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Olfactory receptor 73

mOR-EG, Olfr73, MOR174-9
Olfactory receptors interact with odorant molecules in the nose, to initiate a neuronal response that triggers the perception of a smell. The olfactory receptor proteins are members of a large family of G-protein-coupled receptors (GPCR) arising from single coding-exon genes. Olfactory receptors share a 7-transmembrane domain structure with many neurotransmitter and hormone receptors and are responsible for the recognition and G protein-mediated transduction of odorant signals. The olfactory receptor gene family is the largest in the genome. The nomenclature assigned to the olfactory receptor genes and proteins for this organism is independent of other organisms. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: mu-opioid receptor, ACID, CAN, V1a, Rhodopsin
Papers on mOR-EG
Exchanging ligand-binding specificity between a pair of mouse olfactory receptor paralogs reveals odorant recognition principles.
Pick et al., Lausanne, Switzerland. In Sci Rep, 2014
By exchanging two of three residues, differing at equivalent positions of the putative odorant binding site between the mouse OR paralogs Olfr73 (mOR-EG) and Olfr74 (mOR-EV), we selectively changed ligand preference but remarkably also signaling activation strength in both ORs.
In vivo identification of eugenol-responsive and muscone-responsive mouse odorant receptors.
Matsunami et al., Frankfurt am Main, Germany. In J Neurosci, 2014
Heterologous expression assays confirmed nine eugenol-responsive ORs (Olfr73, Olfr178, Olfr432, Olfr610, Olfr958, Olfr960, Olfr961, Olfr913, and Olfr1234) and four muscone-responsive ORs (Olfr74, Olfr235, Olfr816, and Olfr1440).
Evaluation of the role of g protein-coupled receptor kinase 3 in desensitization of mouse odorant receptors in a Mammalian cell line and in olfactory sensory neurons.
Touhara et al., Tokyo, Japan. In Chem Senses, 2014
Here we show that GRK3 attenuated the agonist responsiveness of a specific mouse odorant receptor for eugenol (mOR-EG) upon agonist pretreatment in HEK293 cells, but GRK3 did not affect the response amplitude or the recovery kinetics upon repeated agonist stimulation.
Ligand-selective activation of heterologously-expressed mammalian olfactory receptor.
Ache et al., Gainesville, United States. In Cell Calcium, 2014
To better understand the mechanisms and molecular range of such ligand selectivity, we expressed the mouse eugenol OR (mOR-EG) in HEK293T cells together with Gα15 to monitor activation of the phospholipase-C (PLC) signaling pathway and/or Gαolf to monitor activation of the adenylate cyclase (AC) signaling pathway, resulting in intracellular Ca(2+) release and/or Ca(2+) influx through a cyclic nucleotide-gated channel, respectively.
Activation of SRE and AP1 by olfactory receptors via the MAPK and Rho dependent pathways.
Galibert et al., Rennes, France. In Cell Signal, 2013
Using real time PCR we found that mOR23, RnI7 and CfOR12A07 induced elevated levels of transcription factors ELK-4, srf, c-fos and c-jun mRNAs whereas mOREG induced an elevated transcription levels of c-fos and c-jun mRNA only.
Functional reconstitution of olfactory receptor complex on baculovirus.
Hamakubo et al., Tokyo, Japan. In Chem Senses, 2012
Sf9 cells were coinfected with recombinant baculoviruses harboring the cDNAs encoding adenylyl cyclase, trimeric G-protein, and the receptor: mOR-EG or S6.
The mouse eugenol odorant receptor: structural and functional plasticity of a broadly tuned odorant binding pocket.
Pick et al., Lausanne, Switzerland. In Biochemistry, 2011
Here we investigated this question for the mouse eugenol receptor (mOR-EG).
Ligand specificity of odorant receptors.
Carloni et al., Trieste, Italy. In J Mol Model, 2007
Recent site-directed mutagenesis experiments on one such receptor (MOR174-9) provide information that helped to identify nine amino-acid residues involved in ligand binding.
Structural basis for a broad but selective ligand spectrum of a mouse olfactory receptor: mapping the odorant-binding site.
GeneRIF
Touhara et al., Chiba, Japan. In J Neurosci, 2005
The odorant-binding site lies in a hydrophobic pocket formed by TM3, TM5, and TM6. Phe252 in TM6 of mOR-EG appears to be critical in switching the receptor conformation from an inactive to an active state.
An odorant derivative as an antagonist for an olfactory receptor.
Touhara et al., Kashiwa, Japan. In Chem Senses, 2004
Here we show that stored isoeugenol has an antagonistic effect on a mouse olfactory receptor, mOR-EG.
[A molecular basis for odorant recognition: olfactory receptor pharmacology].
Review
Touhara et al., Chiba, Japan. In Nihon Yakurigaku Zasshi, 2004
Here we show that mOR-EG, a mouse olfactory receptor that was isolated from a eugenol-responsive cell, recognizes 22 different odorants with EC50 values ranging from a few microM to several hundred microM.
Endoplasmic reticulum degradation impedes olfactory G-protein coupled receptor functional expression.
Moyer et al., Los Angeles, United States. In Bmc Cell Biol, 2004
RESULTS: To develop means to increase the functional expression of ORs, we devised an approach to measure activation of the mOREG OR (Unigene # Mm.196680; Olfr73) through coupling to an olfactory cyclic nucleotide-gated cation channel (CNG).
Structural determinants for membrane trafficking and G protein selectivity of a mouse olfactory receptor.
Touhara et al., Tokyo, Japan. In J Neurochem, 2004
Each OR appears to recognize odorants based on similarities in molecular structures such that mOR-EG, a mouse OR, binds eugenol, vanillin, and some other structurally related odorants.
Odorant response assays for a heterologously expressed olfactory receptor.
Touhara et al., Chiba, Japan. In Biochem Biophys Res Commun, 2003
Odorant responsiveness of a mouse olfactory receptor, mOR-EG, was investigated in various heterologous cells using a variety of detection methods.
Endoplasmic reticulum retention, degradation, and aggregation of olfactory G-protein coupled receptors.
Moyer et al., Los Angeles, United States. In Traffic, 2003
We determined that the mouse odorant receptors mI7 and mOREG are not selected for export from the ER and therefore are not detectable at the Golgi apparatus or plasma membrane.
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