Primate-specific regulation of the human glycosphingolipid gatekeeper UGCG
Nature, Published online: 26 August 2026; doi:10.1038/s41586-026-10927-4 Cryogenic electron microscopy structures of full-length human UGCG, the gatekeeper that dictates the scale and composition of glycosphingolipid diversity, are reported, showing that it uses a metal-independent catalytic mechanism driven by an arginine network.
خواندن متن کامل در نیچربه زبان اصلی، در سایت ناشر باز میشودمتن اصلی (انگلیسی)
Primate-specific regulation of the human glycosphingolipid gatekeeper UGCG
Nature, Published online: 26 August 2026; doi:10.1038/s41586-026-10927-4 Cryogenic electron microscopy structures of full-length human UGCG, the gatekeeper that dictates the scale and composition of glycosphingolipid diversity, are reported, showing that it uses a metal-independent catalytic mechanism driven by an arginine network.