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Volumn 47, Issue 1, 2014, Pages 211-225

Naturally occurring sulfonium-ion glucosidase inhibitors and their derivatives: A promising class of potential antidiabetic agents

Author keywords

[No Author keywords available]

Indexed keywords

ANTIDIABETIC AGENT; BIOLOGICAL PRODUCT; ENZYME INHIBITOR; GLUCOSIDASE; SULFUR DERIVATIVE;

EID: 84892687860     PISSN: 00014842     EISSN: 15204898     Source Type: Journal    
DOI: 10.1021/ar400132g     Document Type: Article
Times cited : (57)

References (53)
  • 1
    • 0033046464 scopus 로고    scopus 로고
    • A randomized double-blind trial of acarbose in type 2 diabetes shows improved glycemic control over 3 years (UK Prospective Diabetes Study 44)
    • Holman, R. R.; Cull, C. A.; Turner, R. C. A randomized double-blind trial of acarbose in type 2 diabetes shows improved glycemic control over 3 years (UK Prospective Diabetes Study 44) Diabetes Care 1999, 22, 960-964
    • (1999) Diabetes Care , vol.22 , pp. 960-964
    • Holman, R.R.1    Cull, C.A.2    Turner, R.C.3
  • 2
    • 13644263258 scopus 로고    scopus 로고
    • Oral antidiabetic agents - Current role in type 2 diabetes mellitus
    • Krentz, A. J.; Bailey, C. J. Oral antidiabetic agents-Current role in type 2 diabetes mellitus Drugs 2005, 65, 385-411
    • (2005) Drugs , vol.65 , pp. 385-411
    • Krentz, A.J.1    Bailey, C.J.2
  • 3
    • 0032943750 scopus 로고    scopus 로고
    • Drug therapy of postprandial hyperglycaemia
    • Mooradian, A. D.; Thurman, J. E. Drug therapy of postprandial hyperglycaemia Drugs 1999, 57, 19-29
    • (1999) Drugs , vol.57 , pp. 19-29
    • Mooradian, A.D.1    Thurman, J.E.2
  • 5
    • 0017519344 scopus 로고
    • Action pattern of human salivary alpha- amylases in vicinity of branch points of amylopectin
    • Abdullah, M.; Whelan, W. J.; Catley, B. J. Action pattern of human salivary alpha- amylases in vicinity of branch points of amylopectin Carbohydr. Res. 1977, 57, 281-289
    • (1977) Carbohydr. Res. , vol.57 , pp. 281-289
    • Abdullah, M.1    Whelan, W.J.2    Catley, B.J.3
  • 6
    • 0034712653 scopus 로고    scopus 로고
    • Subsite mapping of the human pancreatic alpha-amylase active site through structural, kinetic, and mutagenesis techniques
    • Brayer, G. D.; Sidhu, G.; Maurus, R.; Rydberg, E. H.; Braun, C.; Wang, Y. L.; Nguyen, N. T.; Overall, C. H.; Withers, S. G. Subsite mapping of the human pancreatic alpha-amylase active site through structural, kinetic, and mutagenesis techniques Biochemistry 2000, 39, 4778-4791
    • (2000) Biochemistry , vol.39 , pp. 4778-4791
    • Brayer, G.D.1    Sidhu, G.2    Maurus, R.3    Rydberg, E.H.4    Braun, C.5    Wang, Y.L.6    Nguyen, N.T.7    Overall, C.H.8    Withers, S.G.9
  • 7
    • 37449009082 scopus 로고    scopus 로고
    • 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, E. E.; Nichols, B. L.; Rose, D. R. Human intestinal maltase-glucoamylase: Crystal structure of the N -terminal catalytic subunit and basis of inhibition and substrate specificity J. Mol. Biol. 2008, 375, 782-792
    • (2008) J. Mol. Biol. , vol.375 , pp. 782-792
    • Sim, L.1    Quezada-Calvillo, R.2    Sterchi, E.E.3    Nichols, B.L.4    Rose, D.R.5
  • 8
    • 0014443148 scopus 로고
    • Column chromatography of human small-intestinal maltase isomaltase and invertase activities
    • Dahlqvist, A.; Telenius, U. Column chromatography of human small-intestinal maltase isomaltase and invertase activities Biochem. J. 1969, 111, 139-146
    • (1969) Biochem. J. , vol.111 , pp. 139-146
    • Dahlqvist, A.1    Telenius, U.2
  • 9
    • 0014545169 scopus 로고
    • Hydrolysis of the naturally-occurring alpha-glucosides by the human intestinal mucosa
    • Eggermon, E. Hydrolysis of the naturally-occurring alpha-glucosides by the human intestinal mucosa Eur. J. Biochem. 1969, 9, 483-487
    • (1969) Eur. J. Biochem. , vol.9 , pp. 483-487
    • Eggermon, E.1
  • 13
    • 0022455206 scopus 로고
    • Synthesis and alpha-D-glucosidase inhibitory activity of N -substituted valiolamine derivatives as potential oral antidiabetic agents
    • Horii, S.; Fukase, H.; Matsuo, T.; Kameda, Y.; Asano, N.; Matsui, K. Synthesis and alpha-D-glucosidase inhibitory activity of N -substituted valiolamine derivatives as potential oral antidiabetic agents J. Med. Chem. 1986, 29, 1038-1046
    • (1986) J. Med. Chem. , vol.29 , pp. 1038-1046
    • Horii, S.1    Fukase, H.2    Matsuo, T.3    Kameda, Y.4    Asano, N.5    Matsui, K.6
  • 14
    • 36749059401 scopus 로고    scopus 로고
    • Who should benefit from the use of alpha-glucosidase inhibitors?
    • Godbout, A.; Chiasson, J.-L. Who should benefit from the use of alpha-glucosidase inhibitors? Curr. Diabetes Rep. 2007, 7, 333-339
    • (2007) Curr. Diabetes Rep. , vol.7 , pp. 333-339
    • Godbout, A.1    Chiasson, J.-L.2
  • 15
    • 0033385213 scopus 로고    scopus 로고
    • Antidiabetic principles of natural medicines. IV. Aldose reductase and alpha-glucosidase inhibitors from the roots of Salacia oblonga WALL-(Celastraceae): Structure of a new friedelane-type triterpene, kotalagenin 16-acetate
    • Matsuda, H.; Murakami, T.; Yashiro, K.; Yamahara, J.; Yoshikawa, M. Antidiabetic principles of natural medicines. IV. Aldose reductase and alpha-glucosidase inhibitors from the roots of Salacia oblonga WALL-(Celastraceae): Structure of a new friedelane-type triterpene, kotalagenin 16-acetate Chem. Pharm. Bull. 1999, 47, 1725-1729
    • (1999) Chem. Pharm. Bull. , vol.47 , pp. 1725-1729
    • Matsuda, H.1    Murakami, T.2    Yashiro, K.3    Yamahara, J.4    Yoshikawa, M.5
  • 19
    • 0030670829 scopus 로고    scopus 로고
    • Salacinol, potent antidiabetic principle with unique thiosugar sulfonium sulfate structure from the ayurvedic traditional medicine Salacia reticulata in Sri Lanka and India
    • Yoshikawa, M.; Murakami, T.; Shimada, H.; Matsuda, H.; Yamahara, J.; Tanabe, G.; Muraoka, O. Salacinol, potent antidiabetic principle with unique thiosugar sulfonium sulfate structure from the ayurvedic traditional medicine Salacia reticulata in Sri Lanka and India Tetrahedron Lett. 1997, 38, 8367-8370
    • (1997) Tetrahedron Lett. , vol.38 , pp. 8367-8370
    • Yoshikawa, M.1    Murakami, T.2    Shimada, H.3    Matsuda, H.4    Yamahara, J.5    Tanabe, G.6    Muraoka, O.7
  • 20
    • 0031722553 scopus 로고    scopus 로고
    • Kotalanol, a potent alpha- glucosidase inhibitor with thiosugar sulfonium sulfate structure, from antidiabetic ayurvedic medicine Salacia reticulata
    • Yoshikawa, M.; Murakami, T.; Yashiro, K.; Matsuda, H. Kotalanol, a potent alpha- glucosidase inhibitor with thiosugar sulfonium sulfate structure, from antidiabetic ayurvedic medicine Salacia reticulata Chem. Pharm. Bull. 1998, 46, 1339-1340
    • (1998) Chem. Pharm. Bull. , vol.46 , pp. 1339-1340
    • Yoshikawa, M.1    Murakami, T.2    Yashiro, K.3    Matsuda, H.4
  • 21
    • 32144447412 scopus 로고    scopus 로고
    • Synthesis of sulfonium sulfate analogues of disaccharides and their conversion to chain-extended homologues of salacinol: New glycosidase inhibitors
    • Johnston, B. D.; Jensen, H. H.; Pinto, B. M. Synthesis of sulfonium sulfate analogues of disaccharides and their conversion to chain-extended homologues of salacinol: New glycosidase inhibitors J. Org. Chem. 2006, 71, 1111-1118
    • (2006) J. Org. Chem. , vol.71 , pp. 1111-1118
    • Johnston, B.D.1    Jensen, H.H.2    Pinto, B.M.3
  • 22
    • 48049115030 scopus 로고    scopus 로고
    • Salaprinol and ponkoranol with thiosugar sulfonium sulfate structure from Salacia prinoides and alpha-glucosidase inhibitory activity of ponkoranol and kotalanol desulfate
    • Yoshikawa, M.; Xu, F. M.; Nakamura, S.; Wang, T.; Matsuda, H.; Tanabe, G.; Muraoka, O. Salaprinol and ponkoranol with thiosugar sulfonium sulfate structure from Salacia prinoides and alpha-glucosidase inhibitory activity of ponkoranol and kotalanol desulfate Heterocycles 2008, 75, 1397-1405
    • (2008) Heterocycles , vol.75 , pp. 1397-1405
    • Yoshikawa, M.1    Xu, F.M.2    Nakamura, S.3    Wang, T.4    Matsuda, H.5    Tanabe, G.6    Muraoka, O.7
  • 24
    • 63149148929 scopus 로고    scopus 로고
    • Facile synthesis of de- O -sulfated salacinols: Revision of the structure of neosalacinol, a potent alpha-glucosidase inhibitor
    • Tanabe, G.; Xie, W. J.; Ogawa, A.; Cao, C. N.; Minematsu, T.; Yoshikawa, M.; Muraoka, O. Facile synthesis of de- O -sulfated salacinols: Revision of the structure of neosalacinol, a potent alpha-glucosidase inhibitor Bioorg. Med. Chem. Lett. 2009, 19, 2195-2198
    • (2009) Bioorg. Med. Chem. Lett. , vol.19 , pp. 2195-2198
    • Tanabe, G.1    Xie, W.J.2    Ogawa, A.3    Cao, C.N.4    Minematsu, T.5    Yoshikawa, M.6    Muraoka, O.7
  • 25
    • 67849111626 scopus 로고    scopus 로고
    • Structure proof and synthesis of kotalanol and de- O -sulfonated kotalanol, glycosidase inhibitors isolated from an herbal remedy for the treatment of type-2 diabetes
    • Jayakanthan, K.; Mohan, S.; Pinto, B. M. Structure proof and synthesis of kotalanol and de- O -sulfonated kotalanol, glycosidase inhibitors isolated from an herbal remedy for the treatment of type-2 diabetes J. Am. Chem. Soc. 2009, 131, 5621-5626
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 5621-5626
    • Jayakanthan, K.1    Mohan, S.2    Pinto, B.M.3
  • 26
    • 47549112929 scopus 로고    scopus 로고
    • Alpha-glucosidase inhibitor from Kothala-himbutu (Salacia reticulata WIGHT)
    • Ozaki, S.; Oe, H.; Kitamura, S. Alpha-glucosidase inhibitor from Kothala-himbutu (Salacia reticulata WIGHT) J. Nat. Prod. 2008, 71, 981-984
    • (2008) J. Nat. Prod. , vol.71 , pp. 981-984
    • Ozaki, S.1    Oe, H.2    Kitamura, S.3
  • 27
    • 55049117553 scopus 로고    scopus 로고
    • On the structure of the bioactive constituent from ayurvedic medicine Salacia reticulata: Revision of the literature
    • Muraoka, O.; Xie, W. J.; Tanabe, G.; Amer, M. F. A.; Minematsu, T.; Yoshikawa, M. On the structure of the bioactive constituent from ayurvedic medicine Salacia reticulata: revision of the literature Tetrahedron Lett. 2008, 49, 7315-7317
    • (2008) Tetrahedron Lett. , vol.49 , pp. 7315-7317
    • Muraoka, O.1    Xie, W.J.2    Tanabe, G.3    Amer, M.F.A.4    Minematsu, T.5    Yoshikawa, M.6
  • 28
    • 77950237373 scopus 로고    scopus 로고
    • Potent glucosidase inhibitors: De- O -sulfonated ponkoranol and its stereoisomer
    • Eskandari, R.; Kuntz, D. A.; Rose, D. R.; Pinto, B. M. Potent glucosidase inhibitors: De- O -sulfonated ponkoranol and its stereoisomer Org. Lett. 2010, 12, 1632-1635
    • (2010) Org. Lett. , vol.12 , pp. 1632-1635
    • Eskandari, R.1    Kuntz, D.A.2    Rose, D.R.3    Pinto, B.M.4
  • 29
    • 79952438320 scopus 로고    scopus 로고
    • Isolation, structure identification and SAR studies on thiosugar sulfonium salts, neosalaprinol and neoponkoranol, as potent alpha- glucosidase inhibitors
    • Xie, W. J.; Tanabe, G.; Akaki, J.; Morikawa, T.; Ninomiya, K.; Minematsu, T.; Yoshikawa, M.; Wu, X. M.; Muraoka, O. Isolation, structure identification and SAR studies on thiosugar sulfonium salts, neosalaprinol and neoponkoranol, as potent alpha- glucosidase inhibitors Bioorg. Med. Chem. 2011, 19, 2015-2022
    • (2011) Bioorg. Med. Chem. , vol.19 , pp. 2015-2022
    • Xie, W.J.1    Tanabe, G.2    Akaki, J.3    Morikawa, T.4    Ninomiya, K.5    Minematsu, T.6    Yoshikawa, M.7    Wu, X.M.8    Muraoka, O.9
  • 30
    • 34447326170 scopus 로고    scopus 로고
    • Zwitterionic glycosidase inhibitors: Salacinol and related analogues
    • Mohan, S.; Pinto, B. M. Zwitterionic glycosidase inhibitors: salacinol and related analogues Carbohydr. Res. 2007, 342, 1551-1580
    • (2007) Carbohydr. Res. , vol.342 , pp. 1551-1580
    • Mohan, S.1    Pinto, B.M.2
  • 31
    • 77950186186 scopus 로고    scopus 로고
    • Towards the elusive structure of kotalanol, a naturally occurring glucosidase inhibitor
    • Mohan, S.; Pinto, B. M. Towards the elusive structure of kotalanol, a naturally occurring glucosidase inhibitor Nat. Prod. Rep. 2010, 27, 481-488
    • (2010) Nat. Prod. Rep. , vol.27 , pp. 481-488
    • Mohan, S.1    Pinto, B.M.2
  • 32
    • 72149126916 scopus 로고    scopus 로고
    • Sulfonium-ion glycosidase inhibitors isolated from Salacia species used in traditional medicine, and related compouds
    • Mohan, S.; Pinto, B. M. Sulfonium-ion glycosidase inhibitors isolated from Salacia species used in traditional medicine, and related compouds Collect. Czech. Chem. Commun. 2009, 74, 1117-1136
    • (2009) Collect. Czech. Chem. Commun. , vol.74 , pp. 1117-1136
    • Mohan, S.1    Pinto, B.M.2
  • 33
    • 84885925040 scopus 로고    scopus 로고
    • Research progress of synthesis and structure-activity relationship studies on sulfonium-type -glucosidase inhibitors isolated from salacia genus plants
    • Xie, W.; Tanabe, G.; Xu, J.; Wu, X.; Morikawa, T.; Yoshikawa, M.; Muraoka, O. Research progress of synthesis and structure-activity relationship studies on sulfonium-type -glucosidase inhibitors isolated from salacia genus plants Mini-Rev. Org. Chem. 2013, 10, 141-159
    • (2013) Mini-Rev. Org. Chem. , vol.10 , pp. 141-159
    • Xie, W.1    Tanabe, G.2    Xu, J.3    Wu, X.4    Morikawa, T.5    Yoshikawa, M.6    Muraoka, O.7
  • 34
    • 77951135182 scopus 로고    scopus 로고
    • Characteristic alkaline catalyzed degradation of kotalanol, a potent alpha-glucosidase inhibitor isolated from ayurvedic traditional medicine Salacia reticulata, leading to anhydroheptitols: Another structural proof
    • Muraoka, O.; Xie, W. J.; Osaki, S.; Kagawa, A.; Tanabe, G.; Amer, M. F. A.; Minematsu, T.; Morikawa, T.; Yoshikawa, M. Characteristic alkaline catalyzed degradation of kotalanol, a potent alpha-glucosidase inhibitor isolated from ayurvedic traditional medicine Salacia reticulata, leading to anhydroheptitols: another structural proof Tetrahedron 2010, 66, 3717-3722
    • (2010) Tetrahedron , vol.66 , pp. 3717-3722
    • Muraoka, O.1    Xie, W.J.2    Osaki, S.3    Kagawa, A.4    Tanabe, G.5    Amer, M.F.A.6    Minematsu, T.7    Morikawa, T.8    Yoshikawa, M.9
  • 35
    • 77950518862 scopus 로고    scopus 로고
    • Synthesis of a biologically active isomer of kotalanol, a naturally occurring glucosidase inhibitor
    • Eskandari, R.; Jayakanthan, K.; Kuntz, D. A.; Rose, D. R.; Pinto, B. M. Synthesis of a biologically active isomer of kotalanol, a naturally occurring glucosidase inhibitor Bioorg. Med. Chem. 2010, 18, 2829-2835
    • (2010) Bioorg. Med. Chem. , vol.18 , pp. 2829-2835
    • Eskandari, R.1    Jayakanthan, K.2    Kuntz, D.A.3    Rose, D.R.4    Pinto, B.M.5
  • 36
    • 74949102237 scopus 로고    scopus 로고
    • 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, B. D.; Pinto, B. M.; Rose, D. R. 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 Biochemistry 2010, 49, 443-451
    • (2010) Biochemistry , vol.49 , pp. 443-451
    • Sim, L.1    Jayakanthan, K.2    Mohan, S.3    Nasi, R.4    Johnston, B.D.5    Pinto, B.M.6    Rose, D.R.7
  • 37
    • 50149117541 scopus 로고    scopus 로고
    • Studies directed toward the stereochemical structure determination of the naturally occurring glucosidase inhibitor, kotalanol: Synthesis and inhibitory activities against human maltase glucoamylase of seven-carbon, chain-extended homologues of salacinol
    • Nasi, R.; Patrick, B. O.; Sim, L.; Rose, D. R.; Pinto, B. M. Studies directed toward the stereochemical structure determination of the naturally occurring glucosidase inhibitor, kotalanol: Synthesis and inhibitory activities against human maltase glucoamylase of seven-carbon, chain-extended homologues of salacinol J. Org. Chem. 2008, 73, 6172-6181
    • (2008) J. Org. Chem. , vol.73 , pp. 6172-6181
    • Nasi, R.1    Patrick, B.O.2    Sim, L.3    Rose, D.R.4    Pinto, B.M.5
  • 38
    • 77749298218 scopus 로고    scopus 로고
    • Synthesis and biological evaluation of heteroanalogues of kotalanol and de- O -sulfonated kotalanol
    • Mohan, S.; Jayakanthan, K.; Nasi, R.; Kuntz, D. A.; Rose, D. R.; Pinto, B. M. Synthesis and biological evaluation of heteroanalogues of kotalanol and de- O -sulfonated kotalanol Org. Lett. 2010, 12, 1088-1091
    • (2010) Org. Lett. , vol.12 , pp. 1088-1091
    • Mohan, S.1    Jayakanthan, K.2    Nasi, R.3    Kuntz, D.A.4    Rose, D.R.5    Pinto, B.M.6
  • 39
    • 78449237092 scopus 로고    scopus 로고
    • 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, D. R.; Pinto, B. M. 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 Bioorg. Med. Chem. 2010, 18, 7794-7798
    • (2010) Bioorg. Med. Chem. , vol.18 , pp. 7794-7798
    • Mohan, S.1    Sim, L.2    Rose, D.R.3    Pinto, B.M.4
  • 40
    • 79953186418 scopus 로고    scopus 로고
    • Role of the side chain stereochemistry in the α-glucosidase inhibitory activity of kotalanol, a potent natural α-glucosidase inhibitor
    • Xie, W.; Tanabe, G.; Matsuoka, K.; Amer, M. F. A.; Minematsu, T.; Wu, X.; Yoshikawa, M.; Muraoka, O. Role of the side chain stereochemistry in the α-glucosidase inhibitory activity of kotalanol, a potent natural α-glucosidase inhibitor Bioorg. Med. Chem. 2011, 19, 2252-2262
    • (2011) Bioorg. Med. Chem. , vol.19 , pp. 2252-2262
    • Xie, W.1    Tanabe, G.2    Matsuoka, K.3    Amer, M.F.A.4    Minematsu, T.5    Wu, X.6    Yoshikawa, M.7    Muraoka, O.8
  • 42
    • 79960987709 scopus 로고    scopus 로고
    • The effect of heteroatom substitution of sulfur for selenium in glucosidase inhibitors on intestinal alpha-glucosidase activities
    • Eskandari, R.; Jones, K.; Rose, D. R.; Pinto, B. M. The effect of heteroatom substitution of sulfur for selenium in glucosidase inhibitors on intestinal alpha-glucosidase activities Chem. Commun. 2011, 47, 9134-9136
    • (2011) Chem. Commun. , vol.47 , pp. 9134-9136
    • Eskandari, R.1    Jones, K.2    Rose, D.R.3    Pinto, B.M.4
  • 44
    • 77952939601 scopus 로고    scopus 로고
    • Structural basis for substrate selectivity in human maltase-glucoamylase and sucrase-isomaltase N-terminal domains
    • Sim, L.; Willemsma, C.; Mohan, S.; Naim, H. Y.; Pinto, B. M.; Rose, D. R. Structural basis for substrate selectivity in human maltase-glucoamylase and sucrase-isomaltase N-terminal domains J. Biol. Chem. 2010, 285, 17763-17770
    • (2010) J. Biol. Chem. , vol.285 , pp. 17763-17770
    • Sim, L.1    Willemsma, C.2    Mohan, S.3    Naim, H.Y.4    Pinto, B.M.5    Rose, D.R.6
  • 45
    • 37349047777 scopus 로고    scopus 로고
    • Structure and evolution of the mammalian maltase-glucoamylase and sucrase-isomaltase genes
    • Naumoff, D. G. Structure and evolution of the mammalian maltase-glucoamylase and sucrase-isomaltase genes Mol. Biol. 2007, 41, 962-973
    • (2007) Mol. Biol. , vol.41 , pp. 962-973
    • Naumoff, D.G.1
  • 46
    • 77957606215 scopus 로고    scopus 로고
    • Probing the active-site requirements of human intestinal N-terminal maltase glucoamylase: The effect of replacing the sulfate moiety by a methyl ether in ponkoranol, a naturally occurring alpha-glucosidase inhibitor
    • Eskandari, R.; Jones, K.; Rose, D. R.; Pinto, B. M. Probing the active-site requirements of human intestinal N-terminal maltase glucoamylase: The effect of replacing the sulfate moiety by a methyl ether in ponkoranol, a naturally occurring alpha-glucosidase inhibitor Bioorg. Med. Chem. Lett. 2010, 20, 5686-5689
    • (2010) Bioorg. Med. Chem. Lett. , vol.20 , pp. 5686-5689
    • Eskandari, R.1    Jones, K.2    Rose, D.R.3    Pinto, B.M.4
  • 47
    • 80054777640 scopus 로고    scopus 로고
    • Selectivity of 3′- O -methylponkoranol for inhibition of N- and C-terminal maltase glucoamylase and sucrase isomaltase, potential therapeutics for digestive disorders or their sequelae
    • Eskandari, R.; Jones, K.; Rose, D. R.; Pinto, B. M. Selectivity of 3′- O -methylponkoranol for inhibition of N- and C-terminal maltase glucoamylase and sucrase isomaltase, potential therapeutics for digestive disorders or their sequelae Bioorg. Med. Chem. Lett. 2011, 21, 6491-6494
    • (2011) Bioorg. Med. Chem. Lett. , vol.21 , pp. 6491-6494
    • Eskandari, R.1    Jones, K.2    Rose, D.R.3    Pinto, B.M.4
  • 48
    • 79955558036 scopus 로고    scopus 로고
    • Biological evaluation of 3′- O -alkylated analogs of salacinol, the role of hydrophobic alkyl group at 3′ position in the side chain on the alpha-glucosidase inhibitory activity
    • Tanabe, G.; Otani, T.; Cong, W. Y.; Minematsu, T.; Ninomiya, K.; Yoshikawa, M.; Muraoka, O. Biological evaluation of 3′- O -alkylated analogs of salacinol, the role of hydrophobic alkyl group at 3′ position in the side chain on the alpha-glucosidase inhibitory activity Bioorg. Med. Chem. Lett. 2011, 21, 3159-3162
    • (2011) Bioorg. Med. Chem. Lett. , vol.21 , pp. 3159-3162
    • Tanabe, G.1    Otani, T.2    Cong, W.Y.3    Minematsu, T.4    Ninomiya, K.5    Yoshikawa, M.6    Muraoka, O.7
  • 49
    • 84864612064 scopus 로고    scopus 로고
    • In silico design, synthesis and evaluation of 3′- O -benzylated analogs of salacinol, a potent alpha- glucosidase inhibitor isolated from an ayurvedic traditional medicine " Salacia "
    • Tanabe, G.; Nakamura, S.; Tsutsui, N.; Balakishan, G.; Xie, W.; Tsuchiya, S.; Akaki, J.; Morikawa, T.; Ninomiya, K.; Nakanishi, I.; Yoshikawa, M.; Muraoka, O. In silico design, synthesis and evaluation of 3′- O -benzylated analogs of salacinol, a potent alpha- glucosidase inhibitor isolated from an ayurvedic traditional medicine " Salacia " Chem. Commun. 2012, 48, 8646-8648
    • (2012) Chem. Commun. , vol.48 , pp. 8646-8648
    • Tanabe, G.1    Nakamura, S.2    Tsutsui, N.3    Balakishan, G.4    Xie, W.5    Tsuchiya, S.6    Akaki, J.7    Morikawa, T.8    Ninomiya, K.9    Nakanishi, I.10    Yoshikawa, M.11    Muraoka, O.12
  • 50
    • 80955157951 scopus 로고    scopus 로고
    • Structural insight into substrate specificity of human intestinal maltase-glucoamylase
    • Ren, L.; Qin, X.; Cao, X.; Wang, L.; Bai, F.; Bai, G.; Shen, Y. Structural insight into substrate specificity of human intestinal maltase-glucoamylase Protein Cell 2011, 2, 827-836
    • (2011) Protein Cell , vol.2 , pp. 827-836
    • Ren, L.1    Qin, X.2    Cao, X.3    Wang, L.4    Bai, F.5    Bai, G.6    Shen, Y.7
  • 51
    • 83755219909 scopus 로고    scopus 로고
    • Probing the intestinal alpha-glucosidase enzyme specificities of starch-digesting maltase-glucoamylase and sucrase-isomaltase: Synthesis and inhibitory properties of 3′- and 5′-maltose-extended de- O -sulfonated ponkoranol
    • Eskandari, R.; Jones, K.; Reddy, K. R.; Jayakanthan, K.; Chaudet, M.; Rose, D. R.; Pinto, B. M. Probing the intestinal alpha-glucosidase enzyme specificities of starch-digesting maltase-glucoamylase and sucrase-isomaltase: Synthesis and inhibitory properties of 3′- and 5′-maltose-extended de- O -sulfonated ponkoranol Chem. Eur. J. 2011, 17, 14817-14825
    • (2011) Chem. Eur. J. , vol.17 , pp. 14817-14825
    • Eskandari, R.1    Jones, K.2    Reddy, K.R.3    Jayakanthan, K.4    Chaudet, M.5    Rose, D.R.6    Pinto, B.M.7
  • 53
    • 71449128235 scopus 로고    scopus 로고
    • Slowly digestible starch: Concept, mechanism, and proposed extended glycemic index
    • Zhang, G. Y.; Hamaker, B. R. Slowly digestible starch: Concept, mechanism, and proposed extended glycemic index Crit. Rev. Food Sci. Nutr. 2009, 49, 852-867
    • (2009) Crit. Rev. Food Sci. Nutr. , vol.49 , pp. 852-867
    • Zhang, G.Y.1    Hamaker, B.R.2


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