Relevant bibliographies by topics / Relaxin family peptpide receptors

Academic literature on the topic 'Relaxin family peptpide receptors'

Author: Grafiati
Published: 10 December 2022
Last updated: 29 January 2023

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Journal articles on the topic "Relaxin family peptpide receptors"

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Bathgate, R. A. D., M. L. Halls, E. T. van der Westhuizen, G. E. Callander, M. Kocan, and R. J. Summers. "Relaxin Family Peptides and Their Receptors." Physiological Reviews 93, no. 1 (January 2013): 405–80. http://dx.doi.org/10.1152/physrev.00001.2012.

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There are seven relaxin family peptides that are all structurally related to insulin. Relaxin has many roles in female and male reproduction, as a neuropeptide in the central nervous system, as a vasodilator and cardiac stimulant in the cardiovascular system, and as an antifibrotic agent. Insulin-like peptide-3 (INSL3) has clearly defined specialist roles in male and female reproduction, relaxin-3 is primarily a neuropeptide involved in stress and metabolic control, and INSL5 is widely distributed particularly in the gastrointestinal tract. Although they are structurally related to insulin, the relaxin family peptides produce their physiological effects by activating a group of four G protein-coupled receptors (GPCRs), relaxin family peptide receptors 1–4 (RXFP1–4). Relaxin and INSL3 are the cognate ligands for RXFP1 and RXFP2, respectively, that are leucine-rich repeat containing GPCRs. RXFP1 activates a wide spectrum of signaling pathways to generate second messengers that include cAMP and nitric oxide, whereas RXFP2 activates a subset of these pathways. Relaxin-3 and INSL5 are the cognate ligands for RXFP3 and RXFP4 that are closely related to small peptide receptors that when activated inhibit cAMP production and activate MAP kinases. Although there are still many unanswered questions regarding the mode of action of relaxin family peptides, it is clear that they have important physiological roles that could be exploited for therapeutic benefit.
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BATHGATE, ROSS A., RICHARD IVELL, BARBARA M. SANBORN, O. DAVID SHERWOOD, and ROGER J. SUMMERS. "Receptors for Relaxin Family Peptides." Annals of the New York Academy of Sciences 1041, no. 1 (May 2005): 61–76. http://dx.doi.org/10.1196/annals.1282.010.

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Gundlach, Andrew L., Sherie Ma, Qian Sang, Pei-Juan Shen, Loretta Piccenna, Katayoun Sedaghat, Craig M. Smith, et al. "Relaxin Family Peptides and Receptors in Mammalian Brain." Annals of the New York Academy of Sciences 1160, no. 1 (April 2009): 226–35. http://dx.doi.org/10.1111/j.1749-6632.2009.03956.x.

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Kong, Roy C. K., Patrick J. Shilling, Derek K. Lobb, Paul R. Gooley, and Ross A. D. Bathgate. "Membrane receptors: Structure and function of the relaxin family peptide receptors." Molecular and Cellular Endocrinology 320, no. 1-2 (May 2010): 1–15. http://dx.doi.org/10.1016/j.mce.2010.02.003.

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van der Westhuizen, Emma T., Michelle L. Halls, Chrishan S. Samuel, Ross A. D. Bathgate, Elaine N. Unemori, Steven W. Sutton, and Roger J. Summers. "Relaxin family peptide receptors – from orphans to therapeutic targets." Drug Discovery Today 13, no. 15-16 (August 2008): 640–51. http://dx.doi.org/10.1016/j.drudis.2008.04.002.

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Svendsen, Angela Manegold, Milka Vrecl, Louise Knudsen, Anders Heding, John D. Wade, Ross A. D. Bathgate, Pierre De Meyts, and Jane Nøhr. "Dimerization and Negative Cooperativity in the Relaxin Family Peptide Receptors." Annals of the New York Academy of Sciences 1160, no. 1 (April 2009): 54–59. http://dx.doi.org/10.1111/j.1749-6632.2009.03835.x.

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Scott, Daniel J., Tracey Wilkinson, Geoffrey W. Tregear, and Ross A. D. Bathgate. "The relaxin peptide family and their novel G-protein coupled receptors." International Journal of Peptide Research and Therapeutics 10, no. 5-6 (November 2003): 393–400. http://dx.doi.org/10.1007/s10989-004-2389-4.

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Scott, Daniel J., Tracey Wilkinson, Geoffrey W. Tregear, and Ross A. D. Bathgate. "The relaxin peptide family and their novel G-protein coupled receptors." Letters in Peptide Science 10, no. 5-6 (September 2003): 393–400. http://dx.doi.org/10.1007/bf02442569.

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Kania, Alan, Marian H. Lewandowski, and Anna Błasiak. "Relaxin-3 and relaxin family peptide receptors – from structure to functions of a newly discovered mammalian brain system." Postępy Higieny i Medycyny Doświadczalnej 68 (June 24, 2014): 851–64. http://dx.doi.org/10.5604/17322693.1110163.

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Chen, Catherine Z., Noel Southall, Jingbo Xiao, Juan J. Marugan, Marc Ferrer, Xin Hu, Raisa E. Jones, et al. "Identification of Small-Molecule Agonists of Human Relaxin Family Receptor 1 (RXFP1) by Using a Homogenous Cell-Based cAMP Assay." Journal of Biomolecular Screening 18, no. 6 (December 4, 2012): 670–77. http://dx.doi.org/10.1177/1087057112469406.

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The relaxin hormone is involved in a variety of biological functions, including female reproduction and parturition, as well as regulation of cardiovascular, renal, pulmonary, and hepatic functions. It regulates extracellular matrix remodeling, cell invasiveness, proliferation, differentiation, and overall tissue homeostasis. The G protein–coupled receptor (GPCR) relaxin family receptor 1 (RXFP1) is a cognate relaxin receptor that mainly signals through cyclic AMP second messenger. Although agonists of the receptor could have a wide range of pharmacologic utility, until now there have been no reported small-molecule agonists for relaxin receptors. Here, we report the development of a quantitative high-throughput platform for an RXFP1 agonist screen based on homogenous cell-based HTRF cyclic AMP (cAMP) assay technology. Two small molecules of similar structure were independently identified from a screen of more than 365 677 compounds. Neither compound showed activity in a counterscreen with HEK293T cells transfected with an unrelated GPCR vasopressin 1b receptor. These small-molecule agonists also demonstrated selectivity against the RXFP2 receptor, providing a basis for future medicinal chemistry optimization of selective relaxin receptor agonists.
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Dissertations / Theses on the topic "Relaxin family peptpide receptors"

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Wilkinson, Tracey Nicole. "Evolutionary analysis of the relaxin peptide family and their receptors." Connect to thesis, 2006. http://repository.unimelb.edu.au/10187/2315.

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The relaxin-like peptide family consists of relaxin-1, 2 and 3, and the insulin-like peptides (INSL)-3, 4, 5 and 6. The evolution of this family has been controversial; points of contention include the existence of an invertebrate relaxin and the absence of a ruminant relaxin. Using the known members of the relaxin peptide family, all available vertebrate and invertebrate genomes were searched for relaxin peptide sequences. Contrary to previous reports an invertebrate relaxin was not found; sequence similarity searches indicate the family emerged during early vertebrate evolution. Phylogenetic analyses revealed the presence of potential relaxin-3, relaxin and INSL5 homologs in fish; dating their emergence far earlier than previously believed. Furthermore, estimates of mutation rates suggested that the expansion of the family (i.e. the emergence of INSL6, INSL4 and relaxin-1) during mammalia was driven by positive Darwinian selection. In contrast, relaxin-3 is constrained by strong purifying selection, implying a highly conserved function. (For complete abstract open document)
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Book chapters on the topic "Relaxin family peptpide receptors"

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Summers, Roger J. "Relaxin Family Peptides and Their Receptors." In Encyclopedia of Molecular Pharmacology, 1345–53. Cham: Springer International Publishing, 2021. http://dx.doi.org/10.1007/978-3-030-57401-7_10067.

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Summers, Roger J. "Relaxin Family Peptides and Their Receptors." In Encyclopedia of Molecular Pharmacology, 1–8. Cham: Springer International Publishing, 2021. http://dx.doi.org/10.1007/978-3-030-21573-6_10067-1.

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Summers, Roger J., Michelle L. Halls, and Ross A. D. Bathgate. "Relaxin Family Peptide Receptors RXFP1 and RXFP2." In Encyclopedia of Signaling Molecules, 4583–615. Cham: Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-67199-4_362.

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Kocan, Martina, Sheng Yu Ang, and Roger J. Summers. "Relaxin Family Peptide Receptors RXFP3 and RXFP4." In Encyclopedia of Signaling Molecules, 4615–30. Cham: Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-67199-4_583.

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Summers, Roger J., Michelle L. Halls, and Ross A. D. Bathgate. "Relaxin Family Peptide Receptors RXFP1 and RXFP2." In Encyclopedia of Signaling Molecules, 1–32. New York, NY: Springer New York, 2016. http://dx.doi.org/10.1007/978-1-4614-6438-9_362-1.

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Kocan, Martina, Sheng Yu Ang, and Roger J. Summers. "Relaxin Family Peptide Receptors RXFP3 and RXFP4." In Encyclopedia of Signaling Molecules, 1–17. New York, NY: Springer New York, 2016. http://dx.doi.org/10.1007/978-1-4614-6438-9_583-1.

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Martemyanov, Kirill A., Pooja Parameswaran, Irene Aligianis, Mark Handley, Marga Gual-Soler, Tomohiko Taguchi, Jennifer L. Stow, et al. "Relaxin Family Peptide Receptors (RXFP) 1 and 2." In Encyclopedia of Signaling Molecules, 1635–43. New York, NY: Springer New York, 2012. http://dx.doi.org/10.1007/978-1-4419-0461-4_362.

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Martemyanov, Kirill A., Pooja Parameswaran, Irene Aligianis, Mark Handley, Marga Gual-Soler, Tomohiko Taguchi, Jennifer L. Stow, et al. "Relaxin Family Peptide Receptors (RXFP) 3 and 4." In Encyclopedia of Signaling Molecules, 1643–48. New York, NY: Springer New York, 2012. http://dx.doi.org/10.1007/978-1-4419-0461-4_583.

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Bathgate, Ross A. D. "Relaxin Family Peptide Receptors." In xPharm: The Comprehensive Pharmacology Reference, 1–2. Elsevier, 2007. http://dx.doi.org/10.1016/b978-008055232-3.63747-x.

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