: Combined agonist–antagonist genome-wide functional screening id

: Combined agonist–antagonist genome-wide functional screening identifies broadly active antiviral microRNAs. Proc Natl Acad Sci U S A 2010,107(31):13830–13835.PubMedCrossRef 53. Viegas SC, Pfeiffer V, Sittka A, Silva IJ, Vogel J, Arraiano CM: Characterization of the role of ribonucleases in Salmonella small RNA decay. Nucleic Acids Res 2007,35(22):7651–7664.PubMedCrossRef 54. Vogel J, Wagner EG, Gerhart H: Approaches to identify novel non-messenger RNAs in bacteria

and to investigate their biological functions: RNA mining. In Handbook of RNA biochemistry. Edited by: Hartmann RK. Weinheim: Wiley-VCH-Verl; 2005:595–613.CrossRef 55. Datsenko KA, Wanner BL: One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR PLX3397 nmr products. Proc Natl Acad Sci U S A 2000,97(12):6640–6645.PubMedCrossRef Authors’ contributions TS and JY designed CFTRinh-172 all the experiments. JY carried out the experiments. TS and JY wrote the manuscript. Both authors read and approved the final manuscript.”
“Background Heterotrimeric (αβγ) guanine nucleotide binding proteins (G proteins) constitute a family of regulatory GTP hydrolases associated with the cytoplasmic face of the plasma membrane [1–4]. Their activity is characterized

by a cycle of GTP-binding and hydrolysis. The GTP- and GDP-bound complexes define the active and inactive states of the G proteins, respectively. The binding of specific ligands to transmembrane receptors activates the heterotrimeric G protein subunits that are responsible for the flow of BEZ235 price information in many eukaryotic signal transduction pathways

[5]. The traditional G proteins coupled receptors (GPCRs) share a characteristic topological structure of seven transmembrane domains and recognize diverse extracellular signals. The cytoplasmic C-terminal region contains the Gα binding activity. Recently, a new class of seven transmembrane receptors has been identified in humans and other vertebrates and has been classified as belonging to the PAQR superfamily (progestin-adipoQ receptors) [6–10]). Their activity has not been directly associated to heterotrimeric G proteins but indirect Molecular motor evidence suggests that they might be associated to G protein alpha subunits [11, 12]. The PAQR superfamily includes three classes of membrane receptors. Class I PAQRs are adiponectin receptors and include: AdipoR1 (PAQR 1), AdipoR2 (PAQR 2), PAQR 3 and PAQR 6 [13]. These receptors respond to adiponectin that is an insulin-sensitizing peptide hormone found in vertebrates [14, 15]. Low serum adiponectin levels have been identified as a high risk factor for type 2 diabetes and other complications such as atherosclerosis and hepatic steatosis. Adiponectin has been reported to have a positive effect on insulin sensitivity and energy metabolism [16]. Class II PAQRs respond to progesterone and include: mPRα (PAQR 7), mPRβ (PAQR 8) and mPRγ (PAQR 5) [13].

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