing works

Role of Adipokines in Sarcopenia

Lu, W., Feng, W., Lai, J., Yuan, D., Xiao, W., & Li, Y. (2023) · Chinese Medical Journal · doi:10.1097/cm9.0000000000002255 · Cited by 34 · see citing works

Increase in PPARγ inhibitory phosphorylation by Fetuin—A through the activation of Ras-MEK-ERK pathway causes insulin resistance

Das, S., Chattopadhyay, D., Chatterjee, S. K., Mondal, S. A., Majumdar, S. S., Mukhopadhyay, S., Saha, N., Ravichandiran, V., Bhattacharya, S., & Mukherjee, S. (2020) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2020.166050 · Cited by 33 · see citing works

APPL1 Mediates Adiponectin-Induced LKB1 Cytosolic Localization Through the PP2A-PKCζ Signaling Pathway

Deepa, S. S., Zhou, L., Ryu, J., Wang, C., Mao, X., Cai, L., Zhang, N., Musi, N., DeFronzo, R. A., Liu, F., et al. (2011) · Molecular Endocrinology · doi:10.1210/me.2011-0082 · Cited by 68 · see citing works

Globular adiponectin induces LKB1/AMPK-dependent glucose uptake via actin cytoskeleton remodeling

Vu, V. P., Bui, P., Eguchi, M., Xu, A., & Sweeney, G. (2013) · Journal of Molecular Endocrinology · doi:10.1530/jme-13-0059 · Cited by 34 · see citing works

Adiponectin activates AMP-activated protein kinase via LKB1 pathway

Deng, D., Wang, Y., Cheng, Y., & Xiaojie, D. (2012) · Zhonghua neifenmi daixie zazhi · doi:10.3760/cma.j.issn.1000-6699.2012.07.014

Regulation of AMP‐activated protein kinase by LKB1 and CaMKK in adipocytes

Gormand, A., Henriksson, E., Ström, K., Jensen, T. E., Sakamoto, K., & Göransson, O. (2011) · Journal of Cellular Biochemistry · doi:10.1002/jcb.23053 · Cited by 83 · see citing works

Adiponectin increases fatty acid oxidation in skeletal muscle cells by sequential activation of AMP-activated protein kinase, p38 mitogen-activated protein kinase, and peroxisome proliferator-activated receptor

Yoon, M. J. (n.d.) · UCLA - Biblioteca de Ciencias de la Salud · Cited by 3 · see citing works