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Journal Abstract Search

208 related items for PubMed ID: 12419318

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  • 2. The lectin domain of UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 1 is involved in O-glycosylation of a polypeptide with multiple acceptor sites.
    Tenno M, Saeki A, Kézdy FJ, Elhammer AP, Kurosaka A.
    J Biol Chem; 2002 Dec 06; 277(49):47088-96. PubMed ID: 12364335
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  • 4. The lectin domains of polypeptide GalNAc-transferases exhibit carbohydrate-binding specificity for GalNAc: lectin binding to GalNAc-glycopeptide substrates is required for high density GalNAc-O-glycosylation.
    Wandall HH, Irazoqui F, Tarp MA, Bennett EP, Mandel U, Takeuchi H, Kato K, Irimura T, Suryanarayanan G, Hollingsworth MA, Clausen H.
    Glycobiology; 2007 Apr 06; 17(4):374-87. PubMed ID: 17215257
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  • 5. The lectin domain of UDP-N-acetyl-D-galactosamine: polypeptide N-acetylgalactosaminyltransferase-T4 directs its glycopeptide specificities.
    Hassan H, Reis CA, Bennett EP, Mirgorodskaya E, Roepstorff P, Hollingsworth MA, Burchell J, Taylor-Papadimitriou J, Clausen H.
    J Biol Chem; 2000 Dec 08; 275(49):38197-205. PubMed ID: 10984485
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  • 6. An unusual dual sugar-binding lectin domain controls the substrate specificity of a mucin-type O-glycosyltransferase.
    Collette AM, Hassan SA, Schmidt SI, Lara AJ, Yang W, Samara NL.
    Sci Adv; 2024 Mar 08; 10(9):eadj8829. PubMed ID: 38416819
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  • 10. The catalytic and lectin domains of UDP-GalNAc:polypeptide alpha-N-Acetylgalactosaminyltransferase function in concert to direct glycosylation site selection.
    Raman J, Fritz TA, Gerken TA, Jamison O, Live D, Liu M, Tabak LA.
    J Biol Chem; 2008 Aug 22; 283(34):22942-51. PubMed ID: 18562306
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  • 11. Dynamic association between the catalytic and lectin domains of human UDP-GalNAc:polypeptide alpha-N-acetylgalactosaminyltransferase-2.
    Fritz TA, Raman J, Tabak LA.
    J Biol Chem; 2006 Mar 31; 281(13):8613-9. PubMed ID: 16434399
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  • 12. Site-specific O-glycosylation of N-terminal serine residues by polypeptide GalNAc-transferase 2 modulates human δ-opioid receptor turnover at the plasma membrane.
    Lackman JJ, Goth CK, Halim A, Vakhrushev SY, Clausen H, Petäjä-Repo UE.
    Cell Signal; 2018 Jan 31; 42():184-193. PubMed ID: 29097258
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  • 13. The beginnings of mucin biosynthesis: the crystal structure of UDP-GalNAc:polypeptide alpha-N-acetylgalactosaminyltransferase-T1.
    Fritz TA, Hurley JH, Trinh LB, Shiloach J, Tabak LA.
    Proc Natl Acad Sci U S A; 2004 Oct 26; 101(43):15307-12. PubMed ID: 15486088
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  • 14. Cloning, expression and properties of porcine trachea UDP-galnac: polypeptide N-acetylgalactosaminyl transferase.
    Sangadala S, Swain JB, McNear A, Mendicino J.
    Mol Cell Biochem; 2004 Nov 26; 266(1-2):117-26. PubMed ID: 15646032
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  • 15. Unexpected tolerance of glycosylation by UDP-GalNAc:polypeptide alpha-N-acetylgalactosaminyltransferase revealed by electron capture dissociation mass spectrometry: carbohydrate as potential protective groups.
    Yoshimura Y, Matsushita T, Fujitani N, Takegawa Y, Fujihira H, Naruchi K, Gao XD, Manri N, Sakamoto T, Kato K, Hinou H, Nishimura S.
    Biochemistry; 2010 Jul 20; 49(28):5929-41. PubMed ID: 20540529
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  • 16. Characterization of a UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase with an unusual lectin domain from the platyhelminth parasite Echinococcus granulosus.
    Freire T, Fernández C, Chalar C, Maizels RM, Alzari P, Osinaga E, Robello C.
    Biochem J; 2004 Sep 01; 382(Pt 2):501-10. PubMed ID: 15142032
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  • 17. The interdomain flexible linker of the polypeptide GalNAc transferases dictates their long-range glycosylation preferences.
    de Las Rivas M, Lira-Navarrete E, Daniel EJP, Compañón I, Coelho H, Diniz A, Jiménez-Barbero J, Peregrina JM, Clausen H, Corzana F, Marcelo F, Jiménez-Osés G, Gerken TA, Hurtado-Guerrero R.
    Nat Commun; 2017 Dec 05; 8(1):1959. PubMed ID: 29208955
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  • 18. 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.
    Gerken TA, Revoredo L, Thome JJ, Tabak LA, Vester-Christensen MB, Clausen H, Gahlay GK, Jarvis DL, Johnson RW, Moniz HA, Moremen K.
    J Biol Chem; 2013 Jul 05; 288(27):19900-14. PubMed ID: 23689369
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  • 19. Structural basis of carbohydrate transfer activity of UDP-GalNAc: Polypeptide N-acetylgalactosaminyltransferase 7.
    Yu C, Liang L, Yin Y.
    Biochem Biophys Res Commun; 2019 Mar 05; 510(2):266-271. PubMed ID: 30685086
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  • 20. O-glycosylation in Toxoplasma gondii: identification and analysis of a family of UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferases.
    Stwora-Wojczyk MM, Kissinger JC, Spitalnik SL, Wojczyk BS.
    Int J Parasitol; 2004 Mar 09; 34(3):309-22. PubMed ID: 15003492
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