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641 related items for PubMed ID: 18036614

  • 1. Human intestinal maltase-glucoamylase: crystal structure of the N-terminal catalytic subunit and basis of inhibition and substrate specificity.
    Sim L, Quezada-Calvillo R, Sterchi EE, Nichols BL, Rose DR.
    J Mol Biol; 2008 Jan 18; 375(3):782-92. PubMed ID: 18036614
    [Abstract] [Full Text] [Related]

  • 2. Study of the inhibition of two human maltase-glucoamylases catalytic domains by different α-glucosidase inhibitors.
    Ren L, Cao X, Geng P, Bai F, Bai G.
    Carbohydr Res; 2011 Dec 13; 346(17):2688-92. PubMed ID: 22036121
    [Abstract] [Full Text] [Related]

  • 3. Luminal starch substrate "brake" on maltase-glucoamylase activity is located within the glucoamylase subunit.
    Quezada-Calvillo R, Sim L, Ao Z, Hamaker BR, Quaroni A, Brayer GD, Sterchi EE, Robayo-Torres CC, Rose DR, Nichols BL.
    J Nutr; 2008 Apr 13; 138(4):685-92. PubMed ID: 18356321
    [Abstract] [Full Text] [Related]

  • 4. Structural insight into substrate specificity of human intestinal maltase-glucoamylase.
    Ren L, Qin X, Cao X, Wang L, Bai F, Bai G, Shen Y.
    Protein Cell; 2011 Oct 13; 2(10):827-36. PubMed ID: 22058037
    [Abstract] [Full Text] [Related]

  • 5. New glucosidase inhibitors from an ayurvedic herbal treatment for type 2 diabetes: structures and inhibition of human intestinal maltase-glucoamylase with compounds from Salacia reticulata.
    Sim L, Jayakanthan K, Mohan S, Nasi R, Johnston BD, Pinto BM, Rose DR.
    Biochemistry; 2010 Jan 26; 49(3):443-51. PubMed ID: 20039683
    [Abstract] [Full Text] [Related]

  • 6. Modeling of cooked starch digestion process using recombinant human pancreatic α-amylase and maltase-glucoamylase for in vitro evaluation of α-glucosidase inhibitors.
    Cao X, Zhang C, Dong Y, Geng P, Bai F, Bai G.
    Carbohydr Res; 2015 Sep 23; 414():15-21. PubMed ID: 26162745
    [Abstract] [Full Text] [Related]

  • 7. Structure of the complex of a yeast glucoamylase with acarbose reveals the presence of a raw starch binding site on the catalytic domain.
    Sevcík J, Hostinová E, Solovicová A, Gasperík J, Dauter Z, Wilson KS.
    FEBS J; 2006 May 23; 273(10):2161-71. PubMed ID: 16649993
    [Abstract] [Full Text] [Related]

  • 8. Understanding the structural basis for substrate and inhibitor recognition in eukaryotic GH11 xylanases.
    Vardakou M, Dumon C, Murray JW, Christakopoulos P, Weiner DP, Juge N, Lewis RJ, Gilbert HJ, Flint JE.
    J Mol Biol; 2008 Feb 01; 375(5):1293-305. PubMed ID: 18078955
    [Abstract] [Full Text] [Related]

  • 9. Inhibition of recombinant human maltase glucoamylase by salacinol and derivatives.
    Rossi EJ, Sim L, Kuntz DA, Hahn D, Johnston BD, Ghavami A, Szczepina MG, Kumar NS, Sterchi EE, Nichols BL, Pinto BM, Rose DR.
    FEBS J; 2006 Jun 01; 273(12):2673-83. PubMed ID: 16817895
    [Abstract] [Full Text] [Related]

  • 10. Naturally occurring sulfonium-ion glucosidase inhibitors and their derivatives: a promising class of potential antidiabetic agents.
    Mohan S, Eskandari R, Pinto BM.
    Acc Chem Res; 2014 Jan 21; 47(1):211-25. PubMed ID: 23964564
    [Abstract] [Full Text] [Related]

  • 11. Mapping the intestinal alpha-glucogenic enzyme specificities of starch digesting maltase-glucoamylase and sucrase-isomaltase.
    Jones K, Sim L, Mohan S, Kumarasamy J, Liu H, Avery S, Naim HY, Quezada-Calvillo R, Nichols BL, Pinto BM, Rose DR.
    Bioorg Med Chem; 2011 Jul 01; 19(13):3929-34. PubMed ID: 21669536
    [Abstract] [Full Text] [Related]

  • 12. Crystal structure of the polyextremophilic alpha-amylase AmyB from Halothermothrix orenii: details of a productive enzyme-substrate complex and an N domain with a role in binding raw starch.
    Tan TC, Mijts BN, Swaminathan K, Patel BK, Divne C.
    J Mol Biol; 2008 May 09; 378(4):852-70. PubMed ID: 18387632
    [Abstract] [Full Text] [Related]

  • 13. Probing the active-site requirements of human intestinal N-terminal maltase-glucoamylase: Synthesis and enzyme inhibitory activities of a six-membered ring nitrogen analogue of kotalanol and its de-O-sulfonated derivative.
    Mohan S, Sim L, Rose DR, Pinto BM.
    Bioorg Med Chem; 2010 Nov 15; 18(22):7794-8. PubMed ID: 20970346
    [Abstract] [Full Text] [Related]

  • 14. Crystal structure of a catalytic-site mutant alpha-amylase from Bacillus subtilis complexed with maltopentaose.
    Fujimoto Z, Takase K, Doui N, Momma M, Matsumoto T, Mizuno H.
    J Mol Biol; 1998 Mar 27; 277(2):393-407. PubMed ID: 9514750
    [Abstract] [Full Text] [Related]

  • 15. Structure of the Sulfolobus solfataricus alpha-glucosidase: implications for domain conservation and substrate recognition in GH31.
    Ernst HA, Lo Leggio L, Willemoës M, Leonard G, Blum P, Larsen S.
    J Mol Biol; 2006 May 12; 358(4):1106-24. PubMed ID: 16580018
    [Abstract] [Full Text] [Related]

  • 16. Crystal structures of mammalian glutamine synthetases illustrate substrate-induced conformational changes and provide opportunities for drug and herbicide design.
    Krajewski WW, Collins R, Holmberg-Schiavone L, Jones TA, Karlberg T, Mowbray SL.
    J Mol Biol; 2008 Jan 04; 375(1):217-28. PubMed ID: 18005987
    [Abstract] [Full Text] [Related]

  • 17. Structural and functional studies of the yeast class II Hda1 histone deacetylase complex.
    Lee JH, Maskos K, Huber R.
    J Mol Biol; 2009 Aug 28; 391(4):744-57. PubMed ID: 19573535
    [Abstract] [Full Text] [Related]

  • 18. Aglycone specificity of Escherichia coli alpha-xylosidase investigated by transxylosylation.
    Kang MS, Okuyama M, Yaoi K, Mitsuishi Y, Kim YM, Mori H, Kim D, Kimura A.
    FEBS J; 2007 Dec 28; 274(23):6074-84. PubMed ID: 17970751
    [Abstract] [Full Text] [Related]

  • 19. Crystal structure of the Pyrococcus horikoshii isopropylmalate isomerase small subunit provides insight into the dual substrate specificity of the enzyme.
    Yasutake Y, Yao M, Sakai N, Kirita T, Tanaka I.
    J Mol Biol; 2004 Nov 19; 344(2):325-33. PubMed ID: 15522288
    [Abstract] [Full Text] [Related]

  • 20. Crystal structures of Paenibacillus polymyxa beta-glucosidase B complexes reveal the molecular basis of substrate specificity and give new insights into the catalytic machinery of family I glycosidases.
    Isorna P, Polaina J, Latorre-García L, Cañada FJ, González B, Sanz-Aparicio J.
    J Mol Biol; 2007 Aug 31; 371(5):1204-18. PubMed ID: 17585934
    [Abstract] [Full Text] [Related]

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