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127 related items for PubMed ID: 1596914

  • 1. Photolabile derivatives of maltose and maltotriose as ligands for the affinity labelling of the maltodextrin-binding site in porcine pancreatic alpha-amylase.
    Blanc-Muesser M, Driguez H, Lehmann J, Steck J.
    Carbohydr Res; 1992 Jan; 223():129-36. PubMed ID: 1596914
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  • 2. Strong competitive inhibition of porcine pancreatic alpha-amylase by aminodeoxy derivatives of maltose and maltotriose.
    Lehmann J, Schmidt-Schuchardt M, Steck J.
    Carbohydr Res; 1992 Dec 31; 237():177-83. PubMed ID: 1294292
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  • 4. Spacer-modified disaccharide and pseudo-trisaccharide methyl glycosides that mimic maltotriose, as competitive inhibitors for pancreatic alpha-amylase: a demonstration of the "clustering effect".
    Blanc-Muesser M, Vigne L, Driguez H, Lehmann J, Steck J, Urbahns K.
    Carbohydr Res; 1992 Feb 07; 224():59-71. PubMed ID: 1591772
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  • 6. Spacer-modified, photolabile tetrasaccharides as analogues of maltopentaose are versatile probes for porcine pancreatic alpha-amylase.
    Lehmann J, Ziser L.
    Carbohydr Res; 1992 Feb 17; 225(1):83-97. PubMed ID: 1633607
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  • 10. Subsite mapping of the human pancreatic alpha-amylase active site through structural, kinetic, and mutagenesis techniques.
    Brayer GD, Sidhu G, Maurus R, Rydberg EH, Braun C, Wang Y, Nguyen NT, Overall CM, Withers SG.
    Biochemistry; 2000 Apr 25; 39(16):4778-91. PubMed ID: 10769135
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  • 13. The high maltose-producing alpha-amylase of the thermophilic actinomycete, Thermomonospora curvata.
    Collins BS, Kelly CT, Fogarty WM, Doyle EM.
    Appl Microbiol Biotechnol; 1993 Apr 25; 39(1):31-5. PubMed ID: 7763549
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  • 15. Carbohydrate and protein-based inhibitors of porcine pancreatic alpha-amylase: structure analysis and comparison of their binding characteristics.
    Machius M, Vértesy L, Huber R, Wiegand G.
    J Mol Biol; 1996 Jul 19; 260(3):409-21. PubMed ID: 8757803
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  • 16. Spacer-modified oligosaccharides as photoaffinity probes for porcine pancreatic alpha-amylase.
    Lehmann J, Schmidt-Schuchardt M.
    Methods Enzymol; 1994 Jul 19; 247():265-88. PubMed ID: 7898358
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  • 17. Studies of the interaction of the maltose-binding protein of Escherichia coli, a closed-groove binder, with 4,6-O-ethylidenemalto-oligosaccharides (dp 2-5) and its regioselective labelling with 3-azibutyl 1-thio-alpha-(6-3H)maltoside.
    Lehmann J, Schiltz E, Steck J.
    Carbohydr Res; 1992 Jul 20; 232(1):77-87. PubMed ID: 1423352
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