Cloning of adiponectin receptors that mediate antidiabetic metabolic effects

By Toshimasa Yamauchi, J. Kamon, Yusuke Ito, A. Tsuchida, T. Yokomizo, Shunbun Kita, T. Sugiyama, M. Miyagishi, K. Hara, Masaki Tsunoda and 16 more. Nature, 2003

3,219 citations recorded by the source corpus.

Subfields: Epidemiology, Molecular Biology, Physiology

View Paper: https://www.semanticscholar.org/paper/0dfff5419dd02e753a74a7c9f78f640a6e942af8

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Epidemiology

1. Haiming Cao
2. P. Scherer
3. H. Fang
4. R. L. Judd
5. B. Spiegelman
6. Herbert Tilg
7. E. Rosen
8. M. Trujillo

In Molecular Biology

1. H. Fang
2. R. L. Judd
3. P. Scherer
4. A. Hevener
5. B. Spiegelman
6. R. Barnard
7. Christian K. Roberts
8. E. Rosen

In Physiology

1. Haiming Cao
2. P. Scherer
3. H. Fang
4. R. L. Judd
5. B. Spiegelman
6. E. Rosen
7. Herbert Tilg
8. M. Trujillo

Citations in the corpus

• Adipokines in inflammation and metabolic disease (2011, background): “Adiponectin is thought to mediate AMPK activation through interactions with its cell surface receptors: adiponectin receptor 1 and adiponectin receptor 2 (Ref”
• Adiponectin Regulation and Function (2018, positive): “In 2003, through a sequence of expression cloning experiments, AdipoR1 and AdipoR2 were first identified as receptors for adiponectin (381).”
• Adipose tissue-derived factors: impact on health and disease. (2006, background): “Two adiponectin receptors (AdipoRs) were discovered through screening of a skeletal muscle cDNA library for products that display globular adiponectin binding (147).”
• Amino acid coevolution reveals three-dimensional structure and functional domains of insect odorant receptors (2015, neutral): “Importantly, the predicted helical contacts bear no resemblance to those of GPCRs or to those of the Adiponectin Receptor 1, a seven TMH protein that has the same membrane orientation as insect ORs 32 , but which appear to have a convergent helical arrangement to that of GPCRs (Fig.”
• Metabolic Syndrome and Insulin Resistance: Underlying Causes and Modification by Exercise Training (2013, positive): “Two distinct receptors, AdipoR1, which is expressed ubiquitously, and AdipoR2, which is expressed most abundantly in the liver, mediate the biological actions of adiponectin (707).”
• Pathophysiology of Type 2 Diabetes Mellitus (2020, background): “Adiponectin acts through ADIPOR1 and ADIPOR2 receptors [262] and the peroxisome proliferator-activated receptor α (PPARα) pathway, leading to decreased hepatic gluconeogenesis, increased liver and skeletal muscle fatty acid oxidation, increased glucose uptake in skeletal muscle and white adipose tis”
• Adiponectin: mechanistic insights and clinical implications (2012, background): “Adiponectin’s actions are mediated through a number of receptors, such as adiponectin receptors 1 and 2 (ADIPOR1 and ADIPOR2) [10].”
• Adiponectin, a Therapeutic Target for Obesity, Diabetes, and Endothelial Dysfunction (2017, background): “Unlike all other GPCRs reported, AdipoR1 and AdipoR2 have an inverte membrane topology with a cyt plasmic NH2 terminus and a short, extracellular COOH terminal domain of approximately 25 amino acids [31].”
• Adipocytes as regulators of energy balance and glucose homeostasis (2006, background): “One comprises two similar transmembrane proteins with homology to G-protein-coupled receptors, known as adipoR1 and adipoR2 (ref”