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Journal Abstract Search
301 related items for PubMed ID: 8910012
1. 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; 13(5):849-56. PubMed ID: 8910012 [Abstract] [Full Text] [Related]
2. Glycopeptide-preferring polypeptide GalNAc transferase 10 (ppGalNAc T10), involved in mucin-type O-glycosylation, has a unique GalNAc-O-Ser/Thr-binding site in its catalytic domain not found in ppGalNAc T1 or T2. Perrine CL, Ganguli A, Wu P, Bertozzi CR, Fritz TA, Raman J, Tabak LA, Gerken TA. J Biol Chem; 2009 Jul 24; 284(30):20387-97. PubMed ID: 19460755 [Abstract] [Full Text] [Related]
3. 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 24; 1790(10):1244-57. PubMed ID: 19524017 [Abstract] [Full Text] [Related]
4. 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 [Abstract] [Full Text] [Related]
5. UDPgalactose:glycoprotein-N-acetyl-D-galactosamine 3-beta-D-galactosyltransferase activity synthesizing O-glycan core 1 is controlled by the amino acid sequence and glycosylation of glycopeptide substrates. Granovsky M, Bielfeldt T, Peters S, Paulsen H, Meldal M, Brockhausen J, Brockhausen I. Eur J Biochem; 1994 May 01; 221(3):1039-46. PubMed ID: 8181460 [Abstract] [Full Text] [Related]
6. 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 [Abstract] [Full Text] [Related]
7. 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 [Abstract] [Full Text] [Related]
8. 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 [Abstract] [Full Text] [Related]
9. 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 [Abstract] [Full Text] [Related]
10. Control of mucin synthesis: the peptide portion of synthetic O-glycopeptide substrates influences the activity of O-glycan core 1 UDPgalactose:N-acetyl-alpha-galactosaminyl-R beta 3-galactosyltransferase. Brockhausen I, Möller G, Merz G, Adermann K, Paulsen H. Biochemistry; 1990 Nov 06; 29(44):10206-12. PubMed ID: 2125490 [Abstract] [Full Text] [Related]
11. 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 [Abstract] [Full Text] [Related]
12. 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 [Abstract] [Full Text] [Related]
13. The influence of flanking sequence on the O-glycosylation of threonine in vitro. O'Connell BC, Hagen FK, Tabak LA. J Biol Chem; 1992 Dec 15; 267(35):25010-8. PubMed ID: 1460004 [Abstract] [Full Text] [Related]
14. Purification, cloning, and expression of a bovine UDP-GalNAc: polypeptide N-acetyl-galactosaminyltransferase. Hagen FK, Van Wuyckhuyse B, Tabak LA. J Biol Chem; 1993 Sep 05; 268(25):18960-5. PubMed ID: 8360184 [Abstract] [Full Text] [Related]
15. 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 05; 26(4):360-76. PubMed ID: 26610890 [Abstract] [Full Text] [Related]
16. 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 [Abstract] [Full Text] [Related]
17. High density O-glycosylation of the MUC2 tandem repeat unit by N-acetylgalactosaminyltransferase-3 in colonic adenocarcinoma extracts. Inoue M, Takahashi S, Yamashina I, Kaibori M, Okumura T, Kamiyama Y, Vichier-Guerre S, Cantacuzène D, Nakada H. Cancer Res; 2001 Feb 01; 61(3):950-6. PubMed ID: 11221889 [Abstract] [Full Text] [Related]
18. Elucidation of the sugar recognition ability of the lectin domain of UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 3 by using unnatural glycopeptide substrates. Yoshimura Y, Nudelman AS, Levery SB, Wandall HH, Bennett EP, Hindsgaul O, Clausen H, Nishimura S. Glycobiology; 2012 Mar 01; 22(3):429-38. PubMed ID: 22042768 [Abstract] [Full Text] [Related]
19. Ser and Thr acceptor preferences of the GalNAc-Ts vary among isoenzymes to modulate mucin-type O-glycosylation. Daniel EJP, Las Rivas M, Lira-Navarrete E, García-García A, Hurtado-Guerrero R, Clausen H, Gerken TA. Glycobiology; 2020 Oct 21; 30(11):910-922. PubMed ID: 32304323 [Abstract] [Full Text] [Related]
20. Mucin core O-glycosylation is modulated by neighboring residue glycosylation status. Kinetic modeling of the site-specific glycosylation of the apo-porcine submaxillary mucin tandem repeat by UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferases T1 and T2. Gerken TA, Zhang J, Levine J, Elhammer A. J Biol Chem; 2002 Dec 20; 277(51):49850-62. PubMed ID: 12397077 [Abstract] [Full Text] [Related] Page: [Next] [New Search]