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description
| - artículu científicu espublizáu en 2002 (ast)
- vědecký článek publikovaný v roce 2002 (cs)
- наукова стаття, опублікована в серпні 2002 (uk)
- 2002 թուականի Օգոստոսին հրատարակուած գիտական յօդուած (hyw)
- 2002 թվականի օգոստոսին հրատարակված գիտական հոդված (hy)
- vedecký článok (publikovaný 2002/08/09) (sk)
- مقالة علمية (نشرت في 9-8-2002) (ar)
- article publié dans la revue scientifique Journal of Biological Chemistry (fr)
- wetenschappelijk artikel (gepubliceerd op 2002/08/09) (nl)
- im August 2002 veröffentlichter wissenschaftlicher Artikel (de)
- scientific journal article (en)
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author name string
| - Martin Stacey
- Lisa Stubbs
- Hsi-Hsien Lin
- Gin-Wen Chang
- Laura R. Chittenden
- Stephanie L. Sanos
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rdfs:label
| - EMR4, a novel epidermal growth factor (EGF)-TM7 molecule up-regulated in activated mouse macrophages, binds to a putative cellular ligand on B lymphoma cell line A20 (en)
- EMR4, a novel epidermal growth factor (EGF)-TM7 molecule up-regulated in activated mouse macrophages, binds to a putative cellular ligand on B lymphoma cell line A20 (nl)
- EMR4, a novel epidermal growth factor (EGF)-TM7 molecule up-regulated in activated mouse macrophages, binds to a putative cellular ligand on B lymphoma cell line A20 (ast)
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skos:prefLabel
| - EMR4, a novel epidermal growth factor (EGF)-TM7 molecule up-regulated in activated mouse macrophages, binds to a putative cellular ligand on B lymphoma cell line A20 (en)
- EMR4, a novel epidermal growth factor (EGF)-TM7 molecule up-regulated in activated mouse macrophages, binds to a putative cellular ligand on B lymphoma cell line A20 (nl)
- EMR4, a novel epidermal growth factor (EGF)-TM7 molecule up-regulated in activated mouse macrophages, binds to a putative cellular ligand on B lymphoma cell line A20 (ast)
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name
| - EMR4, a novel epidermal growth factor (EGF)-TM7 molecule up-regulated in activated mouse macrophages, binds to a putative cellular ligand on B lymphoma cell line A20 (en)
- EMR4, a novel epidermal growth factor (EGF)-TM7 molecule up-regulated in activated mouse macrophages, binds to a putative cellular ligand on B lymphoma cell line A20 (nl)
- EMR4, a novel epidermal growth factor (EGF)-TM7 molecule up-regulated in activated mouse macrophages, binds to a putative cellular ligand on B lymphoma cell line A20 (ast)
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| - EMR4, a novel epidermal growth factor (EGF)-TM7 molecule up-regulated in activated mouse macrophages, binds to a putative cellular ligand on B lymphoma cell line A20 (en)
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of | - Thy-1 (CD90) is an interacting partner for CD97 on activated endothelial cells
- Detection of alternatively spliced EMR2 mRNAs in colorectal tumor cell lines but rare expression of the molecule in colorectal adenocarcinomas
- Ligation of the adhesion-GPCR EMR2 regulates human neutrophil function
- G protein-coupled receptor 56 and collagen III, a receptor-ligand pair, regulates cortical development and lamination
- From the black widow spider to human behavior: Latrophilins, a relatively unknown class of G protein-coupled receptors, are implicated in psychiatric disorders
- Latrophilin fragments behave as independent proteins that associate and signal on binding of LTX(N4C).
- Anatomical profiling of G protein-coupled receptor expression
- The EGF-TM7 family: a postgenomic view
- Orphan G protein-coupled receptors (GPCRs): biological functions and potential drug targets
- There exist at least 30 human G-protein-coupled receptors with long Ser/Thr-rich N-termini
- Structural diversity of G protein-coupled receptors and significance for drug discovery
- The evolutionary history and tissue mapping of GPR123: specific CNS expression pattern predominantly in thalamic nuclei and regions containing large pyramidal cells
- Post-translational proteolytic processing of the calcium-independent receptor of alpha-latrotoxin (CIRL), a natural chimera of the cell adhesion protein and the G protein-coupled receptor. Role of the G protein-coupled receptor proteolysis site [...]
- The epidermal growth factor-like domains of the human EMR2 receptor mediate cell attachment through chondroitin sulfate glycosaminoglycans
- Expression and regulation of CD97 in colorectal carcinoma cell lines and tumor tissues
- Site-specific N-glycosylation regulates the GPS auto-proteolysis of CD97.
- The macrophage F4/80 receptor is required for the induction of antigen-specific efferent regulatory T cells in peripheral tolerance
- Expression profile of the entire family of Adhesion G protein-coupled receptors in mouse and rat
- Two novel genes, Gpr113, which encodes a family 2 G-protein-coupled receptor, and Trcg1, are selectively expressed in taste receptor cells
- International Union of Basic and Clinical Pharmacology. XCIV. Adhesion G protein-coupled receptors
- VIGR--a novel inducible adhesion family G-protein coupled receptor in endothelial cells
- Overexpression of CD97 confers an invasive phenotype in glioblastoma cells and is associated with decreased survival of glioblastoma patients
- Organ-specific function of adhesion G protein-coupled receptor GPR126 is domain-dependent
- DREG, a developmentally regulated G protein-coupled receptor containing two conserved proteolytic cleavage sites
- Proteolytic cleavage of the EMR2 receptor requires both the extracellular stalk and the GPS motif
- Dissociation of the subunits of the calcium-independent receptor of alpha-latrotoxin as a result of two-step proteolysis.
- Gene structure and transcript analysis of the human and mouse EGF-TM7 molecule, FIRE
- Targeted deletion of the epididymal receptor HE6 results in fluid dysregulation and male infertility
- Adhesion GPCRs as Modulators of Immune Cell Function
- Pleiotropic Impacts of Macrophage and Microglial Deficiency on Development in Rats with Targeted Mutation of the Locus
- Soluble mucus component CLCA1 modulates expression of leukotactic cytokines and BPIFA1 in murine alveolar macrophages but not in bone marrow-derived macrophages.
- ADGRE1 (EMR1, F4/80) Is a Rapidly-Evolving Gene Expressed in Mammalian Monocyte-Macrophages
- Microglial transglutaminase-2 drives myelination and myelin repair via GPR56/ADGRG1 in oligodendrocyte precursor cells.
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