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.


BIOMARKERS

Molecular Biopsy of Human Tumors

- a resource for Precision Medicine *

113 related articles for article (PubMed ID: 7757419)

  • 1. Key involvement of all three GlcNAc hydroxyl groups in the recognition of beta-D-GlcpNAc-(1-->2)-alpha-D-Manp-(1-->6)-beta-D-Glcp-OR by N-acetylglucosaminyltransferase-V.
    Kanie O; Crawley SC; Palcic MM; Hindsgaul O
    Bioorg Med Chem; 1994 Nov; 2(11):1231-41. PubMed ID: 7757419
    [TBL] [Abstract][Full Text] [Related]  

  • 2. Acceptor-substrate recognition by N-acetylglucosaminyltransferase-V: critical role of the 4"-hydroxyl group in beta-D-GlcpNAc-(1-->2)-alpha-D-Manp(1-->6)-beta-D-Glcp-OR.
    Kanie O; Crawley SC; Palcic MM; Hindsgaul O
    Carbohydr Res; 1993 Apr; 243(1):139-64. PubMed ID: 8324760
    [TBL] [Abstract][Full Text] [Related]  

  • 3. Recognition of the acceptor beta-D-GlcpNAc-(1-->2)-alpha-D-Manp- (1-->6)-beta-D-Glcp-OR by N-acetyl-glucosaminyltransferase-V: none of the hydroxyl groups on the Glc-residue are important.
    Linker T; Crawley SC; Hindsgaul O
    Carbohydr Res; 1993 Jul; 245(2):323-31. PubMed ID: 8370029
    [TBL] [Abstract][Full Text] [Related]  

  • 4. Synthesis of beta-D-GlcpNAc-(1-->2)-5a-carba-alpha-D-Man p-(1-->6)-beta-D- Glcp-O(CH2)7CH3: a reactive acceptor analog for N-acetylglucosaminyltransferase-V.
    Ogawa S; Furuya T; Tsunoda H; Hindsgaul O; Stangier K; Palcic MM
    Carbohydr Res; 1995 Jul; 271(2):197-205. PubMed ID: 7664300
    [TBL] [Abstract][Full Text] [Related]  

  • 5. UDP-N-trifluoroacetylglucosamine as an alternative substrate in N-acetylglucosaminyltransferase reactions.
    Sala RF; MacKinnon SL; Palcic MM; Tanner ME
    Carbohydr Res; 1998 Jan; 306(1-2):127-36. PubMed ID: 9691444
    [TBL] [Abstract][Full Text] [Related]  

  • 6. Combined chemical-enzymic synthesis of deoxygenated oligosaccharide analogs: transfer of deoxygenated D-GlcpNAc residues from their UDP-GlcpNAc derivatives using N-acetylglucosaminyltransferase I.
    Srivastava G; Alton G; Hindsgaul O
    Carbohydr Res; 1990 Oct; 207(2):259-76. PubMed ID: 2150183
    [TBL] [Abstract][Full Text] [Related]  

  • 7. Synthesis of Hexp-(1-->4)-beta-D-GlcpNAc-(1-->2)-alpha-D-Manp-(1-->O) (CH2)7 CH3 probes for exploration of the substrate specificity of glycosyltransferases: Part II, Hex = 3-O-methyl-beta-D-Gal, 3-deoxy-beta-D-Gal, 3-deoxy-3-fluoro-beta-D-Gal, 3-amino-3-deoxy-beta-D-Gal, beta-D-Gul, alpha-L-Alt, or beta-L-Gal.
    van Dorst JA; van Heusden CJ; Tikkanen JM; Kamerling JP; Vliegenthart JF
    Carbohydr Res; 1997 Jan; 297(3):209-27. PubMed ID: 9060187
    [TBL] [Abstract][Full Text] [Related]  

  • 8. Synthesis of tetrasaccharide analogues of the N-glycan substrate of beta-(1-->2)-N-acetylglucosaminyltransferase II using trisaccharide precursors and recombinant beta-(1-->2)-N-acetylglucosaminyltransferase I.
    Reck F; Springer M; Paulsen H; Brockhausen I; Sarkar M; Schachter H
    Carbohydr Res; 1994 Jun; 259(1):93-101. PubMed ID: 8039192
    [TBL] [Abstract][Full Text] [Related]  

  • 9. A trisaccharide acceptor analog for N-acetylglucosaminyltransferase V which binds to the enzyme but sterically precludes the transfer reaction.
    Khan SH; Crawley SC; Kanie O; Hindsgaul O
    J Biol Chem; 1993 Feb; 268(4):2468-73. PubMed ID: 8428922
    [TBL] [Abstract][Full Text] [Related]  

  • 10. The trisaccharide beta-D-GlcpNAc-(1----2)-alpha-D-Manp-(1----6)-beta-D-Manp, as its 8-methoxycarbonyloctyl glycoside, is an acceptor selective for N-acetylglucosaminyltransferase V.
    Hindsgaul O; Tahir SH; Srivastava OP; Pierce M
    Carbohydr Res; 1988 Mar; 173(2):263-72. PubMed ID: 2834054
    [TBL] [Abstract][Full Text] [Related]  

  • 11. Synthesis of a tetrasaccharide acceptor for use in the assay of UDP-GlcpNAc:beta-D-Galp-(1----4)-beta-D-GlcpNAc (GlcNAc to Gal) beta(1----3)-N-acetylglucosaminyltransferase activity and the pentasaccharide product that would be formed by its enzymic glycosylation.
    Srivastava G; Hindsgaul O
    Carbohydr Res; 1992 Feb; 224():83-93. PubMed ID: 1534275
    [TBL] [Abstract][Full Text] [Related]  

  • 12. Cloning and expression of a novel UDP-GlcNAc:alpha-D-mannoside beta1,2-N-acetylglucosaminyltransferase homologous to UDP-GlcNAc:alpha-3-D-mannoside beta1,2-N-acetylglucosaminyltransferase I.
    Zhang W; Betel D; Schachter H
    Biochem J; 2002 Jan; 361(Pt 1):153-62. PubMed ID: 11742540
    [TBL] [Abstract][Full Text] [Related]  

  • 13. Control of glycoprotein synthesis. Characterization of (1-->4)-N-acetyl-beta-D-glucosaminyltransferases acting on the alpha-D-(1-->3)- and alpha-D-(1-->6)-linked arms of N-linked oligosaccharides.
    Brockhausen I; Möller G; Yang JM; Khan SH; Matta KL; Paulsen H; Grey AA; Shah RN; Schachter H
    Carbohydr Res; 1992 Dec; 236():281-99. PubMed ID: 1291052
    [TBL] [Abstract][Full Text] [Related]  

  • 14. Control of glycoprotein synthesis: substrate specificity of rat liver UDP-GlcNAc:Man alpha 3R beta 2-N-acetylglucosaminyltransferase I using synthetic substrate analogues.
    Möller G; Reck F; Paulsen H; Kaur KJ; Sarkar M; Schachter H; Brockhausen I
    Glycoconj J; 1992 Aug; 9(4):180-90. PubMed ID: 1422138
    [TBL] [Abstract][Full Text] [Related]  

  • 15. The substrate specificity of the snail Lymnaea stagnalis UDP-GlcNAc:GlcNAc beta-R beta 4-N-acetylglucosaminyltransferase reveals a novel variant pathway of complex-type oligosaccharide synthesis.
    Bakker H; Schoenmakers PS; Koeleman CA; Joziasse DH; van Die I; van den Eijnden DH
    Glycobiology; 1997 Jun; 7(4):539-48. PubMed ID: 9184835
    [TBL] [Abstract][Full Text] [Related]  

  • 16. Combined chemical-enzymic synthesis of a dideoxypentasaccharide for use in a study of the specificity of N-acetyl-glucosaminyltransferase-III.
    Kaur KJ; Hindsgaul O
    Carbohydr Res; 1992 Mar; 226(2):219-31. PubMed ID: 1535553
    [TBL] [Abstract][Full Text] [Related]  

  • 17. A fluorescent assay for the determination of UDP-GlcNAc: Gal beta 1,3GalNAc-R (GlcNAc to GalNAc) beta 1,6-N-acetylglucosaminyltransferase activity.
    Palmerini CA; Datti A; Alunni S; VanderElst IE; Orlacchio A
    Anal Biochem; 1995 Mar; 225(2):315-20. PubMed ID: 7762797
    [TBL] [Abstract][Full Text] [Related]  

  • 18. Control of glycoprotein synthesis. Detection and characterization of a novel branching enzyme from hen oviduct, UDP-N-acetylglucosamine:GlcNAc beta 1-6 (GlcNAc beta 1-2)Man alpha-R (GlcNAc to Man) beta-4-N-acetylglucosaminyltransferase VI.
    Brockhausen I; Hull E; Hindsgaul O; Schachter H; Shah RN; Michnick SW; Carver JP
    J Biol Chem; 1989 Jul; 264(19):11211-21. PubMed ID: 2525556
    [TBL] [Abstract][Full Text] [Related]  

  • 19. Control of glycoprotein synthesis. IX. A terminal Man alpha l-3Man beta 1- sequence in the substrate is the minimum requirement for UDP-N-acetyl-D-glucosamine: alpha-D-mannoside (GlcNAc to Man alpha 1-3) beta 2-N-acetylglucosaminyltransferase I.
    Vella GJ; Paulsen H; Schachter H
    Can J Biochem Cell Biol; 1984 Jun; 62(6):409-17. PubMed ID: 6235906
    [TBL] [Abstract][Full Text] [Related]  

  • 20. Synthetic substrate analogues for UDP-GlcNAc: Man alpha 1-6R beta(1-2)-N-acetylglucosaminyltransferase II. Substrate specificity and inhibitors for the enzyme.
    Reck F; Meinjohanns E; Springer M; Wilkens R; Van Dorst JA; Paulsen H; Möller G; Brockhausen I; Schachter H
    Glycoconj J; 1994 Jun; 11(3):210-6. PubMed ID: 7841796
    [TBL] [Abstract][Full Text] [Related]  

    [Next]    [New Search]
    of 6.