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Autocatalytic cleavage of the EMR2 receptor occurs at a conserved G protein-coupled receptor proteolytic site motif
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Latrophilin fragments behave as independent proteins that associate and signal on binding of LTXN4C
KE Volynski et al.
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Dynamic regulation of a GPCR-tetraspanin-G protein complex on intact cells:: Central role of CD81 in facilitating GPR56-Gαq/11 association
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The epidermal growth factor-like domains of the human EMR2 receptor mediate cell attachment through chondroitin sulfate glycosaminoglycans
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Mutant α-latrotoxin (LTXN4C) does not form pores and causes secretion by receptor stimulation -: This action does not require neurexins
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Proteolytic cleavage of the EMR2 receptor requires both the extracellular stalk and the GPS motif
GW Chang et al.
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R Fredriksson et al.
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Cleavage of polycystin-1 requires the receptor for egg jelly domain and is disrupted by human autosomal-dominant polycystic kidney disease 1-associated mutations
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Post-translational proteolytic processing of the calciumin-dependent receptor of α-latrotoxin (CIRL), a natural chimera of the cell adhesion protein and the G protein-coupled recent -: Role of the G protein-coupled receptor proteolysis site (GPS) motif
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α-latrotoxin, acting via two Ca2+-dependent pathways, triggers exocytosis of two pools of synaptic vesicles
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Latrophilin, neurexin, and their signaling-deficient mutants facilitate α-latrotoxin insertion into membranes but are not involved in pore formation
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Human EMR2, a novel EGF-TM7 molecule on chromosome 19p13.1, is closely related to CD97
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A family of heptahelical receptors with adhesion-like domains: A marriage between two super families
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