Affinage

ADGRE2

Adhesion G protein-coupled receptor E2 · UniProt Q9UHX3

Length
823 aa
Mass
90.5 kDa
Annotated
2026-04-28
37 papers in source corpus 19 papers cited in narrative 19 extracted findings

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

ADGRE2 (EMR2) is a myeloid-restricted adhesion G protein-coupled receptor that transduces mechanical and ligand-dependent signals to drive innate immune cell activation, mast cell degranulation, and leukemic stem cell maintenance. The receptor undergoes autocatalytic cis-proteolysis at the GPS/GAIN domain in the ER, generating noncovalently associated extracellular (NTF) and seven-transmembrane (CTF) subunits whose ligation-induced redistribution into lipid rafts initiates Gα16/Gαz-coupled signaling through PLC-β, Akt, MAPK, and NF-κB, promoting neutrophil activation, macrophage cytokine production, and NLRP3 inflammasome priming (PMID:22310662, PMID:28421075, PMID:33488598, PMID:31969668). The NTF binds chondroitin sulfate and dermatan sulfate glycosaminoglycans via its fourth EGF-like domain in a Ca²⁺- and sulfation-dependent manner, mediating cell–cell and cell–matrix adhesion (PMID:12829604, PMID:15693006). The p.C492Y missense variant destabilizes subunit interaction and causes familial vibratory urticaria by sensitizing mast cells to vibration-induced degranulation (PMID:26841242). In acute myeloid leukemia, ADGRE2 activates a PLCβ/PKC/MEK/ERK/AP1 axis that upregulates DUSP1, maintaining proteostasis in leukemic stem cells through DNAJB1–HSP70 co-chaperone regulation (PMID:39082681).

Mechanistic history

Synthesis pass · year-by-year structured walk · 13 steps
  1. 2000 High

    Identification of EMR2 as a novel EGF-TM7 family GPCR with myeloid-restricted expression established the receptor as distinct from the related CD97 and defined its lineage specificity.

    Evidence Genomic cloning, splice analysis, mAb binding, and flow cytometry on primary leukocytes

    PMID:10903844

    Open questions at the time
    • No ligand identified
    • No signaling mechanism defined
    • Functional role in myeloid cells unknown
  2. 2002 High

    Demonstration that EMR2 exists as a heterodimeric receptor with an extracellular α-subunit and a TM β-subunit resolved its biochemical architecture and refined its expression to CD16+ monocytes and myeloid DCs.

    Evidence Monoclonal antibody immunoprecipitation and flow cytometry across primary blood cell populations

    PMID:11994511

    Open questions at the time
    • Mechanism of heterodimer formation unknown
    • Subunit stoichiometry not addressed
  3. 2003 High

    Identification of chondroitin sulfate GAGs as the ligand for the fourth EGF-like domain and mapping of the GPS cleavage site to Leu517↓Ser518 established the receptor's extracellular recognition mechanism and its autoproteolytic processing requirements.

    Evidence Multivalent probes on mutant CHO cells defective in GAG synthesis; site-directed mutagenesis and cell-free cleavage assays

    PMID:12829604 PMID:12860403

    Open questions at the time
    • Whether GPS cleavage is required for signaling not tested
    • In vivo GAG ligand identity unconfirmed
  4. 2004 High

    Establishing that GPS cleavage is an autocatalytic intramolecular cis-proteolysis occurring in the ER with N-terminal nucleophile hydrolase-like chemistry defined the biogenesis mechanism of the two-subunit receptor.

    Evidence Site-directed mutagenesis of catalytic residues (His, Ser518), cell-free spontaneous hydrolysis, ER localization analysis

    PMID:15150276

    Open questions at the time
    • Structural basis of autocatalysis not resolved at atomic level
    • Whether all splice isoforms are equally processed unclear
  5. 2006 Medium

    Showing that EMR2 expression is dynamically regulated during myeloid differentiation—up by LPS and IL-10 in macrophages, down during DC maturation—placed the receptor within innate immune activation programs.

    Evidence Flow cytometry, ELISA, mAb isoform detection, and siRNA/inhibitor dissection of LPS/IL-10 signaling in primary monocytes and macrophages

    PMID:17174274

    Open questions at the time
    • Transcription factors controlling ADGRE2 expression not identified
    • Functional consequence of isoform switching not tested
  6. 2007 High

    Demonstrating that EMR2 ligation on neutrophils enhances adhesion, migration, superoxide production, and degranulation—with requirement for the transmembrane domain—established the receptor as a functional activator of innate effector responses.

    Evidence Anti-EMR2 antibody ligation with superoxide/degranulation assays, live-cell imaging of translocation to membrane ruffles, dominant-negative TM constructs

    PMID:17928360

    Open questions at the time
    • Downstream G protein identity not determined
    • Physiological ligand triggering in vivo not shown
  7. 2012 High

    Resolution of two distinct post-cleavage receptor complexes—noncovalent heterodimer and independent subunits—and their differential lipid-raft distribution revealed that ligation-induced raft coalescence is the proximal signaling event driving macrophage cytokine production.

    Evidence Lipid raft fractionation, co-immunoprecipitation, GPS mutant constructs, and cytokine ELISA after antibody ligation

    PMID:22310662

    Open questions at the time
    • How raft translocation activates specific G proteins unresolved
    • Relative contribution of heterodimer vs. independent subunits to signaling unclear
  8. 2016 High

    Discovery that p.C492Y destabilizes NTF–CTF interaction and causes familial vibratory urticaria linked mechanical force sensing to subunit dissociation as the activation mechanism and established the first Mendelian disease for an adhesion GPCR.

    Evidence Co-segregation in two kindreds, biochemical subunit interaction assays, vibration-induced mast cell degranulation

    PMID:26841242

    Open questions at the time
    • Structural consequence of C492Y at atomic resolution unknown
    • Whether other destabilizing variants cause related phenotypes untested
  9. 2017 High

    Identification of Gα16 as the coupling partner initiating a PLC-β/Akt/ERK/JNK/NF-κB signaling cascade upon EMR2 activation resolved the G protein identity and downstream pathway architecture in monocytes.

    Evidence siRNA knockdown of Gα16, specific inhibitors of PLC-β/Akt/ERK/JNK/NF-κB, ELISA for IL-8/TNF-α/MMP-9 in THP-1 cells

    PMID:28421075

    Open questions at the time
    • Whether Gα16 is the sole coupling partner in all myeloid lineages unclear
    • Direct Gα16–receptor interaction not shown biochemically
  10. 2020 High

    Comprehensive G protein coupling profiling revealed broad coupling to Gα16, Gα12/13, Gα14, and Gαz, while pharmacological dissection of vibration-stimulated mast cells mapped degranulation to PLC/Ca²⁺/PKC/PI3K plus pertussis-toxin-sensitive signals, defining the full signaling repertoire.

    Evidence Yeast chimeric G protein coupling assay, mammalian cAMP/IP1 assays, Ca²⁺ imaging and pharmacological inhibitor panel in primary mast cells

    PMID:31969668 PMID:32222457

    Open questions at the time
    • Gβγ subunit composition not identified
    • Whether mechanical vs. ligand-mediated activation engages identical G protein sets untested
  11. 2021 High

    Showing that EMR2 provides the second activation signal for NLRP3 inflammasome assembly via Gα16–PLCβ–dependent K⁺ efflux and Ca²⁺ mobilization extended the receptor's role to inflammasome biology.

    Evidence Anti-EMR2 mAb ligation, Gα16/PLCβ siRNA, K⁺ efflux measurement, NLRP3 activation assays in THP-1 and primary monocytes

    PMID:33488598

    Open questions at the time
    • Whether EMR2 is required for NLRP3 activation in vivo not tested
    • Relative contribution vs. other pattern-recognition receptors unknown
  12. 2024 High

    In AML, ADGRE2 was shown to sustain leukemic stem cell proteostasis through a PLCβ/PKC/MEK/ERK/AP1 axis that transcriptionally upregulates DUSP1, which in turn dephosphorylates DNAJB1 to enable HSP70 co-chaperone function, revealing a non-immune pro-survival role.

    Evidence ADGRE2 silencing in AML lines and patient-derived cells, xenograft models, ChIP-seq/RNA-seq, DUSP1 phosphorylation and co-IP of DNAJB1–HSP70

    PMID:39082681

    Open questions at the time
    • Whether ADGRE2 ligand in bone marrow niche is identified
    • Relevance to non-AML malignancies not explored
    • Structural basis for selective AP1 target gene activation unknown
  13. 2024 Medium

    Identification of GNA15 (Gα15) as a direct physical interactor at the ADGRE2 intracellular segment that promotes leukemia cell proliferation via ERK/JNK/p38 provided additional evidence for G protein coupling in a disease context.

    Evidence Co-immunoprecipitation, BrdU proliferation assay, GNA15 siRNA knockdown, phospho-Western blotting

    PMID:39656442

    Open questions at the time
    • Reciprocal IP not reported
    • Whether Gα15 and Gα16 are redundant or additive in leukemia signaling unclear

Open questions

Synthesis pass · forward-looking unresolved questions
  • The endogenous ligand hierarchy in vivo, the structural basis of force-induced NTF–CTF dissociation, and whether ADGRE2 represents a therapeutic target in AML remain unresolved.
  • No cryo-EM or crystal structure of full-length receptor or GAIN domain
  • In vivo genetic loss-of-function studies in conditional knockout mice not reported
  • Therapeutic targeting in AML not validated in clinical studies

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0060089 molecular transducer activity 6 GO:0098772 molecular function regulator activity 4
Localization
GO:0005886 plasma membrane 4 GO:0005576 extracellular region 3 GO:0005783 endoplasmic reticulum 1
Pathway
R-HSA-162582 Signal Transduction 6 R-HSA-1643685 Disease 3 R-HSA-168256 Immune System 3
Partners
DNAJB1DUSP1GNA15PLCB1

Evidence

Reading pass · 19 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2000 EMR2 (ADGRE2) is a member of the EGF-TM7 family of class B GPCRs, containing N-terminal EGF-like domains coupled to a seven-span transmembrane domain via a mucin-like spacer. Expression is restricted to monocytes/macrophages and granulocytes, and unlike CD97 it does not interact with CD55, indicating distinct ligand specificity. Genomic mapping, alternative splicing analysis, monoclonal antibody binding assays, flow cytometry on primary leukocytes Genomics High 10903844
2002 EMR2 is expressed as a heterodimeric receptor consisting of an extracellular alpha subunit and a seven-transmembrane/cytoplasmic beta subunit, with myeloid-restricted expression (highest on CD16+ monocytes, macrophages, and BDCA-3+ myeloid DCs). Monoclonal antibody generation (2A1), immunoprecipitation, flow cytometry on primary blood leukocytes and hematopoietic cell lines, in situ analysis Journal of leukocyte biology High 11994511
2003 The EGF-like domains of EMR2 mediate cell attachment through chondroitin sulfate (CS) glycosaminoglycans; the fourth EGF-like module constitutes the major ligand-binding site, and the interaction is Ca2+- and sulphation-dependent. Multivalent protein probes, antibody-blocking studies, mutant CHO cell lines defective in GAG biosynthesis, enzymatic removal of cell surface GAGs, dose-dependent competition with exogenous CS Blood High 12829604
2003 Proteolytic cleavage of EMR2 occurs at Leu517-Ser518 within the GPS motif, is independent of transmembrane domains, requires the entire extracellular stalk (not GPS alone), and the non-covalent alpha-beta subunit association requires a minimum of eight amino acids in the beta-subunit. An alternatively spliced isoform with truncated stalk fails to undergo cleavage. Site-directed mutagenesis, cell-free cleavage assays, analysis of alternatively spliced isoforms, biochemical fractionation FEBS letters High 12860403
2004 GPS autoproteolysis of EMR2 is an autocatalytic intramolecular reaction at His-Leu↓Ser518; requires Ser, Thr, or Cys at P(+1) and His at P(-2) for efficient cleavage; occurs in the ER; produces two subunits that associate noncovalently. The mechanism resembles N-terminal nucleophile hydrolases performing cis-proteolysis. Site-directed mutagenesis of GPS residues, cell-free system spontaneous hydrolysis assay, biochemical characterization of ER localization of cleavage The Journal of biological chemistry High 15150276
2004 The fourth EGF domain of EMR2 (present on activated lymphocytes and myeloid cells) binds chondroitin sulfate specifically on B cells within peripheral blood, suggesting a role in T cell/DC/macrophage interactions with B cells. Fluorescent beads coated with recombinant CD97 and EMR2, isoform-specific monoclonal antibodies, flow cytometry on peripheral blood leukocytes Journal of leukocyte biology Medium 15498814
2005 In rheumatoid synovial tissue, dermatan sulfate is the endogenous ligand for the largest isoforms of EMR2 and CD97. EMR2 is expressed on macrophages and dendritic cells expressing costimulatory molecules and TNFα in synovium. Immunohistochemistry, double immunofluorescence, EMR2/CD97-specific multivalent fluorescent probe binding assays on synovial tissue sections Arthritis and rheumatism Medium 15693006
2006 EMR2 expression is up-regulated during macrophage differentiation/maturation and down-regulated during dendritic cell maturation; LPS and IL-10 (via an IL-10-mediated pathway) specifically up-regulate EMR2 in monocytes and macrophages. Alternative splicing and glycosylation of EMR2 are regulated during myeloid differentiation. Flow cytometry, ELISA, immunohistochemistry, specific mAb-based detection of isoforms, siRNA/inhibitor dissection of LPS/IL-10 pathways Biochemical and biophysical research communications Medium 17174274
2007 Ligation of EMR2 on neutrophils increases adhesion, migration, superoxide production, and proteolytic enzyme degranulation by potentiating proinflammatory mediator effects; upon activation EMR2 translocates to membrane ruffles and the leading edge; the transmembrane region is critical for these signaling functions. Anti-EMR2 antibody ligation, superoxide assay, degranulation assay, live-cell imaging showing translocation to membrane ruffles, dominant-negative transmembrane domain constructs FASEB journal High 17928360
2012 GPS autoproteolysis produces two distinct EMR2 receptor complexes: a noncovalent alpha-beta heterodimer and two completely independent subunits that distribute differentially in lipid raft microdomains. Receptor ligation induces subunit translocation and colocalization within lipid rafts, leading to signaling and inflammatory cytokine production by macrophages. Biochemical fractionation of lipid rafts, co-immunoprecipitation, antibody-mediated ligation, cytokine ELISA, GPS mutant constructs Molecular and cellular biology High 22310662
2016 A missense variant p.C492Y in ADGRE2 causes familial vibratory urticaria by destabilizing the autoinhibitory noncovalent subunit interaction between the extracellular and transmembrane subunits, sensitizing mast cells to IgE-independent vibration-induced degranulation. Human genetics (variant co-segregation in two kindreds), biochemical subunit interaction assays, mast cell degranulation assays with vibration stimulation The New England journal of medicine High 26841242
2017 Activation of EMR2 via agonistic antibody promotes THP-1 monocyte differentiation and induces IL-8, TNF-α, and MMP-9 expression through a Gα16-initiated signaling cascade activating Akt, ERK, JNK, and NF-κB. Anti-EMR2 antibody ligation, specific signaling inhibitors, siRNA knockdowns of pathway components, ELISA for cytokines, flow cytometry for differentiation markers Frontiers in immunology High 28421075
2018 The membrane-associated NTF (N-terminal fragment) of EMR2 is regulated by site-specific N-glycosylation in the GAIN domain occurring in post-ER compartments; a unique amphipathic alpha-helix in the GAIN domain serves as a putative membrane anchor of the NTF, independent of the CTF. Glycosylation site mutagenesis, subcellular fractionation, glycosidase treatment, confocal imaging of compartment-specific localization Scientific reports Medium 29540735
2020 ADGRE2/EMR2 couples broadly to G proteins (Gα16, Gα12, Gα13, Gα14, Gαz, Gα16/Gαz chimera) as shown by activated truncated receptor forms; EMR2 signals via Gα16 to stimulate IP1 accumulation and induces pertussis-toxin-insensitive inhibition of cAMP, suggesting Gαz coupling. An anti-EMR2 polyclonal antibody activates G protein signaling in vitro. Yeast-based G protein coupling assay with chimeric G proteins, mammalian cAMP assay with pertussis toxin, IP1 accumulation assay, NFAT reporter assay Scientific reports High 31969668
2020 Mechanical activation (vibration) of mast cells expressing p.C492Y-ADGRE2 attached to dermatan sulfate activates phospholipase C, causing transient cytosolic Ca2+ increase and downstream activation of PI3K and ERK1/2 via Gβγ, Gαq/11, and Gαi/o-independent mechanisms; degranulation requires PLC/Ca2+/PKC/PI3K pathways plus pertussis toxin-sensitive signals; prostaglandin D2 synthesis requires ERK1/2, Ca2+, PKC, and PI3K. Vibration stimulation of primary human mast cells, Ca2+ imaging, pharmacological inhibitors of PLC/PI3K/PKC/ERK, pertussis toxin treatment, degranulation assay, prostaglandin D2 ELISA The Journal of investigative dermatology High 32222457
2021 EMR2 activation by agonistic antibody triggers the NLRP3 inflammasome activation (2nd) signal in THP-1 monocytes and primary monocytes via Gα16-dependent PLC-β activation, leading to Akt, MAPK, NF-κB activity, Ca2+ mobilization, and K+ efflux. Anti-EMR2 mAb ligation, siRNA knockdown of Gα16 and PLC-β, K+ efflux measurement, NLRP3 inflammasome activation assays, pharmacological inhibitors Frontiers in immunology High 33488598
2024 ADGRE2 activates a PLCβ/PKC/MEK/ERK signaling cascade that drives AP1 transcriptional activity, which in turn transcriptionally upregulates DUSP1; DUSP1 dephosphorylates Ser16 of the co-chaperone DNAJB1 to facilitate DNAJB1-HSP70 interaction and maintain proteostasis in AML leukemic stem cells. ADGRE2 silencing in AML cell lines and patient-derived cells, xenograft mouse models, ChIP-seq/RNA-seq for AP1 targets, DUSP1 phosphorylation assays, co-immunoprecipitation of DNAJB1-HSP70, combined MEK/AP1/DUSP1 inhibitor treatment Cancer research High 39082681
2024 CD312/ADGRE2 interacts with GNA15 (Gα15) at the transmembrane intracellular segment, and this interaction promotes leukaemia cell proliferation via phosphorylation of ERK, JNK, and p38 in a co-culture system; GNA15 knockdown abrogates this proliferative effect. Co-immunoprecipitation (GNA15-CD312 interaction), BrdU proliferation assay, GNA15 siRNA knockdown, phospho-Western blotting for ERK/JNK/p38 Journal of cellular and molecular medicine Medium 39656442
2019 EMR2 contains an SGD sequence (corresponding to RGD in CD97) that prevents integrin α5β1 binding and angiogenesis induction; substituting SGD→RGD in EMR2 enables it to upregulate MMP-9 and induce angiogenesis via N-cadherin-regulated MMP-9 expression, similar to CD97. Site-directed mutagenesis of RGD/SGD motif, in vitro endothelial tube formation assay, in ovo chick CAM assay, MMP-9 expression analysis, N-cadherin modulation experiments Biochemical and biophysical research communications Medium 31594642

Source papers

Stage 0 corpus · 37 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2003 The epidermal growth factor-like domains of the human EMR2 receptor mediate cell attachment through chondroitin sulfate glycosaminoglycans. Blood 172 12829604
2004 Autocatalytic cleavage of the EMR2 receptor occurs at a conserved G protein-coupled receptor proteolytic site motif. The Journal of biological chemistry 170 15150276
2016 Vibratory Urticaria Associated with a Missense Variant in ADGRE2. The New England journal of medicine 150 26841242
2000 Human EMR2, a novel EGF-TM7 molecule on chromosome 19p13.1, is closely related to CD97. Genomics 85 10903844
2017 miR-99a reveals two novel oncogenic proteins E2F2 and EMR2 and represses stemness in lung cancer. Cell death & disease 83 29072692
2007 Ligation of the adhesion-GPCR EMR2 regulates human neutrophil function. FASEB journal : official publication of the Federation of American Societies for Experimental Biology 82 17928360
2004 Expression of the largest CD97 and EMR2 isoforms on leukocytes facilitates a specific interaction with chondroitin sulfate on B cells. Journal of leukocyte biology 73 15498814
2002 CD97, but not its closely related EGF-TM7 family member EMR2, is expressed on gastric, pancreatic, and esophageal carcinomas. American journal of clinical pathology 73 12428789
2002 The human EGF-TM7 family member EMR2 is a heterodimeric receptor expressed on myeloid cells. Journal of leukocyte biology 57 11994511
2003 Proteolytic cleavage of the EMR2 receptor requires both the extracellular stalk and the GPS motif. FEBS letters 54 12860403
2012 Activation of myeloid cell-specific adhesion class G protein-coupled receptor EMR2 via ligation-induced translocation and interaction of receptor subunits in lipid raft microdomains. Molecular and cellular biology 50 22310662
2015 Expression of CD11c and EMR2 on neutrophils: potential diagnostic biomarkers for sepsis and systemic inflammation. Clinical and experimental immunology 47 26153037
2005 Identification of the epidermal growth factor-TM7 receptor EMR2 and its ligand dermatan sulfate in rheumatoid synovial tissue. Arthritis and rheumatism 43 15693006
2006 CD312, the human adhesion-GPCR EMR2, is differentially expressed during differentiation, maturation, and activation of myeloid cells. Biochemical and biophysical research communications 42 17174274
2017 Activation of Adhesion GPCR EMR2/ADGRE2 Induces Macrophage Differentiation and Inflammatory Responses via Gα16/Akt/MAPK/NF-κB Signaling Pathways. Frontiers in immunology 41 28421075
2006 An unusual mode of concerted evolution of the EGF-TM7 receptor chimera EMR2. FASEB journal : official publication of the Federation of American Societies for Experimental Biology 41 17068111
2010 Leukocyte adhesion-GPCR EMR2 is aberrantly expressed in human breast carcinomas and is associated with patient survival. Oncology reports 39 21174063
2020 G Protein-Coupling of Adhesion GPCRs ADGRE2/EMR2 and ADGRE5/CD97, and Activation of G Protein Signalling by an Anti-EMR2 Antibody. Scientific reports 27 31969668
2020 Critical Signaling Events in the Mechanoactivation of Human Mast Cells through p.C492Y-ADGRE2. The Journal of investigative dermatology 24 32222457
2016 Increased EMR2 expression on neutrophils correlates with disease severity and predicts overall mortality in cirrhotic patients. Scientific reports 20 27905560
2011 EMR2 receptor ligation modulates cytokine secretion profiles and cell survival of lipopolysaccharide-treated neutrophils. Chang Gung medical journal 20 22035891
2010 Differential expression of the EGF-TM7 family members CD97 and EMR2 in lipid-laden macrophages in atherosclerosis, multiple sclerosis and Gaucher disease. Immunology letters 17 20167235
2003 Detection of alternatively spliced EMR2 mRNAs in colorectal tumor cell lines but rare expression of the molecule in colorectal adenocarcinomas. Virchows Archiv : an international journal of pathology 17 12761622
2021 Stimulation of Vibratory Urticaria-Associated Adhesion-GPCR, EMR2/ADGRE2, Triggers the NLRP3 Inflammasome Activation Signal in Human Monocytes. Frontiers in immunology 16 33488598
2019 The role of the RGD motif in CD97/ADGRE5-and EMR2/ADGRE2-modulated tumor angiogenesis. Biochemical and biophysical research communications 12 31594642
2024 Adhesion GPCR ADGRE2 Maintains Proteostasis to Promote Progression in Acute Myeloid Leukemia. Cancer research 10 39082681
2018 Membrane-association of EMR2/ADGRE2-NTF is regulated by site-specific N-glycosylation. Scientific reports 10 29540735
2004 Crystallization and preliminary X-ray diffraction analysis of three EGF domains of EMR2, a 7TM immune-system molecule. Acta crystallographica. Section D, Biological crystallography 10 15103144
2011 Comparative domain modeling of human EGF-like module EMR2 and study of interaction of the fourth domain of EGF with chondroitin 4-sulphate. Journal of biomedical research 5 23554678
2024 Research Progress of EMR2 Receptor Function in Glioma and its Potential Application as Therapeutic Target. Current health sciences journal 3 40144939
2017 Affinity Binding of EMR2 Expressing Cells by Surface-Grafted Chondroitin Sulfate B. Biomacromolecules 3 28437084
2025 Long-lasting changes in circulating dendritic cell and monocyte subsets, and altered expression of EMR2, CD97 and EMR3 on these cells in the posttraumatic course. Clinical & translational immunology 2 40529451
2024 CD312 Promotes Paediatric Acute Lymphoblastic Leukaemia Through GNA15-Mediated Non-Classical GPCR Signalling Pathway. Journal of cellular and molecular medicine 2 39656442
2023 The Posttraumatic Increase of the Adhesion GPCR EMR2/ADGRE2 on Circulating Neutrophils Is Not Related to Injury Severity. Cells 2 37998392
2024 Investigating the role of non-synonymous variant D67N of ADGRE2 in chronic myeloid leukemia. BMC cancer 1 39501172
2020 Author Correction: G Protein-Coupling of Adhesion GPCRs ADGRE2/EMR2 and ADGRE5/CD97, and Activation of G Protein Signalling by an Anti-EMR2 Antibody. Scientific reports 1 32184438
2026 Myeloid-driven inflammation highlights ADGRE2 as a biomarker in prurigo nodularis: Integrated multiomics analysis. The Journal of investigative dermatology 0 41544890