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Journal Abstract Search

1006 related items for PubMed ID: 20540529

  • 1. 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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  • 5. 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 20; 17(4):374-87. PubMed ID: 17215257
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  • 9. N-acetylgalactosamine glycosylation of MUC1 tandem repeat peptides by pancreatic tumor cell extracts.
    Nishimori I, Perini F, Mountjoy KP, Sanderson SD, Johnson N, Cerny RL, Gross ML, Fontenot JD, Hollingsworth MA.
    Cancer Res; 1994 Jul 15; 54(14):3738-44. PubMed ID: 8033093
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  • 10. Site directed processing: role of amino acid sequences and glycosylation of acceptor glycopeptides in the assembly of extended mucin type O-glycan core 2.
    Brockhausen I, Dowler T, Paulsen H.
    Biochim Biophys Acta; 2009 Oct 15; 1790(10):1244-57. PubMed ID: 19524017
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  • 13. 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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  • 16. Lectin domains of polypeptide GalNAc transferases exhibit glycopeptide binding specificity.
    Pedersen JW, Bennett EP, Schjoldager KT, Meldal M, Holmér AP, Blixt O, Cló E, Levery SB, Clausen H, Wandall HH.
    J Biol Chem; 2011 Sep 16; 286(37):32684-96. PubMed ID: 21768105
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  • 17. Specificity of O-glycosylation by bovine colostrum UDP-GalNAc: polypeptide alpha-N-acetylgalactosaminyltransferase using synthetic glycopeptide substrates.
    Brockhausen I, Toki D, Brockhausen J, Peters S, Bielfeldt T, Kleen A, Paulsen H, Meldal M, Hagen F, Tabak LA.
    Glycoconj J; 1996 Oct 16; 13(5):849-56. PubMed ID: 8910012
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  • 18. Function of conserved aromatic residues in the Gal/GalNAc-glycosyltransferase motif of UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 1.
    Tenno M, Saeki A, Elhammer AP, Kurosaka A.
    FEBS J; 2007 Dec 16; 274(23):6037-45. PubMed ID: 17970754
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  • 19. Mucin-type O-glycosylation is controlled by short- and long-range glycopeptide substrate recognition that varies among members of the polypeptide GalNAc transferase family.
    Revoredo L, Wang S, Bennett EP, Clausen H, Moremen KW, Jarvis DL, Ten Hagen KG, Tabak LA, Gerken TA.
    Glycobiology; 2016 Apr 16; 26(4):360-76. PubMed ID: 26610890
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  • 20. 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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