Atomic and Specificity Details of Mucin 1 O-Glycosylation Process by Multiple Polypeptide GalNAc-Transferase Isoforms Unveiled by NMR and Molecular Modeling.
Jacs Au
Coelho, Helena H; Rivas, Matilde de Las ML; Grosso, Ana S AS; Diniz, Ana A; Soares, Cátia O CO; Francisco, Rodrigo A RA; Dias, Jorge S JS; Compañon, Ismael I; Sun, Lingbo L; Narimatsu, Yoshiki Y; Vakhrushev, Sergey Y SY; Clausen, Henrik H; Cabrita, Eurico J EJ; Jiménez-Barbero, Jesús J; Corzana, Francisco F; Hurtado-Guerrero, Ramon R; Marcelo, Filipa F
Initiation of GalNAc-type O-glycosylation in the endoplasmic reticulum promotes cancer cell invasiveness.
Proceedings Of The National Academy Of Sciences Of The United States Of America
Gill, David J DJ; Tham, Keit Min KM; Chia, Joanne J; Wang, Shyi Chyi SC; Steentoft, Catharina C; Clausen, Henrik H; Bard-Chapeau, Emilie A EA; Bard, Frederic A FA
The lectin domain of the polypeptide GalNAc transferase family of glycosyltransferases (ppGalNAc Ts) acts as a switch directing glycopeptide substrate glycosylation in an N- or C-terminal direction, further controlling mucin type O-glycosylation.
The Journal Of Biological Chemistry
Gerken, Thomas A TA; Revoredo, Leslie L; Thome, Joseph J C JJ; Tabak, Lawrence A LA; Vester-Christensen, Malene Bech MB; Clausen, Henrik H; Gahlay, Gagandeep K GK; Jarvis, Donald L DL; Johnson, Roy W RW; Moniz, Heather A HA; Moremen, Kelley K