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Journal Abstract Search

183 related items for PubMed ID: 6457829

  • 1. Lysosomal enzyme targeting. N-Acetylglucosaminylphosphotransferase selectively phosphorylates native lysosomal enzymes.
    Reitman ML, Kornfeld S.
    J Biol Chem; 1981 Dec 10; 256(23):11977-80. PubMed ID: 6457829
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  • 2. Steps in the phosphorylation of the high mannose oligosaccharides of lysosomal enzymes.
    Kornfeld S, Reitman ML, Varki A, Goldberg D, Gabel CA.
    Ciba Found Symp; 1982 Dec 10; (92):138-56. PubMed ID: 6295719
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  • 3. Identification of a variant of mucolipidosis III (pseudo-Hurler polydystrophy): a catalytically active N-acetylglucosaminylphosphotransferase that fails to phosphorylate lysosomal enzymes.
    Varki AP, Reitman ML, Kornfeld S.
    Proc Natl Acad Sci U S A; 1981 Dec 10; 78(12):7773-7. PubMed ID: 6461005
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  • 5. UDP-N-acetylglucosamine:glycoprotein N-acetylglucosamine-1-phosphotransferase. Proposed enzyme for the phosphorylation of the high mannose oligosaccharide units of lysosomal enzymes.
    Reitman ML, Kornfeld S.
    J Biol Chem; 1981 May 10; 256(9):4275-81. PubMed ID: 6452459
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  • 6. Subfractionation of rat liver Golgi apparatus: separation of enzyme activities involved in the biosynthesis of the phosphomannosyl recognition marker in lysosomal enzymes.
    Deutscher SL, Creek KE, Merion M, Hirschberg CB.
    Proc Natl Acad Sci U S A; 1983 Jul 10; 80(13):3938-42. PubMed ID: 6306653
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  • 7. Processing of the phosphorylated recognition marker in lysosomal enzymes. Characterization and partial purification of a microsomal alpha-N-acetylglucosaminyl phosphodiesterase.
    Waheed A, Hasilik A, von Figura K.
    J Biol Chem; 1981 Jun 10; 256(11):5717-21. PubMed ID: 6263889
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  • 8. Characterization of UDP-N-acetylglucosamine:glycoprotein N-acetylglucosamine-1-phosphotransferase from Acanthamoeba castellanii.
    Ketcham CM, Kornfeld S.
    J Biol Chem; 1992 Jun 05; 267(16):11654-9. PubMed ID: 1317874
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  • 10. Identification of a rat liver alpha-N-acetylglucosaminyl phosphodiesterase capable of removing "blocking" alpha-N-acetylglucosamine residues from phosphorylated high mannose oligosaccharides of lysosomal enzymes.
    Varki A, Kornfeld S.
    J Biol Chem; 1980 Sep 25; 255(18):8398-401. PubMed ID: 6251056
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  • 12. Glycoprotein phosphorylation in simple eucaryotic organisms. Identification of UDP-GlcNAc:glycoprotein N-acetylglucosamine-1-phosphotransferase activity and analysis of substrate specificity.
    Lang L, Couso R, Kornfeld S.
    J Biol Chem; 1986 May 15; 261(14):6320-5. PubMed ID: 2939074
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  • 17. Bovine UDP-N-acetylglucosamine:lysosomal-enzyme N-acetylglucosamine-1-phosphotransferase. II. Enzymatic characterization and identification of the catalytic subunit.
    Bao M, Elmendorf BJ, Booth JL, Drake RR, Canfield WM.
    J Biol Chem; 1996 Dec 06; 271(49):31446-51. PubMed ID: 8940156
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  • 19. Structural requirements for efficient processing and activation of recombinant human UDP-N-acetylglucosamine:lysosomal-enzyme-N-acetylglucosamine-1-phosphotransferase.
    Kudo M, Canfield WM.
    J Biol Chem; 2006 Apr 28; 281(17):11761-8. PubMed ID: 16507578
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  • 20. [Lysosomal hydrolases have specific conformational domains for acquisition of mannose-6-phosphate].
    Himeno M, Tanaka Y.
    Nihon Rinsho; 1995 Dec 28; 53(12):2892-7. PubMed ID: 8577031
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