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Receptor
About: Receptor is a research topic. Over the lifetime, 159318 publications have been published within this topic receiving 8299881 citations.
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TL;DR: A comprehensive set of recombinant secreted proteins and the extracellular domains of transmembrane proteins, which constitute most of the protein components of the Extracellular space, are produced, useful for discovering new ligands and receptors and assessing the functional selectivity ofextracellular regulatory proteins.
Abstract: To understand the system of secreted proteins and receptors involved in cell-cell signaling, we produced a comprehensive set of recombinant secreted proteins and the extracellular domains of transmembrane proteins, which constitute most of the protein components of the extracellular space. Each protein was tested in a suite of assays that measured metabolic, growth, or transcriptional responses in diverse cell types. The pattern of responses across assays was analyzed for the degree of functional selectivity of each protein. One of the highly selective proteins was a previously undescribed ligand, designated interleukin-34 (IL-34), which stimulates monocyte viability but does not affect responses in a wide spectrum of other assays. In a separate functional screen, we used a collection of extracellular domains of transmembrane proteins to discover the receptor for IL-34, which was a known cytokine receptor, colony-stimulating factor 1 (also called macrophage colony-stimulating factor) receptor. This systematic approach is thus useful for discovering new ligands and receptors and assessing the functional selectivity of extracellular regulatory proteins.
717 citations
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716 citations
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TL;DR: The molecular cloning and pharmacologic characterization of a third member of this receptor family is reported, which characterizes it as an MSH receptor specific to the heptapeptide core common to adrenocorticotropic hormone and alpha-, beta-, and gamma-MSH.
715 citations
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TL;DR: Data indicate that ephrin-B2-EphB4 interactions are intrinsically required in vascular endothelial cells and are consistent with the idea that they mediate bidirectional signaling essential for angiogenesis.
715 citations
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TL;DR: It is proposed that a C-terminal turn, centred on this glycine, plays an important part in specifying receptor interactions of G proteins in the Gi/G0/Gz family.
Abstract: AGONIST-BOUND receptors activate heterotrimeric (αβγ) G proteins by catalysing replacement of GDP bound to the α-subunit by GTP1–5. Mutations in the C terminus of the α-subunit6,7, its covalent modification by pertussis toxin-catalysed ribosylation of ADP8, peptide-specific antibodies directed against it9–11, and peptides mimicking C-terminal sequences12, all inhibit receptor-mediated activation of G proteins. The logical prediction—that specific amino-acid residues at the C-termini of α-subunits can determine the abilities of individual G proteins to discriminate among specific subsets of receptors—has so far not been tested experimentally. Different hormone receptors specifically activate Gq or Gi whose α-subunits (αq or αi) stimulate phosphatidylinositol-specific phospholipase C or inhibit adenylyl cyclase, respectively1–5. Here we replace C-terminal amino acids of αq with the corresponding residues of αi2 to create αq/αi2 chimaeras that can mediate stimulation of phospholipase C by receptors otherwise coupled exclusively to Gj. A minimum of three ai2 amino acids, including a glycine three residues from the C terminus, suffices to switch the receptor specificity of the αq/αi2 chimaeras. We propose that a C-terminal turn, centred on this glycine, plays an important part in specifying receptor interactions of G proteins in the Gi/G0/Gz family.
715 citations