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165 related items for PubMed ID: 12634323

  • 1. Five Lec1 CHO cell mutants have distinct Mgat1 gene mutations that encode truncated N-acetylglucosaminyltransferase I.
    Chen W, Stanley P.
    Glycobiology; 2003 Jan; 13(1):43-50. PubMed ID: 12634323
    [Abstract] [Full Text] [Related]

  • 2. Engineering novel Lec1 glycosylation mutants in CHO-DUKX cells: molecular insights and effector modulation of N-acetylglucosaminyltransferase I.
    Zhong X, Cooley C, Seth N, Juo ZS, Presman E, Resendes N, Kumar R, Allen M, Mosyak L, Stahl M, Somers W, Kriz R.
    Biotechnol Bioeng; 2012 Jul; 109(7):1723-34. PubMed ID: 22252477
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  • 3. Glycosylation defect in Lec1 Chinese hamster ovary mutant is due to a point mutation in N-acetylglucosaminyltransferase I gene.
    Puthalakath H, Burke J, Gleeson PA.
    J Biol Chem; 1996 Nov 01; 271(44):27818-22. PubMed ID: 8910379
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  • 4. Independent Lec1A CHO glycosylation mutants arise from point mutations in N-acetylglucosaminyltransferase I that reduce affinity for both substrates. Molecular consequences based on the crystal structure of GlcNAc-TI.
    Chen W, Unligil UM, Rini JM, Stanley P.
    Biochemistry; 2001 Jul 31; 40(30):8765-72. PubMed ID: 11467936
    [Abstract] [Full Text] [Related]

  • 5. Lec3 Chinese hamster ovary mutants lack UDP-N-acetylglucosamine 2-epimerase activity because of mutations in the epimerase domain of the Gne gene.
    Hong Y, Stanley P.
    J Biol Chem; 2003 Dec 26; 278(52):53045-54. PubMed ID: 14561743
    [Abstract] [Full Text] [Related]

  • 6. Cloning and expression of the murine gene and chromosomal location of the human gene encoding N-acetylglucosaminyltransferase I.
    Kumar R, Yang J, Eddy RL, Byers MG, Shows TB, Stanley P.
    Glycobiology; 1992 Aug 26; 2(4):383-93. PubMed ID: 1421759
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  • 7. Control of carbohydrate processing: the lec1A CHO mutation results in partial loss of N-acetylglucosaminyltransferase I activity.
    Stanley P, Chaney W.
    Mol Cell Biol; 1985 Jun 26; 5(6):1204-11. PubMed ID: 2993857
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  • 8. Chinese hamster ovary (CHO) cells may express six beta 4-galactosyltransferases (beta 4GalTs). Consequences of the loss of functional beta 4GalT-1, beta 4GalT-6, or both in CHO glycosylation mutants.
    Lee J, Sundaram S, Shaper NL, Raju TS, Stanley P.
    J Biol Chem; 2001 Apr 27; 276(17):13924-34. PubMed ID: 11278604
    [Abstract] [Full Text] [Related]

  • 9. Molecular analysis of three gain-of-function CHO mutants that add the bisecting GlcNAc to N-glycans.
    Stanley P, Sundaram S, Tang J, Shi S.
    Glycobiology; 2005 Jan 27; 15(1):43-53. PubMed ID: 15329358
    [Abstract] [Full Text] [Related]

  • 10. An Arabidopsis thaliana cDNA complements the N-acetylglucosaminyltransferase I deficiency of CHO Lec1 cells.
    Bakker H, Lommen A, Jordi W, Stiekema W, Bosch D.
    Biochem Biophys Res Commun; 1999 Aug 11; 261(3):829-32. PubMed ID: 10441510
    [Abstract] [Full Text] [Related]

  • 11. Transfection of a human gene that corrects the Lec1 glycosylation defect: evidence for transfer of the structural gene for N-acetylglucosaminyltransferase I.
    Kumar R, Stanley P.
    Mol Cell Biol; 1989 Dec 11; 9(12):5713-7. PubMed ID: 2531285
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  • 12. Cloning and expression of N-acetylglucosaminyltransferase I, the medial Golgi transferase that initiates complex N-linked carbohydrate formation.
    Kumar R, Yang J, Larsen RD, Stanley P.
    Proc Natl Acad Sci U S A; 1990 Dec 11; 87(24):9948-52. PubMed ID: 1702225
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  • 14. Complex asparagine-linked oligosaccharides in Mgat1-null embryos.
    Campbell RM, Metzler M, Granovsky M, Dennis JW, Marth JD.
    Glycobiology; 1995 Jul 11; 5(5):535-43. PubMed ID: 8563140
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  • 15. A point mutation causes mistargeting of Golgi GlcNAc-TV in the Lec4A Chinese hamster ovary glycosylation mutant.
    Weinstein J, Sundaram S, Wang X, Delgado D, Basu R, Stanley P.
    J Biol Chem; 1996 Nov 01; 271(44):27462-9. PubMed ID: 8910328
    [Abstract] [Full Text] [Related]

  • 16. Core fucosylation of high-mannose-type oligosaccharides in GlcNAc transferase I-deficient (Lec1) CHO cells.
    Lin AI, Philipsberg GA, Haltiwanger RS.
    Glycobiology; 1994 Dec 01; 4(6):895-901. PubMed ID: 7734851
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  • 20. Recombinant Miltenberger I and II human blood group antigens: the role of glycosylation in cell surface expression and antigenicity of glycophorin A.
    Ugorski M, Blackall DP, Påhlsson P, Shakin-Eshleman SH, Moore J, Spitalnik SL.
    Blood; 1993 Sep 15; 82(6):1913-20. PubMed ID: 8400241
    [Abstract] [Full Text] [Related]


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