-
1
-
-
0033046464
-
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
-
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
-
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
-
4
-
-
0029035072
-
Intestinal brush-border glycohydrolases - Structure, function and development
-
Vanbeers, E. H.; Buller, H. A.; Grand, R. J.; Einerhand, A. W. C.; Dekker, J. Intestinal brush-border glycohydrolases-Structure, function and development Crit. Rev. Biochem. Mol. Biol. 1995, 30, 197-262
-
(1995)
Crit. Rev. Biochem. Mol. Biol.
, vol.30
, pp. 197-262
-
-
Vanbeers, E.H.1
Buller, H.A.2
Grand, R.J.3
Einerhand, A.W.C.4
Dekker, J.5
-
5
-
-
0017519344
-
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
-
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
-
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
-
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
-
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
-
10
-
-
41549159900
-
Luminal starch substrate "brake" on maltase-glucoamylase activity is located within the glucoamylase subunit
-
Quezada-Calvillo, R.; Sim, L.; Ao, Z. H.; Hamaker, B. R.; Quaroni, A.; Brayer, G. D.; Sterchi, E. E.; Robayo-Torres, C. C.; Rose, D. R.; Nichols, B. L. Luminal starch substrate "Brake" on maltase-glucoamylase activity is located within the glucoamylase subunit. Journal of Nutrition J. Nutr. 2008, 138, 685-692
-
(2008)
Journal of Nutrition
, vol.138
, pp. 685-692
-
-
Quezada-Calvillo, R.1
Sim, L.2
Ao, Z.H.3
Hamaker, B.R.4
Quaroni, A.5
Brayer, G.D.6
Sterchi, E.E.7
Robayo-Torres, C.C.8
Rose, D.R.9
Nichols, B.L.10
-
11
-
-
0017716475
-
Alpha-glucosidase inhibitors - New complex oligosaccharides of microbial origin
-
Schmidt, D. D.; Frommer, W.; Junge, B.; Muller, L.; Wingender, W.; Truscheit, E.; Schafer, D. Alpha-glucosidase inhibitors-new complex oligosaccharides of microbial origin Naturwissenschaften 1977, 64, 535-536
-
(1977)
Naturwissenschaften
, vol.64
, pp. 535-536
-
-
Schmidt, D.D.1
Frommer, W.2
Junge, B.3
Muller, L.4
Wingender, W.5
Truscheit, E.6
Schafer, D.7
-
12
-
-
0022580975
-
A double-blind-study on the efficacy and tolerance of a new alpha-glucosidase inhibitor in type-2 diabetics
-
Katsilambros, N.; Philippides, P.; Toskas, A.; Protopapas, J.; Frangaki, D.; Marangos, M.; Siskoudis, P.; Anastasopoulou, K.; Xetteri, H.; Hillebrand, I. A double-blind-study on the efficacy and tolerance of a new alpha-glucosidase inhibitor in type-2 diabetics Arzneimittelforschung 1986, 36-2, 1136-1138
-
(1986)
Arzneimittelforschung
, vol.362
, pp. 1136-1138
-
-
Katsilambros, N.1
Philippides, P.2
Toskas, A.3
Protopapas, J.4
Frangaki, D.5
Marangos, M.6
Siskoudis, P.7
Anastasopoulou, K.8
Xetteri, H.9
Hillebrand, I.10
-
13
-
-
0022455206
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
23
-
-
40949137811
-
Effect of five-membered sugar mimics on mammalian glycogen-degrading enzymes and various glucosidases
-
Minami, Y.; Kurlyarna, C.; Ikeda, K.; Kato, A.; Takebayashi, K.; Adachi, I.; Fleet, G. W. J.; Kettawan, A.; Karnoto, T.; Asano, N. Effect of five-membered sugar mimics on mammalian glycogen-degrading enzymes and various glucosidases Bioorg. Med. Chem. 2008, 16, 2734-2740
-
(2008)
Bioorg. Med. Chem.
, vol.16
, pp. 2734-2740
-
-
Minami, Y.1
Kurlyarna, C.2
Ikeda, K.3
Kato, A.4
Takebayashi, K.5
Adachi, I.6
Fleet, G.W.J.7
Kettawan, A.8
Karnoto, T.9
Asano, N.10
-
24
-
-
63149148929
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
41
-
-
84867579129
-
Role of the side chain stereochemistry in the α-glucosidase inhibitory activity of kotalanol, a potent natural α-glucosidase inhibitor. Part 2
-
Tanabe, G.; Matsuoka, K.; Yoshinaga, M.; Xie, W.; Tsutsui, N.; A. Amer, M. F.; Nakamura, S.; Nakanishi, I.; 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. Part 2 Bioorg. Med. Chem. 2012, 20, 6321-6334
-
(2012)
Bioorg. Med. Chem.
, vol.20
, pp. 6321-6334
-
-
Tanabe, G.1
Matsuoka, K.2
Yoshinaga, M.3
Xie, W.4
Tsutsui, N.5
Amer M F, A.6
Nakamura, S.7
Nakanishi, I.8
Wu, X.9
Yoshikawa, M.10
Muraoka, O.11
-
42
-
-
79960987709
-
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
-
43
-
-
79959518480
-
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, H. Y.; Quezada-Calvillo, R.; Nichols, B. L.; Pinto, B. M.; Rose, D. R. Mapping the intestinal alpha-glucogenic enzyme specificities of starch digesting maltase-glucoamylase and sucrase-isomaltase Bioorg. Med. Chem. 2011, 19, 3929-3934
-
(2011)
Bioorg. Med. Chem.
, vol.19
, pp. 3929-3934
-
-
Jones, K.1
Sim, L.2
Mohan, S.3
Kumarasamy, J.4
Liu, H.5
Avery, S.6
Naim, H.Y.7
Quezada-Calvillo, R.8
Nichols, B.L.9
Pinto, B.M.10
Rose, D.R.11
-
44
-
-
77952939601
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
52
-
-
84866433568
-
Modulation of starch digestion for slow glucose release through "toggling" of activities of mucosal alpha-glucosidases
-
Lee, B. H.; Eskandari, R.; Jones, K.; Reddy, K. R.; Quezada-Calvillo, R.; Nichols, B. L.; Rose, D. R.; Hamaker, B. R.; Pinto, B. M. Modulation of starch digestion for slow glucose release through "toggling" of activities of mucosal alpha-glucosidases J. Biol. Chem. 2012, 287, 31929-31938
-
(2012)
J. Biol. Chem.
, vol.287
, pp. 31929-31938
-
-
Lee, B.H.1
Eskandari, R.2
Jones, K.3
Reddy, K.R.4
Quezada-Calvillo, R.5
Nichols, B.L.6
Rose, D.R.7
Hamaker, B.R.8
Pinto, B.M.9
-
53
-
-
71449128235
-
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
|