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Journal Abstract Search

184 related items for PubMed ID: 12364335

  • 21. 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; 26(4):360-76. PubMed ID: 26610890
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  • 24. UDP-N-acetyl-α-D-galactosamine:polypeptide N-acetylgalactosaminyl-transferase from the snail Biomphalaria glabrata - substrate specificity and preference of glycosylation sites.
    Taus C, Windwarder M, Altmann F, Grabherr R, Staudacher E.
    Glycoconj J; 2014 Dec; 31(9):661-70. PubMed ID: 25338825
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  • 25. Substrate specificities of three members of the human UDP-N-acetyl-alpha-D-galactosamine:Polypeptide N-acetylgalactosaminyltransferase family, GalNAc-T1, -T2, and -T3.
    Wandall HH, Hassan H, Mirgorodskaya E, Kristensen AK, Roepstorff P, Bennett EP, Nielsen PA, Hollingsworth MA, Burchell J, Taylor-Papadimitriou J, Clausen H.
    J Biol Chem; 1997 Sep 19; 272(38):23503-14. PubMed ID: 9295285
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  • 26. An efficient approach for the characterization of mucin-type glycopeptides: the effect of O-glycosylation on the conformation of synthetic mucin peptides.
    Hashimoto R, Fujitani N, Takegawa Y, Kurogochi M, Matsushita T, Naruchi K, Ohyabu N, Hinou H, Gao XD, Manri N, Satake H, Kaneko A, Sakamoto T, Nishimura S.
    Chemistry; 2011 Feb 18; 17(8):2393-404. PubMed ID: 21264968
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  • 29. Identification of common and unique peptide substrate preferences for the UDP-GalNAc:polypeptide alpha-N-acetylgalactosaminyltransferases T1 and T2 derived from oriented random peptide substrates.
    Gerken TA, Raman J, Fritz TA, Jamison O.
    J Biol Chem; 2006 Oct 27; 281(43):32403-16. PubMed ID: 16912039
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  • 30. Cloning of a human UDP-N-acetyl-alpha-D-Galactosamine:polypeptide N-acetylgalactosaminyltransferase that complements other GalNAc-transferases in complete O-glycosylation of the MUC1 tandem repeat.
    Bennett EP, Hassan H, Mandel U, Mirgorodskaya E, Roepstorff P, Burchell J, Taylor-Papadimitriou J, Hollingsworth MA, Merkx G, van Kessel AG, Eiberg H, Steffensen R, Clausen H.
    J Biol Chem; 1998 Nov 13; 273(46):30472-81. PubMed ID: 9804815
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  • 31. cDNA cloning and expression of UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase T1 from Toxoplasma gondii.
    Wojczyk BS, Stwora-Wojczyk MM, Hagen FK, Striepen B, Hang HC, Bertozzi CR, Roos DS, Spitalnik SL.
    Mol Biochem Parasitol; 2003 Oct 13; 131(2):93-107. PubMed ID: 14511808
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  • 32. The specificity of UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase as inferred from a database of in vivo substrates and from the in vitro glycosylation of proteins and peptides.
    Elhammer AP, Poorman RA, Brown E, Maggiora LL, Hoogerheide JG, Kézdy FJ.
    J Biol Chem; 1993 May 15; 268(14):10029-38. PubMed ID: 8486674
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  • 33. Role of peptide sequence and neighboring residue glycosylation on the substrate specificity of the uridine 5'-diphosphate-alpha-N-acetylgalactosamine:polypeptide N-acetylgalactosaminyl transferases T1 and T2: kinetic modeling of the porcine and canine submaxillary gland mucin tandem repeats.
    Gerken TA, Tep C, Rarick J.
    Biochemistry; 2004 Aug 03; 43(30):9888-900. PubMed ID: 15274643
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  • 34. Studies of acceptor site specificities for three members of UDP-GalNAc:N-acetylgalactosaminyltransferases by using a synthetic peptide mimicking the tandem repeat of MUC5AC.
    Tetaert D, Richet C, Gagnon J, Boersma A, Degand P.
    Carbohydr Res; 2001 Jul 03; 333(2):165-71. PubMed ID: 11448678
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  • 35. A novel human UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase, GalNAc-T7, with specificity for partial GalNAc-glycosylated acceptor substrates.
    Bennett EP, Hassan H, Hollingsworth MA, Clausen H.
    FEBS Lett; 1999 Oct 29; 460(2):226-30. PubMed ID: 10544240
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  • 36. An acetylation site in lectin domain modulates the biological activity of polypeptide GalNAc-transferase-2.
    Zlocowski N, Lorenz V, Bennett EP, Clausen H, Nores GA, Irazoqui FJ.
    Biol Chem; 2013 Jan 29; 394(1):69-77. PubMed ID: 23096348
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  • 37. 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 29; 42():184-193. PubMed ID: 29097258
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  • 38. Studies on the order and site specificity of GalNAc transfer to MUC1 tandem repeats by UDP-GalNAc: polypeptide N-acetylgalactosaminyltransferase from milk or mammary carcinoma cells.
    Stadie TR, Chai W, Lawson AM, Byfield PG, Hanisch FG.
    Eur J Biochem; 1995 Apr 01; 229(1):140-7. PubMed ID: 7744025
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  • 39. Determination of the site-specific O-glycosylation pattern of the porcine submaxillary mucin tandem repeat glycopeptide. Model proposed for the polypeptide:galnac transferase peptide binding site.
    Gerken TA, Owens CL, Pasumarthy M.
    J Biol Chem; 1997 Apr 11; 272(15):9709-19. PubMed ID: 9092502
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  • 40. Dynamic epigenetic regulation of initial O-glycosylation by UDP-N-Acetylgalactosamine:Peptide N-acetylgalactosaminyltransferases. site-specific glycosylation of MUC1 repeat peptide influences the substrate qualities at adjacent or distant Ser/Thr positions.
    Hanisch FG, Müller S, Hassan H, Clausen H, Zachara N, Gooley AA, Paulsen H, Alving K, Peter-Katalinic J.
    J Biol Chem; 1999 Apr 09; 274(15):9946-54. PubMed ID: 10187769
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