|
Adiponectin Receptor
The adiponectin receptors (AdipoRs) include the following two receptors, which are bound and activated by adiponectin: * Adiponectin receptor 1 (AdipoR1, PAQR1) * Adiponectin receptor 2 (AdipoR2, PAQR2) They are members of the progestin and adipoQ receptor (PAQR) family. In 2016, the University of Tokyo announced that it would launch an investigation into claims of fabrication of AdipoR1 and AdipoR2 identification data, as accused by an anonymous person/group called Ordinary_researchers In 2010s, a series of separate allegations of scientific misconducts were raised involving several scientific papers from various Japanese universities. Shigeaki Kato In February 1996, Shigeaki Kato, who had studied in the laboratory of Pierre Ch .... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Receptor (biochemistry)
In biochemistry and pharmacology, receptors are chemical structures, composed of protein, that receive and transduce signals that may be integrated into biological systems. These signals are typically chemical messengers which bind to a receptor and cause some form of cellular/tissue response, e.g. a change in the electrical activity of a cell. There are three main ways the action of the receptor can be classified: relay of signal, amplification, or integration. Relaying sends the signal onward, amplification increases the effect of a single ligand, and integration allows the signal to be incorporated into another biochemical pathway. Receptor proteins can be classified by their location. Transmembrane receptors include ligand-gated ion channels, G protein-coupled receptors, and enzyme-linked hormone receptors. Intracellular receptors are those found inside the cell, and include cytoplasmic receptors and nuclear receptors. A molecule that binds to a receptor is called a ligand ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Adiponectin
Adiponectin (also referred to as GBP-28, apM1, AdipoQ and Acrp30) is a protein hormone and adipokine, which is involved in regulating glucose levels as well as fatty acid breakdown. In humans it is encoded by the ''ADIPOQ'' gene and it is produced in primarily in adipose tissue, but also in muscle, and even in the brain. Structure Adiponectin is a 244-amino-acid-long polypeptide (protein). There are four distinct regions of adiponectin. The first is a short signal sequence that targets the hormone for secretion outside the cell; next is a short region that varies between species; the third is a 65-amino acid region with similarity to collagenous proteins; the last is a globular domain. Overall this protein shows similarity to the complement 1Q factors (C1Q). However, when the 3-dimensional structure of the globular region was determined, a striking similarity to TNFα was observed, despite unrelated protein sequences. Function Adiponectin is a protein hormone that modulates ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Adiponectin Receptor 1
Adiponectin receptor 1 (AdipoR1) is a protein which in humans is encoded by the ''ADIPOR1'' gene. It is a member of the progestin and adipoQ receptor (PAQR) family, and is also known as PAQR1. Structure Similar to G protein-coupled receptors (GPCRs), AdipoR1 also possesses 7 transmembrane domains. However, AdipoR1 is orientated oppositely to GPCRs in the membrane (i.e., cytoplasmic N-terminus, extracellular C-terminus) and does not associate with G proteins. Function The adiponectin receptors, AdipoR1 and AdipoR2, serve as receptors for globular and full-length adiponectin and mediate increased AMP-activated protein kinase, AMPK and Peroxisome proliferator-activated receptor alpha, PPAR-α ligand activities, as well as fatty acid oxidation and glucose uptake by adiponectin. In 2016, the University of Tokyo announced that it would launch an investigation into claims of fabrication of AdipoR1 and AdipoR2 identification data, as accused by an anonymous person/group called Ordinar ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Adiponectin Receptor 2
Adiponectin receptor 2 (AdipoR2) is a protein which in humans is encoded by the ''ADIPOR2'' gene. It is a member of the progestin and adipoQ receptor (PAQR) family, and is also known as PAQR2. Structure Similar to G protein-coupled receptors (GPCRs), AdipoR2 also possesses 7 transmembrane domains. However, AdipoR2 is orientated oppositely to GPCRs in the membrane (i.e., cytoplasmic N-terminus, extracellular C-terminus) and does not associate with G proteins. Function The adiponectin receptors, AdipoR1 and AdipoR2, serve as receptors for globular and full-length adiponectin and mediate increased AMPK and PPAR-α ligand activities, as well as fatty acid oxidation and glucose uptake by adiponectin. In 2016, the University of Tokyo announced that it would launch an investigation into claims of fabrication of AdipoR1 and AdipoR2 identification data, as accused by an anonymous person/group called Ordinary_researchers. [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Progestin And AdipoQ Receptor
The progestin and adipoQ receptor (PAQR) family is a group of receptors related to but distinct from the G protein-coupled receptor family, which have the similar seven transmembrane structure, but the N-terminal is located on the inner side of the cell. It includes at least 11 receptors (PAQR1–PAQR11), including the adiponectin (adipoQ) receptors (AdipoRs), the membrane progesterone receptors (mPRs), and others. In 2016, the University of Tokyo announced that it would launch an investigation into claims of fabrication of AdipoRs identification data, as accused by an anonymous person/group called Ordinary_researchers.University of Tokyo to investigate data manipulation charges against ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Ordinary Researchers
In 2010s, a series of separate allegations of scientific misconducts were raised involving several scientific papers from various Japanese universities. Shigeaki Kato In February 1996, Shigeaki Kato, who had studied in the laboratory of Pierre Chambon, established his laboratory at the Institute for Molecular and Cellular Biology of the University of Tokyo. Kato was one of the most well-funded researchers in Japan and published many papers in prominent journals. From 2007, Kato and one former member of his laboratory taught research ethics at the annual meeting of the . In mid-2011, the Kato lab withdrew papers published in the Journal of Steroid Biochemistry and Molecular Biology in 2004 and 2007 due to duplicate publications. On October 26, 2011, an extensive correction of the Kato laboratory's paper was publicly announced in Nature. The first author of this Nature paper is the former member who taught research ethics at the annual meeting of the . This correction raised susp ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
.svg "Click for more on -> Receptor (biochemistry)")