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The molecular mechanisms N. meningitidis employ to manipulate the immune system, translocate the mucosal Human-associated bacteria encode a variety of bioactive small molecules with growing evidence for N-acyl Here, we heterologously expressed an N-acyltransferase encoded in the obligate human pathogen N. meningitidis and identified 30 N-acyl amides with representative members serving as agonists of the G-protein coupled During this process, we also characterized two mammalian N-acyl amides derived from the bovine medium

October 2022 N-terminal alterations turn the gut hormone GLP-2 into an antagonist with gradual loss of Searching for antagonist activity, we performed systematic N-terminal truncations of human GLP-2(1-33

September 2022 Isoforms of GPR35 have distinct extracellular N-termini that allosterically modify receptor-transducer known to be expressed as two distinct isoforms that differ only in the length of their extracellular N-termini Our results reveal that the extended N-terminus of the long isoform limits G protein activation yet elevates We found that a proposed disulfide bridge between the N-terminus and extracellular loop 3, present in is crucial for constitutive G13 activation, while an additional cysteine contributed by the extended N-terminus

➡️https://www.ecosystem.drgpcr.com/adhesion-gpcrs/n-terminal-fragment-shedding-contributes-to-signaling-of-the-full-length-adhesion-receptor-adgrl3 ➡️ https:// www.ecosystem.drgpcr.com/adhesion-gpcrs/n-terminal-fragment-shedding-contributes-to-signaling-of-the-full-length-adhesion-receptor-adgrl3

Van Meir Site Specific N-Glycosylation Of The N-Terminal Fragment Of ADGRG6 Drives Proteolytic Processing Van Meir on the web Google Scholar Site Specific N-Glycosylation Of The N-Terminal Fragment Of ADGRG6 Furthermore, are there spatial roles of N-glycosylation in ADGRG6 processing, trafficking, signalling We observed that N-glycosylation specifically takes place in the NTF and not the CTF of ADGRG6. Our results demonstrate that specific N-glycan residues in different domains of the extracellular NTF

This new Nature Chemical Biology paper reveals cryo-EM structures of Gq-bound PTH1R—highlighting how N-linked