These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Journal Abstract Search

191 related items for PubMed ID: 38416819

  • 1. 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; 10(9):eadj8829. PubMed ID: 38416819
    [Abstract] [Full Text] [Related]

  • 2.
    ; . PubMed ID:
    [No Abstract] [Full Text] [Related]

  • 3. 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]

  • 4. 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]

  • 5. 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]

  • 6.
    ; . PubMed ID:
    [No Abstract] [Full Text] [Related]

  • 7.
    ; . PubMed ID:
    [No Abstract] [Full Text] [Related]

  • 8. 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]

  • 9. 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
    [Abstract] [Full Text] [Related]

  • 10. 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
    [Abstract] [Full Text] [Related]

  • 11. 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]

  • 12. 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
    [Abstract] [Full Text] [Related]

  • 13. 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 30; 33(10):817-836. PubMed ID: 37555669
    [Abstract] [Full Text] [Related]

  • 14. 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 30; 22(3):429-38. PubMed ID: 22042768
    [Abstract] [Full Text] [Related]

  • 15. Structural basis of carbohydrate transfer activity by human UDP-GalNAc: polypeptide alpha-N-acetylgalactosaminyltransferase (pp-GalNAc-T10).
    Kubota T, Shiba T, Sugioka S, Furukawa S, Sawaki H, Kato R, Wakatsuki S, Narimatsu H.
    J Mol Biol; 2006 Jun 09; 359(3):708-27. PubMed ID: 16650853
    [Abstract] [Full Text] [Related]

  • 16. 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
    [Abstract] [Full Text] [Related]

  • 17. 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
    [Abstract] [Full Text] [Related]

  • 18. 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]

  • 19. 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 03; 13(5):849-56. PubMed ID: 8910012
    [Abstract] [Full Text] [Related]

  • 20. Dynamic interplay between catalytic and lectin domains of GalNAc-transferases modulates protein O-glycosylation.
    Lira-Navarrete E, de Las Rivas M, Compañón I, Pallarés MC, Kong Y, Iglesias-Fernández J, Bernardes GJ, Peregrina JM, Rovira C, Bernadó P, Bruscolini P, Clausen H, Lostao A, Corzana F, Hurtado-Guerrero R.
    Nat Commun; 2015 May 05; 6():6937. PubMed ID: 25939779
    [Abstract] [Full Text] [Related]

    Page: [Next] [New Search]
    of 10.