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Ernst, H.A., Leggio, L.L., Willemoes, M., Leonard, G., Blum, P. and Larsen, S. (2006) Structure of the Sulfolobus Solfataricus Alpha-Glucosidase: Implications for Domain Conservation and Substrate Recognition in GH31. Journal of Molecular Biology, 358, 1106-1124.
https://doi.org/10.1016/j.jmb.2006.02.056

has been cited by the following article:

• TITLE: Computational Study on the Comparative Differences in the Activity of Inhibitors of Human versus Rat Alpha-Glucosidase

  AUTHORS: Shinya Nakamura, Kazuko Shimada, Genzoh Tanabe, Osamu Muraoka, Isao Nakanishi

  KEYWORDS: Homology Modeling, MM/PBSA, Alpha-Glucosidase, Salacinol, Acarbose, Species Difference

  JOURNAL NAME: Open Journal of Medicinal Chemistry, Vol.7 No.2, June 15, 2017

  ABSTRACT: Differences between the inhibitory activities of specific compounds on analogous enzymes isolated from different animal species are one of the critical issues to evaluate when exploring structure-activity relationships. The activity of acarbose is about ten times stronger in rat than in human, and that of neosalacinol is similar in both species. Binding affinities of acarbose and neosalacinol to four catalytic domains of alpha-glucosidases in human and rat were compared to investigate the cause of activity differences among species. Species difference was brought about complicatedly by the balance of interaction with four domains, and the result was indicated that larger ligand would show larger species difference in activity.