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doi: 10.1182/blood-2007-06-095018 197 LiKAndersonKJPengQNobleALuBKellyAPet al
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Giordano et al., Human- and machine-centred designs of molecules and materials for sustainability and decarbonization
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Rspondins bind both the E3 ubiquitin ligase and a member of Lgr family (Lgr4, Lgr5, and Lgr6) to form a ternary structure that abolishes the ubiquitination activity of the E3 ligase and thus augments Wnt activity by allowing surface accumulation of Fzd receptors
