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GRM1 (glutamate receptor, metabotropic 1)

Written2013-08Jairo Sierra, Suzie Chen
Department of Chemical Biology, Susan Lehman Cullman Laboratory for Cancer Research, Ernest Mario School of Pharmacy, Rutgers, The State University of New Jersey, 164 Frelinghuysen Road, Piscataway, NJ 08854-8020, USA

(Note : for Links provided by Atlas : click)

Identity

Alias_namesregulatory subunit 85
Alias_symbol (synonym)GPRC1A
mGlu1
MGLUR1
PPP1R85
Other aliasMGLU1
SCAR13
HGNC (Hugo) GRM1
LocusID (NCBI) 2911
Atlas_Id 43851
Location 6q24.3  [Link to chromosome band 6q24]
Location_base_pair Starts at 146029198 and ends at 146437598 bp from pter ( according to hg19-Feb_2009)  [Mapping GRM1.png]
Fusion genes
(updated 2016)
BCLAF1 (6q23.3) / GRM1 (6q24.3)COL12A1 (6q13) / GRM1 (6q24.3)MEF2A (15q26.3) / GRM1 (6q24.3)
TBL1XR1 (3q26.32) / GRM1 (6q24.3)

DNA/RNA

 
  Figure 1. Human GRM1 has 10 exons, which are depicted by boxes and shown with the relative position to one another. Adapted from DiRaddo et al., 2013.
Description The mGluR1 gene contains 10 exons, which span a region of 409953 bp.
Transcription The transcribed matured mRNA is 6939 bps in length.

Protein

Note GRM1 encodes five alternative splice variants (1a, 1b, 1c, 1d, and 1e) (Zhu et al., 1999). All five variants contain the same N-terminal, but differ in the amino acid composition of their C-terminal domains due to the alternative splicings (DiRaddo et al., 2013).
 
  Figure 2. There are five human mGluR1 isoforms. The black boxes represent the seven-transmembrane domains of mGluR1. Alternative splicing of mGluR1 mRNA produces five mGluR1 isoforms each with a unique C-termini, which is highlighted by the different colors. The shortest isoform, mGluR1e, is truncated before the seven-transmembrane domains, which results in the expression of only the amino terminal fragment (Costantino and Pellicciari, 1996). Adapted from Hermans and Challiss, 2001.
Description mGluR1 is an 1194 amino acid seven-transmembrane domain G-protein coupled receptor normally expressed in neuronal and glial cells in the brain (Stephan et al., 1996; Hermans and Challiss, 2001). Its natural ligand is the excitatory neurotransmitter, L-glutamate. Structurally, mGluR1 has various domains that are necessary for its functions. The N-terminus forms two large extracellular lobes separated by a cavity where the ligand glutamate binds to and is referred to as the amino terminal domain (ATD) or "Venus Fly Trap" (O'Hara et al., 1993; Beqollari and Kammermeier, 2010). ATD is separated from the trans-membrane region of mGluR1 by a 70 amino acid cysteine rich domain (CRD), which is essential for dimerization, and activation of the receptor (Huang et al., 2011). The seven alpha-helical transmembrane domains (TMD) precede the cysteine rich region. Following the TMD is the carboxyl terminus of mGluR1, also known as the intracellular cytoplasmic tail domain (CTD). CTD is involved in modulating G-protein coupling and selectivity (Pin et al., 2003; Seebahn et al., 2013). The CTD is also the region subjected to alternative splicings, regulated by phosphorylation, and modulatory protein-protein interactions (Niswender and Conn, 2010). The CRD is consisted of three beta-pleated sheets and nine cysteine residues. CRD plays a key role in facilitating the allosteric coupling between the ATD and the TMD regions during ligand binding and receptor activation (Niswender and Conn, 2010). Upon activation of mGluR1 by glutamate, the signal induced is transmitted from the ATD through the CRDs, by way of a disulfide bridge formed between the 9th cysteine of the CRD and a cysteine residue in lobe 2 of the ATD (Rondard et al., 2006; Muto et al., 2007). As a result, a conformational change takes place that brings the C-terminal regions of the CRDs closer to one another and elicits cysteine-cysteine interaction in the e2 loop of the TMD (Muto et al., 2007). This conformational change produces a shift in the TMD to induce G-protein activation (El Moustaine et al., 2012).
Expression mGluR1 is normally expressed in the central nervous system and is activated by its natural ligand, L-glutamate (Teh and Chen, 2012a). Upon activation, mGluR1 couples to Gα/q11 proteins to induce phosphatidylinositol (4,5)-biphosphate (PIP2) hydrolysis leading to the formation of two-second messengers, inositol 1,4,5-triphosphate (IP3) and diacyglycerol (DAG) (Conn and Pin, 1997; Hermans and Challiss, 2001). These second messengers stimulate intracellular calcium release from the endoplasmic reticulum (ER) stores and activate protein kinase C (PKC), resulting in the stimulation of G-protein-independent signal transduction pathways (Hermans and Challiss, 2001; Goudet et al., 2009). Such pathways include the mitogen activated protein kinase pathway (MAPK) and the phosphatidylinositol-3-kinase (PI3K)/AKT pathway (Marín, et al., 2006; Shin et al., 2010).
 
  Figure 3. Diagram of the proposed signal transduction pathways elicited by stimulated mGluR1. Adapted from Teh and Chen, 2012b.
Localisation Cell membrane of neurons.
Function mGluR1 activation is involved in mediating neuronal excitability, synaptic plasticity, and feedback inhibition of neurotransmitter release (Speyer et al., 2012). All of which promotes learning and memory formation in the central nervous system (Hermans and Challiss, 2001).

Mutations

Note Over 20 somatic missense mutations in the ligand binding and intracellular regulatory domains of mGluR1 have been identified in various tumors types (Sjöblom et al., 2006; Kan et al., 2010; Esseltine et al., 2013). A number of these mutations result in irregular mGluR1 stimulation of G protein coupling, biased ERK1/ERK2 phosphorylation, and intracellular retention in the endoplasmic reticulum (ER) (Esseltine et al., 2013). Such changes in mGluR1 signaling lead to abnormal receptor activity in numerous human cancers.

Implicated in

Note
  
Entity Melanoma
Disease Melanoma is the most severe form of skin cancer and arises from the aberrant transformation of melanocytes. The most common mutations identified as drivers of melanomagenesis include B-RAF and N-RAS activating mutations as well the tumor suppressors INK4a/ARF and PTEN (Teh and Chen, 2012a).
Oncogenesis Glutamate signaling via mGluR1 has been shown to affect cell survival, cell differentiation and cell proliferation of non-neuronal tissues (Skerry and Genever, 2001; Shin et al., 2008). Chen and colleagues demonstrated the ectopic expression of mGluR1 in mouse melanocytes was sufficient to induce spontaneous metastatic melanoma development in transgenic mouse models, TG3 and Tg(Grm1)EPv (E) (Pollock et al., 2003). The ectopic expression of human mGluR1 was also detected in human melanoma cell lines and biopsy samples. To date, ~175 melanoma biopsy samples from primary to metastatic lesions have ben examined and found GRM1 mRNA and protein to be expressed in ~ 60% of the samples (Pollock et al., 2003; Namkoong et al., 2007). Moreover, expression and activation of mGluR1 in melanoma cells has been shown to activate the MAPK and P13K/AKT pathways, two of the most frequently stimulated signaling cascades in melanoma (Marín et al., 2006; Shin et al., 2010).
  
  
Entity Breast cancer (triple-negative breast cancer)
Disease Triple-negative breast cancer, are malignant tumors in breast tissue that lack estrogen receptor and progesterone receptor and amplification of the HER2 gene (Engebraaten et al., 2013).
Oncogenesis Speyer and colleagues described mGluR1 expression as a potential oncogene in mammary breast pathogenesis. They detected mGluR1 expression in multiple triple-negative breast cancer cell lines (TNBC) (Speyer et al., 2012). This group also provided evidences that the growth of TNBC cells was inhibited when mGluR1 expression was reduced by an shRNA or treatment with mGluR1 antagonist, Bay36-7620 (Speyer et al., 2012).
  

Bibliography

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Beqollari D, Kammermeier PJ.
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Two newly identified exons in human GRM1 express a novel splice variant of metabotropic glutamate 1 receptor.
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Somatic mutations in GRM1 in cancer alter metabotropic glutamate receptor 1 intracellular localization and signaling.
Esseltine JL, Willard MD, Wulur IH, Lajiness ME, Barber TD, Ferguson SS.
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Structural, signalling and regulatory properties of the group I metabotropic glutamate receptors: prototypic family C G-protein-coupled receptors.
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PMID 11672421
 
Interdomain movements in metabotropic glutamate receptor activation.
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Diverse somatic mutation patterns and pathway alterations in human cancers.
Kan Z, Jaiswal BS, Stinson J, Janakiraman V, Bhatt D, Stern HM, Yue P, Haverty PM, Bourgon R, Zheng J, Moorhead M, Chaudhuri S, Tomsho LP, Peters BA, Pujara K, Cordes S, Davis DP, Carlton VE, Yuan W, Li L, Wang W, Eigenbrot C, Kaminker JS, Eberhard DA, Waring P, Schuster SC, Modrusan Z, Zhang Z, Stokoe D, de Sauvage FJ, Faham M, Seshagiri S.
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PMID 20668451
 
Stimulation of oncogenic metabotropic glutamate receptor 1 in melanoma cells activates ERK1/2 via PKCepsilon.
Marin YE, Namkoong J, Cohen-Solal K, Shin SS, Martino JJ, Oka M, Chen S.
Cell Signal. 2006 Aug;18(8):1279-86. Epub 2005 Nov 21.
PMID 16305822
 
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Metabotropic glutamate receptor 1 and glutamate signaling in human melanoma.
Namkoong J, Shin SS, Lee HJ, Marin YE, Wall BA, Goydos JS, Chen S.
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PMID 17332361
 
Metabotropic glutamate receptors: physiology, pharmacology, and disease.
Niswender CM, Conn PJ.
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PMID 20055706
 
The ligand-binding domain in metabotropic glutamate receptors is related to bacterial periplasmic binding proteins.
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PMID 8338667
 
Evolution, structure, and activation mechanism of family 3/C G-protein-coupled receptors.
Pin JP, Galvez T, Prezeau L.
Pharmacol Ther. 2003 Jun;98(3):325-54. (REVIEW)
PMID 12782243
 
Melanoma mouse model implicates metabotropic glutamate signaling in melanocytic neoplasia.
Pollock PM, Cohen-Solal K, Sood R, Namkoong J, Martino JJ, Koganti A, Zhu H, Robbins C, Makalowska I, Shin SS, Marin Y, Roberts KG, Yudt LM, Chen A, Cheng J, Incao A, Pinkett HW, Graham CL, Dunn K, Crespo-Carbone SM, Mackason KR, Ryan KB, Sinsimer D, Goydos J, Reuhl KR, Eckhaus M, Meltzer PS, Pavan WJ, Trent JM, Chen S.
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PMID 16787923
 
Comment on "The consensus coding sequences of human breast and colorectal cancers".
Rubin AF, Green P.
Science. 2007 Sep 14;317(5844):1500.
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Seebahn A, Sticht H, Enz R.
Methods Enzymol. 2013;520:257-79. doi: 10.1016/B978-0-12-391861-1.00012-5.
PMID 23332704
 
Oncogenic activities of metabotropic glutamate receptor 1 (Grm1) in melanocyte transformation.
Shin SS, Namkoong J, Wall BA, Gleason R, Lee HJ, Chen S.
Pigment Cell Melanoma Res. 2008 Jun;21(3):368-78. doi: 10.1111/j.1755-148X.2008.00452.x. Epub 2008 Apr 23.
PMID 18435704
 
AKT2 is a downstream target of metabotropic glutamate receptor 1 (Grm1).
Shin SS, Wall BA, Goydos JS, Chen S.
Pigment Cell Melanoma Res. 2010 Feb;23(1):103-11. doi: 10.1111/j.1755-148X.2009.00648.x. Epub 2009 Oct 20.
PMID 19843246
 
The consensus coding sequences of human breast and colorectal cancers.
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Skerry TM, Genever PG.
Trends Pharmacol Sci. 2001 Apr;22(4):174-81. (REVIEW)
PMID 11282417
 
Metabotropic glutamate receptor-1: a potential therapeutic target for the treatment of breast cancer.
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Breast Cancer Res Treat. 2012 Apr;132(2):565-73. doi: 10.1007/s10549-011-1624-x. Epub 2011 Jun 17.
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Citation

This paper should be referenced as such :
Sierra, J ; Chen, S
GRM1 (glutamate receptor, metabotropic 1)
Atlas Genet Cytogenet Oncol Haematol. 2014;18(4):224-228.
Free journal version : [ pdf ]   [ DOI ]
On line version : http://AtlasGeneticsOncology.org/Genes/GRM1ID43851ch6q24.html


External links

Nomenclature
HGNC (Hugo)GRM1   4593
Cards
AtlasGRM1ID43851ch6q24
Entrez_Gene (NCBI)GRM1  2911  glutamate metabotropic receptor 1
AliasesGPRC1A; MGLU1; MGLUR1; PPP1R85; 
SCAR13
GeneCards (Weizmann)GRM1
Ensembl hg19 (Hinxton)ENSG00000152822 [Gene_View]
Ensembl hg38 (Hinxton)ENSG00000152822 [Gene_View]  chr6:146029198-146437598 [Contig_View]  GRM1 [Vega]
ICGC DataPortalENSG00000152822
TCGA cBioPortalGRM1
AceView (NCBI)GRM1
Genatlas (Paris)GRM1
WikiGenes2911
SOURCE (Princeton)GRM1
Genetics Home Reference (NIH)GRM1
Genomic and cartography
GoldenPath hg38 (UCSC)GRM1  -     chr6:146029198-146437598 +  6q24.3   [Description]    (hg38-Dec_2013)
GoldenPath hg19 (UCSC)GRM1  -     6q24.3   [Description]    (hg19-Feb_2009)
EnsemblGRM1 - 6q24.3 [CytoView hg19]  GRM1 - 6q24.3 [CytoView hg38]
Mapping of homologs : NCBIGRM1 [Mapview hg19]  GRM1 [Mapview hg38]
OMIM604473   614831   
Gene and transcription
Genbank (Entrez)AB208837 AK308550 BC111844 BC136280 BC143777
RefSeq transcript (Entrez)NM_000838 NM_001114329 NM_001278064 NM_001278065 NM_001278066 NM_001278067
RefSeq genomic (Entrez)
Consensus coding sequences : CCDS (NCBI)GRM1
Cluster EST : UnigeneHs.32945 [ NCBI ]
CGAP (NCI)Hs.32945
Alternative Splicing GalleryENSG00000152822
Gene ExpressionGRM1 [ NCBI-GEO ]   GRM1 [ EBI - ARRAY_EXPRESS ]   GRM1 [ SEEK ]   GRM1 [ MEM ]
Gene Expression Viewer (FireBrowse)GRM1 [ Firebrowse - Broad ]
SOURCE (Princeton)Expression in : [Datasets]   [Normal Tissue Atlas]  [carcinoma Classsification]  [NCI60]
GenevisibleExpression in : [tissues]  [cell-lines]  [cancer]  [perturbations]  
BioGPS (Tissue expression)2911
GTEX Portal (Tissue expression)GRM1
Protein : pattern, domain, 3D structure
UniProt/SwissProtQ13255   [function]  [subcellular_location]  [family_and_domains]  [pathology_and_biotech]  [ptm_processing]  [expression]  [interaction]
NextProtQ13255  [Sequence]  [Exons]  [Medical]  [Publications]
With graphics : InterProQ13255
Splice isoforms : SwissVarQ13255
PhosPhoSitePlusQ13255
Domaine pattern : Prosite (Expaxy)G_PROTEIN_RECEP_F3_1 (PS00979)    G_PROTEIN_RECEP_F3_2 (PS00980)    G_PROTEIN_RECEP_F3_3 (PS00981)    G_PROTEIN_RECEP_F3_4 (PS50259)   
Domains : Interpro (EBI)ANF_lig-bd_rcpt    GPCR_3    GPCR_3_9-Cys_dom    GPCR_3_C    GPCR_3_CS    GPCR_3_mtglu_rcpt    GPCR_3_mtglu_rcpt_1    Metabotropic_Glu_rcpt_Homer-bd    Peripla_BP_I   
Domain families : Pfam (Sanger)7tm_3 (PF00003)    ANF_receptor (PF01094)    GluR_Homer-bdg (PF10606)    NCD3G (PF07562)   
Domain families : Pfam (NCBI)pfam00003    pfam01094    pfam10606    pfam07562   
Domain families : Smart (EMBL)GluR_Homer-bdg (SM01229)  
Conserved Domain (NCBI)GRM1
DMDM Disease mutations2911
Blocks (Seattle)GRM1
PDB (SRS)3KS9    4OR2   
PDB (PDBSum)3KS9    4OR2   
PDB (IMB)3KS9    4OR2   
PDB (RSDB)3KS9    4OR2   
Structural Biology KnowledgeBase3KS9    4OR2   
SCOP (Structural Classification of Proteins)3KS9    4OR2   
CATH (Classification of proteins structures)3KS9    4OR2   
SuperfamilyQ13255
Human Protein AtlasENSG00000152822
Peptide AtlasQ13255
HPRD05129
IPIIPI00012363   IPI00514867   IPI00184484   
Protein Interaction databases
DIP (DOE-UCLA)Q13255
IntAct (EBI)Q13255
FunCoupENSG00000152822
BioGRIDGRM1
STRING (EMBL)GRM1
ZODIACGRM1
Ontologies - Pathways
QuickGOQ13255
Ontology : AmiGOactivation of MAPKK activity  activation of MAPK activity  G-protein coupled receptor activity  protein binding  nucleus  plasma membrane  integral component of plasma membrane  G-protein coupled receptor signaling pathway  adenylate cyclase-inhibiting G-protein coupled glutamate receptor signaling pathway  G-protein coupled glutamate receptor signaling pathway  chemical synaptic transmission  locomotory behavior  glutamate receptor activity  glutamate receptor activity  postsynaptic density  sensory perception of pain  dendrite  G-protein coupled receptor dimeric complex  G-protein coupled receptor homodimeric complex  dimeric G-protein coupled receptor signaling pathway  presynaptic membrane  positive regulation of cytosolic calcium ion concentration involved in phospholipase C-activating G-protein coupled signaling pathway  regulation of sensory perception of pain  regulation of synaptic transmission, glutamatergic  cellular response to electrical stimulus  chemical synaptic transmission, postsynaptic  regulation of postsynaptic cytosolic calcium ion concentration  neurotransmitter receptor activity involved in regulation of postsynaptic cytosolic calcium ion concentration  
Ontology : EGO-EBIactivation of MAPKK activity  activation of MAPK activity  G-protein coupled receptor activity  protein binding  nucleus  plasma membrane  integral component of plasma membrane  G-protein coupled receptor signaling pathway  adenylate cyclase-inhibiting G-protein coupled glutamate receptor signaling pathway  G-protein coupled glutamate receptor signaling pathway  chemical synaptic transmission  locomotory behavior  glutamate receptor activity  glutamate receptor activity  postsynaptic density  sensory perception of pain  dendrite  G-protein coupled receptor dimeric complex  G-protein coupled receptor homodimeric complex  dimeric G-protein coupled receptor signaling pathway  presynaptic membrane  positive regulation of cytosolic calcium ion concentration involved in phospholipase C-activating G-protein coupled signaling pathway  regulation of sensory perception of pain  regulation of synaptic transmission, glutamatergic  cellular response to electrical stimulus  chemical synaptic transmission, postsynaptic  regulation of postsynaptic cytosolic calcium ion concentration  neurotransmitter receptor activity involved in regulation of postsynaptic cytosolic calcium ion concentration  
Pathways : BIOCARTARegulation of ck1/cdk5 by type 1 glutamate receptors [Genes]   
Pathways : KEGG   
REACTOMEQ13255 [protein]
REACTOME PathwaysR-HSA-6794361 [pathway]   
NDEx NetworkGRM1
Atlas of Cancer Signalling NetworkGRM1
Wikipedia pathwaysGRM1
Orthology - Evolution
OrthoDB2911
GeneTree (enSembl)ENSG00000152822
Phylogenetic Trees/Animal Genes : TreeFamGRM1
HOVERGENQ13255
HOGENOMQ13255
Homologs : HomoloGeneGRM1
Homology/Alignments : Family Browser (UCSC)GRM1
Gene fusions - Rearrangements
Fusion : MitelmanBCLAF1/GRM1 [6q23.3/6q24.3]  [inv(6)(q23q24)]  
Fusion : MitelmanCOL12A1/GRM1 [6q13/6q24.3]  [inv(6)(q13q24)]  
Fusion : MitelmanMEF2A/GRM1 [15q26.3/6q24.3]  [t(6;15)(q24;q25)]  
Fusion : MitelmanTBL1XR1/GRM1 [3q26.32/6q24.3]  [t(3;6)(q26;q24)]  
Polymorphisms : SNP and Copy number variants
NCBI Variation ViewerGRM1 [hg38]
dbSNP Single Nucleotide Polymorphism (NCBI)GRM1
dbVarGRM1
ClinVarGRM1
1000_GenomesGRM1 
Exome Variant ServerGRM1
ExAC (Exome Aggregation Consortium)GRM1 (select the gene name)
Genetic variants : HAPMAP2911
Genomic Variants (DGV)GRM1 [DGVbeta]
DECIPHERGRM1 [patients]   [syndromes]   [variants]   [genes]  
CONAN: Copy Number AnalysisGRM1 
Mutations
ICGC Data PortalGRM1 
TCGA Data PortalGRM1 
Broad Tumor PortalGRM1
OASIS PortalGRM1 [ Somatic mutations - Copy number]
Somatic Mutations in Cancer : COSMICGRM1  [overview]  [genome browser]  [tissue]  [distribution]  
Mutations and Diseases : HGMDGRM1
LOVD (Leiden Open Variation Database)Whole genome datasets
LOVD (Leiden Open Variation Database)LOVD - Leiden Open Variation Database
LOVD (Leiden Open Variation Database)LOVD 3.0 shared installation
BioMutasearch GRM1
DgiDB (Drug Gene Interaction Database)GRM1
DoCM (Curated mutations)GRM1 (select the gene name)
CIViC (Clinical Interpretations of Variants in Cancer)GRM1 (select a term)
intoGenGRM1
NCG5 (London)GRM1
Cancer3DGRM1(select the gene name)
Impact of mutations[PolyPhen2] [SIFT Human Coding SNP] [Buck Institute : MutDB] [Mutation Assessor] [Mutanalyser]
Diseases
OMIM604473    614831   
Orphanet21758    22932   
MedgenGRM1
Genetic Testing Registry GRM1
NextProtQ13255 [Medical]
TSGene2911
GENETestsGRM1
Target ValidationGRM1
Huge Navigator GRM1 [HugePedia]
snp3D : Map Gene to Disease2911
BioCentury BCIQGRM1
ClinGenGRM1
Clinical trials, drugs, therapy
Chemical/Protein Interactions : CTD2911
Chemical/Pharm GKB GenePA28990
Clinical trialGRM1
Miscellaneous
canSAR (ICR)GRM1 (select the gene name)
Probes
Litterature
PubMed113 Pubmed reference(s) in Entrez
GeneRIFsGene References Into Functions (Entrez)
CoreMineGRM1
EVEXGRM1
GoPubMedGRM1
iHOPGRM1
REVIEW articlesautomatic search in PubMed
Last year publicationsautomatic search in PubMed

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