239 related articles for article (PubMed ID: 18669915)
1. Conservation of peptide acceptor preferences between Drosophila and mammalian polypeptide-GalNAc transferase ortholog pairs.
Gerken TA; Ten Hagen KG; Jamison O
Glycobiology; 2008 Nov; 18(11):861-70. PubMed ID: 18669915
[TBL] [Abstract][Full Text] [Related]
2. 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; 281(43):32403-16. PubMed ID: 16912039
[TBL] [Abstract][Full Text] [Related]
3. 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; 284(30):20387-97. PubMed ID: 19460755
[TBL] [Abstract][Full Text] [Related]
4. 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; 43(30):9888-900. PubMed ID: 15274643
[TBL] [Abstract][Full Text] [Related]
5. Emerging paradigms for the initiation of mucin-type protein O-glycosylation by the polypeptide GalNAc transferase family of glycosyltransferases.
Gerken TA; Jamison O; Perrine CL; Collette JC; Moinova H; Ravi L; Markowitz SD; Shen W; Patel H; Tabak LA
J Biol Chem; 2011 Apr; 286(16):14493-507. PubMed ID: 21349845
[TBL] [Abstract][Full Text] [Related]
6. 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; 288(27):19900-14. PubMed ID: 23689369
[TBL] [Abstract][Full Text] [Related]
7. 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; 277(51):49850-62. PubMed ID: 12397077
[TBL] [Abstract][Full Text] [Related]
8. 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
[TBL] [Abstract][Full Text] [Related]
9. 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; 382(Pt 2):501-10. PubMed ID: 15142032
[TBL] [Abstract][Full Text] [Related]
10. Functional conservation of subfamilies of putative UDP-N-acetylgalactosamine:polypeptide N-acetylgalactosaminyltransferases in Drosophila, Caenorhabditis elegans, and mammals. One subfamily composed of l(2)35Aa is essential in Drosophila.
Schwientek T; Bennett EP; Flores C; Thacker J; Hollmann M; Reis CA; Behrens J; Mandel U; Keck B; Schäfer MA; Haselmann K; Zubarev R; Roepstorff P; Burchell JM; Taylor-Papadimitriou J; Hollingsworth MA; Clausen H
J Biol Chem; 2002 Jun; 277(25):22623-38. PubMed ID: 11925450
[TBL] [Abstract][Full Text] [Related]
11. 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; 30(11):910-922. PubMed ID: 32304323
[TBL] [Abstract][Full Text] [Related]
12. Polypeptide N-acetylgalactosaminyltransferase (GalNAc-T) isozyme surface charge governs charge substrate preferences to modulate mucin type O-glycosylation.
Ballard CJ; Paserba MR; Paul Daniel EJ; Hurtado-Guerrero R; Gerken TA
Glycobiology; 2023 Oct; 33(10):817-836. PubMed ID: 37555669
[TBL] [Abstract][Full Text] [Related]
13. 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
[TBL] [Abstract][Full Text] [Related]
14. 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; 17(4):374-87. PubMed ID: 17215257
[TBL] [Abstract][Full Text] [Related]
15. 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; 34(3):309-22. PubMed ID: 15003492
[TBL] [Abstract][Full Text] [Related]
16. Characterization of ppGalNAc-T18, a member of the vertebrate-specific Y subfamily of UDP-N-acetyl-α-D-galactosamine:polypeptide N-acetylgalactosaminyltransferases.
Li X; Wang J; Li W; Xu Y; Shao D; Xie Y; Xie W; Kubota T; Narimatsu H; Zhang Y
Glycobiology; 2012 May; 22(5):602-15. PubMed ID: 22171061
[TBL] [Abstract][Full Text] [Related]
17. 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; 394(1):69-77. PubMed ID: 23096348
[TBL] [Abstract][Full Text] [Related]
18. 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; 266(1-2):117-26. PubMed ID: 15646032
[TBL] [Abstract][Full Text] [Related]
19. 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; 274(15):9946-54. PubMed ID: 10187769
[TBL] [Abstract][Full Text] [Related]
20. 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; 272(38):23503-14. PubMed ID: 9295285
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]