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QRFP receptor

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Target not currently curated in GtoImmuPdb

Target id: 333

Nomenclature: QRFP receptor

Family: QRFP receptor

Gene and Protein Information Click here for help
class A G protein-coupled receptor
Species TM AA Chromosomal Location Gene Symbol Gene Name Reference
Human 7 431 4q27 QRFPR pyroglutamylated RFamide peptide receptor 12
Mouse 7 433 3 3B Qrfpr pyroglutamylated RFamide peptide receptor 22
Rat 7 433 2q25 Qrfpr pyroglutamylated RFamide peptide receptor
Gene and Protein Information Comments
Both the rat and mouse Qrfpr genes have shorter B isoforms (those in the table above being the longer A isoforms): rat Qrfprb is 415 aa [13] and is located on chromosome 4q31, mouse QrfprB is 416 aa [22] and is located on chromosome 6 C1.
Previous and Unofficial Names Click here for help
AQ27 [9] | SP9155 [12] | GPR103 | G protein-coupled receptor 103 | peptide p518 receptor
Database Links Click here for help
Specialist databases
GPCRdb qrfpr_human (Hs), qrfpr_mouse (Mm), qrfpr_rat (Rn)
Other databases
Alphafold
ChEMBL Target
Ensembl Gene
Entrez Gene
Human Protein Atlas
KEGG Gene
OMIM
Pharos
RefSeq Nucleotide
RefSeq Protein
UniProtKB
Wikipedia
Natural/Endogenous Ligands Click here for help
QRFP26 {Sp: Mouse}
QRFP43 {Sp: Mouse}
QRFP26 {Sp: Rat}
QRFP43 {Sp: Rat}
QRFP26 (26RFa) {Sp: Human}
QRFP43 (43RFa) {Sp: Human}

Download all structure-activity data for this target as a CSV file go icon to follow link

Agonists
Key to terms and symbols Click column headers to sort
Ligand Sp. Action Value Parameter Reference
[125I]QRFP43 (human) Peptide Ligand is labelled Ligand is radioactive Hs Full agonist 7.8 – 10.3 pKd 9,22
pKd 7.8 – 10.3 (Kd 1.58x10-8 – 5.01x10-11 M) [9,22]
QRFP26 {Sp: Mouse} Peptide Ligand is endogenous in the given species Mm Full agonist 8.2 pEC50 12
pEC50 8.2 (EC50 6x10-9 M) [12]
QRFP26 (26RFa) {Sp: Human} Peptide Ligand is endogenous in the given species Hs Full agonist 8.1 pEC50 4,12
pEC50 8.1 (EC50 7x10-9 M) [4,12]
QRFP43 (43RFa) {Sp: Human} Peptide Ligand is endogenous in the given species Hs Full agonist 6.9 – 8.6 pEC50 8,21
pEC50 6.9 – 8.6 (EC50 2.7x10-9 M) [8,21]
QRFP43 {Sp: Rat} Peptide Hs Full agonist 7.6 pEC50 22
pEC50 7.6 (EC50 2.3x10-8 M) [22]
QRFP43 (43RFa) {Sp: Human} Peptide Mm Full agonist 7.1 – 7.4 pEC50 22
pEC50 7.1 – 7.4 (EC50 7.3x10-8 – 4.2x10-8 M) This range compares the A and B isoforms of mouse Qrfpr. [22]
LV-2186 Peptide Hs Agonist 7.2 pEC50 1
pEC50 7.2 (EC50 6.64x10-8 M) [1]
Description: Measuring LV-2186-induced increase in intracellular calcium in human QRFPR-transfected CHO cells.
QRFP43 {Sp: Rat} Peptide Mm Full agonist 7.0 – 7.2 pEC50 22
pEC50 7.0 – 7.2 (EC50 9.1x10-8 – 6.3x10-8 M) This range compares the A and B isoforms of mouse Qrfpr. [22]
QRFP43 {Sp: Mouse} Peptide Ligand is endogenous in the given species Mm Full agonist 6.7 – 7.2 pEC50 22
pEC50 6.7 – 7.2 (EC50 1.94x10-7 – 7x10-8 M) This range compares the A and B isoforms of mouse Qrfpr. [22]
LV-2172 Peptide Hs Agonist 6.8 pEC50 19
pEC50 6.8 (EC50 1.64x10-7 M) [19]
LV-2211 Peptide Hs Agonist 6.5 pEC50 16
pEC50 6.5 (EC50 3.27x10-7 M) [16]
Description: Measuring intracellular Ca2+ mobilisation induced by the 26RFa(20–26) analog in CHO-G16-hQRFPR-transfected cells
QRFP43 (43RFa) {Sp: Human} Peptide Rn Full agonist 7.8 – 9.3 pIC50 4,9,22
pIC50 7.8 – 9.3 (IC50 1.6x10-8 – 5.2x10-10 M) [4,9,22]
[125I]QRFP43 (human) Peptide Ligand is labelled Ligand is radioactive Mm Full agonist 7.4 – 7.5 pIC50 22
pIC50 7.4 – 7.5 (IC50 3.8x10-8 – 3.2x10-8 M) This is the binding range comparing the A and B isoforms of mouse Qrfpr. [22]
QRFP26 {Sp: Rat} Peptide Ligand is endogenous in the given species Rn Full agonist - - 4
[4]
[125I]26RFa (human) Peptide Ligand is labelled Ligand is radioactive Hs Agonist - - 3
[3]
View species-specific agonist tables
Agonist Comments
In competitive binding experiments, various lengths of QRFP inhibited the binding of [125I-Tyr32]QRFP with AQ27. QRFP(43) proved the most potent in competition with an IC50 of 0.52 nM. Deletion of the N-terminal sequence in QRFP gradually diminished its binding affinity to AQ27 and was almost parallel to the decrease of cAMP production-inhibitory activities [9].
Antagonists
Key to terms and symbols View all chemical structures Click column headers to sort
Ligand Sp. Action Value Parameter Reference
compound 25e [PMID: 25875054] Small molecule or natural product Hs Antagonist 7.3 pIC50 10-11
pIC50 7.3 (IC50 4.6x10-8 M) [10-11]
Primary Transduction Mechanisms Click here for help
Transducer Effector/Response
Gi/Go family
Gq/G11 family
Adenylyl cyclase inhibition
Phospholipase C stimulation
References:  9,12
Tissue Distribution Click here for help
GPR103 transcripts of 4.0, 2.6 and 1.4 kb were detected in the thalamus and hypothalamus, with a further 9.5 kb signal in the hypothalamus and a 1.4 kb signal in the pituitary. Transcripts were also observed in the frontal and occipital cortices, basal forebrain, midbrain and pons.

Both SP9155 (GPR103) receptor and the P518 (QRFP) precursor mRNAs exhibited highest expression in brain. Coordinate expression of receptor and ligand mRNAs in most brain regions, however, in peripheral tissues receptor was nonexistent or expressed at low levels. In brain, receptor most abundant in retina, trigeminal ganglion, hypothalamus, and vestibular nucleus, whereas peptide mRNA most abundant in cerebellum, medulla, retina, and vestibular nucleus. In peripheral tissues, significant expression of SP9155 receptor found only in heart, kidney, and testes RNAs. The P518 precursor mRNA was found in prostate, testes, colon, thyroid, parathyroid, coronary artery, and bladder
Species:  Human
Technique:  Northern blot, quantitative PCR.
References:  12,15
Quantitative autoradiography was used to measure binding of [125I]-QRFP43 in human tissues from a range of organs including heart, lungs, kidney and adrenal. Tissue profiling revealed a remarkably discrete distribution amongst the tissues tested with highest densities of specific [125I]-QRFP43 binding to adrenals predominately to the zona reticularis and glomerulosa. Specific binding was below the level for detection in the zona fasciculata of the cortex and medulla. Over the concentration range tested, [125I]-QRFP43 binding to zona reticularis was saturable. The ligand bound with high affinity (KD =1.06±0.7nM, mean±s.e.mean) with a Bmax of 51.6±5.7fmol mg-1 protein. A one site fit was preferred to a two-site model and Hill coefficients were close to unity (nH=1.2±0.2) indicating the ligand was binding with a single affinity.
Species:  Human
Technique:  Radioligand binding.
References:  14
SP9155 (GPR130A) receptor mRNA highly expressed in brain, particularly hypothalamus, cortex, and spinal cord. P518 (QRFP) precursor was expressed at low levels relative to the receptor. In peripheral tissues, both SP9155 and P518 precursor were found in low abundance.

Quantitative RT-PCR analysis of the mRNA distribution of QRFP, GPR103A, and GPR103B in 15 different mouse tissues: QRFP mRNA was detected in CNS, eye, and testis, whereas both GPR103 mRNAs were found in CNS, eye, testis, and adrenal gland. However, in situ hybridization shows little, if any, overlap in the distributions of GPR103A and GPR103B mRNA in brain.
Species:  Mouse
Technique:  Quantitative PCR, quantitative RT-PCR, in situ hybridization.
References:  12,22
Highest level of AQ27 (GPR103A) mRNA detected in adrenal gland (8.7 copiesx10-3/ng poly(A)+RNA).
High level detected in hypothalamus.
Moderate levels detected in thalamus, midbrain, medulla oblongata, testis, and eye.

Brain: Strong signals for GPR103A detected in neurons within the piriform cortex, cortex-amygdala transition zone, ventral pallidum, lateral preoptic area, ventromedial hypothalamic nucleus, zona incerta, posterior hypothalamic area, marginal zone median geniculate, dorsal raphe nucleus, nucleus of the brachium inferior colliculus, intergeniculate leaf, locus caeruleus, and central gray α/β part.

Adrenal Gland: Detected in the cortex, high level of mRNA expression detected in the zona glomerulosa with moderate levels found in the zona fasciculata and zona reticularis
Species:  Rat
Technique:  Quantitative RT-PCR, in situ hybridisation.
References:  9
26RFa recognition sites are widely distributed throughout the rat CNS, from the olfactory bulb to the spinal cord, whereas expression of GPR103A mRNA is more discrete, in particular in the thalamus, the midbrain, the pons, and the medulla oblongata, suggesting that 26RFa can bind to a receptor(s) other than GPR103A. Competition experiments confirmed that 26RFa interacts with an RFamide peptide receptor distinct from GPR103A that may be NPFF2. The wide distribution of 26RFa binding sites suggests that 26RFa has multiple functions in the CNS that are mediated by at least two distinct receptors. Note, however, that the authors appear to be unaware of the predicted GPR103B gene. Quantification of the autoradiographic signal has revealed that 26RFa receptors are particularly abundant in nuclei associated with feeding and arousal behavior, reproduction function, control of arterial blood pressure, and transmission and/or integration of olfactory, visual, and nociceptive stimuli.
Species:  Rat
Technique:  Radioligand binding, in situ hybridisation histochemistry.
References:  3
Expression Datasets Click here for help

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Log average relative transcript abundance in mouse tissues measured by qPCR from Regard, J.B., Sato, I.T., and Coughlin, S.R. (2008). Anatomical profiling of G protein-coupled receptor expression. Cell, 135(3): 561-71. [PMID:18984166] [Raw data: website]

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Functional Assays Click here for help
Measurement of intracellular Ca2+ and cAMP changes in CHO or HEK293 cells transfected with human GPR103 after stimulation with QRFP.
Species:  Human
Tissue:  CHO or HEK293 cells transfected with human GPR103.
Response measured:  Changes in intracellular calcium and cAMP.
References:  9,22
Competition binding assays were performed by using [125I-Tyr-32]-QRFP on monolayers of COS-7 cells transiently transfected with GPR103A or GPR103B cDNA.
Species:  Mouse
Tissue:  COS-7 cells.
Response measured:  Binding of [125I-Tyr-32]-QRFP.
References:  22
In HEK293 cells transiently transfected with mouse GPR103A, or GPR103B cDNA, rat QRFP induced a transient increase of intracellular Ca2+ levels in a dose-dependent manner.
Species:  Mouse
Tissue:  HEK293 cells.
Response measured:  Measurement of changes in intracellular Ca2+.
References:  22
Competition binding assays using [125I-Tyr-32]-QRFP on monolayers of COS-7 cells transiently transfected with GPR103 cDNA.
Species:  Human
Tissue:  COS-7 cells.
Response measured:  Binding of [125I-Tyr-32]-QRFP.
References:  22
Physiological Functions Click here for help
Central administration of QRFP in mice, induced feeding behaviour, accompanied by increased general locomotor activity, metabolic rate and influenced blood pressure. The orexigenic action of QRFP is at least partly mediated through the neuropeptide Y (NPY) pathway, and QRFP mRNA level was increased in genetically obese ob/ob and db/db mice.
Species:  Mouse
Tissue:  Brain
References:  22
i.c.v. injection of 26RFa, 43RFa, 26RFa20–26 and 9RFa stimulated food consumption while 26RFa1–16 and 26RFa8–16 had no effect. A dose-dependent stimulation of locomotor activity was observed after i.c.v. administration of 26RFa, 43RFa and 26RFa1–16, but not 26RFa20–26, 26RFa8–16 or 9Rfa.
Species:  Mouse
Tissue:  Brain
References:  6
Effects of 26RFa on gonadotropin secretion were evaluated in the rat by a combination of in vitro and in vivo approaches. At the pituitary, 26RFa dose-dependently enhanced basal and gonadotropin-releasing hormone (GnRH)-stimulated luteinizing hormone (LH) secretion from male and cyclic female rats. Intracerebral injection of 26RFa evoked a significant increase in serum LH levels in cyclic and ovariectomized females. Moreover, expression of the genes encoding 26RFa and its putative receptor, GPR103, was demonstrated in rat pituitary throughout postnatal development.
Species:  Rat
Tissue:  Brain
References:  18
Effects of chronic administration of QRFP43 on feeding behaviour, body weight regulation, and energy expenditure in mice. Intracerebroventricular infusion of QRFP43 for 13d resulted in a significant increase in body weight and fat mass with hyperphagia. Weight gain and hyperphagia were more evident when mice were fed a moderately high-fat diet. Pair feeding of QRFP43-infused mice did not increase body weight but significantly increased fat mass and plasma concentrations of insulin, leptin, and cholesterol when compared with controls. Moreover, significant decreases in rectal temperature and expression of brown adipose tissue uncoupling protein-1 mRNA were observed in QRFP43-infused ad libitum- and pair-fed mice.
Species:  Mouse
Tissue:  Brain
References:  17
26RFa dose-dependently reduced glucose-induced insulin release, inhibited the insulin responses to both arginine and exendin-4 and did not affect glucagon output. The inhibitory effect of 26RFa on exendin-4-induced insulin secretion was not observed in pancreata from pertussis toxin-treated rats, thus suggesting that 26RFa may inhibit insulin secretion, at least in part, via a pertussis toxin-sensitive Gi protein coupled to the adenylyl cyclase system.
Species:  Rat
Tissue:  Pancreas
References:  7
Intravenous injection of QRFP43 into rats stimulates aldosterone secretion. Human QRFP(43) at doses of 40–400 nmol/kg of weight increased plasma aldosterone levels 5–15 min after administration. Five minutes after administration, plasma aldosterone concentrations in the treated rats reached about 5 times those in the untreated rats and then gradually declined reaching the basal level at 60 min. Results indicate that QRFP acts directly on the zona glomerulosa to induce aldosterone secretion in rats.
Species:  Rat
Tissue:  Adrenal gland
References:  9
i.c.v. administration of 2 nmol QRFP43 significantly elevated plasma LH and FSH at 40 minutes post-injection. The stimulatory effect of i.c.v. administration of QRFP43 on LH levels appeared to be larger than that on FSH levels.
Species:  Rat
Tissue:  Brain
References:  20
Physiological Consequences of Altering Gene Expression Click here for help
GPR103A-/- mice exhibited a thinned osteochondral growth plate, a thickening of trabecular branches, and a reduction in osteoclast number, suggestive of an early arrest of osteochondral bone formation. Microcomputed tomography confirmed reduction in trabecular bone and connective tissue densities. Whole-body radiography followed by morphometric analysis revealed kyphosis in mutant animals. Reverse transcription-PCR showed GPR103 expression in human skull, mouse spine, and several osteoblast cell lines. Dexamethasone, inhibitor of osteoblast growth and inducer of osteoblast differentiation, inhibited GPR103 expression in human osteoblast primary cultures. These results suggest that osteopenia in GPR103-/- mice may be mediated directly by the loss of GPR103A expression in bone.
Species:  Mouse
Tissue: 
Technique:  Gene targeting in embryonic stem cells
References:  2,23
Phenotypes, Alleles and Disease Models Click here for help Mouse data from MGI

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Allele Composition & genetic background Accession Phenotype Id Phenotype Reference
Qrfprtm1Lex Qrfprtm1Lex/Qrfprtm1Lex
involves: 129S/SvEvBrd * C57BL/6J
MGI:2677633  MP:0000130 abnormal cancellous bone morphology PMID: 16382160 
Qrfprtm1Lex Qrfprtm1Lex/Qrfprtm1Lex
involves: 129S/SvEvBrd * C57BL/6J
MGI:2677633  MP:0004173 abnormal intervertebral disk morphology PMID: 16382160 
Qrfprtm1Lex Qrfprtm1Lex/Qrfprtm1Lex
involves: 129S/SvEvBrd * C57BL/6J
MGI:2677633  MP:0003049 abnormal lumbar vertebrae morphology PMID: 16382160 
Qrfprtm1Lex Qrfprtm1Lex/Qrfprtm1Lex
involves: 129S/SvEvBrd * C57BL/6J
MGI:2677633  MP:0006392 abnormal nucleus pulposus morphology PMID: 16382160 
Qrfprtm1Lex Qrfprtm1Lex/Qrfprtm1Lex
involves: 129S/SvEvBrd * C57BL/6J
MGI:2677633  MP:0005225 abnormal vertebrae development PMID: 16382160 
Qrfprtm1Lex Qrfprtm1Lex/Qrfprtm1Lex
involves: 129S/SvEvBrd * C57BL/6J
MGI:2677633  MP:0000137 abnormal vertebrae morphology PMID: 16382160 
Qrfprtm1Lex Qrfprtm1Lex/Qrfprtm1Lex
involves: 129S/SvEvBrd * C57BL/6J
MGI:2677633  MP:0010121 decreased bone mineral density PMID: 16382160 
Qrfprtm1Lex Qrfprtm1Lex/Qrfprtm1Lex
involves: 129S/SvEvBrd * C57BL/6J
MGI:2677633  MP:0000160 kyphosis PMID: 16382160 
Gene Expression and Pathophysiology Comments
It has been recently shown that GPR103 and orexin receptors (OXRs) form constitutive and induced functional hetero-dimers at the neuronal level [5]. Treatment of the neuroblastoma cell line SH-SY5Y with Aβ42 reduces the expression of GPR103 and OXRs. In accordance, GPR103/OXRs mRNA is down-regulated in the anterior hippocampus of Alzheimer's disease (AD) patients. These results suggest that a reduction in GPR103/OXRs hetero-dimers in AD patients may promote cellular damage resulting in memory defects [5].

References

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1. Alim K, Lefranc B, Sopkova-de Oliveira Santos J, Dubessy C, Picot M, Boutin JA, Vaudry H, Chartrel N, Vaudry D, Chuquet J et al.. (2018) Design, Synthesis, Molecular Dynamics Simulation, and Functional Evaluation of a Novel Series of 26RFa Peptide Analogues Containing a Mono- or Polyalkyl Guanidino Arginine Derivative. J Med Chem, 61 (22): 10185-10197. [PMID:30358997]

2. Baribault H, Danao J, Gupte J, Yang L, Sun B, Richards W, Tian H. (2006) The G-protein-coupled receptor GPR103 regulates bone formation. Mol Cell Biol, 26 (2): 709-17. [PMID:16382160]

3. Bruzzone F, Lectez B, Alexandre D, Jégou S, Mounien L, Tollemer H, Chatenet D, Leprince J, Vallarino M, Vaudry H et al.. (2007) Distribution of 26RFa binding sites and GPR103 mRNA in the central nervous system of the rat. J Comp Neurol, 503 (4): 573-91. [PMID:17534937]

4. Chartrel N, Dujardin C, Anouar Y, Leprince J, Decker A, Clerens S, Do-Régo JC, Vandesande F, Llorens-Cortes C, Costentin J et al.. (2003) Identification of 26RFa, a hypothalamic neuropeptide of the RFamide peptide family with orexigenic activity. Proc Natl Acad Sci USA, 100 (25): 15247-52. [PMID:14657341]

5. Davies J, Chen J, Pink R, Carter D, Saunders N, Sotiriadis G, Bai B, Pan Y, Howlett D, Payne A et al.. (2015) Orexin receptors exert a neuroprotective effect in Alzheimer's disease (AD) via heterodimerization with GPR103. Sci Rep, 5: 12584. [PMID:26223541]

6. do Rego JC, Leprince J, Chartrel N, Vaudry H, Costentin J. (2006) Behavioral effects of 26RFamide and related peptides. Peptides, 27 (11): 2715-21. [PMID:16730856]

7. Egido EM, Hernández R, Leprince J, Chartrel N, Vaudry H, Marco J, Silvestre RA. (2007) 26RFa, a novel orexigenic neuropeptide, inhibits insulin secretion in the rat pancreas. Peptides, 28 (4): 725-30. [PMID:16777265]

8. Fukusumi S, Fujii R, Hinuma S. (2006) Recent advances in mammalian RFamide peptides: the discovery and functional analyses of PrRP, RFRPs and QRFP. Peptides, 27 (5): 1073-86. [PMID:16500002]

9. Fukusumi S, Yoshida H, Fujii R, Maruyama M, Komatsu H, Habata Y, Shintani Y, Hinuma S, Fujino M. (2003) A new peptidic ligand and its receptor regulating adrenal function in rats. J Biol Chem, 278 (47): 46387-95. [PMID:12960173]

10. Georgsson J, Bergström F, Nordqvist A, Watson MJ, Blundell CD, Johansson MJ, Petersson AU, Yuan ZQ, Zhou Y, Kristensson L et al.. (2014) GPR103 antagonists demonstrating anorexigenic activity in vivo: design and development of pyrrolo[2,3-c]pyridines that mimic the C-terminal Arg-Phe motif of QRFP26. J Med Chem, 57 (14): 5935-48. [PMID:24937104]

11. Georgsson J, Bergström F, Nordqvist A, Watson MJ, Blundell CD, Johansson MJ, Petersson AU, Yuan ZQ, Zhou Y, Kristensson L et al.. (2015) Correction to GPR103 Antagonists Demonstrating Anorexigenic Activity in Vivo: Design and Development of Pyrrolo[2,3-c]pyridines That Mimic the C-Terminal Arg-Phe Motif of QRFP26. J Med Chem, 58 (9): 4086. [PMID:25875054]

12. Jiang Y, Luo L, Gustafson EL, Yadav D, Laverty M, Murgolo N, Vassileva G, Zeng M, Laz TM, Behan J et al.. (2003) Identification and characterization of a novel RF-amide peptide ligand for orphan G-protein-coupled receptor SP9155. J Biol Chem, 278 (30): 27652-7. [PMID:12714592]

13. Kampe J, Wiedmer P, Pfluger PT, Castaneda TR, Burget L, Mondala H, Kerr J, Liaw C, Oldfield BJ, Tschöp MH et al.. (2006) Effect of central administration of QRFP(26) peptide on energy balance and characterization of a second QRFP receptor in rat. Brain Res, 1119 (1): 133-49. [PMID:16996040]

14. Kuc RE, Mitchell JD, Davenport AD. (2006) The novel ligand [125I]-QRFP43 reveals a remarkably discrete distribution of the orphan receptor GPR103 in human adrenal. Proceedings of the British Pharmacological Society, 4 (2): abst186.

15. Lee DK, Nguyen T, Lynch KR, Cheng R, Vanti WB, Arkhitko O, Lewis T, Evans JF, George SR, O'Dowd BF. (2001) Discovery and mapping of ten novel G protein-coupled receptor genes. Gene, 275 (1): 83-91. [PMID:11574155]

16. Lefranc B, Alim K, Neveu C, Le Marec O, Dubessy C, Boutin JA, Chuquet J, Vaudry D, Prévost G, Picot M et al.. (2021) Point-Substitution of Phenylalanine Residues of 26RFa Neuropeptide: A Structure-Activity Relationship Study. Molecules, 26 (14). DOI: 10.3390/molecules26144312 [PMID:34299587]

17. Moriya R, Sano H, Umeda T, Ito M, Takahashi Y, Matsuda M, Ishihara A, Kanatani A, Iwaasa H. (2006) RFamide peptide QRFP43 causes obesity with hyperphagia and reduced thermogenesis in mice. Endocrinology, 147 (6): 2916-22. [PMID:16543370]

18. Navarro VM, Fernández-Fernández R, Nogueiras R, Vigo E, Tovar S, Chartrel N, Le Marec O, Leprince J, Aguilar E, Pinilla L et al.. (2006) Novel role of 26RFa, a hypothalamic RFamide orexigenic peptide, as putative regulator of the gonadotropic axis. J Physiol (Lond.), 573 (Pt 1): 237-49. [PMID:16543265]

19. Neveu C, Lefranc B, Tasseau O, Do-Rego JC, Bourmaud A, Chan P, Bauchat P, Le Marec O, Chuquet J, Guilhaudis L et al.. (2012) Rational design of a low molecular weight, stable, potent, and long-lasting GPR103 aza-β3-pseudopeptide agonist. J Med Chem, 55 (17): 7516-24. [PMID:22800498]

20. Patel SR, Murphy KG, Thompson EL, Patterson M, Curtis AE, Ghatei MA, Bloom SR. (2008) Pyroglutamylated RFamide peptide 43 stimulates the hypothalamic-pituitary-gonadal axis via gonadotropin-releasing hormone in rats. Endocrinology, 149 (9): 4747-54. [PMID:18535111]

21. Southern C, Cook JM, Neetoo-Isseljee Z, Taylor DL, Kettleborough CA, Merritt A, Bassoni DL, Raab WJ, Quinn E, Wehrman TS et al.. (2013) Screening β-Arrestin Recruitment for the Identification of Natural Ligands for Orphan G-Protein-Coupled Receptors. J Biomol Screen, 18 (5): 599-609. [PMID:23396314]

22. Takayasu S, Sakurai T, Iwasaki S, Teranishi H, Yamanaka A, Williams SC, Iguchi H, Kawasawa YI, Ikeda Y, Sakakibara I et al.. (2006) A neuropeptide ligand of the G protein-coupled receptor GPR103 regulates feeding, behavioral arousal, and blood pressure in mice. Proc Natl Acad Sci USA, 103 (19): 7438-43. [PMID:16648250]

23. Zhang Q, Qiu P, Arreaza MG, Simon JS, Golovko A, Laverty M, Vassileva G, Gustafson EL, Rojas-Triana A, Bober LA et al.. (2007) P518/Qrfp sequence polymorphisms in SAMP6 osteopenic mouse. Genomics, 90 (5): 629-35. [PMID:17869477]

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