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Volumn 103, Issue , 2015, Pages 133-162

Re-exploring promising α-glucosidase inhibitors for potential development into oral anti-diabetic drugs: Finding needle in the haystack

Author keywords

Anti diabetic drugs; Drug development; Natural; Synthetic; glucosidase inhibitors

Indexed keywords

ACARBOSE; ALKALOID DERIVATIVE; ALPHA GLUCOSIDASE INHIBITOR; AMINOCYCLITOL; AMINOSUGAR; ANTHRAQUINONE DERIVATIVE; CHALCONE DERIVATIVE; CURCUMIN; CYCLITOL; FLAVONOID; IMINOSUGAR; MACROLIDE; MIGLITOL; ORAL ANTIDIABETIC AGENT; PEPTIDE DERIVATIVE; STEROID; STILBENE DERIVATIVE; TERPENE DERIVATIVE; TERPHENYL DERIVATIVE; THIADIAZOLE DERIVATIVE; THIOSUGAR; UREA DERIVATIVE; VOGLIBOSE; XANTHONE DERIVATIVE; ALPHA GLUCOSIDASE; ANTIDIABETIC AGENT; GLYCOSIDASE INHIBITOR;

EID: 84941131320     PISSN: 02235234     EISSN: 17683254     Source Type: Journal    
DOI: 10.1016/j.ejmech.2015.08.043     Document Type: Review
Times cited : (222)

References (181)
  • 1
    • 0021324682 scopus 로고
    • The effect of a new specific alpha-amylase inhibitor on post-prandial glucose and insulin excursions in normal subjects and type 2 (non-insulin-dependent) diabetic patients
    • H.G. Eichler, A. Korn, S. Gasic, W. Prison, J. Businger, The effect of a new specific alpha-amylase inhibitor on post-prandial glucose and insulin excursions in normal subjects and type 2 (non-insulin-dependent) diabetic patients, Diabetologia 26 (1984) 278-281.
    • (1984) Diabetologia , vol.26 , pp. 278-281
    • Eichler, H.G.1    Korn, A.2    Gasic, S.3    Prison, W.4    Businger, J.5
  • 2
    • 84874383315 scopus 로고    scopus 로고
    • Inflammation in the pathogenesis of microvascular complications in diabetes
    • D.V. Nguyen, L.C. Shawand, M.B. Grant, Inflammation in the pathogenesis of microvascular complications in diabetes, Front. Endocrinol. (Lausanne) 3 (2012) 1-7.
    • (2012) Front. Endocrinol. (Lausanne) , vol.3 , pp. 1-7
    • Nguyen, D.V.1    Shawand, L.C.2    Grant, M.B.3
  • 3
    • 2342466734 scopus 로고    scopus 로고
    • Global prevalence of diabetes: Estimates for the year 2000 and projections for 2030
    • S. Wild, G. Roglic, A. Green, R. Sicree, H. King, Global prevalence of diabetes: estimates for the year 2000 and projections for 2030, Diabetes Care 27 (2004) 1047-1053.
    • (2004) Diabetes Care , vol.27 , pp. 1047-1053
    • Wild, S.1    Roglic, G.2    Green, A.3    Sicree, R.4    King, H.5
  • 5
    • 84860448540 scopus 로고    scopus 로고
    • Diabetes: A tale of two cultures
    • A. Alzaid, Diabetes: a tale of two cultures, Br. J. Diabetes Vas. Dis. 12 (2012) 57-59.
    • (2012) Br. J. Diabetes Vas. Dis. , vol.12 , pp. 57-59
    • Alzaid, A.1
  • 6
    • 0019963604 scopus 로고
    • The prevalence of diabetes mellitus in male Saudi Arabs
    • R.A. Bacchus, J.L. Bell, M. Madkour, B. Kilshaw, The prevalence of diabetes mellitus in male Saudi Arabs, Diabetologia 23 (1982) 330-332.
    • (1982) Diabetologia , vol.23 , pp. 330-332
    • Bacchus, R.A.1    Bell, J.L.2    Madkour, M.3    Kilshaw, B.4
  • 7
    • 0023181462 scopus 로고
    • Prevalence of diabetes mellitus in rural Saudi Arabia
    • H.H. Fatani, S.A. Mira, A.G. El-Zubier, Prevalence of diabetes mellitus in rural Saudi Arabia, Diabetes Care 10 (1987) 180-183.
    • (1987) Diabetes Care , vol.10 , pp. 180-183
    • Fatani, H.H.1    Mira, S.A.2    El-Zubier, A.G.3
  • 8
    • 0026560282 scopus 로고
    • Prevalence and health-care features of hyperglycemia in semiurban-rural communities in southern Saudi Arabia
    • H.A. Abu-Zeid, A.S. Al-Kassab, Prevalence and health-care features of hyperglycemia in semiurban-rural communities in southern Saudi Arabia, Diabetes Care 15 (1992) 484-489.
    • (1992) Diabetes Care , vol.15 , pp. 484-489
    • Abu-Zeid, H.A.1    Al-Kassab, A.S.2
  • 9
    • 0029812844 scopus 로고    scopus 로고
    • Diabetes mellitus and impaired glucose tolerance in Saudi Arabia
    • M.A. El-Hazmi, A.S. Warsy, A.R. Al-Swailem, et al., Diabetes mellitus and impaired glucose tolerance in Saudi Arabia, Ann. Saudi Med. 16 (1996) 381-385.
    • (1996) Ann. Saudi Med. , vol.16 , pp. 381-385
    • El-Hazmi, M.A.1    Warsy, A.S.2    Al-Swailem, A.R.3
  • 10
    • 0030791516 scopus 로고    scopus 로고
    • Prevalence of glucose intolerance in urban and rural communities in Saudi Arabia
    • A.R. Al-Nuaim, Prevalence of glucose intolerance in urban and rural communities in Saudi Arabia, Diabet. Med. 14 (1997) 595-602.
    • (1997) Diabet. Med. , vol.14 , pp. 595-602
    • Al-Nuaim, A.R.1
  • 11
    • 84941041896 scopus 로고    scopus 로고
    • (accessed August)
    • American Diabetes Association, USA. http://www.diabetes.org/advocacy/news-events/cost-of-diabetes.html (accessed August 2015).
    • (2015)
  • 12
    • 56749104677 scopus 로고    scopus 로고
    • Recent advances in the management of type 2 diabetes mellitus: A review
    • B.T. Srinivasan, J. Jarvis, K. Khunti, M.J. Davies, Recent advances in the management of type 2 diabetes mellitus: a review, Postgrad. Med. J. 84 (2008) 524-531.
    • (2008) Postgrad. Med. J. , vol.84 , pp. 524-531
    • Srinivasan, B.T.1    Jarvis, J.2    Khunti, K.3    Davies, M.J.4
  • 14
    • 33745048293 scopus 로고    scopus 로고
    • Structure of the Sulfolobus solfataricus α-Glucosidase: Implications for domain conservation and substrate recognition in GH3
    • H.A. Ernst, et al., Structure of the Sulfolobus solfataricus α-Glucosidase: implications for domain conservation and substrate recognition in GH3, J. Mol. Biol. 358 (2006) 1106-1124.
    • (2006) J. Mol. Biol. , vol.358 , pp. 1106-1124
    • Ernst, H.A.1
  • 15
    • 0026055308 scopus 로고
    • A classification of glycosyl hydrolases based on amino-acid sequence similarities
    • B. Henrissat, A classification of glycosyl hydrolases based on amino-acid sequence similarities, Biochem. J. 280 (1991) 309-316.
    • (1991) Biochem. J. , vol.280 , pp. 309-316
    • Henrissat, B.1
  • 16
    • 0027225980 scopus 로고
    • New families in the classification of glycosyl hydrolases based on aminoacid sequence similarities
    • B. Henrissat, A. Bairoch, New families in the classification of glycosyl hydrolases based on aminoacid sequence similarities, Biochem. J. 293 (1993) 781-788.
    • (1993) Biochem. J. , vol.293 , pp. 781-788
    • Henrissat, B.1    Bairoch, A.2
  • 17
    • 13644263258 scopus 로고    scopus 로고
    • Oral antidiabetic agents: Current role in type 2 diabetes mellitus
    • A.J. Krentz, C.J. Bailey, Oral antidiabetic agents: current role in type 2 diabetes mellitus, Drugs 65 (2005) (2005) 385-411.
    • (2005) Drugs , vol.65 , Issue.2005 , pp. 385-411
    • Krentz, A.J.1    Bailey, C.J.2
  • 19
    • 0017668659 scopus 로고
    • Glucosidase inhibition: A new approach to the treatment of diabetes, obesity, and hypcrlipoproteinaemia
    • W. Puts, U. Keup, I.J.P. Krause, G. Thomas, F. HoO'meister, Glucosidase inhibition: a new approach to the treatment of diabetes, obesity, and hypcrlipoproteinaemia, Naturwissenschafien 64 (1977) 536-537.
    • (1977) Naturwissenschafien , vol.64 , pp. 536-537
    • Puts, W.1    Keup, U.2    Krause, I.J.P.3    Thomas, G.4    HoO'meister, F.5
  • 20
    • 0037832251 scopus 로고    scopus 로고
    • Naturally occurring iminosugars and related compounds: Structure, distribution, and biological activity
    • N. Asano, Naturally occurring iminosugars and related compounds: structure, distribution, and biological activity, Curr. Top. Med. Chem. 3 (2003) 471-484.
    • (2003) Curr. Top. Med. Chem. , vol.3 , pp. 471-484
    • Asano, N.1
  • 22
    • 0022455206 scopus 로고
    • Synthesis and alpha-D-glucosidase inhibitory activity of N-substituted valiolamine derivatives as potential oral antidiabetic agents
    • S. Horii, H. Fukase, T. Matsuo, Y. Kameda, N. Asano, K. Matsui, Synthesis and alpha-D-glucosidase inhibitory activity of N-substituted valiolamine derivatives as potential oral antidiabetic agents, J. Med. Chem. 29 (1986) 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
  • 23
    • 65449150953 scopus 로고    scopus 로고
    • Voglibose Ph-3 study group. Voglibose for prevention of type 2 diabetes mellitus: A randomised, doubleblind trial in Japanese individuals with impaired glucose tolerance
    • R. Kawamori, N. Tajima, Y. Iwamoto, A. Kashiwagi, K. Shimamoto, K. Kaku, Voglibose Ph-3 study group. Voglibose for prevention of type 2 diabetes mellitus: a randomised, doubleblind trial in Japanese individuals with impaired glucose tolerance, Lancet 373 (2009) 1607-1614.
    • (2009) Lancet , vol.373 , pp. 1607-1614
    • Kawamori, R.1    Tajima, N.2    Iwamoto, Y.3    Kashiwagi, A.4    Shimamoto, K.5    Kaku, K.6
  • 24
    • 0036139934 scopus 로고    scopus 로고
    • Efficacy and safety of voglibose in comparison with acarbose in type 2 diabetic patients
    • A. Vichayanrat, S. Ploybutr, M. Tunlakit, P. Watanakejorn, Efficacy and safety of voglibose in comparison with acarbose in type 2 diabetic patients, Diabetes Res. Clin. Pract. 55 (2002) 99-103.
    • (2002) Diabetes Res. Clin. Pract. , vol.55 , pp. 99-103
    • Vichayanrat, A.1    Ploybutr, S.2    Tunlakit, M.3    Watanakejorn, P.4
  • 25
    • 0013969908 scopus 로고
    • The structure of nojirimycin, a piperidinose sugar antibiotic
    • S. Inoue, T. Tsuruoka, T. Niida, The structure of nojirimycin, a piperidinose sugar antibiotic, Antibiot. 19 (1966) 288-292.
    • (1966) Antibiot , vol.19 , pp. 288-292
    • Inoue, S.1    Tsuruoka, T.2    Niida, T.3
  • 26
    • 0021738039 scopus 로고
    • Novel glycosidase inhibitors, nojirimycin B and Dmannonic δ- Lactam. Isolation, structure determination and biological property
    • T. Niwa, T. Tsuruoka, H. Goi, Y. Kodama, J. ltoh, S. lnoue, Y. Yamada, T. Niida, M. Nobe, Y. Ogawa, Novel glycosidase inhibitors, nojirimycin B and Dmannonic δ- lactam. Isolation, structure determination and biological property, J. Antibiot. 37 (1984) 1579-1586.
    • (1984) J. Antibiot. , vol.37 , pp. 1579-1586
    • Niwa, T.1    Tsuruoka, T.2    Goi, H.3    Kodama, Y.4    Ltoh, J.5    Lnoue, S.6    Yamada, Y.7    Niida, T.8    Nobe, M.9    Ogawa, Y.10
  • 28
    • 0021922401 scopus 로고
    • Molecular structure and glycosidase-inhibitory activity of nojirimycin bisulfite adduct
    • Y. Kodama, T. Tsuruoka, T. Niwa, S. Inoue, Molecular structure and glycosidase-inhibitory activity of nojirimycin bisulfite adduct, J. Antibiot. 38 (1985) 116-118.
    • (1985) J. Antibiot. , vol.38 , pp. 116-118
    • Kodama, Y.1    Tsuruoka, T.2    Niwa, T.3    Inoue, S.4
  • 29
    • 0022814210 scopus 로고
    • Synthesis of 5-amino-5-deoxy-D-galactopyranose and I,5-dideoxy-1,5-imino-D-galactitol, and their inhibition of α- And β-galactosidases
    • G. Legler, S. Pohl, Synthesis of 5-amino-5-deoxy-D-galactopyranose and I,5-dideoxy-1,5-imino-D-galactitol, and their inhibition of α- and β-galactosidases, Carbohydr. Res. 155 (1986) 119-129.
    • (1986) Carbohydr. Res. , vol.155 , pp. 119-129
    • Legler, G.1    Pohl, S.2
  • 30
    • 0023806974 scopus 로고
    • Inhibition of a-galactosidase by galactostatin, galactostatin-lactam and 1-deoxygalactostatin
    • Y. Miyake, M. Ebata, Inhibition of a-galactosidase by galactostatin, galactostatin-lactam and 1-deoxygalactostatin, Agric. Biol. Chem. 52 (1988) 1649-1654.
    • (1988) Agric. Biol. Chem. , vol.52 , pp. 1649-1654
    • Miyake, Y.1    Ebata, M.2
  • 31
    • 84998392032 scopus 로고
    • The structure of moraoline, a piperidine alkaloid from Morus species
    • (in Japanese)
    • M. Yagi, T. Kouno, Y. Aoyagi, H. Murai, The structure of moraoline, a piperidine alkaloid from Morus species, Nippon. Nougei Kagaku Kaishi 50 (1976) 571-572 (in Japanese).
    • (1976) Nippon. Nougei Kagaku Kaishi , vol.50 , pp. 571-572
    • Yagi, M.1    Kouno, T.2    Aoyagi, Y.3    Murai, H.4
  • 32
    • 0001426638 scopus 로고    scopus 로고
    • Chemistry and structure-activity relationships of glucosidase inhibitors
    • J. Kuhlmann, W. Puis (Eds.), Springer-Verlag, Berlin, Heidelberg, New York
    • B. Junge, M. Matzke, J. Stohefuss, Chemistry and structure-activity relationships of glucosidase inhibitors, in: J. Kuhlmann, W. Puis (Eds.), Handbook of Experimental Pharmacology, vol. 119, Springer-Verlag, Berlin, Heidelberg, New York, 1996, pp. 411-482.
    • (1996) Handbook of Experimental Pharmacology , vol.119 , pp. 411-482
    • Junge, B.1    Matzke, M.2    Stohefuss, J.3
  • 33
    • 0023106004 scopus 로고
    • Miglitol may have a blood glucose lowering effect unrelated to inhibition of α-glucosidase
    • P.H. Joubert, G.N. Foukaridis, M.L. Bopape, Miglitol may have a blood glucose lowering effect unrelated to inhibition of α-glucosidase, Eur. J. Clin. Pharmacol. 31 (1987) 123.
    • (1987) Eur. J. Clin. Pharmacol. , vol.31 , pp. 123
    • Joubert, P.H.1    Foukaridis, G.N.2    Bopape, M.L.3
  • 34
    • 0025063161 scopus 로고
    • The effect of miglitol and acarbose after an oral glucose load: A novel hypoglycaemic mechanism?
    • P.H. Joubert, H.L. Venter, G.N. Foukaridis, The effect of miglitol and acarbose after an oral glucose load: a novel hypoglycaemic mechanism? Br. J. Clin. Pharmacol. 30 (1990) 391-396.
    • (1990) Br. J. Clin. Pharmacol. , vol.30 , pp. 391-396
    • Joubert, P.H.1    Venter, H.L.2    Foukaridis, G.N.3
  • 36
    • 0037097039 scopus 로고    scopus 로고
    • Acarbose for prevention of type 2 diabetes mellitus: The STOPNIDDM randomised trial
    • J.L. Chiasson, et al., Acarbose for prevention of type 2 diabetes mellitus: the STOPNIDDM randomised trial, Lancet 359 (2002) 2072-2077.
    • (2002) Lancet , vol.359 , pp. 2072-2077
    • Chiasson, J.L.1
  • 37
    • 0027724063 scopus 로고
    • Acarbose. An update of its pharmacology and therapeutic use in diabetes mellitus
    • J.A. Balfour, D. McTavish, Acarbose. An update of its pharmacology and therapeutic use in diabetes mellitus, Drugs 46 (1993) 1025-1054.
    • (1993) Drugs , vol.46 , pp. 1025-1054
    • Balfour, J.A.1    McTavish, D.2
  • 38
    • 11844294865 scopus 로고    scopus 로고
    • Alpha-glucosidase inhibitors for patients with type 2 diabetes: Results from a cochrane systematic review and meta-analysis
    • F.A. van de Laar, P.L. Lucassen, R.P. Akkermans, E.H. van de Lisdonk, G.E. Rutten, C. van Weel, Alpha-glucosidase inhibitors for patients with type 2 diabetes: results from a cochrane systematic review and meta-analysis, Diabetes Care 28 (2005) 154-163
    • (2005) Diabetes Care , vol.28 , pp. 154-163
    • Van De-Laar, F.A.1    Lucassen, P.L.2    Akkermans, R.P.3    Van De-Lisdonk, E.H.4    Rutten, G.E.5    Van Weel, C.6
  • 40
    • 0034607947 scopus 로고    scopus 로고
    • Sugar-mimic glycosidase inhibitors: Natural occurrence, biological activity and prospects for therapeutic application
    • N. Asano, R.J. Nash, R.J. Molyneux, G.W.J. Fleet, Sugar-mimic glycosidase inhibitors: natural occurrence, biological activity and prospects for therapeutic application, Tetrahedron Asymmetry 11 (2000) (2000) 1645-1680.
    • (2000) Tetrahedron Asymmetry , vol.11 , Issue.2000 , pp. 1645-1680
    • Asano, N.1    Nash, R.J.2    Molyneux, R.J.3    Fleet, G.W.J.4
  • 41
    • 0242287992 scopus 로고    scopus 로고
    • Glycosidase inhibitors: Update and perspectives on practical use
    • N. Asano, Glycosidase inhibitors: update and perspectives on practical use, Glycobiology 13 (2003) 93R-104R.
    • (2003) Glycobiology , vol.13 , pp. 93R-104R
    • Asano, N.1
  • 42
    • 27244456033 scopus 로고    scopus 로고
    • Iminosugar inhibitors for treating the lysosomal glycosphingolipidoses
    • T.D. Butters, R.A. Dwek, F.M. Platt, Iminosugar inhibitors for treating the lysosomal glycosphingolipidoses, Glycobiology 15 (2005) 43R-52R.
    • (2005) Glycobiology , vol.15 , pp. 43R-52R
    • Butters, T.D.1    Dwek, R.A.2    Platt, F.M.3
  • 43
    • 67649497359 scopus 로고    scopus 로고
    • Sugar-mimicking glycosidase inhibitors: Bioactivity and application
    • N. Asano, Sugar-mimicking glycosidase inhibitors: bioactivity and application, Cell. Mol. Life Sci. 66 (2009) 1479-1492.
    • (2009) Cell. Mol. Life Sci. , vol.66 , pp. 1479-1492
    • Asano, N.1
  • 44
    • 84870991117 scopus 로고    scopus 로고
    • A prospect for pyrrolidine iminosugars as antidiabetic α-glucosidase inhibitors
    • A. Trapero, A. Llebaria, A prospect for pyrrolidine iminosugars as antidiabetic α-glucosidase inhibitors, J. Med. Chem. 55 (2012) 10345-10346.
    • (2012) J. Med. Chem. , vol.55 , pp. 10345-10346
    • Trapero, A.1    Llebaria, A.2
  • 45
    • 63249126630 scopus 로고    scopus 로고
    • 3,4-dihydroxypyrrolidine as glycosidase inhibitor
    • K. Suzuki, T. Nakahara, O. Kanie, 3,4-Dihydroxypyrrolidine as glycosidase inhibitor, Curr. Top. Med. Chem. 9 (2009) 34-57.
    • (2009) Curr. Top. Med. Chem. , vol.9 , pp. 34-57
    • Suzuki, K.1    Nakahara, T.2    Kanie, O.3
  • 46
    • 80052454406 scopus 로고    scopus 로고
    • Iminosugars as therapeutic agents: Recent advances and promising trends
    • R.J. Nash, A. Kato, C.Y. Yu, G.W. Fleet, Iminosugars as therapeutic agents: recent advances and promising trends, Future Med. Chem. 3 (2011) 1513-1521.
    • (2011) Future Med. Chem. , vol.3 , pp. 1513-1521
    • Nash, R.J.1    Kato, A.2    Yu, C.Y.3    Fleet, G.W.4
  • 48
    • 77953443670 scopus 로고    scopus 로고
    • Carbasugars: Synthesis and functions
    • B. Fraser-Reid, K. Tatsuta, J. Thiem (Eds.), Springer, Verlag Berlin Heidelberg, Chapter
    • Y. Kobayashi, Carbasugars: synthesis and functions, in: B. Fraser-Reid, K. Tatsuta, J. Thiem (Eds.), Glycoscience, Springer, Verlag Berlin Heidelberg, 2008, pp. 1914-1997. Chapter-DOI 10-1007/978-3-540-30429-6-49.
    • (2008) Glycoscience , pp. 1914-1997
    • Kobayashi, Y.1
  • 49
    • 77957150234 scopus 로고    scopus 로고
    • Synthesis and biological activity of naturally occurring α-glucosidase inhibitors
    • D.J. Wardrop, S.L. Waidyarachchi, Synthesis and biological activity of naturally occurring α-glucosidase inhibitors, Nat. Prod. Rep. 27 (2010) 1431-1468.
    • (2010) Nat. Prod. Rep. , vol.27 , pp. 1431-1468
    • Wardrop, D.J.1    Waidyarachchi, S.L.2
  • 51
    • 0000315722 scopus 로고
    • 2-hydroxymethyl-3,4-dihydroxypyrrolidine in fruits of Angylocalyx boutiqueanus
    • R.J. Nash, E.A. Bell, J.M. Williams, 2-Hydroxymethyl-3,4-dihydroxypyrrolidine in fruits of Angylocalyx boutiqueanus, Phytochemistry 24 (1985) 1620-1622.
    • (1985) Phytochemistry , vol.24 , pp. 1620-1622
    • Nash, R.J.1    Bell, E.A.2    Williams, J.M.3
  • 52
    • 49549135253 scopus 로고
    • 2,5-dihydroxymethyl-3,4-dihydroxypyrrolidine dans les feuilles de Derris elliptica
    • A. Welter, J. Jadot, G. Dardenne, M. Marlier, J. Casimir, 2,5-Dihydroxymethyl-3,4-dihydroxypyrrolidine dans les feuilles de Derris elliptica, Phytochemistry 15 (1976) 747-749.
    • (1976) Phytochemistry , vol.15 , pp. 747-749
    • Welter, A.1    Jadot, J.2    Dardenne, G.3    Marlier, M.4    Casimir, J.5
  • 55
    • 0024227021 scopus 로고
    • α-homonojirimycin [2,6-dideoxy-2,6-imino-d-glycero-l-guloheptitol] from omphalea diandra L.: Isolation and glucosidase inhibition
    • G.C. Kite, Linda E. Fellows, George W.J. Fleet, Paul S. Liu, Anthony M. Scofield, Neal G. Smith, α-Homonojirimycin [2,6-dideoxy-2,6-imino-d-glycero-l-guloheptitol] from omphalea diandra L.: isolation and glucosidase inhibition, Tetrahedron Lett. 29 (1988) 6483-6485.
    • (1988) Tetrahedron Lett. , vol.29 , pp. 6483-6485
    • Kite, G.C.1    Fellows, L.E.2    Fleet, G.W.J.3    Liu, P.S.4    Scofield, A.M.5    Smith, N.G.6
  • 59
    • 0033231003 scopus 로고    scopus 로고
    • Revised structure of a homonojirimycin isomer from Aglaonema treubii: First example of a naturally occurring alpha-homoallonojirimycin
    • O.R. Martin, P. Compain, H. Kizu, N. Asano, Revised structure of a homonojirimycin isomer from Aglaonema treubii: first example of a naturally occurring alpha-homoallonojirimycin, Bioorg. Med. Chem. Lett. 9 (1999) 3171-3174.
    • (1999) Bioorg. Med. Chem. Lett. , vol.9 , pp. 3171-3174
    • Martin, O.R.1    Compain, P.2    Kizu, H.3    Asano, N.4
  • 60
    • 84885184188 scopus 로고    scopus 로고
    • α-glucosidase-inhibitory iminosugars from the leaves of suregada glomerulata
    • R.-Y. Yan, H.-Q. Wanga, C. Liu, J. Kang, R.-Y. Chen, α-Glucosidase-inhibitory iminosugars from the leaves of suregada glomerulata, Bioorg. Med. Chem. 21 (2013) 6796-6803.
    • (2013) Bioorg. Med. Chem. , vol.21 , pp. 6796-6803
    • Yan, R.-Y.1    Wanga, H.-Q.2    Liu, C.3    Kang, J.4    Chen, R.-Y.5
  • 64
    • 60749132180 scopus 로고    scopus 로고
    • Total syntheses of casuarine and its 6-O-α-glucoside: Complementary inhibition towards glycoside hydrolases of the GH31 and GH37 families
    • Cardona, C. Parmeggiani, E. Faggi, C. Bonaccini, P. Gratteri, L. Sim, T.M. Gloster, S. Roberts, G.J. Davies, D.R. Rose, A. Goti, Total syntheses of casuarine and its 6-O-α-glucoside: complementary inhibition towards glycoside hydrolases of the GH31 and GH37 families, Chem. Eur. J. 15 (2009) 1627-1636.
    • (2009) Chem. Eur. J. , vol.15 , pp. 1627-1636
    • Cardona, C.P.1    Faggi, E.2    Bonaccini, C.3    Gratteri, P.4    Sim, L.5    Gloster, T.M.6    Roberts, S.7    Davies, G.J.8    Rose, D.R.9    Goti, A.10
  • 65
    • 0031722553 scopus 로고    scopus 로고
    • Kotalanol, a potent alpha-glucosidase inhibitor with thiosugar sulfonium sulfate structure, from antidiabetic ayurvedic medicine Salacia reticulata
    • M. Yoshikawa, T. Murakami, K. Yashiro, H. Matsuda, Kotalanol, a potent alpha-glucosidase inhibitor with thiosugar sulfonium sulfate structure, from antidiabetic ayurvedic medicine Salacia reticulata, Chem. Pharm. Bull. (Tokyo) 46 (1998) 1339-1340.
    • (1998) Chem. Pharm. Bull. (Tokyo) , vol.46 , pp. 1339-1340
    • Yoshikawa, M.1    Murakami, T.2    Yashiro, K.3    Matsuda, H.4
  • 66
    • 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
    • M. Yoshikawa, T. Murakamia, H. Shimadaa, H. Matsudaa, Y. Yamaharab, G. Tanabec, O. Muraokac, Salacinol, potent antidiabetic principle with unique thiosugar sulfonium sulfate structure from the ayurvedic traditional medicine salacia reticulata in Sri Lanka and India, Tetrahedron Lett. 38 (48) (1997) 8367-8370.
    • (1997) Tetrahedron Lett. , vol.38 , Issue.48 , pp. 8367-8370
    • Yoshikawa, M.1    Murakamia, T.2    Shimadaa, H.3    Matsudaa, H.4    Yamaharab, Y.5    Tanabec, G.6    Muraokac, O.7
  • 67
    • 84924129937 scopus 로고    scopus 로고
    • Salacinol and related analogs: New leads for type 2 diabetes therapeutic candidates from the Thai traditional natural medicine Salacia chinensis
    • T. Morikawa, J. Akaki, K. Ninomiya, E. Kinouchi, G. Tanabe, Y. Pongpiriyadacha, M. Yoshikawa, O. Muraoka, Salacinol and related analogs: new leads for type 2 diabetes therapeutic candidates from the Thai traditional natural medicine Salacia chinensis, Nutrients 7 (2015) 1480-1493.
    • (2015) Nutrients , vol.7 , pp. 1480-1493
    • Morikawa, T.1    Akaki, J.2    Ninomiya, K.3    Kinouchi, E.4    Tanabe, G.5    Pongpiriyadacha, Y.6    Yoshikawa, M.7    Muraoka, O.8
  • 68
    • 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
    • R. Nasi, B.O. Patrick, L. Sim, D.R. Rose, B.M. Pinto, 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. 73 (2008) 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
  • 69
    • 74949102237 scopus 로고    scopus 로고
    • New glucosidase inhibitors from an ayurvedic herbal treatment for type 2 diabetes: Structures and inhibition of human intestinal maltaseglucoamylase with compounds from Salacia reticulata
    • L. Sim, K. Jayakanthan, S. Mohan, R. Nasi, B.D. Johnston, B.M. Pinto, D.R. Rose, New glucosidase inhibitors from an ayurvedic herbal treatment for type 2 diabetes: structures and inhibition of human intestinal maltaseglucoamylase with compounds from Salacia reticulata, Biochemistry 49 (2010) 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
  • 70
    • 14844363557 scopus 로고    scopus 로고
    • Galloyl, caffeoyl and hexahydroxydiphenoyl esters of dihydrochalcone glucosides from Balanophora tobiracola
    • T. Tanaka, R. Uehara, K. Nishida, I. Kouno, Galloyl, caffeoyl and hexahydroxydiphenoyl esters of dihydrochalcone glucosides from Balanophora tobiracola, Phytochemistry 66 (2005) 675-681.
    • (2005) Phytochemistry , vol.66 , pp. 675-681
    • Tanaka, T.1    Uehara, R.2    Nishida, K.3    Kouno, I.4
  • 73
    • 0031887718 scopus 로고    scopus 로고
    • Antidiabetic principles of natural medicines. II. Aldose reductase and alpha-glucosidase inhibitors from Brazilian natural medicine, the leaves of myrcia multiflora DC. (Myrtaceae): Structures of myrciacitrins I and II and myrciaphenones A and B
    • M. Yoshikawa, H. Shimada, N. Nishida, Y. Li, I. Toguchida, J. Yamahara, H. Matsuda, Antidiabetic principles of natural medicines. II. Aldose reductase and alpha-glucosidase inhibitors from Brazilian natural medicine, the leaves of myrcia multiflora DC. (Myrtaceae): structures of myrciacitrins I and II and myrciaphenones A and B, Chem. Pharm. Bull. (Tokyo) 46 (1998) 113-119.
    • (1998) Chem. Pharm. Bull. (Tokyo) , vol.46 , pp. 113-119
    • Yoshikawa, M.1    Shimada, H.2    Nishida, N.3    Li, Y.4    Toguchida, I.5    Yamahara, J.6    Matsuda, H.7
  • 74
    • 51049114028 scopus 로고    scopus 로고
    • Acylated flavonol monorhamnosides, α-glucosidase inhibitors, from Machilus philippinensis, School
    • S. Lee, Hsiao-Ching Lin, Chien-Kuang Chen, Acylated flavonol monorhamnosides, α-glucosidase inhibitors, from Machilus philippinensis, School, Phytochemistry 69 (2008) 2347-2353.
    • (2008) Phytochemistry , vol.69 , pp. 2347-2353
    • Lee, S.1    Lin, H.-C.2    Chen, C.-K.3
  • 75
    • 0034877810 scopus 로고    scopus 로고
    • α-glucosidase inhibitory action of natural acylated anthocyanins. 2. α-glucosidase inhibition by isolated acylated anthocyanins
    • T. Matsui, T. Ueda, T. Oki, K. Sugita, N. Terahara, K. Matsumoto, α-Glucosidase inhibitory action of natural acylated anthocyanins. 2. α-glucosidase inhibition by isolated acylated anthocyanins, J. Agric. Food Chem. 49 (2001) 1952-1956.
    • (2001) J. Agric. Food Chem. , vol.49 , pp. 1952-1956
    • Matsui, T.1    Ueda, T.2    Oki, T.3    Sugita, K.4    Terahara, N.5    Matsumoto, K.6
  • 76
    • 22044456421 scopus 로고    scopus 로고
    • Strong antihyperglycemic effects of water-soluble fraction of Brazilian propolis and its bioactive constituent, 3, 4, 5-tri-O-caffeoylquinic acid
    • T. Matsui, S. Ebuchi, T. Fujise, K. Abesundara, S. Doi, H. Yamada, K. Matsumoto, Strong antihyperglycemic effects of water-soluble fraction of Brazilian propolis and its bioactive constituent, 3, 4, 5-tri-O-caffeoylquinic acid, Biol. Pharm. Bull. 27 (2004) 1797-1803.
    • (2004) Biol. Pharm. Bull. , vol.27 , pp. 1797-1803
    • Matsui, T.1    Ebuchi, S.2    Fujise, T.3    Abesundara, K.4    Doi, S.5    Yamada, H.6    Matsumoto, K.7
  • 78
    • 77956628381 scopus 로고    scopus 로고
    • Yeast α-glucosidase inhibition by isoflavones from plants of Leguminosae as an in vitro alternative to acarbose
    • C.W. Choi, Y.H. Choi, M.R. Cha, D.S. Yoo, Y.S. Kim, G.H. Yon, K.S. Hong, Y.H. Kim, S.Y. Ryu, Yeast α-glucosidase inhibition by isoflavones from plants of Leguminosae as an in vitro alternative to acarbose, J. Agric. Food Chem. 58 (2010) 9988-9993.
    • (2010) J. Agric. Food Chem. , vol.58 , pp. 9988-9993
    • Choi, C.W.1    Choi, Y.H.2    Cha, M.R.3    Yoo, D.S.4    Kim, Y.S.5    Yon, G.H.6    Hong, K.S.7    Kim, Y.H.8    Ryu, S.Y.9
  • 83
    • 33748933010 scopus 로고    scopus 로고
    • Anti-atherosclerotic and anti-inflammatory activities of catecholic xanthones and flavonoids isolated from Cudrania tricuspidata
    • K.H. Park, Y.D. Park, J.M. Han, K.R. Im, B.W. Lee, I.Y. Jeong, T.S. Jeong, W.S. Lee, Anti-atherosclerotic and anti-inflammatory activities of catecholic xanthones and flavonoids isolated from Cudrania tricuspidata, Bioorg. Med. Chem. Lett. 16 (2006) 5580-5583.
    • (2006) Bioorg. Med. Chem. Lett. , vol.16 , pp. 5580-5583
    • Park, K.H.1    Park, Y.D.2    Han, J.M.3    Im, K.R.4    Lee, B.W.5    Jeong, I.Y.6    Jeong, T.S.7    Lee, W.S.8
  • 85
    • 0034623853 scopus 로고    scopus 로고
    • Tetraoxygenated naturally occurring xanthones
    • V. Peres, T.J. Nagem, F.F. Oliveira, Tetraoxygenated naturally occurring xanthones, Phytochemistry 55 (2000) 683-710.
    • (2000) Phytochemistry , vol.55 , pp. 683-710
    • Peres, V.1    Nagem, T.J.2    Oliveira, F.F.3
  • 86
    • 80053649817 scopus 로고    scopus 로고
    • α-glucosidase inhibition and antihyperglycemic activity of prenylated xanthones from Garcinia mangostana
    • H.W. Ryu, J.K. Cho, M.J. Curtis-Long, H.J. Yuk, Y.S. Kim, S. Jung, K.H. Park, α-Glucosidase inhibition and antihyperglycemic activity of prenylated xanthones from Garcinia mangostana, Phytochemistry 72 (2011) 2148-2154.
    • (2011) Phytochemistry , vol.72 , pp. 2148-2154
    • Ryu, H.W.1    Cho, J.K.2    Curtis-Long, M.J.3    Yuk, H.J.4    Kim, Y.S.5    Jung, S.6    Park, K.H.7
  • 87
    • 0142180507 scopus 로고
    • Qinghai People's Publishing House, Xining, China
    • Y.C. Yang, Tibetan Medicine, Qinghai People's Publishing House, Xining, China, 1991, pp. 111-112.
    • (1991) Tibetan Medicine , pp. 111-112
    • Yang, Y.C.1
  • 88
    • 0028027642 scopus 로고
    • Bellidifolin: A potent hypoglycemic agent in streptozotocin (STZ)-induced diabetic rats from Swertia japonica
    • P. Basnet, S. Kadota, M. Shimizu, T. Namba, Bellidifolin: a potent hypoglycemic agent in streptozotocin (STZ)-induced diabetic rats from Swertia japonica, Planta Med. 60 (1994) 507-511.
    • (1994) Planta Med. , vol.60 , pp. 507-511
    • Basnet, P.1    Kadota, S.2    Shimizu, M.3    Namba, T.4
  • 89
    • 84903816346 scopus 로고    scopus 로고
    • Xanthones from Swertia mussotii as multitargetdirected antidiabetic agents
    • H. Zheng, Cui-Ting Luo, Heru Chen, Juan-Na Lin, Chun-Ling Ye, Shuang-Shuang Mao, Yu-Lin Li, Xanthones from Swertia mussotii as multitargetdirected antidiabetic agents, ChemMedChem 9 (2014) 1374-1379.
    • (2014) ChemMedChem , vol.9 , pp. 1374-1379
    • Zheng, H.1    Luo, C.-T.2    Chen, H.3    Lin, J.-N.4    Ye, C.-L.5    Mao, S.-S.6    Li, Y.-L.7
  • 90
    • 0028835878 scopus 로고
    • Antidiabetic plants and their active constituents
    • R.J. Marles, N.R. Farnsworth, Antidiabetic plants and their active constituents, Phytomedicine 2 (1995) 137-189.
    • (1995) Phytomedicine , vol.2 , pp. 137-189
    • Marles, R.J.1    Farnsworth, N.R.2
  • 91
    • 47949113690 scopus 로고    scopus 로고
    • Hypoglycemic effect of 13-membered ring thiocyclitol, a novel-glucosidase inhibitor from Kothala-himbutu (Salacia reticulate)
    • H. Oe, S. Ozaki, Hypoglycemic effect of 13-membered ring thiocyclitol, a novel-glucosidase inhibitor from Kothala-himbutu (Salacia reticulate), Biosci. Biotechnol. Biochem. 72 (2008) 1962-1964
    • (2008) Biosci. Biotechnol. Biochem. , vol.72 , pp. 1962-1964
    • Oe, H.1    Ozaki, S.2
  • 92
    • 55049117553 scopus 로고    scopus 로고
    • On the structure of the bioactive constituent from ayurvedic medicine Salacia reticulata: Revision of the literature
    • O. Muraoka, Xie Weijia, Tanabe Genzoh, F. A. Amer Mumen, Minematsu Toshie, Yoshikawa Masayuki, On the structure of the bioactive constituent from ayurvedic medicine Salacia reticulata: revision of the literature, Tetrahedron Letters 49 (2008) 7315-7317.
    • (2008) Tetrahedron Letters , vol.49 , pp. 7315-7317
    • Muraoka, O.1    Weijia, X.2    Genzoh, T.3    Amer Mumen, F.A.4    Toshie, M.5    Masayuki, Y.6
  • 94
    • 84905379140 scopus 로고    scopus 로고
    • Identification of α-glucosidase inhibitors from the leaves of Pluchea indica Less., a traditional Indonesian herb: Promotion of natural product use
    • I.S. Arsiningtyas, Maria D.P.T. Gunawan-Puteri, Eisuke Kato, Jun Kawabata, Identification of α-glucosidase inhibitors from the leaves of Pluchea indica Less., a traditional Indonesian herb: promotion of natural product use, Nat. Prod. Res. 28 (2014) 1350-1353.
    • (2014) Nat. Prod. Res. , vol.28 , pp. 1350-1353
    • Arsiningtyas, I.S.1    Gunawan-Puteri, M.D.P.T.2    Kato, E.3    Kawabata, J.4
  • 95
    • 84907500898 scopus 로고    scopus 로고
    • Caffeoylquinic acid derivatives isolated fromthe aerial parts of Gynura divaricata and their yeast α-glucosidase and PTP1B inhibitory activity
    • J. Chen, S. Mangelinckx, L. Maa, Z. Wang, W. Li, N.D. Kimpe, Caffeoylquinic acid derivatives isolated fromthe aerial parts of Gynura divaricata and their yeast α-glucosidase and PTP1B inhibitory activity, Fitoterapia 99 (2014) 1-6.
    • (2014) Fitoterapia , vol.99 , pp. 1-6
    • Chen, J.1    Mangelinckx, S.2    Maa, L.3    Wang, Z.4    Li, W.5    Kimpe, N.D.6
  • 96
    • 0034757397 scopus 로고    scopus 로고
    • Two new pyrrolidine alkaloids, radicamines A and B, as inhibitors of α-glucosidase from Lobelia chinensis Lour
    • M. Shibano, D. Tsukamoto, A. Masuda, Y. Tanaka, G. Kusano, Two new pyrrolidine alkaloids, radicamines A and B, as inhibitors of α-glucosidase from Lobelia chinensis Lour, Chem. Pharm. Bull. 49 (2001) 1362-1365.
    • (2001) Chem. Pharm. Bull. , vol.49 , pp. 1362-1365
    • Shibano, M.1    Tsukamoto, D.2    Masuda, A.3    Tanaka, Y.4    Kusano, G.5
  • 97
    • 0030939363 scopus 로고    scopus 로고
    • Studies on the constituents of Broussonetia species. II. Six new pyrrolidine alkaloids, broussonetine A, B, E, F and broussonetinine A and B, as inhibitors of glycosidases from Broussonetia kazinoki Sieb
    • M. Shibano, S. Kitagawa, S. Nakamura, N. Akazawa, G. Kusano, Studies on the constituents of Broussonetia species. II. Six new pyrrolidine alkaloids, broussonetine A, B, E, F and broussonetinine A and B, as inhibitors of glycosidases from Broussonetia kazinoki Sieb, Chem. Pharm. Bull. (Tokyo) 45 (1997) 700-705.
    • (1997) Chem. Pharm. Bull. (Tokyo) , vol.45 , pp. 700-705
    • Shibano, M.1    Kitagawa, S.2    Nakamura, S.3    Akazawa, N.4    Kusano, G.5
  • 99
    • 84855992305 scopus 로고    scopus 로고
    • Anti-acetylcholinesterase, anti-α-glucosidase, anti-leishmanial and anti-fungal activities of chemical constituents of Beilschmiedia species
    • A. Mollataghi, E. Coudiere, H.A. Hadi, M.R. Mukhtar, K. Awang, M. Litaudon, A. Ata, Anti-acetylcholinesterase, anti-α-glucosidase, anti-leishmanial and anti-fungal activities of chemical constituents of Beilschmiedia species, Fitoterapia 83 (2012) 298-302.
    • (2012) Fitoterapia , vol.83 , pp. 298-302
    • Mollataghi, A.1    Coudiere, E.2    Hadi, H.A.3    Mukhtar, M.R.4    Awang, K.5    Litaudon, M.6    Ata, A.7
  • 101
    • 0028587702 scopus 로고
    • Curcuminoids as potent inhibitors of lipid peroxidation
    • S. Sreejayan, M.N.A. Rao, Curcuminoids as potent inhibitors of lipid peroxidation, J. Pharm. Pharmacol. 46 (1994) 1013-1016.
    • (1994) J. Pharm. Pharmacol. , vol.46 , pp. 1013-1016
    • Sreejayan, S.1    Rao, M.N.A.2
  • 102
    • 84941120973 scopus 로고    scopus 로고
    • H.S. Lee, KR Pat. 2003090395 (2003)
    • H.S. Lee, KR Pat. 2003090395 (2003).
  • 104
    • 70449670766 scopus 로고    scopus 로고
    • Bioactive natural products from two Sudanese medicinal plants Diospyros mespiliformis and Croton zambesicus
    • I.E. Mohamed, E.B.E. El Nur, M.I. Choudhary, S.N. Khan, Bioactive natural products from two Sudanese medicinal plants Diospyros mespiliformis and Croton zambesicus, Rec. Nat. Prod. 3 (2009) 198-203
    • (2009) Rec. Nat. Prod. , vol.3 , pp. 198-203
    • Mohamed, I.E.1    El Nur, E.B.E.2    Choudhary, M.I.3    Khan, S.N.4
  • 105
    • 84874610030 scopus 로고    scopus 로고
    • Synthesis of novel triterpene and N-allylated/N-alkylated niacin hybrids as α-glucosidase inhibitors
    • Narender, T. et al. Synthesis of novel triterpene and N-allylated/N-alkylated niacin hybrids as α-glucosidase inhibitors. Eur. J. Med. Chem., 63(2013) 162-169.
    • (2013) Eur. J. Med. Chem. , vol.63 , pp. 162-169
    • Narender, T.1
  • 106
    • 65649134270 scopus 로고    scopus 로고
    • Triterpene acids isolated from Lagerstroemia speciosa leaves as alpha-glucosidase inhibitors
    • W. Hou, Y. Li, Q. Zhang, X. Wei, A. Peng, L. Chen, Y. Wei, Triterpene acids isolated from Lagerstroemia speciosa leaves as alpha-glucosidase inhibitors, Phytother. Res. 23 (2009) 614-618.
    • (2009) Phytother. Res. , vol.23 , pp. 614-618
    • Hou, W.1    Li, Y.2    Zhang, Q.3    Wei, X.4    Peng, A.5    Chen, L.6    Wei, Y.7
  • 107
    • 0036906475 scopus 로고    scopus 로고
    • Hypoglycaemic activity of Alpinia galanga rhizome and its extracts in rabbits
    • M.S. Akhtar, M.A. Khan, M.T. Malik, Hypoglycaemic activity of Alpinia galanga rhizome and its extracts in rabbits, Fitoterapia 73 (2002) 623-628.
    • (2002) Fitoterapia , vol.73 , pp. 623-628
    • Akhtar, M.S.1    Khan, M.A.2    Malik, M.T.3
  • 109
    • 84922309917 scopus 로고    scopus 로고
    • Molecular docking and inhibition Kinetics of αa-glucosidase activity by labdane diterpenes isolated from tora seeds (Alpinia nigra B.L. Burtt.)
    • S. Ghosh, L.L. Rangan, Molecular docking and inhibition Kinetics of αa-glucosidase activity by labdane diterpenes isolated from tora seeds (Alpinia nigra B.L. Burtt.), Appl. Biochem. Biotechnol. 175 (2015) 1477-1489.
    • (2015) Appl. Biochem. Biotechnol. , vol.175 , pp. 1477-1489
    • Ghosh, S.1    Rangan, L.L.2
  • 110
    • 84899550690 scopus 로고    scopus 로고
    • The screening of potential α-glucosidase inhibitors from the polygonum multiflorum extract using ultrafiltration combined with liquid chromatography-tandem mass spectrometry
    • D. Yang, J. Zhao, S. Liu, F. Songa, Z. Liu, The screening of potential α-glucosidase inhibitors from the polygonum multiflorum extract using ultrafiltration combined with liquid chromatography-tandem mass spectrometry, Anal. Methods 6 (2014) 3353-3359.
    • (2014) Anal. Methods , vol.6 , pp. 3353-3359
    • Yang, D.1    Zhao, J.2    Liu, S.3    Songa, F.4    Liu, Z.5
  • 112
    • 84899514386 scopus 로고    scopus 로고
    • Two sarcoviolins with antioxidative and α-glucosidase inhibitory activity from the edible mushroom Sarcodon leucopus collected in Tibet
    • K. Ma, J. Han, L. Bao, T. Wei, H. Liu, Two sarcoviolins with antioxidative and α-glucosidase inhibitory activity from the edible mushroom Sarcodon leucopus collected in Tibet, J. Nat. Prod. 77 (2014) 942-947.
    • (2014) J. Nat. Prod. , vol.77 , pp. 942-947
    • Ma, K.1    Han, J.2    Bao, L.3    Wei, T.4    Liu, H.5
  • 113
    • 0033034494 scopus 로고    scopus 로고
    • Two new bromophenols from the red alga Odonthalia corymbifera
    • 13
    • H. Kurihara, T. Mitani, J. Kawabata, K. Takahashi, Two new bromophenols from the red alga Odonthalia corymbifera, J. Nat. Prod. 62 (1999) 882-884, 13.
    • (1999) J. Nat. Prod. , vol.62 , pp. 882-884
    • Kurihara, H.1    Mitani, T.2    Kawabata, J.3    Takahashi, K.4
  • 114
    • 0000144109 scopus 로고    scopus 로고
    • Inhibitory potencies of bromophenols from Rhodomelaceae algae against α-glucosidase activity
    • H. Kurihara, T. Mitani, J. Kawabata, K. Takahashi, Inhibitory potencies of bromophenols from Rhodomelaceae algae against α-glucosidase activity, Fish. Sci. 65 (1999) 300-303.
    • (1999) Fish. Sci. , vol.65 , pp. 300-303
    • Kurihara, H.1    Mitani, T.2    Kawabata, J.3    Takahashi, K.4
  • 115
    • 56049105599 scopus 로고    scopus 로고
    • Potent alpha-glucosidase inhibitors purified from the red alga Grateloupia elliptica
    • K.Y. Kim, K.A. Nam, H. Kurihara, S.M. Kim, Potent alpha-glucosidase inhibitors purified from the red alga Grateloupia elliptica, Phytochem 69 (2008) 2820-2825.
    • (2008) Phytochem , vol.69 , pp. 2820-2825
    • Kim, K.Y.1    Nam, K.A.2    Kurihara, H.3    Kim, S.M.4
  • 116
    • 77956111538 scopus 로고    scopus 로고
    • Alpha-glucosidase inhibitory activity of bromophenol purified from the red alga Polyopes lancifolia
    • K.Y. Kim, T.H. Nguyen, H. Kurihara, S.M. Kim, Alpha-glucosidase inhibitory activity of bromophenol purified from the red alga Polyopes lancifolia, J. Food. Sci. 75 (2010) H145-H150.
    • (2010) J. Food. Sci. , vol.75 , pp. H145-H150
    • Kim, K.Y.1    Nguyen, T.H.2    Kurihara, H.3    Kim, S.M.4
  • 117
    • 80053303634 scopus 로고    scopus 로고
    • Synthesis and α-glucosidase inhibitory mechanisms of bis(2,3-dibromo-4,5-dihydroxybenzyl) ether, a potential marine bromophenol α-glucosidase inhibitor
    • M. Liu, W. Zhang, J. Wei, X. Lin, Synthesis and α-glucosidase inhibitory mechanisms of bis(2,3-dibromo-4,5-dihydroxybenzyl) ether, a potential marine bromophenol α-glucosidase inhibitor, Mar. Drugs 9 (2011) 1554-1565.
    • (2011) Mar. Drugs , vol.9 , pp. 1554-1565
    • Liu, M.1    Zhang, W.2    Wei, J.3    Lin, X.4
  • 118
    • 39549083242 scopus 로고    scopus 로고
    • Alpha-glucosidase inhibitors from the seeds of Syagrus romanzoffiana
    • S.H. Lam, J.M. Chen, C.J. Kang, C.H. Chen, S.S. Lee, Alpha-glucosidase inhibitors from the seeds of Syagrus romanzoffiana, Phytochemistry 69 (2008) 1173-1178.
    • (2008) Phytochemistry , vol.69 , pp. 1173-1178
    • Lam, S.H.1    Chen, J.M.2    Kang, C.J.3    Chen, C.H.4    Lee, S.S.5
  • 119
    • 54349083268 scopus 로고    scopus 로고
    • α-glucosidase inhibitors from Garcinia brevipedicellata (Clusiaceae)
    • J. Ngoupayo, T.K. Tabopda, M.A. Ali, E. Tsamo, α-Glucosidase inhibitors from Garcinia brevipedicellata (Clusiaceae), Chem. Pharm. Bull. 56 (2008) 1466-1469.
    • (2008) Chem. Pharm. Bull. , vol.56 , pp. 1466-1469
    • Ngoupayo, J.1    Tabopda, T.K.2    Ali, M.A.3    Tsamo, E.4
  • 120
    • 84881376889 scopus 로고    scopus 로고
    • Synthesis and α-glucosidase inhibitory activity evaluation of N-substituted aminomethyl-β-D-glucopyranosides
    • X. Bian, X. Fan, C. Ke, Y. Luan, G. Zhao, A. Zeng, Synthesis and α-glucosidase inhibitory activity evaluation of N-substituted aminomethyl-β-D-glucopyranosides, Bioorg. Med. Chem. 21 (2013) 5442-5450.
    • (2013) Bioorg. Med. Chem. , vol.21 , pp. 5442-5450
    • Bian, X.1    Fan, X.2    Ke, C.3    Luan, Y.4    Zhao, G.5    Zeng, A.6
  • 121
    • 0025371332 scopus 로고
    • Inhibitory effect of pseudo-aminosugars on oligosaccharide glucosidases I and II and on lysosomal α-glucosidase from rat liver
    • M. Takeuchi, K. Kamata, M. Yoshida, Y. Kameda, K. Matsui, Inhibitory effect of pseudo-aminosugars on oligosaccharide glucosidases I and II and on lysosomal α-glucosidase from rat liver, J. Biochem. 108 (1990) 42-46.
    • (1990) J. Biochem. , vol.108 , pp. 42-46
    • Takeuchi, M.1    Kamata, K.2    Yoshida, M.3    Kameda, Y.4    Matsui, K.5
  • 122
    • 84868089029 scopus 로고    scopus 로고
    • A-geminal dihydroxymethyl piperidine and pyrrolidine iminosugars: Synthesis, conformational analysis, glycosidase inhibitory activity, and molecular docking studies
    • N.J. Pawar, V.S. Parihar, S.T. Chavan, R. Joshi, P.V. Joshi, S.G. Sabharwal, V.G. Puranik, D.D. Dhavale, a-Geminal dihydroxymethyl piperidine and pyrrolidine iminosugars: synthesis, conformational analysis, glycosidase inhibitory activity, and molecular docking studies, J. Org. Chem. 77 (2012) 7873-7882.
    • (2012) J. Org. Chem. , vol.77 , pp. 7873-7882
    • Pawar, N.J.1    Parihar, V.S.2    Chavan, S.T.3    Joshi, R.4    Joshi, P.V.5    Sabharwal, S.G.6    Puranik, V.G.7    Dhavale, D.D.8
  • 123
    • 0035815146 scopus 로고    scopus 로고
    • A new class of glycosidase inhibitor: Synthesis of salacinol and its stereoisomers
    • A. Ghavami, B.D. Johnston, B.M. Pinto, A new class of glycosidase inhibitor: synthesis of salacinol and its stereoisomers, J. Org. Chem. 66 (2001) 2312-2317.
    • (2001) J. Org. Chem. , vol.66 , pp. 2312-2317
    • Ghavami, A.1    Johnston, B.D.2    Pinto, B.M.3
  • 128
    • 84881227220 scopus 로고    scopus 로고
    • C-branched iminosugars: α-glucosidase inhibition by enantiomers of isoDMDP, isoDGDP, and isoDAB-L-isoDMDP compared to miglitol and miglustat
    • S.F. Jenkinson, D. Best, A.W. Saville, J. Mui, et al., C-Branched iminosugars: α-glucosidase inhibition by enantiomers of isoDMDP, isoDGDP, and isoDAB-L-isoDMDP compared to miglitol and miglustat, J. Org. Chem. 78 (2013) 7380-7397.
    • (2013) J. Org. Chem. , vol.78 , pp. 7380-7397
    • Jenkinson, S.F.1    Best, D.2    Saville, A.W.3    Mui, J.4
  • 129
    • 56349119576 scopus 로고    scopus 로고
    • Synthesis and biological evaluation of a 2-aryl polyhydroxylated pyrrolidine alkaloid-based library
    • E. Tsou, S. Chen, M. Yang, S. Wang, T.R. Cheng, W. Cheng, Synthesis and biological evaluation of a 2-aryl polyhydroxylated pyrrolidine alkaloid-based library, Bioorg. Med. Chem. 16 (2008) 10198-10204.
    • (2008) Bioorg. Med. Chem. , vol.16 , pp. 10198-10204
    • Tsou, E.1    Chen, S.2    Yang, M.3    Wang, S.4    Cheng, T.R.5    Cheng, W.6
  • 131
    • 33847759128 scopus 로고    scopus 로고
    • Synthesis of S-alkylated sulfoniumions and their glucosidase inhibitory activities against recombinant human maltase glucoamylase
    • S. Mohan, L. Sim, D.R. Rose, B.M. Pinto, Synthesis of S-alkylated sulfoniumions and their glucosidase inhibitory activities against recombinant human maltase glucoamylase, Carbohyd. Res. 342 (2007) 901-912.
    • (2007) Carbohyd. Res. , vol.342 , pp. 901-912
    • Mohan, S.1    Sim, L.2    Rose, D.R.3    Pinto, B.M.4
  • 132
    • 79960343811 scopus 로고    scopus 로고
    • Selection of the biological activity of DNJ neoglycoconjugates through click. Length variation of the side chain
    • N. Ardes-Guisot, D.S. Alonzi, G. Reinkensmeier, et al., Selection of the biological activity of DNJ neoglycoconjugates through click. length variation of the side chain, Org. Biomol. Chem. 9 (2011) 5373-5388.
    • (2011) Org. Biomol. Chem. , vol.9 , pp. 5373-5388
    • Ardes-Guisot, N.1    Alonzi, D.S.2    Reinkensmeier, G.3
  • 134
    • 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 α-glucosidase inhibitor
    • R. Eskandari, Kyra Jones, David R. Rose, B. Mario Pinto, 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 α-glucosidase inhibitor, Bioorg. Med. Chem. Lett. 20 (2010) 5686-5689.
    • (2010) Bioorg. Med. Chem. Lett. , vol.20 , pp. 5686-5689
    • Eskandari, R.1    Jones, K.2    Rose, D.R.3    Mario Pinto, B.4
  • 135
    • 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
    • K. Jayakanthan, S. Mohan, B.M. Pinto, 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. 131 (2009) 5621-5626.
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 5621-5626
    • Jayakanthan, K.1    Mohan, S.2    Pinto, B.M.3
  • 136
    • 77749298218 scopus 로고    scopus 로고
    • Synthesis and biological evaluation of heteroanalogues of kotalanol and de-osulfonated kotalanol
    • S. Mohan, K. Jayakanthan, R. Nasi, D.A. Kuntz, D.R. Rose, B.M. Pinto, Synthesis and biological evaluation of heteroanalogues of kotalanol and de-Osulfonated kotalanol, Org. Lett. 12 (2010) 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
  • 137
    • 27644560989 scopus 로고    scopus 로고
    • Sulfonamide chalcone as a new class of α-glucosidase inhibitors
    • W.D. Seo, J.H. Kim, J.E. Kang, et al., Sulfonamide chalcone as a new class of α-glucosidase inhibitors, Bioorg. Med. Chem. Lett. 15 (2005) 5514-5516.
    • (2005) Bioorg. Med. Chem. Lett. , vol.15 , pp. 5514-5516
    • Seo, W.D.1    Kim, J.H.2    Kang, J.E.3
  • 138
    • 75849129602 scopus 로고    scopus 로고
    • Synthesis and evaluation of the α-glucosidase inhibitory activity of 3-[4-(phenylsulfonamido)benzoyl]-2H-1-benzopyran-2-one derivatives
    • S. Wang, J. Yan, X. Wang, Z. Yang, F. Lin, T. Zhang, Synthesis and evaluation of the α-glucosidase inhibitory activity of 3-[4-(phenylsulfonamido)benzoyl]-2H-1-benzopyran-2-one derivatives, Eur. J. Med. Chem. 45 (2010) 1250-1255.
    • (2010) Eur. J. Med. Chem. , vol.45 , pp. 1250-1255
    • Wang, S.1    Yan, J.2    Wang, X.3    Yang, Z.4    Lin, F.5    Zhang, T.6
  • 139
    • 84900006607 scopus 로고    scopus 로고
    • Synthesis and biological evaluation of new substituted 3-[4 (Phenylsulfonamido)benzoyl]-2H-1-benzopyran-2-one derivatives as α-glucosidase inhibitors
    • Y. Wang, T. Zhang, J. Liang, F. Meng, S. Wang, Synthesis and biological evaluation of new substituted 3-[4 (Phenylsulfonamido)benzoyl]-2H-1-benzopyran-2-one derivatives as α-glucosidase inhibitors, J. Chem. Vol. (2014) 6. Article ID 590129, http://dx.doi.org/10.1155/2014/590129.
    • (2014) J. Chem. Vol. , pp. 6
    • Wang, Y.1    Zhang, T.2    Liang, J.3    Meng, F.4    Wang, S.5
  • 140
    • 21044454550 scopus 로고    scopus 로고
    • Syntheses and biological activities of chalcone and 1,5-benzothiazepine derivatives: Promising new free-radical scavengers, and esterase, urease, and α-glucosidase inhibitors
    • F.L. Ansari, S. Umbreen, L. Hussain, et al., Syntheses and biological activities of chalcone and 1,5-benzothiazepine derivatives: promising new free-radical scavengers, and esterase, urease, and α-glucosidase inhibitors, Chem. Biodivers. 2 (2005) 487-496.
    • (2005) Chem. Biodivers. , vol.2 , pp. 487-496
    • Ansari, F.L.1    Umbreen, S.2    Hussain, L.3
  • 141
    • 84861864708 scopus 로고    scopus 로고
    • Synthesis of antihyperglycemic, α-glucosidase inhibitory, and DPPH free radical scavenging furanochalcones
    • R.R. Rao, A.K. Tiwari, P.P. Reddy, et al., Synthesis of antihyperglycemic, α-glucosidase inhibitory, and DPPH free radical scavenging furanochalcones, Med. Chem. Res. 21 (2012) 760-774.
    • (2012) Med. Chem. Res. , vol.21 , pp. 760-774
    • Rao, R.R.1    Tiwari, A.K.2    Reddy, P.P.3
  • 142
  • 143
    • 33745633857 scopus 로고    scopus 로고
    • Synthesis and pharmacological activities of xanthone derivatives as α-glucosidase inhibitors
    • Y. Liu, L. Zou, L. Ma, W. Chen, B. Wang, Z. Xu, Synthesis and pharmacological activities of xanthone derivatives as α-glucosidase inhibitors, Bioorg. Med. Chem. 14 (2006) 5683-5690.
    • (2006) Bioorg. Med. Chem. , vol.14 , pp. 5683-5690
    • Liu, Y.1    Zou, L.2    Ma, L.3    Chen, W.4    Wang, B.5    Xu, Z.6
  • 144
    • 33947097019 scopus 로고    scopus 로고
    • Synthesis of xanthone derivatives with extended p-systems as α-glucosidase inhibitors: Insight into the probable binding mode
    • Y. Liu, L. Ma, W. Chen, B. Wang, Z. Xu, Synthesis of xanthone derivatives with extended p-systems as α-glucosidase inhibitors: Insight into the probable binding mode, Bioorg. Med. Chem. 15 (2007) 2810-2814.
    • (2007) Bioorg. Med. Chem. , vol.15 , pp. 2810-2814
    • Liu, Y.1    Ma, L.2    Chen, W.3    Wang, B.4    Xu, Z.5
  • 146
    • 33745842592 scopus 로고    scopus 로고
    • Development of peptidic dopamine transporter inhibitors via aromatic modificationmediated conformational restriction
    • J.-G. Ding, J.-H. Shi, D.-F. Cui, L.-F. Xu, S.-H. Duan, L.-H. Guo, J. Fei, Development of peptidic dopamine transporter inhibitors via aromatic modificationmediated conformational restriction, J. Med. Chem. 49 (2006) 4048-4051.
    • (2006) J. Med. Chem. , vol.49 , pp. 4048-4051
    • Ding, J.-G.1    Shi, J.-H.2    Cui, D.-F.3    Xu, L.-F.4    Duan, S.-H.5    Guo, L.-H.6    Fei, J.7
  • 147
    • 33644635257 scopus 로고    scopus 로고
    • Toward a detailed understanding of base excision repair enzymes: Transition state and mechanistic analyses of N-glycoside hydrolysis and N-glycoside transfer
    • P.J. Berti, J.A.B. McCann, Toward a detailed understanding of base excision repair enzymes: transition state and mechanistic analyses of N-glycoside hydrolysis and N-glycoside transfer, Chem. Rev. 106 (2006) 506-555.
    • (2006) Chem. Rev. , vol.106 , pp. 506-555
    • Berti, P.J.1    McCann, J.A.B.2
  • 148
    • 0001749787 scopus 로고    scopus 로고
    • Structural insight into the aromatic amino acid hydroxylases and their disease-related mutant forms
    • T. Flatmark, R.C. Stevens, Structural insight into the aromatic amino acid hydroxylases and their disease-related mutant forms, Chem. Rev. 99 (1999) 2137-2160.
    • (1999) Chem. Rev. , vol.99 , pp. 2137-2160
    • Flatmark, T.1    Stevens, R.C.2
  • 149
    • 80052930257 scopus 로고    scopus 로고
    • Toward potent α-glucosidase inhibitors based on xanthones: A closer look into the structure-activity correlations
    • G. Li, J. He, A. Zhang, Y. Wan, B. Wang, W. Chen, Toward potent α-glucosidase inhibitors based on xanthones: a closer look into the structure-activity correlations, Eur. J. Med. Chem. 46 (2011) 4050-4055.
    • (2011) Eur. J. Med. Chem. , vol.46 , pp. 4050-4055
    • Li, G.1    He, J.2    Zhang, A.3    Wan, Y.4    Wang, B.5    Chen, W.6
  • 150
    • 69749110735 scopus 로고    scopus 로고
    • Alpha-glucosidase inhibitory effect of anti-diabetic metal ions and their complexes
    • Y. Yutaka, H. Ryoko, Y. Hiroyuki, S. Hiromu, Alpha-glucosidase inhibitory effect of anti-diabetic metal ions and their complexes, Biochimie 91 (2009) 1339-1341.
    • (2009) Biochimie , vol.91 , pp. 1339-1341
    • Yutaka, Y.1    Ryoko, H.2    Hiroyuki, Y.3    Hiromu, S.4
  • 151
    • 84937764132 scopus 로고    scopus 로고
    • Silver(I) complexes of 2,4-dihydroxybenzaldehyde-amino acid Schiff bases-novel noncompetitive α-glucosidase inhibitors
    • J. Zheng, L. Ma, Silver(I) complexes of 2,4-dihydroxybenzaldehyde-amino acid Schiff bases-Novel noncompetitive α-glucosidase inhibitors, Bioorg. Med. Chem. Lett. 25 (2015) 2156-2161.
    • (2015) Bioorg. Med. Chem. Lett. , vol.25 , pp. 2156-2161
    • Zheng, J.1    Ma, L.2
  • 152
    • 42749087181 scopus 로고    scopus 로고
    • Binding mode analyses and pharmacophore model development for sulfonamide chalcone derivatives, a new class of alpha-glucosidase inhibitors
    • K. Bharatham, N. Bharatham, K.H. Park, K.W. Lee, Binding mode analyses and pharmacophore model development for sulfonamide chalcone derivatives, a new class of alpha-glucosidase inhibitors, J. Mol. Graph. Model 26 (2008) 1202-1212.
    • (2008) J. Mol. Graph. Model , vol.26 , pp. 1202-1212
    • Bharatham, K.1    Bharatham, N.2    Park, K.H.3    Lee, K.W.4
  • 153
    • 0021750054 scopus 로고
    • Inositol trisphosphate, a novel second messenger in cellular signal transduction
    • M.J. Berridge, R.F. Irvine, Inositol trisphosphate, a novel second messenger in cellular signal transduction, Nature 312 (1984) 315-321.
    • (1984) Nature , vol.312 , pp. 315-321
    • Berridge, M.J.1    Irvine, R.F.2
  • 154
    • 0027397544 scopus 로고
    • Inositol trisphosphate and calcium signalling
    • M.J. Berridge, Inositol trisphosphate and calcium signalling, Nature 361 (1993) 315-325.
    • (1993) Nature , vol.361 , pp. 315-325
    • Berridge, M.J.1
  • 155
    • 0035347166 scopus 로고    scopus 로고
    • Back in the water: The return of the inositol phosphates
    • R.F. Irvine, M.J. Schell, Back in the water: the return of the inositol phosphates, Nat. Rev. Mol. Cell Biol. 2 (2001) 327-338.
    • (2001) Nat. Rev. Mol. Cell Biol. , vol.2 , pp. 327-338
    • Irvine, R.F.1    Schell, M.J.2
  • 156
    • 77957110729 scopus 로고    scopus 로고
    • Asymmetric synthesis of hydroxy-skipped bishomoinositols as potential glycosidase inhibitors
    • T. Mahapatra, S. Nanda, Asymmetric synthesis of hydroxy-skipped bishomoinositols as potential glycosidase inhibitors, Tetrahedron Asymmetry 21 (2010) 2199-2205.
    • (2010) Tetrahedron Asymmetry , vol.21 , pp. 2199-2205
    • Mahapatra, T.1    Nanda, S.2
  • 157
    • 84870237734 scopus 로고    scopus 로고
    • Synthesis of novel mono and bis-indole conduritol derivatives and their a/b-glycosidase inhibitory effects
    • H. Çavdar, O. Talaz, D. Ekinci, Synthesis of novel mono and bis-indole conduritol derivatives and their a/b-glycosidase inhibitory effects, Bioorg. Med. Chem. Lett. 22 (2012) 7499-7503.
    • (2012) Bioorg. Med. Chem. Lett. , vol.22 , pp. 7499-7503
    • Çavdar, H.1    Talaz, O.2    Ekinci, D.3
  • 158
    • 29244469393 scopus 로고    scopus 로고
    • Polycyclitols - Novel conduritol and carbasugar hybrids as new glycosidase inhibitors
    • G. Mehta, S.S. Ramesh, Polycyclitols - novel conduritol and carbasugar hybrids as new glycosidase inhibitors, Can. J. Chem. 83 (2005) 581-594.
    • (2005) Can. J. Chem. , vol.83 , pp. 581-594
    • Mehta, G.1    Ramesh, S.S.2
  • 160
    • 84879478601 scopus 로고    scopus 로고
    • Quercitylcinnamates, a new series of antidiabetic bioconjugates possessing α-glucosidase inhibition and antioxidant
    • E. Rattanangkool, et al., Quercitylcinnamates, a new series of antidiabetic bioconjugates possessing α-glucosidase inhibition and antioxidant, Eur. J. Med. Chem. 66 (2013) 296-304.
    • (2013) Eur. J. Med. Chem. , vol.66 , pp. 296-304
    • Rattanangkool, E.1
  • 161
    • 77949838793 scopus 로고    scopus 로고
    • Synthesis, biological activity, and molecular modeling studies of 1H-1,2,3-triazole derivatives of carbohydrates as α-glucosidases inhibitors
    • S.B. Ferreira, A.C.R. Sodero, M.F.C. Cardoso, E.S. Lima, C.R. Kaiser, F.P. Silva Jr., V.F. Ferreira, Synthesis, biological activity, and molecular modeling studies of 1H-1,2,3-triazole derivatives of carbohydrates as α-glucosidases inhibitors, J. Med. Chem. 53 (2010) 2364-2375.
    • (2010) J. Med. Chem. , vol.53 , pp. 2364-2375
    • Ferreira, S.B.1    Sodero, A.C.R.2    Cardoso, M.F.C.3    Lima, E.S.4    Kaiser, C.R.5    Silva, F.P.6    Ferreira, V.F.7
  • 163
    • 84920848432 scopus 로고    scopus 로고
    • Synthesis of novel inhibitors of α-glucosidase based on the benzothiazole skeleton containing benzohydrazide moiety and their molecular docking studies
    • M. Taha, N.H. Ismail, S. Lalani, M.Q. Fatmi, et al., Synthesis of novel inhibitors of α-glucosidase based on the benzothiazole skeleton containing benzohydrazide moiety and their molecular docking studies, Eur. J. Med. Chem. 92 (2015) 387-400.
    • (2015) Eur. J. Med. Chem. , vol.92 , pp. 387-400
    • Taha, M.1    Ismail, N.H.2    Lalani, S.3    Fatmi, M.Q.4
  • 164
    • 84901929620 scopus 로고    scopus 로고
    • Discovery of novel oxindole derivatives as potent α-glucosidase inhibitors
    • M. Khan, M. Yousaf, A. Wadood, et al., Discovery of novel oxindole derivatives as potent α-glucosidase inhibitors, Bioorg. Med. Chem. 22 (2014) 3441-3448.
    • (2014) Bioorg. Med. Chem. , vol.22 , pp. 3441-3448
    • Khan, M.1    Yousaf, M.2    Wadood, A.3
  • 165
    • 0030202106 scopus 로고
    • Novel α-glucosidase inhibitors identified using multiple cyclic peptide combinatorial libraries
    • J. Eichler, A.W. Lucka, C. Pinilla, R.A. Houghten, Novel α-glucosidase inhibitors identified using multiple cyclic peptide combinatorial libraries, Mol. Divers. 1 (1995) 233-240.
    • (1995) Mol. Divers. , vol.1 , pp. 233-240
    • Eichler, J.1    Lucka, A.W.2    Pinilla, C.3    Houghten, R.A.4
  • 166
    • 80051793911 scopus 로고    scopus 로고
    • Novel peptides derived from egg white protein inhibiting alpha-glucosidase
    • Z. Yu, Y. Yin, W. Zhao, Y. Yu, B. Liu, J. Liu, F. Chen, Novel peptides derived from egg white protein inhibiting alpha-glucosidase, Food Chem. 129 (2011) 1376-1382.
    • (2011) Food Chem. , vol.129 , pp. 1376-1382
    • Yu, Z.1    Yin, Y.2    Zhao, W.3    Yu, Y.4    Liu, B.5    Liu, J.6    Chen, F.7
  • 167
    • 0034987346 scopus 로고    scopus 로고
    • Tibolone: A steroid with a tissue-specific mode of action
    • H.J.J. Kloosterboer, Tibolone: a steroid with a tissue-specific mode of action, Steroid Biochem. Mol. Biol. 76 (2001) 231-238.
    • (2001) Steroid Biochem. Mol. Biol. , vol.76 , pp. 231-238
    • Kloosterboer, H.J.J.1
  • 169
    • 9644287713 scopus 로고    scopus 로고
    • Tibolone is metabolized by the 3alpha/3beta-hydroxysteroid dehydrogenase activities of the four human isozymes of the aldo-keto reductase 1C subfamily: Inversion of stereospecificity with a delta5(10)-3-ketosteroid
    • S. Steckelbroeck, Y.B. Oyesanmi Jin, H.J. Kloosterboer, T.M. Penning, Tibolone is metabolized by the 3alpha/3beta-hydroxysteroid dehydrogenase activities of the four human isozymes of the aldo-keto reductase 1C subfamily: inversion of stereospecificity with a delta5(10)-3-ketosteroid, Mol. Pharmacol. 66 (2004) 1702-1711.
    • (2004) Mol. Pharmacol. , vol.66 , pp. 1702-1711
    • Steckelbroeck, S.1    Oyesanmi Jin, Y.B.2    Kloosterboer, H.J.3    Penning, T.M.4
  • 170
    • 4344581290 scopus 로고    scopus 로고
    • Tibolone: A selective tissue estrogenic activity regulator (STEAR)
    • M.J. Reed, H.J. Kloosterboer, Tibolone: a selective tissue estrogenic activity regulator (STEAR), Maturitas 48 (2004) 4-6.
    • (2004) Maturitas , vol.48 , pp. 4-6
    • Reed, M.J.1    Kloosterboer, H.J.2
  • 171
    • 37149008949 scopus 로고    scopus 로고
    • Science at the interface of chemistry and biology: Discoveries of α-glucosidase inhibitors and antiglycation agents
    • Atta-ur-Rahman, M.I. Choudhary, F.Z. Basha, G. Abbas, S.N. Khan, S.A.A. Shah, Science at the interface of chemistry and biology: discoveries of α-glucosidase inhibitors and antiglycation agents, Pure Appl. Chem. 79 (2007) 2263-2268
    • (2007) Pure Appl. Chem. , vol.79 , pp. 2263-2268
    • Atta-ur-Rahman, M.I.C.1    Basha, F.Z.2    Abbas, G.3    Khan, S.N.4    Shah, S.A.A.5
  • 172
    • 84875993094 scopus 로고    scopus 로고
    • Fungal transformation of cedryl acetate and α-glucosidase inhibition assay, quantum mechanical calculations and molecular docking studies of its metabolites
    • S. Sultan, et al., Fungal transformation of cedryl acetate and α-glucosidase inhibition assay, quantum mechanical calculations and molecular docking studies of its metabolites, Eur. J. Med. Chem. 62 (2013) 764-770.
    • (2013) Eur. J. Med. Chem. , vol.62 , pp. 764-770
    • Sultan, S.1
  • 173
    • 34247636613 scopus 로고    scopus 로고
    • Synthesis of andrographolide derivatives: A new family of α-glucosidase inhibitors
    • H.W. Xu, G.F. Dai, G.Z. Liu, J.F. Wang, H.M. Liu, Synthesis of andrographolide derivatives: a new family of α-glucosidase inhibitors, Bioorg Med. Chem. 2007 (15) (2007) 4247-4255.
    • (2007) Bioorg Med. Chem. , vol.2007 , Issue.15 , pp. 4247-4255
    • Xu, H.W.1    Dai, G.F.2    Liu, G.Z.3    Wang, J.F.4    Liu, H.M.5
  • 174
    • 75849139352 scopus 로고    scopus 로고
    • Modification of 15-akylidene andrographolide derivatives as alpha-glucosidase inhibitor
    • H.W. Xu, G. Liu, D. Gui-Fu, C. Wu, H. Liu, Modification of 15-akylidene andrographolide derivatives as alpha-glucosidase inhibitor, Drug Discov. Ther. 1 (2007) 73-77.
    • (2007) Drug Discov. Ther. , vol.1 , pp. 73-77
    • Xu, H.W.1    Liu, G.2    Gui-Fu, D.3    Wu, C.4    Liu, H.5
  • 176
    • 0001216096 scopus 로고    scopus 로고
    • Recent insights into inhibition, structure, and mechanism of configuration-retaining glycosidases
    • T.D. Heightman, A.T. Vasella, Recent insights into inhibition, structure, and mechanism of configuration-retaining glycosidases, Angew. Chem. 111 (1999) 794-815.
    • (1999) Angew. Chem. , vol.111 , pp. 794-815
    • Heightman, T.D.1    Vasella, A.T.2
  • 177
    • 0035925104 scopus 로고    scopus 로고
    • Polyhydroxylated alkaloids - Natural occurrence and therapeutic applications
    • A.A. Watson, G.W.J. Fleet, N. Asano, R.J. Molyneux, R.J. Nash, Polyhydroxylated alkaloids - natural occurrence and therapeutic applications, Phytochemistry 56 (2001) 265-295.
    • (2001) Phytochemistry , vol.56 , pp. 265-295
    • Watson, A.A.1    Fleet, G.W.J.2    Asano, N.3    Molyneux, R.J.4    Nash, R.J.5
  • 180
    • 79751486202 scopus 로고    scopus 로고
    • A novel competitive class of α-glucosidase inhibitors: (E)-1-phenyi-3-(4-styrylphenyi)urea derivatives
    • J.Y. Kim, J.W. Lee, Y.S. Kim, et al., A novel competitive class of α-glucosidase inhibitors: (E)-1-phenyi-3-(4-styrylphenyi)urea derivatives, ChemBioChem 11 (2010) 2725-2737.
    • (2010) ChemBioChem , vol.11 , pp. 2725-2737
    • Kim, J.Y.1    Lee, J.W.2    Kim, Y.S.3


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