Affinage

GPR37

Prosaposin receptor GPR37 · UniProt O15354

Length
613 aa
Mass
67.1 kDa
Annotated
2026-04-28
44 papers in source corpus 25 papers cited in narrative 25 extracted findings

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

GPR37 (Pael-R) is a brain-enriched orphan GPCR that functions at the intersection of protein quality control and neuroprotective signaling, with roles spanning dopaminergic neuron survival, pain modulation, cell migration, and macrophage efferocytosis. Misfolded GPR37 accumulates in the ER and triggers ER stress-mediated death selectively in dopaminergic neurons; this toxicity is counteracted by Parkin-mediated ubiquitination and proteasomal degradation, and by the ER-resident E3 ligase HRD1 (PMID:12150907, PMID:12670421, PMID:17059562). Properly folded, surface-delivered GPR37 is activated by prosaposin/prosaptide, coupling through Gi/o to inhibit cAMP, activate ERK, and protect astrocytes from oxidative stress (PMID:23690594). GPR37 knockout mice display reduced striatal dopamine, altered vulnerability to dopaminergic neurotoxins, impaired GnRH neuron migration, and attenuated adenosine A2A receptor-mediated modulation of parkinsonian tremor (PMID:17889953, PMID:31143101, PMID:25862943).

Mechanistic history

Synthesis pass · year-by-year structured walk · 10 steps
  1. 1997 High

    Cloning of GPR37 established it as a novel brain-enriched seven-transmembrane orphan GPCR without identifiable endogenous ligands or classical second-messenger coupling, setting the stage for functional deorphanization.

    Evidence cDNA cloning with Northern blot, in situ hybridization, radioligand binding, and Ca²⁺/cAMP assays in COS7/HEK293 cells

    PMID:9144577

    Open questions at the time
    • No ligand identified
    • No signaling pathway activated in initial assays
    • Physiological role unknown
  2. 2002 High

    Identification of GPR37 as a Parkin substrate linked receptor misfolding and ER stress to dopaminergic cell death, providing a direct molecular connection between GPR37 accumulation and Parkinson's disease-related neurodegeneration.

    Evidence Yeast two-hybrid, co-immunoprecipitation, ubiquitination assays, cell death rescue by Parkin; CHIP–Hsp70 complex facilitation of Parkin-mediated Pael-R ubiquitination

    PMID:12150907 PMID:14579121

    Open questions at the time
    • Whether endogenous levels of GPR37 (not overexpressed) cause toxicity in neurons
    • Mechanism by which GPR37 misfolding is sensed
  3. 2003 High

    In vivo Drosophila and mouse models demonstrated that GPR37 accumulation selectively kills dopaminergic neurons in a Parkin-dependent manner, validating the Parkin–Pael-R axis in an organismal context and establishing cell-type selectivity of toxicity.

    Evidence Drosophila transgenic/genetic epistasis with dopaminergic neuron counting; Pael-R localization to Lewy body cores in human PD brain

    PMID:12670421 PMID:14991825

    Open questions at the time
    • Molecular basis for selective vulnerability of dopaminergic neurons
    • Whether Lewy body accumulation is cause or consequence
  4. 2006 High

    Discovery that the ER-resident E3 ligase HRD1 independently ubiquitinates and degrades GPR37 revealed a second quality-control pathway (ERAD) beyond Parkin, and mouse models confirmed that ER stress and dopamine synthesis both contribute to GPR37-induced neurodegeneration.

    Evidence Co-IP, ubiquitination assay, siRNA knockdown of HRD1 with caspase-3 activation; in vivo adenoviral overexpression in Parkin-KO and ORP150-KO mice with dopamine synthesis inhibitor rescue

    PMID:17059562 PMID:17116640

    Open questions at the time
    • Relative contribution of HRD1 vs. Parkin to endogenous GPR37 turnover
    • Whether dopamine metabolites directly modify GPR37
  5. 2007 High

    Bidirectional genetic manipulation in mice established GPR37 as a physiological regulator of striatal dopamine metabolism, moving the gene's role beyond a pure toxicity substrate to a functional modulator of the nigrostriatal system.

    Evidence GPR37 knockout and transgenic mice with HPLC dopamine/DOPAC measurement and neurotoxin challenge

    PMID:17889953

    Open questions at the time
    • Signaling pathway linking GPR37 to dopamine synthesis or release
    • Receptor activation state of endogenous GPR37 in these models
  6. 2009 High

    Dissection of GPR37 trafficking determinants revealed that the N-terminal ectodomain retains the receptor intracellularly, while co-expression with D2R or A2AR or the PDZ scaffold syntenin-1 rescues surface delivery, establishing GPR37 as a trafficking-regulated receptor whose functional availability depends on interaction partners.

    Evidence N-terminal truncation, FACS surface expression, co-immunoprecipitation with D2R/A2AR, syntenin-1 interaction

    PMID:19799451

    Open questions at the time
    • Whether N-terminal cleavage occurs endogenously
    • Stoichiometry and in vivo relevance of GPR37–D2R heteromers
  7. 2013 High

    Deorphanization of GPR37 by prosaposin/prosaptide established it as a Gi/o-coupled receptor that inhibits cAMP, activates ERK, and protects astrocytes from oxidative stress, transforming understanding from a passive toxicity substrate to an active signaling receptor.

    Evidence Endocytosis assay, ligand binding, ERK phosphorylation, GTPγS binding, cAMP assay, pertussis toxin sensitivity, siRNA knockdown, oxidative stress protection in primary astrocytes

    PMID:23690594

    Open questions at the time
    • Whether prosaposin is the primary endogenous ligand in vivo
    • Structural basis of ligand–receptor interaction
  8. 2013 Medium

    The C-terminal cysteine-rich domain was identified as a negative regulator of GPR37 surface expression and a determinant of receptor-mediated apoptosis, and additional C-terminal interactors PICK1 and GABARAPL2 were shown to modulate GPR37 levels.

    Evidence Cysteine mutagenesis with flow cytometry and apoptosis assay; GST pulldown with PICK1 and GABARAPL2; cell death rescue by PICK1 overexpression

    PMID:23398388 PMID:24749734 PMID:29496607

    Open questions at the time
    • Whether GABARAPL2 mediates autophagic degradation of GPR37 in neurons
    • Functional interplay between C-terminal partners
    • GABARAPL2 interaction confirmed by only a single pulldown method
  9. 2015 Medium

    GPR37 was shown to be required for A2A receptor-mediated modulation of parkinsonian tremor, establishing a functional epistatic relationship between GPR37 and adenosine signaling in motor circuits.

    Evidence GPR37 KO mice with pilocarpine-induced tremulous jaw movements and pharmacological A2A receptor manipulation

    PMID:25862943

    Open questions at the time
    • Whether GPR37–A2AR heteromerization is necessary for the behavioral phenotype
    • Downstream signaling mediating the interaction
  10. 2019 Medium

    GPR37 was found to regulate GnRH neuron and olfactory ensheathing cell migration during development, extending its physiological roles beyond dopaminergic circuits to developmental neurobiology.

    Evidence Nasal explant pharmacological inhibition and GPR37 KO mouse analysis of GnRH neuron migration and olfactory bulb innervation

    PMID:31143101

    Open questions at the time
    • Ligand activating GPR37 during GnRH neuron migration
    • Downstream effectors of GPR37 in migrating cells

Open questions

Synthesis pass · forward-looking unresolved questions
  • Key unresolved questions include the identity of the primary endogenous ligand(s) in vivo, the structural basis of GPR37 activation, whether GPR37 functions primarily as a monomer or in heteromeric complexes in native tissue, and the mechanism by which GPR37 signaling modulates dopamine metabolism.
  • No solved receptor structure
  • No consensus on primary endogenous ligand in brain
  • Mechanism linking GPR37 signaling to dopamine synthesis/release undefined

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0060089 molecular transducer activity 2 GO:0098772 molecular function regulator activity 2
Localization
GO:0005886 plasma membrane 3 GO:0005783 endoplasmic reticulum 2 GO:0005634 nucleus 1
Pathway
R-HSA-1643685 Disease 3 R-HSA-5357801 Programmed Cell Death 3 R-HSA-112316 Neuronal System 2 R-HSA-162582 Signal Transduction 2 R-HSA-392499 Metabolism of proteins 2
Partners
ADORA2ADRD2GABARAPL2HRD1PICK1PRKNSDCBPSTUB1

Evidence

Reading pass · 25 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
1997 GPR37 (hETBR-LP) was cloned as a novel 614-amino acid, seven-transmembrane domain GPCR enriched in the brain, particularly in Purkinje cells and hippocampal neurons; recombinant expression confirmed it did not bind ET-1, ET-3, bombesin, or neuropeptide Y, nor did it mobilize Ca2+ or alter cAMP, establishing it as an orphan receptor. cDNA cloning, Northern blot, in situ hybridization, radioligand binding assay, Ca2+/cAMP functional assays in COS7 and HEK293 cells Biochemical and biophysical research communications High 9144577
2002 GPR37/Pael-R was identified as a substrate of the E3 ubiquitin ligase Parkin via yeast two-hybrid; when overexpressed in cells, Pael-R becomes unfolded, insoluble, and ubiquitinated, accumulates in the ER, and induces ER stress-induced cell death that is suppressed by Parkin-mediated ubiquitination and degradation. Yeast two-hybrid, co-immunoprecipitation, ubiquitination assay, cell death assay Molecular cell High 12150907 14579121
2002 CHIP forms a complex with Hsp70, Parkin, and Pael-R in vitro and in vivo; CHIP promotes dissociation of Hsp70 from Parkin and Pael-R, thereby facilitating Parkin-mediated ubiquitination of Pael-R and enhancing Parkin's ability to suppress Pael-R-induced cell death. Co-immunoprecipitation (in vitro and in vivo), in vitro ubiquitination assay, cell death assay Molecular cell High 12150907
2003 Panneuronal expression of Pael-R in Drosophila caused age-dependent selective degeneration of dopaminergic neurons; co-expression of Parkin degraded Pael-R and suppressed its toxicity, while interfering with endogenous Drosophila Parkin promoted Pael-R accumulation and augmented toxicity, placing Parkin downstream of Pael-R accumulation in dopaminergic neurodegeneration. Drosophila transgenic expression, genetic epistasis, dopaminergic neuron counting Neuron High 12670421
2003 Pael-R, Parkin, alpha-synuclein, and ubiquitin were found to accumulate in Lewy bodies of Parkinson's disease patients, with Pael-R localized to the core of Lewy bodies. Immunohistochemistry on post-mortem human brain tissue (Parkinson's disease and MSA cases) Annals of neurology Medium 14991825
2003 Glup/PACRG, encoded by a gene adjacent to Parkin, forms a large molecular chaperone complex (containing Hsp70, Hsp90, and chaperonin components) that associates with Pael-R, suppresses Pael-R-induced cell death, and facilitates inclusion body formation when the proteasome is inhibited. Co-immunoprecipitation, protein complex isolation, cell death assay, siRNA knockdown, immunofluorescence The Journal of biological chemistry Medium 14532270
2006 HRD1, an ER-resident ubiquitin ligase, interacts with Pael-R through its proline-rich domain, promotes Pael-R ubiquitination and degradation, and siRNA-mediated knockdown of HRD1 causes Pael-R accumulation and caspase-3 activation; ATF6 overexpression induces HRD1 and accelerates Pael-R degradation. Co-immunoprecipitation, ubiquitination assay, siRNA knockdown, caspase-3 activation measurement Journal of neurochemistry High 17059562
2006 Adenoviral vector-mediated overexpression of Pael-R in the substantia nigra of mice induced ER stress and selective death of dopaminergic neurons; this neurodegeneration was enhanced in mice deficient in Parkin or the ER chaperone ORP150, and was partially blocked by a dopamine synthesis inhibitor. In vivo adenoviral vector injection, Parkin/ORP150 knockout mice, dopaminergic neuron counting, pharmacological inhibition Human molecular genetics High 17116640
2007 Pael-R knockout mice showed ~40% reduction in striatal dopamine, while Pael-R transgenic mice showed increased striatal DOPAC and vesicular dopamine content; Pael-R transgenic nigrostriatal neurons were more vulnerable and knockout neurons less vulnerable to PD-related neurotoxins, establishing GPR37 as a regulator of dopamine metabolism in the nigrostriatal system. Pael-R knockout and transgenic mouse models, HPLC dopamine measurement, neurotoxin challenge Neuroscience research High 17889953
2007 Drosophila thioredoxin (TRX), acting primarily as a molecular chaperone, suppressed Pael-R-induced dopaminergic neurotoxicity; redox-defective TRX mutants retained chaperone activity and still partially suppressed Pael-R toxicity, indicating chaperone (not antioxidant) activity is the primary mechanism of suppression. Drosophila co-expression, site-directed mutagenesis of TRX, dopaminergic neuron counting, locomotor assay The Journal of biological chemistry Medium 17301052
2008 HRD1's proline-rich domain is necessary to promote Pael-R degradation, while its transmembrane domain is required for transferring Pael-R from the ER to the cytosol for proteasomal degradation; a transmembrane-domain mutant of HRD1 was markedly unstable. Domain deletion/mutagenesis of HRD1, co-immunoprecipitation, degradation assay Journal of pharmacological sciences Medium 18344614
2008 Parkin knockout/Pael-R transgenic double mice exhibited progressive and selective loss of dopaminergic and noradrenergic neurons without inclusion body formation, with persistent unfolded protein response activation, elevated dopamine/metabolites, and later reduction in mitochondrial complex I activity. Double transgenic/knockout mouse model, catecholaminergic neuron counting, UPR markers, mitochondrial complex I activity assay Journal of neurochemistry High 18691389
2009 GPR37 surface expression is dramatically enhanced by removal of its N-terminal domain (first ~210 amino acids); coexpression with adenosine A2A receptor or dopamine D2 receptor increases GPR37 surface expression, with co-immunoprecipitation confirming GPR37-D2R physical association that modestly alters D2R agonist/antagonist affinity; interaction with the PDZ scaffold syntenin-1 also dramatically increases GPR37 surface expression. N-terminal truncation, co-immunoprecipitation, FACS surface expression, radioligand binding Biochemistry High 19799451
2009 rAAV2/6-mediated overexpression of Pael-R in the rat nigrostriatal system caused rapid insoluble accumulation of Pael-R, severe and selective loss of nigral dopaminergic neurons and nigrostriatal fibers, striatal dopamine depletion, and spontaneous motor impairments; GABAergic neurons of the globus pallidus were unaffected, demonstrating selective vulnerability of nigral dopaminergic neurons to Pael-R accumulation. In vivo AAV vector injection in rats, immunohistochemistry, HPLC dopamine measurement, behavioral testing Neurobiology of disease High 19348945
2013 Prosaptide (the active fragment of prosaposin) and full-length prosaposin activate GPR37 signaling: prosaptide promoted GPR37 endocytosis, bound to GPR37, stimulated ERK phosphorylation in a pertussis toxin-sensitive manner, stimulated 35S-GTPγS binding, and inhibited forskolin-stimulated cAMP production; prosaposin/prosaptide protected primary astrocytes against oxidative stress in a GPR37-dependent manner (attenuated by GPR37 siRNA knockdown), identifying prosaposin/prosaptide as GPR37 ligands. GPCR endocytosis assay, ligand binding, ERK phosphorylation assay, 35S-GTPγS binding, cAMP assay, pertussis toxin treatment, siRNA knockdown, oxidative stress protection assay Proceedings of the National Academy of Sciences of the United States of America High 23690594
2013 The C-terminal cysteine-rich domain of GPR37 controls receptor plasma membrane expression and function: deletion of six cysteines in this region promoted plasma membrane expression and signaling, while removal of the C-terminal cysteine-rich domain protected against GPR37-mediated apoptosis and cell death. Site-directed mutagenesis, flow cytometry surface expression, signaling assay, apoptosis/cell death assay Journal of neurochemistry Medium 23398388
2014 PICK1 interacts with GPR37/PAELR via its PDZ domain binding the C-terminal PDZ motif of PAELR; pulldown with GST-ct-PAELR retained recombinant and native PICK1 from rat brain; PICK1 overexpression reduced PAELR expression and attenuated PAELR-induced cell death during rotenone treatment in a proteasome-dependent manner. GST pulldown, co-immunoprecipitation, cell death assay, proteasome inhibitor treatment Journal of neurochemistry Medium 24749734
2015 Deletion of GPR37 attenuated pilocarpine-induced tremulous jaw movements (a model of parkinsonian tremor), and the ability of adenosine A2A receptor activation to control tremulous jaw movements was lost in GPR37-null mice, indicating that A2A receptor-mediated modulation of parkinsonian tremor requires GPR37. GPR37 knockout mice, behavioral tremulous jaw movement assay, pharmacological A2A receptor manipulation Behavioural brain research Medium 25862943
2018 GABARAPL2 interacts with the cysteine-rich region (-CCCCCC-EEC) of GPR37's C-terminal tail; affinity chromatography showed Myc-tagged GABARAPL2 was retained by GST-ct-PAELR; transient transfection of GABARAPL2 in HEK293 cells reduced PAELR expression, suggesting autophagy-mediated regulation of GPR37 levels. Affinity chromatography (GST pulldown), in-silico modelling, transient transfection, Western blot Neuroscience letters Low 29496607
2019 GPR37 is expressed in migrating GnRH neurons and olfactory ensheathing cells (OECs); pharmacological inhibition of GPR37 signaling in nasal explants attenuated GnRH neuronal migration and OEC movement; GPR37-deficient mice showed decreased olfactory bulb nerve layer and attenuated/delayed GnRH neuron maturation and migration into the brain. PCR, immunocytochemistry, nasal explant inhibition assay, GPR37 knockout mouse analysis Frontiers in cellular neuroscience Medium 31143101
2024 Osteocalcin (OCN), a bone-derived protein, activates GPR37 in a subpopulation of VTA GABAergic neurons to decrease potassium currents via cAMP reduction and subsequent THIK-1 (K2P13.1) channel suppression, increasing neuronal excitability and priming rapid visual escape; GPR37 KO and conditional GPR37 KO in VTA GABAergic neurons delayed escape, and reconstituting OCN-GPR37 signaling in VTA restored normal response. Knockout mice, conditional knockout, single-cell transcriptomics, electrophysiology, chemogenetics, ex vivo calcium imaging bioRxivpreprint Medium bio_10.1101_2024.08.12.607510
2024 GPR37 mediates the analgesic and pro-resolving effects of protectin DX (PDX) in macrophages: PDX binds GPR37 and induces calcium responses in peritoneal macrophages, promotes GPR37-dependent macrophage phagocytosis and efferocytosis, and GPR37 KO mice showed deficits in fracture-induced postoperative pain resolution and abolished PDX analgesia. Gpr37 knockout mice, ligand binding assay, calcium imaging in macrophages, efferocytosis assay, behavioral pain assay, lipidomics bioRxivpreprint Medium bio_10.1101_2025.11.10.687700
2024 GPR37 contains endogenous ligands present in brain extracts, as detected using the GzESTY cell-based Gi/o/z signaling assay, supporting ongoing deorphanization of GPR37. Cell-based GPCR signaling assay (GzESTY) with brain extract stimulation bioRxivpreprint Low bio_10.1101_2024.07.26.605282
2025 Intrathecal activation of spinal GPR37 by agonists TX14A and protectin D1 dose-dependently inhibited capsaicin-induced long-term increase in nociception and produced an 'unpriming' effect in the hyperalgesic priming model; global GPR37 knockout abolished these long-term effects; ex vivo Ca2+ imaging showed i.th. TX14A rescued dorsal horn interneurons from long-term potentiation/depression, suggesting GPR37 agonism erases spinal pain memory. Intrathecal drug administration, GPR37 knockout mice, behavioral pain assays, ex vivo Ca2+ imaging of spinal dorsal horn bioRxivpreprint Medium bio_10.1101_2025.11.25.690482
2025 Protectin D1 (PD1) attenuates abdominal aortic aneurysm progression in a GPR37-dependent manner in macrophages: PD1 enhanced macrophage efferocytosis of apoptotic vascular smooth muscle cells via GPR37-dependent calcium signaling and reduced macrophage-derived TNF-α and IL-1β; GPR37-dependent effects were confirmed in isolated macrophages and murine AAA models. Murine AAA models (elastase+BAPN), GPR37 knockout mice, macrophage efferocytosis assay, calcium signaling, scRNA-seq, cytokine measurement bioRxivpreprint Medium bio_10.1101_2025.10.20.683538

Source papers

Stage 0 corpus · 44 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2002 CHIP is associated with Parkin, a gene responsible for familial Parkinson's disease, and enhances its ubiquitin ligase activity. Molecular cell 404 12150907
2003 Parkin suppresses dopaminergic neuron-selective neurotoxicity induced by Pael-R in Drosophila. Neuron 301 12670421
2003 Parkin facilitates the elimination of expanded polyglutamine proteins and leads to preservation of proteasome function. The Journal of biological chemistry 231 12676955
2013 GPR37 and GPR37L1 are receptors for the neuroprotective and glioprotective factors prosaptide and prosaposin. Proceedings of the National Academy of Sciences of the United States of America 191 23690594
2006 Suppressive effects of 4-phenylbutyrate on the aggregation of Pael receptors and endoplasmic reticulum stress. Journal of neurochemistry 150 16539653
2004 Pael-R is accumulated in Lewy bodies of Parkinson's disease. Annals of neurology 125 14991825
2013 Pathway Analysis of ChIP-Seq-Based NRF1 Target Genes Suggests a Logical Hypothesis of their Involvement in the Pathogenesis of Neurodegenerative Diseases. Gene regulation and systems biology 115 24250222
2009 Identification of a novel Zn2+-binding domain in the autosomal recessive juvenile Parkinson-related E3 ligase parkin. The Journal of biological chemistry 109 19339245
2013 Endoplasmic reticulum stress and Parkinson's disease: the role of HRD1 in averting apoptosis in neurodegenerative disease. Oxidative medicine and cellular longevity 102 23710284
2003 Parkin: a multipurpose neuroprotective agent? Neuron 92 12691660
2006 Pael receptor induces death of dopaminergic neurons in the substantia nigra via endoplasmic reticulum stress and dopamine toxicity, which is enhanced under condition of parkin inactivation. Human molecular genetics 89 17116640
2006 A ubiquitin ligase HRD1 promotes the degradation of Pael receptor, a substrate of Parkin. Journal of neurochemistry 78 17059562
2012 Protective effects of 4-phenylbutyrate derivatives on the neuronal cell death and endoplasmic reticulum stress. Biological & pharmaceutical bulletin 67 22223342
2009 GPR37 surface expression enhancement via N-terminal truncation or protein-protein interactions. Biochemistry 59 19799451
2003 A product of the human gene adjacent to parkin is a component of Lewy bodies and suppresses Pael receptor-induced cell death. The Journal of biological chemistry 59 14532270
1997 A novel endothelin receptor type-B-like gene enriched in the brain. Biochemical and biophysical research communications 57 9144577
2003 Pael receptor, endoplasmic reticulum stress, and Parkinson's disease. Journal of neurology 55 14579121
2012 Mutation in Parkinson disease-associated, G-protein-coupled receptor 37 (GPR37/PaelR) is related to autism spectrum disorder. PloS one 48 23251443
2009 Targeted overexpression of the parkin substrate Pael-R in the nigrostriatal system of adult rats to model Parkinson's disease. Neurobiology of disease 48 19348945
2008 Pael-R transgenic mice crossed with parkin deficient mice displayed progressive and selective catecholaminergic neuronal loss. Journal of neurochemistry 48 18691389
2020 TGF-β/Smad3 Signalling Modulates GABA Neurotransmission: Implications in Parkinson's Disease. International journal of molecular sciences 43 31963327
2015 Drug Discovery Opportunities at the Endothelin B Receptor-Related Orphan G Protein-Coupled Receptors, GPR37 and GPR37L1. Frontiers in pharmacology 41 26635605
2007 Pael receptor is involved in dopamine metabolism in the nigrostriatal system. Neuroscience research 39 17889953
2008 Novel functions of ubiquitin ligase HRD1 with transmembrane and proline-rich domains. Journal of pharmacological sciences 35 18344614
2007 Thioredoxin suppresses Parkin-associated endothelin receptor-like receptor-induced neurotoxicity and extends longevity in Drosophila. The Journal of biological chemistry 35 17301052
2008 Immunohistochemical localization of a ubiquitin ligase HRD1 in murine brain. Journal of neuroscience research 34 18241051
2013 The Parkinson's disease-associated GPR37 receptor-mediated cytotoxicity is controlled by its intracellular cysteine-rich domain. Journal of neurochemistry 30 23398388
2017 Folding Underlies Bidirectional Role of GPR37/Pael-R in Parkinson Disease. Trends in pharmacological sciences 28 28629580
2014 A low level of GPR37 is associated with human hepatocellular carcinoma progression and poor patient survival. Pathology, research and practice 28 25169131
2016 Neuroprotection by Endoplasmic Reticulum Stress-Induced HRD1 and Chaperones: Possible Therapeutic Targets for Alzheimer's and Parkinson's Disease. Medical sciences (Basel, Switzerland) 19 29083378
2015 Adenosine A2A receptor-mediated control of pilocarpine-induced tremulous jaw movements is Parkinson's disease-associated GPR37 receptor-dependent. Behavioural brain research 17 25862943
2019 GPR37 Signaling Modulates Migration of Olfactory Ensheathing Cells and Gonadotropin Releasing Hormone Cells in Mice. Frontiers in cellular neuroscience 12 31143101
2012 [Molecular pharmacological studies on the protection mechanism against endoplasmic reticulum stress-induced neurodegenerative disease]. Yakugaku zasshi : Journal of the Pharmaceutical Society of Japan 12 23208051
2014 The protein interacting with C-kinase (PICK1) interacts with and attenuates parkin-associated endothelial-like (PAEL) receptor-mediated cell death. Journal of neurochemistry 11 24749734
2016 [Physiological Roles of Ubiquitin Ligases Related to the Endoplasmic Reticulum]. Yakugaku zasshi : Journal of the Pharmaceutical Society of Japan 8 27252059
2018 A novel modelling mechanism of PAEL receptor and GABARAPL2 interaction involved in Parkinson's disease. Neuroscience letters 7 29496607
2014 [Pharmacological studies on neurodegenerative diseases focusing on refolding and degradation of unfolded proteins in the endoplasmic reticulum]. Yakugaku zasshi : Journal of the Pharmaceutical Society of Japan 7 24694815
2012 Downregulation of Pael-R expression in a Parkinson's disease cell model reduces apoptosis. Journal of clinical neuroscience : official journal of the Neurosurgical Society of Australasia 6 22898202
2024 5-Phenyl valeric acid attenuates α-synuclein aggregation and endoplasmic reticulum stress in rotenone-induced Parkinson's disease rats: A molecular mechanistic study. Biochemical pharmacology 4 38852645
2004 [Protective effects of HRD1 and 4-phenylbutyric acid against neuronal cell death]. Nihon yakurigaku zasshi. Folia pharmacologica Japonica 4 15572843
2006 Cloning and developmental expression of a chick G-protein-coupled receptor SCGPR1. Gene expression patterns : GEP 3 17251065
2004 [Neurodegeneration caused by ER stress?--the pathogenetic mechanisms underlying AR-JP]. Nihon yakurigaku zasshi. Folia pharmacologica Japonica 2 15572841
2014 The Pael-R gene does not mediate the changes in rotenone-induced Parkinson's disease model cells. Neural regeneration research 1 25206827
2007 [Animal models for familial Parkinson's disease]. Rinsho shinkeigaku = Clinical neurology 0 18210841