메뉴 건너뛰기




Volumn 10, Issue 12, 2010, Pages 1139-1155

Recent advances in the allosteric inhibition of glycogen phosphorylase

Author keywords

Allosteric inhibition; Glycogen phosphorylase; Inhibitor; Structure based drug design

Indexed keywords

GLUCOSE 1 PHOSPHATE; GLYCOGEN; GLYCOGEN PHOSPHORYLASE; INDOLE; PHOSPHATE BINDING PROTEIN;

EID: 78549267168     PISSN: 13895575     EISSN: None     Source Type: Journal    
DOI: 10.2174/1389557511009011139     Document Type: Article
Times cited : (33)

References (169)
  • 2
    • 0024322304 scopus 로고
    • The allosteric transition of glycogenphosphorylase
    • Barford, D.; Johnson, L. N. The allosteric transition of glycogenphosphorylase. Nature (London, UK), 1989, 340, 609-616.
    • (1989) Nature (London, UK) , vol.340 , pp. 609-616
    • Barford, D.1    Johnson, L.N.2
  • 3
    • 0035110957 scopus 로고    scopus 로고
    • Glycogen phosphory-lase inhibitors for treatment of type 2 diabetes mellitus
    • Treadway, J. L.; Mendys, P.; Hoover, D. J. Glycogen phosphory-lase inhibitors for treatment of type 2 diabetes mellitus. Exp. Opin.Invest. Drugs, 2001, 10(3), 439-454.
    • (2001) Exp. Opin.Invest. Drugs , vol.10 , Issue.3 , pp. 439-454
    • Treadway, J.L.1    Mendys, P.2    Hoover, D.J.3
  • 4
    • 0023860930 scopus 로고
    • Human brain glycogen phosphorylase. Cloning, se-quence analysis, chromosomal mapping, tissue expression, andcomparison with the human liver and muscle isozymes
    • Newgard, C. B., Littman D. R., van Genderen C., Smith, M., andFletterick R. J. Human brain glycogen phosphorylase. Cloning, se-quence analysis, chromosomal mapping, tissue expression, andcomparison with the human liver and muscle isozymes. J. Biol.Chem., 1988, 263(8), 3850-3957.
    • (1988) J. Biol.Chem , vol.263 , Issue.8 , pp. 3850-3957
    • Newgard, C.B.1    Littman, D.R.2    van Genderen, C.3    Smith, M.4    Andfletterick, R.J.5
  • 5
    • 0019325629 scopus 로고
    • Zanotti,G. Proposals for the catalytic mechanism of glycogen phosphory-lase b prompted by crystallographic studies on glucose-1-phosphate
    • Johnson, L. N., Jenkins, J. A., Wilson, K. S., Stura, E. A., Zanotti,G. Proposals for the catalytic mechanism of glycogen phosphory-lase b prompted by crystallographic studies on glucose-1-phosphate. J. Mol. Biol., 1980, 140, 565-580.
    • (1980) J. Mol. Biol , vol.140 , pp. 565-580
    • Johnson, L.N.1    Jenkins, J.A.2    Wilson, K.S.3    Stura, E.A.4
  • 7
    • 0036185751 scopus 로고    scopus 로고
    • The 1.76 angstrom resolution crystal structure of glycogenphosphorylase B complexed with glucose, and CP320626, a poten-tial antidiabetic drug
    • Oikonomakos, N. G., Zographos, S. E., Skamnaki, V. T., Archon-tis, G. The 1.76 angstrom resolution crystal structure of glycogenphosphorylase B complexed with glucose, and CP320626, a poten-tial antidiabetic drug. Bioorg. Med. Chem., 2002, 10(5), 1313-1319.
    • (2002) Bioorg. Med. Chem , vol.10 , Issue.5 , pp. 1313-1319
    • Oikonomakos, N.G.1    Zographos, S.E.2    Skamnaki, V.T.3    Archon-Tis, G.4
  • 8
    • 0029788096 scopus 로고    scopus 로고
    • Role of the Active Site Gate ofGlycogen Phosphorylase in Allosteric Inhibition and SubstrateBinding
    • Buchbinder, J. L., Fletterick, R. J., Role of the Active Site Gate ofGlycogen Phosphorylase in Allosteric Inhibition and SubstrateBinding. J. Biol. Chem., 1996, 271, 22305-22309.
    • (1996) J. Biol. Chem , vol.271 , pp. 22305-22309
    • Buchbinder, J.L.1    Fletterick, R.J.2
  • 9
    • 78549253592 scopus 로고    scopus 로고
    • Use of glycogen phosphorylase inhibitors to inhibittumor growth
    • EP 1177791
    • Krasner, A. S. Use of glycogen phosphorylase inhibitors to inhibittumor growth. Eur. Pat. Appl.; EP 1177791 2002; 28.
    • (2002) Eur. Pat. Appl. , pp. 28
    • Krasner, A.S.1
  • 10
    • 0019212552 scopus 로고
    • Growth-related glycogen levels of human intestine carcinoma cell linesgrown in vitro and in vivo in nude mice
    • Rousset, M.; Dussaulx, E.; Chevalier, G.; Zweibaum, A. Growth-related glycogen levels of human intestine carcinoma cell linesgrown in vitro and in vivo in nude mice. J. Nat. Cancer Inst., 1980,65, 885-889.
    • (1980) J. Nat. Cancer Inst , vol.65 , pp. 885-889
    • Rousset, M.1    Dussaulx, E.2    Chevalier, G.3    Zweibaum, A.4
  • 11
    • 0036889606 scopus 로고    scopus 로고
    • Glycogen phosphorylase as a molecular targetfor type 2 diabetes therapy
    • Oikonomakos, N. G. Glycogen phosphorylase as a molecular targetfor type 2 diabetes therapy. Curr. Protein Pept. Sci., 2002, 3(6),561-586.
    • (2002) Curr. Protein Pept. Sci , vol.3 , Issue.6 , pp. 561-586
    • Oikonomakos, N.G.1
  • 14
    • 0037648878 scopus 로고    scopus 로고
    • Glucoseanalog inhibitors of glycogen phosphorylases as potential antidia-betic agents: Recent developments
    • Somsak, L.; Nagy, V.; Hadady, Z.; Docsa, T.; Gergely, P. Glucoseanalog inhibitors of glycogen phosphorylases as potential antidia-betic agents: Recent developments. Curr. Pharm. Des., 2003,9(15), 1177-1189.
    • (2003) Curr. Pharm. Des , vol.9 , Issue.15 , pp. 1177-1189
    • Somsak, L.1    Nagy, V.2    Hadady, Z.3    Docsa, T.4    Gergely, P.5
  • 17
    • 23644444478 scopus 로고    scopus 로고
    • Glycogen phos-phorylase inhibition in type 2 diabetes therapy: A systematicevaluation of metabolic and functional effects in rat skeletal mus-cle
    • Baker, D. J.; Timmons, J. A.; Greenhaff, P. L. Glycogen phos-phorylase inhibition in type 2 diabetes therapy: A systematicevaluation of metabolic and functional effects in rat skeletal mus-cle. Diabetes, 2005, 54(8), 2453-2459.
    • (2005) Diabetes , vol.54 , Issue.8 , pp. 2453-2459
    • Baker, D.J.1    Timmons, J.A.2    Greenhaff, P.L.3
  • 18
    • 33748311966 scopus 로고    scopus 로고
    • Theexperimental type 2 diabetes therapy glycogen phosphorylase inhi-bition can impair aerobic muscle function during prolonged con-traction
    • Baker, D. J.; Greenhaff, P. L.; MacInnes, A.; Timmons, J. A. Theexperimental type 2 diabetes therapy glycogen phosphorylase inhi-bition can impair aerobic muscle function during prolonged con-traction. Diabetes, 2006, 55(6), 1855-1861.
    • (2006) Diabetes , vol.55 , Issue.6 , pp. 1855-1861
    • Baker, D.J.1    Greenhaff, P.L.2    Macinnes, A.3    Timmons, J.A.4
  • 19
    • 0028988972 scopus 로고
    • Mutations inpaired -helixes at the subunit interface of glycogen phosphorylasealter homotropic and heterotropic cooperativity
    • Buchbinder, J. L.; Guinovart, J. J.; Fletterick, R. J. Mutations inpaired -helixes at the subunit interface of glycogen phosphorylasealter homotropic and heterotropic cooperativity. Biochemistry,1995, 34(19), 6423-6432.
    • (1995) Biochemistry , vol.34 , Issue.19 , pp. 6423-6432
    • Buchbinder, J.L.1    Guinovart, J.J.2    Fletterick, R.J.3
  • 20
    • 9544234747 scopus 로고
    • Glycogen phosphorylase structuresand function
    • Fletterick, R. J.; Sprang, S. R. Glycogen phosphorylase structuresand function. Acc. Chem. Res., 1982, 15(11), 361-369.
    • (1982) Acc. Chem. Res , vol.15 , Issue.11 , pp. 361-369
    • Fletterick, R.J.1    Sprang, S.R.2
  • 22
    • 0018867079 scopus 로고
    • The structures and related functionsof phosphorylase a
    • Fletterick, R. J.; Madsen, N. B. The structures and related functionsof phosphorylase a. Ann. Rev. Biochem., 1980, 49, 31-61.
    • (1980) Ann. Rev. Biochem , vol.49 , pp. 31-61
    • Fletterick, R.J.1    Madsen, N.B.2
  • 23
    • 0034660681 scopus 로고    scopus 로고
    • A new allosteric site in glycogen phosphory-lase b as a target for drug interactions
    • Oikonomakos, N. G.; Skamnaki, V. T.; Tsitsanou, K. E.; Gavalas, N. G.; Johnson, L. N. A new allosteric site in glycogen phosphory-lase b as a target for drug interactions. Structure, 2000, 8(6), 575-584.
    • (2000) Structure , vol.8 , Issue.6 , pp. 575-584
    • Oikonomakos, N.G.1    Skamnaki, V.T.2    Tsitsanou, K.E.3    Gavalas, N.G.4    Johnson, L.N.5
  • 24
    • 4444341801 scopus 로고    scopus 로고
    • Intervention of hepatic glucose production. Small moleculeregulators of potential targets for type 2 diabetes therapy
    • Barf, T. Intervention of hepatic glucose production. Small moleculeregulators of potential targets for type 2 diabetes therapy. Mini-Rev.Med. Chem., 2004, 4(8), 897-908.
    • (2004) Mini-Rev.Med. Chem , vol.4 , Issue.8 , pp. 897-908
    • Barf, T.1
  • 25
    • 33746906704 scopus 로고    scopus 로고
    • Glycogen Phosphorylase Inhibitors
    • Henke B. R.; Sparks S. M. Glycogen Phosphorylase Inhibitors. Mini-Rev. Med. Chem., 2006, 6(8), 845-857.
    • (2006) Mini-Rev. Med. Chem , vol.6 , Issue.8 , pp. 845-857
    • Henke, B.R.1    Sparks, S.M.2
  • 26
    • 33645794959 scopus 로고    scopus 로고
    • Glycogen phos-phorylase inhibition as a therapeutic target: A review of the recentpatent literature
    • Baker, D. J.; Greenhaff, P. L.; Timmons, J. A. Glycogen phos-phorylase inhibition as a therapeutic target: a review of the recentpatent literature. Exp. Opin. Ther. Pat., 2006, 16(4), 459-466.
    • (2006) Exp. Opin. Ther. Pat , vol.16 , Issue.4 , pp. 459-466
    • Baker, D.J.1    Greenhaff, P.L.2    Timmons, J.A.3
  • 28
    • 41949086319 scopus 로고    scopus 로고
    • Advances in glycogen phos-phorylase inhibitor design
    • Oikonomakos, N. G.; Somsak, L. Advances in glycogen phos-phorylase inhibitor design. Curr. Opin. Invest. Drugs, 2008, 9(4),379-395.
    • (2008) Curr. Opin. Invest. Drugs , vol.9 , Issue.4 , pp. 379-395
    • Oikonomakos, N.G.1    Somsak, L.2
  • 29
    • 0020481297 scopus 로고
    • Catalytic site of glycogen phosphorylase: Structureof the T state and specificity for -D-glucose
    • Sprang, S. R.; Goldsmith, E. J.; Fletterick, R. J.; Withers, S. G.; Madsen, N. B. Catalytic site of glycogen phosphorylase: Structureof the T state and specificity for -D-glucose. Biochemistry, 1982,21(21), 5364-5371.
    • (1982) Biochemistry , vol.21 , Issue.21 , pp. 5364-5371
    • Sprang, S.R.1    Goldsmith, E.J.2    Fletterick, R.J.3    Withers, S.G.4    Madsen, N.B.5
  • 32
    • 20144373860 scopus 로고    scopus 로고
    • Kinetic and crystallographicstudies on 2-(-D-glucopyranosyl)-5-methyl-1,3,4-oxadiazole, -benzothiazole, and -benzimidazole, inhibitors of muscle glycogenphosphorylase b. Evidence for a new binding site
    • Chrysina, E. D.; Kosmopoulou, M. N.; Tiraidis, C.; Kardakaris, R.; Bischler, N.; Leonidas, D. D.; Hadady, Z.; Somsak, L.; Docsa, T.; Gergely, P.; Oikonomakos, N. G. Kinetic and crystallographicstudies on 2-(-D-glucopyranosyl)-5-methyl-1,3,4-oxadiazole, -benzothiazole, and -benzimidazole, inhibitors of muscle glycogenphosphorylase b. Evidence for a new binding site. Protein Sci.,2005, 14(4), 873-888.
    • (2005) Protein Sci , vol.14 , Issue.4 , pp. 873-888
    • Chrysina, E.D.1    Kosmopoulou, M.N.2    Tiraidis, C.3    Kardakaris, R.4    Bischler, N.5    Leonidas, D.D.6    Hadady, Z.7    Somsak, L.8    Docsa, T.9    Gergely, P.10    Oikonomakos, N.G.11
  • 35
    • 0036185751 scopus 로고    scopus 로고
    • The 1.76.ANG. resolution crystal structure of glycogenphosphorylase b complexed with glucose, and CP 320626, a poten-tial antidiabetic drug
    • Oikonomakos, N. G.; Zographos, S. E.; Skamnaki, V. T.; Archon-tis, G. The 1.76.ANG. resolution crystal structure of glycogenphosphorylase b complexed with glucose, and CP 320626, a poten-tial antidiabetic drug. Bioorg. Med. Chem., 2002, 10(5), 1313-1319.
    • (2002) Bioorg. Med. Chem , vol.10 , Issue.5 , pp. 1313-1319
    • Oikonomakos, N.G.1    Zographos, S.E.2    Skamnaki, V.T.3    Archon-Tis, G.4
  • 37
    • 0025598298 scopus 로고
    • Comparison of thebinding of glucose and glucose 1-phosphate derivatives to T-stateglycogen phosphorylase b
    • Martin, J. L.; Johnson, L. N.; Withers, S. G. Comparison of thebinding of glucose and glucose 1-phosphate derivatives to T-stateglycogen phosphorylase b. Biochemistry, 1990, 29(44), 10745-10757.
    • (1990) Biochemistry , vol.29 , Issue.44 , pp. 10745-10757
    • Martin, J.L.1    Johnson, L.N.2    Withers, S.G.3
  • 38
    • 78549295987 scopus 로고    scopus 로고
    • Sugar-derived heterocycles and their precursors asinhibitors against glycogen phosphorylases (GP). Top
    • Khan, M. T. H. Sugar-derived heterocycles and their precursors asinhibitors against glycogen phosphorylases (GP). Top. Heterocycl.Chem., 2007, 9, 33-52.
    • (2007) Heterocycl.Chem , vol.9 , pp. 33-52
    • Khan, M.T.H.1
  • 39
    • 72649098245 scopus 로고    scopus 로고
    • Synthesis of new glycosyl biuret and urea de-rivatives as potential glycoenzyme inhibitors
    • Felfoldi, N.; Toth, M.; Chrysina, E. D.; Charavgi, M-D.; Alexacou, K-M.; Somsak, L. Synthesis of new glycosyl biuret and urea de-rivatives as potential glycoenzyme inhibitors. Carbohydr. Res.,2010, 345(2), 208-213.
    • (2010) Carbohydr. Res , vol.345 , Issue.2 , pp. 208-213
    • Felfoldi, N.1    Toth, M.2    Chrysina, E.D.3    Charavgi, M.-D.4    Alexacou, K.-M.5    Somsak, L.6
  • 40
    • 69349102811 scopus 로고    scopus 로고
    • Synthesis and glycogen phosphorylaseinhibitory activity of N-(-D-glucopyranosyl)amides possessing1,4-benzodioxane moiety
    • Czako, Z.; Juhasz, L.; Kenez, A.; Czifrak, K.; Somsak, L.; Docsa, T.; Gergely, P.; Antus, S. Synthesis and glycogen phosphorylaseinhibitory activity of N-(-D-glucopyranosyl)amides possessing1,4-benzodioxane moiety. Bioorg. Med. Chem., 2009, 17(18),6738-6741.
    • (2009) Bioorg. Med. Chem , vol.17 , Issue.18 , pp. 6738-6741
    • Czako, Z.1    Juhasz, L.2    Kenez, A.3    Czifrak, K.4    Somsak, L.5    Docsa, T.6    Gergely, P.7    Antus, S.8
  • 41
    • 48749129542 scopus 로고    scopus 로고
    • Diabetes mellitus increases the risk ofactive tuberculosis: A systematic review of 13 observational studies
    • Jeon, C. Y.; Murray, M. B. Diabetes mellitus increases the risk ofactive tuberculosis: a systematic review of 13 observational studies PLoS Med., 2008, 5(7), 1091-1101.
    • (2008) PLoS Med , vol.5 , Issue.7 , pp. 1091-1101
    • Jeon, C.Y.1    Murray, M.B.2
  • 42
    • 65349185611 scopus 로고    scopus 로고
    • Synthetic studies in butenonyl C-glycosides: Preparation of polyfunctional alkanonyl glycosides andtheir enzyme inhibitory activity
    • Bisht, S. S.; Fatima, S.; Tamrakar, A. K.; Rahuja, N.; Jaiswal, N.; Srivastava, Ar. K.; Tripathi, R. P. Synthetic studies in butenonyl C-glycosides: Preparation of polyfunctional alkanonyl glycosides andtheir enzyme inhibitory activity. Bioorg. Med. Chem. Lett., 2009,19(10), 2699-2703.
    • (2009) Bioorg. Med. Chem. Lett , vol.19 , Issue.10 , pp. 2699-2703
    • Bisht, S.S.1    Fatima, S.2    Tamrakar, A.K.3    Rahuja, N.4    Jaiswal, N.5    Srivastava Ar., K.6    Tripathi, R.P.7
  • 43
    • 7744243992 scopus 로고    scopus 로고
    • Bioisosterism: A rational approach indrug design
    • Patani, G. A.; LaVoie, E. J. Bioisosterism: A rational approach indrug design. Chem. Rev., 1996, 96(8), 3147-3176.
    • (1996) Chem. Rev , vol.96 , Issue.8 , pp. 3147-3176
    • Patani, G.A.1    Lavoie, E.J.2
  • 44
    • 11844255399 scopus 로고    scopus 로고
    • Bioisosterism: A useful strategy formolecular modification and drug design
    • Lima, L. M. A.; Barreiro, E. J. Bioisosterism: a useful strategy formolecular modification and drug design. Curr. Med. Chem., 2005,12(1), 23-49.
    • (2005) Curr. Med. Chem , vol.12 , Issue.1 , pp. 23-49
    • Lima, L.M.A.1    Barreiro, E.J.2
  • 45
    • 33646237557 scopus 로고    scopus 로고
    • The quest for bioisosteric re-placements
    • Wagener, M.; Lommerse, J. P. M. The quest for bioisosteric re-placements. J. Chem. Inf. Model., 2006, 46(2), 677-85.
    • (2006) J. Chem. Inf. Model , vol.46 , Issue.2 , pp. 677-685
    • Wagener, M.1    Lommerse, J.P.M.2
  • 47
    • 42449155497 scopus 로고    scopus 로고
    • Crystallographic andcomputational studies on 4-phenyl-N-(-D-glucopyranosyl)-1H-1,2,3-triazole-1-acetamide, an inhibitor of glycogen phosphory-lase: Comparison with -βD-glucose, N-acetyl-βD-glucopyranosylamine and N-benzoyl-N'-βD-glucopyranosyl ureabinding
    • Alexacou, K-M.; Hayes, J. M.; Tiraidis, C.; Zographos, S. E.; Leonidas, D. D.; Chrysina, E. D.; Archontis, G.; Oikonomakos, N.G.; Paul, J. V.; Varghese, B.; Loganathan, D. Crystallographic andcomputational studies on 4-phenyl-N-(-D-glucopyranosyl)-1H-1,2,3-triazole-1-acetamide, an inhibitor of glycogen phosphory-lase: comparison with -βD-glucose, N-acetyl-βD-glucopyranosylamine and N-benzoyl-N'-βD-glucopyranosyl ureabinding. Proteins: Struct. Funct. Bioinformatics, 2008, 71(3),1307-1323.
    • (2008) Proteins: Struct. Funct. Bioinformatics , vol.71 , Issue.3 , pp. 1307-1323
    • Alexacou, K.-M.1    Hayes, J.M.2    Tiraidis, C.3    Zographos, S.E.4    Leonidas, D.D.5    Chrysina, E.D.6    Archontis, G.7    Oikonomakos, N.G.8    Paul, J.V.9    Varghese, B.10    Loganathan, D.11
  • 48
    • 75449087225 scopus 로고    scopus 로고
    • Synthesis of 1-(glucopyranosyl)-1,2,3-triazoles and their evaluation as glycogenphosphorylase inhibitors
    • Bokor, E.; Docsa, T.; Gergely, P.; Somsak, L. Synthesis of 1-(glucopyranosyl)-1,2,3-triazoles and their evaluation as glycogenphosphorylase inhibitors. Bioorg. Med. Chem., 2010, 18(3), 1171-1180.
    • (2010) Bioorg. Med. Chem , vol.18 , Issue.3 , pp. 1171-1180
    • Bokor, E.1    Docsa, T.2    Gergely, P.3    Somsak, L.4
  • 49
    • 65249125749 scopus 로고    scopus 로고
    • Synthesis ofglucoconjugates of oleanolic acid as inhibitors of glycogen phos-phorylase
    • Cheng, K.; Liu, J.; Liu, X.; Li, H.; Sun, H.; Xie, J. Synthesis ofglucoconjugates of oleanolic acid as inhibitors of glycogen phos-phorylase. Carbohydr. Res., 2009, 344(7), 841-850.
    • (2009) Carbohydr. Res , vol.344 , Issue.7 , pp. 841-850
    • Cheng, K.1    Liu, J.2    Liu, X.3    Li, H.4    Sun, H.5    Xie, J.6
  • 50
    • 66749111878 scopus 로고    scopus 로고
    • Synthesis and struc-ture-activity relationships of C-glycosylated oxadiazoles as inhibi-tors of glycogen phosphorylase
    • Toth, M.; Kun, S.; Bokor, E.; Benltifa, M.; Tallec, G.; Vidal, S.; Docsa, T.; Gergely, P.; Somsak, L.; Praly, J-P. Synthesis and struc-ture-activity relationships of C-glycosylated oxadiazoles as inhibi-tors of glycogen phosphorylase. Bioorg. Med. Chem., 2009, 17(13),4773-4785.
    • (2009) Bioorg. Med. Chem , vol.17 , Issue.13 , pp. 4773-4785
    • Toth, M.1    Kun, S.2    Bokor, E.3    Benltifa, M.4    Tallec, G.5    Vidal, S.6    Docsa, T.7    Gergely, P.8    Somsak, L.9    Praly, J-P.10
  • 53
    • 58149144765 scopus 로고    scopus 로고
    • Probing multivalency for the inhibition of an enzyme:Glycogen phosphorylase as a case study
    • Cecioni, S.; Argintaru, O-A.; Docsa, T.; Gergely, P.; Praly, J-P.; Vidal, S. Probing multivalency for the inhibition of an enzyme:glycogen phosphorylase as a case study. New J. Chem., 2009,33(1), 148-156.
    • (2009) New J. Chem , vol.33 , Issue.1 , pp. 148-156
    • Cecioni, S.1    Argintaru, O.-A.2    Docsa, T.3    Gergely, P.4    Praly, J.-P.5    Vidal, S.6
  • 54
    • 0016787902 scopus 로고
    • Nature of the binding site for aromatic com-pounds in glycogen phosphorylase b
    • Soman, G.; Philip, G. Nature of the binding site for aromatic com-pounds in glycogen phosphorylase b. Biochem. J., 1975, 147, 369-371.
    • (1975) Biochem. J , vol.147 , pp. 369-371
    • Soman, G.1    Philip, G.2
  • 55
    • 0018243091 scopus 로고
    • Synergistic regula-tion of phosphorylase a by glucose and caffeine
    • Kasvinsky, P. J.; Shechosky, S.; Fletterick, R. J. Synergistic regula-tion of phosphorylase a by glucose and caffeine. J. Biol. Chem.,1978, 253(24), 9102-9106.
    • (1978) J. Biol. Chem , vol.253 , Issue.24 , pp. 9102-9106
    • Kasvinsky, P.J.1    Shechosky, S.2    Fletterick, R.J.3
  • 56
    • 0020492229 scopus 로고
    • Analysis of an allosteric binding site: The nucleoside in-hibitor site of phosphorylase a
    • Sprang, S.; Fletterick, R.; Stern, M.; Yang, D.; Madsen, N.; Stur-tevant J. Analysis of an allosteric binding site: the nucleoside in-hibitor site of phosphorylase a. Biochemistry, 1982, 21(9), 2036-2048.
    • (1982) Biochemistry , vol.21 , Issue.9 , pp. 2036-2048
    • Sprang, S.1    Fletterick, R.2    Stern, M.3    Yang, D.4    Madsen, N.5    Stur-Tevant, J.6
  • 57
    • 0034671986 scopus 로고    scopus 로고
    • StructuralBasis of the Synergistic Inhibition of Glycogen Phosphorylase a byCaffeine and a Potential Antidiabetic Drug
    • Tsitsanou, K. E.; Skamnaki, V. T.; Oikonomakos, N. G. StructuralBasis of the Synergistic Inhibition of Glycogen Phosphorylase a byCaffeine and a Potential Antidiabetic Drug. Arch. Biochem. Bio-phys., 2000, 384(2), 245-254.
    • (2000) Arch. Biochem. Bio-phys , vol.384 , Issue.2 , pp. 245-254
    • Tsitsanou, K.E.1    Skamnaki, V.T.2    Oikonomakos, N.G.3
  • 59
    • 23244439356 scopus 로고    scopus 로고
    • Indirubin-3'-aminooxy-acetate in-hibits glycogen phosphorylase by binding at the inhibitor and theallosteric site. Broad specificities of the two sites
    • Kosmopoulou, M. N.; Leonidas, D. D.; Chrysina, E. D.; Eisen-brand, G.; Oikonomakos, N. G. Indirubin-3'-aminooxy-acetate in-hibits glycogen phosphorylase by binding at the inhibitor and theallosteric site. Broad specificities of the two sites. Lett. Drug Des.Discov., 2005, 2(5), 377-390.
    • (2005) Lett. Drug Des.Discov , vol.2 , Issue.5 , pp. 377-390
    • Kosmopoulou, M.N.1    Leonidas, D.D.2    Chrysina, E.D.3    Eisen-Brand, G.4    Oikonomakos, N.G.5
  • 60
    • 2942544255 scopus 로고    scopus 로고
    • Binding of the potential antitumour agent indirubin-5-sulphonateat the inhibitor site of rabbit muscle glycogen phosphorylase b.Comparison with ligand binding to pCDK2-cyclin A complex
    • Kosmopoulou M. N; Leonidas D. D; Chrysina E. D; Bischler N.; Eisenbrand G.; Sakarellos C. E; Pauptit R.; Oikonomakos N. G. Binding of the potential antitumour agent indirubin-5-sulphonateat the inhibitor site of rabbit muscle glycogen phosphorylase b.Comparison with ligand binding to pCDK2-cyclin A complex. Eur.J. Biochem., 2004, 271(11), 2280-90.
    • (2004) Eur.J. Biochem , vol.271 , Issue.11 , pp. 2280-2290
    • Kosmopoulou, M.N.1    Leonidas, D.D.2    Chrysina, E.D.3    Bischler, N.4    Eisenbrand, G.5    Sakarellos, C.E.6    Pauptit, R.7    Oikonomakos, N.G.8
  • 63
    • 0032882213 scopus 로고    scopus 로고
    • Allosteric inhibition ofglycogen phosphorylase a by the potential antidiabetic drug 3-isopropyl 4-(2-chlorophenyl)-1,4-dihydro-1-ethyl-2-methyl-pyri-dine-3,5,6-tricarboxylate
    • Oikonomakos, N. G.; Tsitsanou, K. E.; Zographos, S. E.; Skam-naki, V. T.; Goldmann, S.; Bischoff, H. Allosteric inhibition ofglycogen phosphorylase a by the potential antidiabetic drug 3-isopropyl 4-(2-chlorophenyl)-1,4-dihydro-1-ethyl-2-methyl-pyri-dine-3,5,6-tricarboxylate. Protein Sci., 1999, 8(10), 1930-1945.
    • (1999) Protein Sci , vol.8 , Issue.10 , pp. 1930-1945
    • Oikonomakos, N.G.1    Tsitsanou, K.E.2    Zographos, S.E.3    Skam-Naki, V.T.4    Goldmann, S.5    Bischoff, H.6
  • 64
    • 0014806776 scopus 로고
    • Effect of glucose 6-phosphate onthe nucleotide site of glycogen phosphorylase b. General approachfor negative heterotropic interactions
    • Wang, J. H.; Tu, J. I.; Lo, F. M. Effect of glucose 6-phosphate onthe nucleotide site of glycogen phosphorylase b. General approachfor negative heterotropic interactions. J. Biol. Chem., 1970, 245,3115-3121.
    • (1970) J. Biol. Chem , vol.245 , pp. 3115-3121
    • Wang, J.H.1    Tu, J.I.2    Lo, F.M.3
  • 65
    • 0020525283 scopus 로고
    • Effect of glucose-6-P on thecatalytic and structural properties of glycogen phosphorylase a
    • Melpidou, A. E.; Oikonomakos, N. G. Effect of glucose-6-P on thecatalytic and structural properties of glycogen phosphorylase a. FEBS Lett., 1983, 154(1), 105-110.
    • (1983) FEBS Lett , vol.154 , Issue.1 , pp. 105-110
    • Melpidou, A.E.1    Oikonomakos, N.G.2
  • 66
    • 0027236184 scopus 로고
    • Crystallographic binding studies on the al-losteric inhibitor glucose-6-phosphate to T state glycogen phos-phorylase b
    • Johnson, L. N.; Snape, P.; Martin, J. L.; Acharya, K. R.; Barford, D.; Oikonomakos, N.G. Crystallographic binding studies on the al-losteric inhibitor glucose-6-phosphate to T state glycogen phos-phorylase b. J. Mol. Biol., 1993, 232(1), 253-67.
    • (1993) J. Mol. Biol , vol.232 , Issue.1 , pp. 253-267
    • Johnson, L.N.1    Snape, P.2    Martin, J.L.3    Acharya, K.R.4    Barford, D.5    Oikonomakos, N.G.6
  • 67
    • 3042545941 scopus 로고    scopus 로고
    • Westergaard, N.Identification, synthesis, and characterization of new glycogenphosphorylase inhibitors binding to the allosteric AMP site
    • Kristiansen, M.; Andersen, B.; Iversen, L. F.; Westergaard, N.Identification, synthesis, and characterization of new glycogenphosphorylase inhibitors binding to the allosteric AMP site. J. Med.Chem., 2004, 47(14), 3537-3545.
    • (2004) J. Med.Chem , vol.47 , Issue.14 , pp. 3537-3545
    • Kristiansen, M.1    Andersen, B.2    Iversen, L.F.3
  • 68
    • 0024260626 scopus 로고
    • Weakly polar interactions in proteins
    • Burley, S. K.; Petsko, G. A. Weakly polar interactions in proteins. Adv. Protein Chem., 1988, 39, 125-89.
    • (1988) Adv. Protein Chem , vol.39 , pp. 125-189
    • Burley, S.K.1    Petsko, G.A.2
  • 71
  • 73
    • 25144501079 scopus 로고    scopus 로고
    • FR258900, a novel glycogen phosphorylase inhibitor iso-lated from Fungus No. 138354. I. Taxonomy, fermentation, isola-tion and biological activities
    • Furukawa, S.; Tsurumi, Y.; Murakami, K.; Nakanishi, T.; Ohsumi, K.; Hashimoto, M.; Nishikawa, M.; Takase, S.; Nakayama, O.; Hino, M. FR258900, a novel glycogen phosphorylase inhibitor iso-lated from Fungus No. 138354. I. Taxonomy, fermentation, isola-tion and biological activities. J. Antibiot., 2005, 58(8), 497-502.
    • (2005) J. Antibiot , vol.58 , Issue.8 , pp. 497-502
    • Furukawa, S.1    Tsurumi, Y.2    Murakami, K.3    Nakanishi, T.4    Ohsumi, K.5    Hashimoto, M.6    Nishikawa, M.7    Takase, S.8    Nakayama, O.9    Hino, M.10
  • 74
    • 25144503390 scopus 로고    scopus 로고
    • FR258900, a novel glycogen phosphorylase inhibitor isolatedfrom Fungus No. 138354. II. Anti-hyperglycemic effects in dia-betic animal models
    • Furukawa, S.; Murakami, K.; Nakanishi, T.; Nakayama, O.; Hino, M. FR258900, a novel glycogen phosphorylase inhibitor isolatedfrom Fungus No. 138354. II. Anti-hyperglycemic effects in dia-betic animal models. J. Antibiot., 2005, 58(8), 503-506.
    • (2005) J. Antibiot , vol.58 , Issue.8 , pp. 503-506
    • Furukawa, S.1    Murakami, K.2    Nakanishi, T.3    Nakayama, O.4    Hino, M.5
  • 75
    • 34547610188 scopus 로고    scopus 로고
    • G FR258900, a potential anti-hyperglycemic drug, binds at the allosteric site of glycogen phos-phorylase
    • Tiraidis C.; Alexacou K-M.; Zographos S. E; Leonidas D. D; Gimisis T.; Oikonomakos N. G FR258900, a potential anti-hyperglycemic drug, binds at the allosteric site of glycogen phos-phorylase. Protein Sci., 2007, 16(8), 1773-82.
    • (2007) Protein Sci , vol.16 , Issue.8 , pp. 1773-1782
    • Tiraidis, C.1    Alexacou, K.-M.2    Zographos, S.E.3    Leonidas, D.D.4    Gimisis, T.5    Oikonomakos, N.6
  • 82
    • 34548833897 scopus 로고    scopus 로고
    • Pentacyclic triterpenes. Part 5: Synthesis andSAR study of corosolic acid derivatives as inhibitors of glycogenphosphorylases
    • Wen, X.; Xia, J.; Cheng, K.; Zhang, L.; Zhang, P.; Liu, J.; Zhang, L.; Ni, P.; Sun, H. Pentacyclic triterpenes. Part 5: Synthesis andSAR study of corosolic acid derivatives as inhibitors of glycogenphosphorylases. Bioorg. Med. Chem. Lett., 2007, 17(21), 5777-5782.
    • (2007) Bioorg. Med. Chem. Lett , vol.17 , Issue.21 , pp. 5777-5782
    • Wen, X.1    Xia, J.2    Cheng, K.3    Zhang, L.4    Zhang, P.5    Liu, J.6    Zhang, L.7    Ni, P.8    Sun, H.9
  • 83
    • 25844437477 scopus 로고    scopus 로고
    • Penta-cyclic triterpenes. Part 1: The first examples of naturally occurringpentacyclic triterpenes as a new class of inhibitors of glycogenphosphorylases
    • Wen, X.; Sun, H.; Liu, J.; Wu, G.; Zhang, L.; Wu, X.; Ni, P. Penta-cyclic triterpenes. Part 1: The first examples of naturally occurringpentacyclic triterpenes as a new class of inhibitors of glycogenphosphorylases. Bioorg. Med. Chem. Lett., 2005, 15(22), 4944-4948.
    • (2005) Bioorg. Med. Chem. Lett , vol.15 , Issue.22 , pp. 4944-4948
    • Wen, X.1    Sun, H.2    Liu, J.3    Wu, G.4    Zhang, L.5    Wu, X.6    Ni, P.7
  • 84
    • 29544449934 scopus 로고    scopus 로고
    • Pentacyclic triterpenes. Part 2: Synthesis and biological evaluationof maslinic acid derivatives as glycogen phosphorylase inhibitors
    • Wen, X.; Zhang, P.; Liu, J.; Zhang, L.; Wu, X.; Ni, P.; Sun, H. Pentacyclic triterpenes. Part 2: Synthesis and biological evaluationof maslinic acid derivatives as glycogen phosphorylase inhibitors. Bioorg. Med. Chem. Lett., 2006, 16(3), 722-726.
    • (2006) Bioorg. Med. Chem. Lett , vol.16 , Issue.3 , pp. 722-726
    • Wen, X.1    Zhang, P.2    Liu, J.3    Zhang, L.4    Wu, X.5    Ni, P.6    Sun, H.7
  • 85
    • 33646027276 scopus 로고    scopus 로고
    • Pentacyclic triterpenes. Part 3: Synthesis and biological evaluationof oleanolic acid derivatives as novel inhibitors of glycogen phos-phorylase
    • Chen, J.; Liu, J.; Zhang, L.; Wu, G.; Hua, W.; Wu, X.; Sun, H. Pentacyclic triterpenes. Part 3: Synthesis and biological evaluationof oleanolic acid derivatives as novel inhibitors of glycogen phos-phorylase. Bioorg. Med. Chem. Lett., 2006, 16(11), 2915-2919.
    • (2006) Bioorg. Med. Chem. Lett , vol.16 , Issue.11 , pp. 2915-2919
    • Chen, J.1    Liu, J.2    Zhang, L.3    Wu, G.4    Hua, W.5    Wu, X.6    Sun, H.7
  • 86
    • 67650122852 scopus 로고    scopus 로고
    • Synthesis and biological evaluation of asiatic acid derivatives asinhibitors of glycogen phosphorylases
    • Zhang, L.; Chen, J.; Gong, Y.; Liu, J.; Zhang, Lu.; Hua, W.; Sun, H. Synthesis and biological evaluation of asiatic acid derivatives asinhibitors of glycogen phosphorylases. Chem. Biodivers., 2009,6(6), 864-874.
    • (2009) Chem. Biodivers , vol.6 , Issue.6 , pp. 864-874
    • Zhang, L.1    Chen, J.2    Gong, Y.3    Liu, J.4    Zhang, L.5    Hua, W.6    Sun, H.7
  • 87
    • 68549135086 scopus 로고    scopus 로고
    • Efficientaccess to isomeric 2,3-dihydroxy lupanes: First synthesis of alphi-tolic acid
    • Hao, J.; Zhang, X.; Zhang, P.; Liu, J.; Zhang, L.; Sun, H. Efficientaccess to isomeric 2,3-dihydroxy lupanes: first synthesis of alphi-tolic acid. Tetrahedron, 2009, 65(38), 7975-7984.
    • (2009) Tetrahedron , vol.65 , Issue.38 , pp. 7975-7984
    • Hao, J.1    Zhang, X.2    Zhang, P.3    Liu, J.4    Zhang, L.5    Sun, H.6
  • 88
    • 71849096607 scopus 로고    scopus 로고
    • Terpenoids. III: Synthesis and biological evaluation of 23-hydroxybetulinic acid derivatives as novel inhibitors of glycogenphosphorylase
    • Zhu, P.; Bi, Y.; Xu, J.; Li, Z.; Liu, J.; Zhang, L.; Ye, W.; Wu, X. Terpenoids. III: Synthesis and biological evaluation of 23-hydroxybetulinic acid derivatives as novel inhibitors of glycogenphosphorylase. Bioorg. Med. Chem. Lett., 2009, 19(24), 6966-6969.
    • (2009) Bioorg. Med. Chem. Lett , vol.19 , Issue.24 , pp. 6966-6969
    • Zhu, P.1    Bi, Y.2    Xu, J.3    Li, Z.4    Liu, J.5    Zhang, L.6    Ye, W.7    Wu, X.8
  • 89
    • 58149175937 scopus 로고    scopus 로고
    • Practical Synthesis ofBredemolic Acid, a Natural Inhibitor of Glycogen Phosphorylase
    • Cheng, K.; Zhang, P.; Liu, J.; Xie, J.; Sun, H. Practical Synthesis ofBredemolic Acid, a Natural Inhibitor of Glycogen Phosphorylase. J. Nat. Prod., 2008, 71(11), 1877-1880.
    • (2008) J. Nat. Prod , vol.71 , Issue.11 , pp. 1877-1880
    • Cheng, K.1    Zhang, P.2    Liu, J.3    Xie, J.4    Sun, H.5
  • 90
    • 52149087225 scopus 로고    scopus 로고
    • Synthesisand biological evaluation of novel pyrazolo[4,3-b]oleanane deriva-tives as inhibitors of glycogen phosphorylase
    • Chen, J.; Gong, Y.; Liu, J.; Hua, W.; Zhang, L.; Sun, H. Synthesisand biological evaluation of novel pyrazolo[4,3-b]oleanane deriva-tives as inhibitors of glycogen phosphorylase. Chem. Biodivers.,2008, 5(7), 1304-1312.
    • (2008) Chem. Biodivers , vol.5 , Issue.7 , pp. 1304-1312
    • Chen, J.1    Gong, Y.2    Liu, J.3    Hua, W.4    Zhang, L.5    Sun, H.6
  • 91
    • 49649085088 scopus 로고    scopus 로고
    • New pentacyclic triterpenes fromGypsophila oldhamiana and their biological evaluation as glycogenphosphorylase inhibitors
    • Luo, J-G.; Liu, J.; Kong, L-Y. New pentacyclic triterpenes fromGypsophila oldhamiana and their biological evaluation as glycogenphosphorylase inhibitors. Chem. Biodivers., 2008, 5(5), 751-757.
    • (2008) Chem. Biodivers. , vol.5 , Issue.5 , pp. 751-757
    • Luo, J.-G.1    Liu, J.2    Kong, L.-Y.3
  • 92
    • 69949137712 scopus 로고    scopus 로고
    • Synthesis of 3-Deoxypentacyclic Triterpene Derivatives as Inhibi-tors of Glycogen Phosphorylase
    • Zhang, P.; Hao, J.; Liu, J.; Lu, Q.; Sheng, H.; Zhang, L.; Sun, H. Synthesis of 3-Deoxypentacyclic Triterpene Derivatives as Inhibi-tors of Glycogen Phosphorylase. J. Nat. Prod., 2009, 72(8), 1414-1418.
    • (2009) J. Nat. Prod , vol.72 , Issue.8 , pp. 1414-1418
    • Zhang, P.1    Hao, J.2    Liu, J.3    Lu, Q.4    Sheng, H.5    Zhang, L.6    Sun, H.7
  • 94
    • 13844311049 scopus 로고    scopus 로고
    • CoMFA and DockingStudies on Glycogen Phosphorylase a Inhibitors as AntidiabeticAgents
    • Prathipati, P.; Pandey, G.; Saxena, A. K. CoMFA and DockingStudies on Glycogen Phosphorylase a Inhibitors as AntidiabeticAgents. J. Chem. Inform. Comput. Sci., 2005, 45(1), 136-145.
    • (2005) J. Chem. Inform. Comput. Sci , vol.45 , Issue.1 , pp. 136-145
    • Prathipati, P.1    Pandey, G.2    Saxena, A.K.3
  • 95
    • 78549263489 scopus 로고    scopus 로고
    • Preparation of indole-2-carboxamidederivatives as glycogen phosphorylase inhibitors for treatment ofdiabetes
    • WO 2003091213
    • Onda, K.; Suzuki, T.; Shiraki, R.; Yonetoku, Y.; Ogiyama, T.; Maruyama, T.; Momose, K. Preparation of indole-2-carboxamidederivatives as glycogen phosphorylase inhibitors for treatment ofdiabetes. PCT. Int. Appl.; WO 2003091213, 2003.
    • (2003) PCT. Int. Appl
    • Onda, K.1    Suzuki, T.2    Shiraki, R.3    Yonetoku, Y.4    Ogiyama, T.5    Maruyama, T.6    Momose, K.7
  • 97
    • 78549239324 scopus 로고    scopus 로고
    • Preparation of indolecarbox-amides that possess glycogen phosphorylase inhibitory activity
    • WO 2003074517
    • Stocker, A.; Whittamore, P. R. O. Preparation of indolecarbox-amides that possess glycogen phosphorylase inhibitory activity. PCT. Int. Appl.; WO 2003074517, 2003.
    • (2003) PCT. Int. Appl.
    • Stocker, A.1    Whittamore, P.R.O.2
  • 98
    • 78549250155 scopus 로고    scopus 로고
    • Preparation of N-carbamoylmethylindolecarbox-amides as glycogen phosphorylase inhibitors
    • WO2003074485
    • Morley, A. D. Preparation of N-carbamoylmethylindolecarbox-amides as glycogen phosphorylase inhibitors. PCT. Int. Appl.; WO2003074485, 2003.
    • (2003) PCT. Int. Appl
    • Morley, A.D.1
  • 99
    • 24944556021 scopus 로고    scopus 로고
    • Preparation ofindolamide derivatives that possess glycogen phosphorylase inhibi-tory activity
    • WO 2003074484
    • Whittamore, P. R. O.; Bennett, S. N. L.; Simpson, I. Preparation ofindolamide derivatives that possess glycogen phosphorylase inhibi-tory activity. PCT. Int. Appl.; WO 2003074484, 2003.
    • (2003) PCT. Int. Appl
    • Whittamore, P.R.O.1    Bennett, S.N.L.2    Simpson, I.3
  • 100
    • 78549270897 scopus 로고    scopus 로고
    • Preparation of indole deriva-tives as inhibitors of human liver glycogen phosphorylase a
    • WO 2003037864
    • Nakamura, T.; Takagi, M.; Ueda, N. Preparation of indole deriva-tives as inhibitors of human liver glycogen phosphorylase a. PCT.Int. Appl.; WO 2003037864, 2003.
    • (2003) PCT.Int. Appl
    • Nakamura, T.1    Takagi, M.2    Ueda, N.3
  • 101
    • 78549268878 scopus 로고    scopus 로고
    • Preparation of N-heterocyclyl indole-2-carboxamides as glycogen phosphorylase inhibitors
    • WO 2003074513
    • Birch, A. M.; Morley, A. D. Preparation of N-heterocyclyl indole-2-carboxamides as glycogen phosphorylase inhibitors. PCT. Int.Appl.; WO 2003074513, 2003.
    • (2003) PCT. Int.Appl
    • Birch, A.M.1    Morley, A.D.2
  • 102
    • 78549267925 scopus 로고    scopus 로고
    • Preparation of indole-2-carboxamidederivatives as glycogen phosphorylase inhibitors
    • WO 2005020985
    • Bennett, S. N. L.; Simpson, I.: Preparation of indole-2-carboxamidederivatives as glycogen phosphorylase inhibitors. PCT. Int. Appl.;WO 2005020985, 2005.
    • (2005) PCT. Int. Appl
    • Bennett, S.N.L.1    Simpson, I.2
  • 103
    • 78549267925 scopus 로고    scopus 로고
    • Preparation ofindole-2-carboxamide derivatives as glycogen phosphorylase in-hibitors
    • WO 2005019172
    • Bennett, S. N. L.; Simpson, I.; Whittamore, P. R. O. Preparation ofindole-2-carboxamide derivatives as glycogen phosphorylase in-hibitors. PCT. Int. Appl.; WO 2005019172, 2005.
    • (2005) PCT. Int. Appl
    • Bennett, S.N.L.1    Simpson, I.2    Whittamore, P.R.O.3
  • 104
  • 106
    • 78549274475 scopus 로고    scopus 로고
    • Preparation of 2-amino-1-functionalizedtetralin derivatives and related glycogen phosphorylase inhibitors
    • WO 2006053274
    • Wu, G.; Sher, P. M. Preparation of 2-amino-1-functionalizedtetralin derivatives and related glycogen phosphorylase inhibitors. PCT. Int. Appl.; WO 2006053274, 2006.
    • (2006) PCT. Int. Appl
    • Wu, G.1    Sher, P.M.2
  • 110
    • 51449085578 scopus 로고    scopus 로고
    • Synthesis andpharmacological evaluation of bis-3-(3,4-di chlorophenyl)acryl-amide derivatives as glycogen phosphorylase inhibitors
    • Onda, K.; Shiraki, R.; Yonetoku, Y.; Momose, K.; Katayama, N.; Orita, M.; Yamaguchi, T.; Ohta, M.; Tsukamoto, S-I. Synthesis andpharmacological evaluation of bis-3-(3,4-di chlorophenyl)acryl-amide derivatives as glycogen phosphorylase inhibitors. Bioorg.Med. Chem., 2008, 16(18), 8627-8634.
    • (2008) Bioorg.Med. Chem , vol.16 , Issue.18 , pp. 8627-8634
    • Onda, K.1    Shiraki, R.2    Yonetoku, Y.3    Momose, K.4    Katayama, N.5    Orita, M.6    Yamaguchi, T.7    Ohta, M.8    Tsukamoto, S.-I.9
  • 111
  • 115
    • 33746289921 scopus 로고    scopus 로고
    • Reductive Amination of GlycosylAldoses: Synthesis of N-Glycosylated -Glycosyl Amino Alcoholsand their Enzyme Inhibitory Effect
    • Verma, S. S.; Mishra, R. C.; Tamarakar, A. K.; Tripathi, B. K.; Srivastava, A. K.; Tripathi, R. P. Reductive Amination of GlycosylAldoses: Synthesis of N-Glycosylated -Glycosyl Amino Alcoholsand their Enzyme Inhibitory Effect. J. Carbohydr. Chem., 2004,23(8-9), 493-511.
    • (2004) J. Carbohydr. Chem , vol.23 , Issue.8-9 , pp. 493-511
    • Verma, S.S.1    Mishra, R.C.2    Tamarakar, A.K.3    Tripathi, B.K.4    Srivastava, A.K.5    Tripathi, R.P.6
  • 117
    • 78549241039 scopus 로고    scopus 로고
    • Preparation of substituted 1H-indole-2-carboxamides and 6H-thieno[2,3-b]pyrrole-5-carboxamides as an-tidiabetic agents
    • WO 2003072570
    • Gammill, R. B. Preparation of substituted 1H-indole-2-carboxamides and 6H-thieno[2,3-b]pyrrole-5-carboxamides as an-tidiabetic agents. PCT. Int. Appl.; WO 2003072570, 2003.
    • (2003) PCT. Int. Appl
    • Gammill, R.B.1
  • 118
    • 58849114053 scopus 로고    scopus 로고
    • O.Matched molecular pair analysis of activity and properties of gly-cogen phosphorylase inhibitors
    • Birch, A. M.; Kenny, P. W.; Simpson, I.; Whittamore, P. R.O.Matched molecular pair analysis of activity and properties of gly-cogen phosphorylase inhibitors. Bioorg. Med. Chem. Lett., 2009,19(3), 850-853.
    • (2009) Bioorg. Med. Chem. Lett , vol.19 , Issue.3 , pp. 850-853
    • Birch, A.M.1    Kenny, P.W.2    Simpson, I.3    Whittamore, P.R.O.4
  • 120
    • 33751001756 scopus 로고    scopus 로고
    • Sen-sitivity of glycogen phosphorylase isoforms to indole site inhibitorsis markedly dependent on the activation state of the enzyme
    • Freeman, S.; Bartlett, J. B.; Convey, G.; Hardern, I.; Teague, J. L.; Loxham, S. J. G.; Allen, J. M.; Poucher, S. M.; Charles, A. D. Sen-sitivity of glycogen phosphorylase isoforms to indole site inhibitorsis markedly dependent on the activation state of the enzyme. Br. J.Pharmacol., 2006, 149(6), 775-85.
    • (2006) Br. J.Pharmacol , vol.149 , Issue.6 , pp. 775-785
    • Freeman, S.1    Bartlett, J.B.2    Convey, G.3    Hardern, I.4    Teague, J.L.5    Loxham, S.J.G.6    Allen, J.M.7    Poucher, S.M.8    Charles, A.D.9
  • 121
    • 78549289969 scopus 로고    scopus 로고
    • Preparation of bicyclic pyrrolyl amides as glycogen phosphorylaseinhibitors
    • WO 2002020530
    • Bartlett, J. B.; Freeman, S.; Kenny, P.; Morley, A.; Whittamore, P. Preparation of bicyclic pyrrolyl amides as glycogen phosphorylaseinhibitors. PCT. Int. Appl.; WO 2002020530, 2002.
    • (2002) PCT. Int. Appl
    • Bartlett, J.B.1    Freeman, S.2    Kenny, P.3    Morley, A.4    Whittamore, P.5
  • 123
    • 78549288976 scopus 로고    scopus 로고
    • Preparation ofsubstituted 1H-indole-2-carboxamides and 6H-thieno[2,3-b]pyrrole-5-carboxamides as antidiabetic agents
    • WO 2004041780
    • Bussolotti, D. L.; Gammill, R. B.; Polivkova, J. Preparation ofsubstituted 1H-indole-2-carboxamides and 6H-thieno[2,3-b]pyrrole-5-carboxamides as antidiabetic agents. PCT. Int. Appl.;WO 2004041780, 2004.
    • (2004) PCT. Int. Appl
    • Bussolotti, D.L.1    Gammill, R.B.2    Polivkova, J.3
  • 124
    • 78549270531 scopus 로고    scopus 로고
    • A preparation of indolecarbox-amide and thieno[2,3-b]pyrrolecarboxamide derivatives, useful asantidiabetic agents
    • US 2004220229
    • Bussolotti, D. L.; Gammill, R. B. A preparation of indolecarbox-amide and thieno[2,3-b]pyrrolecarboxamide derivatives, useful asantidiabetic agents. U.S. Pat. Appl. Publ.; US 2004220229, 2004.
    • (2004) U.S. Pat. Appl. Publ
    • Bussolotti, D.L.1    Gammill, R.B.2
  • 125
    • 78549267925 scopus 로고    scopus 로고
    • Preparation of thienopyrrole carbox-amides as glycogen phosphorylase inhibitors
    • WO2005020986
    • Bennett, S. N. L.; Simpson, I. Preparation of thienopyrrole carbox-amides as glycogen phosphorylase inhibitors. PCT. Int. Appl.; WO2005020986, 2005.
    • (2005) PCT. Int. Appl
    • Bennett, S.N.L.1    Simpson, I.2
  • 126
    • 78549283223 scopus 로고    scopus 로고
    • Prepa-ration of thieno[3,2-b]pyrrole amide derivatives as glycogen phos-phorylase inhibitors
    • WO 2005020987
    • Birch, A. M.; Simpson, I.; Stocker, A.; Whittamore, P. R. O. Prepa-ration of thieno[3,2-b]pyrrole amide derivatives as glycogen phos-phorylase inhibitors. PCT. Int. Appl.; WO 2005020987, 2005.
    • (2005) PCT. Int. Appl
    • Birch, A.M.1    Simpson, I.2    Stocker, A.3    Whittamore, P.R.O.4
  • 127
    • 78549267925 scopus 로고    scopus 로고
    • Preparation ofthieno[2,3-b]pyrrole-5-carboxamide derivatives as glycogen phos-phorylase inhibitors
    • WO 2005018637
    • Bennett, S. N. L.; Simpson, I.; Whittamore, P. R. O. Preparation ofthieno[2,3-b]pyrrole-5-carboxamide derivatives as glycogen phos-phorylase inhibitors. PCT. Int. Appl.; WO 2005018637, 2005.
    • (2005) PCT. Int. Appl
    • Bennett, S.N.L.1    Simpson, I.2    Whittamore, P.R.O.3
  • 128
    • 77955003882 scopus 로고    scopus 로고
    • Triglyceride and triglyceride-likeprodrugs of glycogen phosphorylase inhibiting compounds
    • US 2004142938
    • Sher, P. M.; Ellsworth, B. A. Triglyceride and triglyceride-likeprodrugs of glycogen phosphorylase inhibiting compounds. U.S.Pat. Appl. Publ.; US 2004142938, 2004.
    • (2004) U.S.Pat. Appl. Publ
    • Sher, P.M.1    Ellsworth, B.A.2
  • 129
    • 78549258245 scopus 로고    scopus 로고
    • Lactam glycogen phos-phorylase inhibitors and their use in disease treatment
    • US 2004002495
    • Sher, P.; Wu, G.; Stouch, T.; Ellsworth, B. Lactam glycogen phos-phorylase inhibitors and their use in disease treatment. U.S. Pat.Appl. Publ.; US 2004002495, 2004.
    • (2004) U.S. Pat.Appl. Publ
    • Sher, P.1    Wu, G.2    Stouch, T.3    Ellsworth, B.4
  • 130
    • 78549267922 scopus 로고    scopus 로고
    • Prepara-tion of heteroaroylaminotetralins and related compounds as glyco-gen phosphorylase inhibitors
    • US2006111338
    • Sher, P. M.; Nirschl, A. A.; Meng, W.; Washburn, W. N. Prepara-tion of heteroaroylaminotetralins and related compounds as glyco-gen phosphorylase inhibitors. U.S. Pat. Appl. Publ.; US2006111338, 2006.
    • (2006) U.S. Pat. Appl. Publ
    • Sher, P.M.1    Nirschl, A.A.2    Meng, W.3    Washburn, W.N.4
  • 133
    • 34548575720 scopus 로고    scopus 로고
    • Discoveringbenzamide derivatives as glycogen phosphorylase inhibitors andtheir binding site at the enzyme
    • Chen, L.; Li, H.; Liu, J.; Zhang, L.; Liu, H.; Jiang, H. Discoveringbenzamide derivatives as glycogen phosphorylase inhibitors andtheir binding site at the enzyme. Bioorg. Med. Chem., 2007, 15(21),6763-6774.
    • (2007) Bioorg. Med. Chem , vol.15 , Issue.21 , pp. 6763-6774
    • Chen, L.1    Li, H.2    Liu, J.3    Zhang, L.4    Liu, H.5    Jiang, H.6
  • 134
    • 78549254262 scopus 로고    scopus 로고
    • Preparation of benzoylureidopyridylpiperidines for thetreatment of type 2 diabetes
    • WO 2004078743
    • Schoenafinger, K.; Kadereit, D.; Defossa, E.; Herling, A.; Klabun-de, T.: Preparation of benzoylureidopyridylpiperidines for thetreatment of type 2 diabetes. PCT. Int. Appl.; WO 2004078743,2004.
    • (2004) PCT. Int. Appl
    • Schoenafinger, K.1    Kadereit, D.2    Defossa, E.3    Herling, A.4    Klabun-de, T.5
  • 138
    • 78549264185 scopus 로고    scopus 로고
    • Preparation of heteroaroy-laminotetralins and related compounds as glycogen phosphorylaseinhibitors:
    • US 2005148586
    • Beavers, M. P.; Dudash, J.; Zhang, Y. Preparation of heteroaroy-laminotetralins and related compounds as glycogen phosphorylaseinhibitors: U.S. Pat. Appl. Publ.; US 2005148586, 2005.
    • (2005) U.S. Pat. Appl. Publ
    • Beavers, M.P.1    Dudash, J.2    Zhang, Y.3
  • 140
    • 78549241369 scopus 로고    scopus 로고
    • Preparation of 7-amino-4-quinolone-3-carboxylic acids and related compounds for the treatment of type 2diabetes
    • WO 2005073231
    • Defossa, E.; Kadereit, D.; Klabunde, T.; Schmoll, D.; Herling, A.; Wendt, K.-U.; Ruf, S. Preparation of 7-amino-4-quinolone-3-carboxylic acids and related compounds for the treatment of type 2diabetes. PCT. Int. Appl.; WO 2005073231, 2005.
    • (2005) PCT. Int. Appl
    • Defossa, E.1    Kadereit, D.2    Klabunde, T.3    Schmoll, D.4    Herling, A.5    Wendt, K.-U.6    Ruf, S.7
  • 141
    • 78549241369 scopus 로고    scopus 로고
    • Preparation of 7-amino-4-quinolone-3-carboxylic acids and related compounds for the treatment of type 2diabetes
    • WO 2005073230
    • Defossa, E.; Kadereit, D.; Ruf, S.; Klabunde, T.; Schmoll, D.; Herling, A.; Wendt, K.-U. Preparation of 7-amino-4-quinolone-3-carboxylic acids and related compounds for the treatment of type 2diabetes: PCT. Int. Appl.; WO 2005073230, 2005.
    • (2005) PCT. Int. Appl
    • Defossa, E.1    Kadereit, D.2    Ruf, S.3    Klabunde, T.4    Schmoll, D.5    Herling, A.6    Wendt, K.-U.7
  • 142
    • 78549242417 scopus 로고    scopus 로고
    • Preparation of 7-phenylamino-4-quinolone-3-carboxylic acids and related compounds for the treat-ment of type 2 diabetes
    • WO 2005073229
    • Defossa, E.; Kadereit, D.; Ruf, S.; Klabunde, T.; Schmoll, D.; Herling, A.; Wendt, K.-U. Preparation of 7-phenylamino-4-quinolone-3-carboxylic acids and related compounds for the treat-ment of type 2 diabetes. PCT. Int. Appl.; WO 2005073229, 2005.
    • (2005) PCT. Int. Appl
    • Defossa, E.1    Kadereit, D.2    Ruf, S.3    Klabunde, T.4    Schmoll, D.5    Herling, A.6    Wendt, K.-U.7
  • 143
    • 77952515041 scopus 로고    scopus 로고
    • Preparation ofheterocyclic amide derivatives having glycogen phosphorylase in-hibitory activity
    • 2003074531
    • Whittamore, P. R. O.; Bennett, S. N. L.; Simpson, I. Preparation ofheterocyclic amide derivatives having glycogen phosphorylase in-hibitory activity. PCT. Int. Appl.; 2003074531, 2003.
    • (2003) PCT. Int. Appl
    • Whittamore, P.R.O.1    Bennett, S.N.L.2    Simpson, I.3
  • 144
    • 78549247926 scopus 로고    scopus 로고
    • Preparation of heterocyclic amides as inhibitors of glycogen phos-phorylase
    • WO 2003074532
    • Birch, A. M.; Morley, A. D.; Stocker, A.; Whittamore, P. R. O. Preparation of heterocyclic amides as inhibitors of glycogen phos-phorylase. PCT. Int. Appl.; WO 2003074532, 2003.
    • (2003) PCT. Int. Appl
    • Birch, A.M.1    Morley, A.D.2    Stocker, A.3    Whittamore, P.R.O.4
  • 145
    • 78549260802 scopus 로고    scopus 로고
    • N-(Pyridin-2-yl)-substitutedbicyclic heterocyclic carboxamide derivatives as antidiabeticagents, and their preparation, pharmaceutical compositions, and methods of use as inhibitors of glycogen phosphorylase
    • WO 2004092158
    • Bussolotti, D. L.; Gammill, R. B. N-(Pyridin-2-yl)-substitutedbicyclic heterocyclic carboxamide derivatives as antidiabeticagents, and their preparation, pharmaceutical compositions, and methods of use as inhibitors of glycogen phosphorylase. PCT. Int.Appl.; WO 2004092158, 2004.
    • (2004) PCT. Int.Appl
    • Bussolotti, D.L.1    Gammill, R.B.2
  • 146
    • 33749318517 scopus 로고    scopus 로고
    • Synthesis and structure-activity relationships of 3-phenyl-2-propenamides as inhibitors ofglycogen phosphorylase a
    • Li, Y. H.; Coppo, F. T.; Evans, K. A.; Graybill, T. L.; Patel, M.; Gale J.; Li H.; Tavares F.; Thomson S. A. Synthesis and structure-activity relationships of 3-phenyl-2-propenamides as inhibitors ofglycogen phosphorylase a. Bioorg. Med. Chem. Lett., 2006, 16(22),5892-5896.
    • (2006) Bioorg. Med. Chem. Lett , vol.16 , Issue.22 , pp. 5892-5896
    • Li, Y.H.1    Coppo, F.T.2    Evans, K.A.3    Graybill, T.L.4    Patel, M.5    Gale, J.6    Li, H.7    Tavares, F.8    Thomson, S.A.9
  • 147
    • 78549279239 scopus 로고    scopus 로고
    • Preparation of fused pyrrolylcarboxamides as glycogenphosphorylase inhibitors
    • EP 1391460
    • Daisy, J. Preparation of fused pyrrolylcarboxamides as glycogenphosphorylase inhibitors. Eur. Pat. Appl.; EP 1391460, 2004.
    • (2004) Eur. Pat. Appl
    • Daisy, J.1
  • 148
    • 78549236590 scopus 로고    scopus 로고
    • Preparation of bicyclic pyrrolylcarboxamides as glycogenphosphorylase inhibitors
    • EP 1088824
    • Joe, D. Preparation of bicyclic pyrrolylcarboxamides as glycogenphosphorylase inhibitors. Eur. Pat. Appl.; EP 1088824, 2001.
    • (2001) Eur. Pat. Appl
    • Joe, D.1
  • 150
    • 66449105241 scopus 로고    scopus 로고
    • Glycogenphosphorylase Inhibitory effects of 2-oxo-1,2-dihydropyridin-3-ylamide derivatives
    • Karis, N. D.; Loughlin, W. A.; Jenkins, I. D.; Healy, P.C. Glycogenphosphorylase Inhibitory effects of 2-oxo-1,2-dihydropyridin-3-ylamide derivatives. Bioorg. Med. Chem., 2009, 17(13), 4724-4733.
    • (2009) Bioorg. Med. Chem , vol.17 , Issue.13 , pp. 4724-4733
    • Karis, N.D.1    Loughlin, W.A.2    Jenkins, I.D.3    Healy, P.C.4
  • 151
    • 34247884384 scopus 로고    scopus 로고
    • Synthesisand glycogen phosphorylase inhibitor activity of 2,3-dihydrobenzo[1,4]dioxin derivatives
    • Juhasz L.; Docsa T.; Brunyaszki A.; Gergely P.; Antus S. Synthesisand glycogen phosphorylase inhibitor activity of 2,3-dihydrobenzo[1,4]dioxin derivatives. Bioorg. Med. Chem., 2007,15(13), 4048-56.
    • (2007) Bioorg. Med. Chem , vol.15 , Issue.13 , pp. 4048-4056
    • Juhasz, L.1    Docsa, T.2    Brunyaszki, A.3    Gergely, P.4    Antus, S.5
  • 152
    • 31544439364 scopus 로고    scopus 로고
    • Eisenbrand, G.Natural flavonoids are potent inhibitors of glycogen phosphorylase.Mol. Nutr
    • Jakobs, S.; Fridrich, D.; Hofem, S.; Pahlke, G.; Eisenbrand, G.Natural flavonoids are potent inhibitors of glycogen phosphorylase.Mol. Nutr. Food Res., 2006, 50(1), 52-57.
    • (2006) Food Res , vol.50 , Issue.1 , pp. 52-57
    • Jakobs, S.1    Fridrich, D.2    Hofem, S.3    Pahlke, G.4
  • 154
    • 41349106377 scopus 로고    scopus 로고
    • A norses-quiterpene lactone and a benzoic acid derivative from the leaves ofCyclocarya paliurus and their glucosidase and glycogen phosphory-lase inhibiting activities
    • Li, J.; Lu, Y.; Su, X.; Li, F.; She, Z.; He, X.; Lin, Y. A norses-quiterpene lactone and a benzoic acid derivative from the leaves ofCyclocarya paliurus and their glucosidase and glycogen phosphory-lase inhibiting activities. Planta Med., 2008, 74(3), 287-289.
    • (2008) Planta Med , vol.74 , Issue.3 , pp. 287-289
    • Li, J.1    Lu, Y.2    Su, X.3    Li, F.4    She, Z.5    He, X.6    Lin, Y.7
  • 155
    • 44449105030 scopus 로고    scopus 로고
    • Evaluation of novel hyphodermin derivatives asGlycogen Phosphorylase a inhibitors
    • Loughlin, W. A.; Pierens, G. K.; Petersson, M. J.; Henderson, L.C.; Healy, P. C. Evaluation of novel hyphodermin derivatives asGlycogen Phosphorylase a inhibitors. Bioorg. Med. Chem., 2008,16(11), 6172-6178.
    • (2008) Bioorg. Med. Chem , vol.16 , Issue.11 , pp. 6172-6178
    • Loughlin, W.A.1    Pierens, G.K.2    Petersson, M.J.3    Henderson, L.C.4    Healy, P.C.5
  • 156
    • 69949145117 scopus 로고    scopus 로고
    • Glycogenphosphorylase a inhibitors with a phenethylphenylphthalimideskeleton derived from thalidomide-related -glucosidase inhibitorsand liver X receptor antagonists
    • Motoshima, K.; Ishikawa, M.; Sugita, K.; Hashimoto, Y. Glycogenphosphorylase a inhibitors with a phenethylphenylphthalimideskeleton derived from thalidomide-related -glucosidase inhibitorsand liver X receptor antagonists. Biol. Pharm. Bull., 2009, 32(9),1618-1620.
    • (2009) Biol. Pharm. Bull , vol.32 , Issue.9 , pp. 1618-1620
    • Motoshima, K.1    Ishikawa, M.2    Sugita, K.3    Hashimoto, Y.4
  • 159
    • 0036314290 scopus 로고    scopus 로고
    • Human skeletal muscle expresses a glycogen-targeting subunit of PP1 that is identical to the insulin-sensitiveglycogen-targeting subunit GL of liver
    • Munro, S.; Cuthbertson, D. J. R.; Cunningham, J.; Sales, M.; Cohen, P. T. W. Human skeletal muscle expresses a glycogen-targeting subunit of PP1 that is identical to the insulin-sensitiveglycogen-targeting subunit GL of liver. Diabetes, 2002, 51(3), 591-598.
    • (2002) Diabetes , vol.51 , Issue.3 , pp. 591-598
    • Munro, S.1    Cuthbertson, D.J.R.2    Cunningham, J.3    Sales, M.4    Cohen, P.T.W.5
  • 160
    • 0032535595 scopus 로고    scopus 로고
    • Identification ofthe separate domains in the hepatic glycogen-targeting subunit ofprotein phosphatase 1 that interact with phosphorylase a, glycogenand protein phosphatase 1
    • Armstrong, C. G.; Doherty, M. J.; Cohen, P. T. W. Identification ofthe separate domains in the hepatic glycogen-targeting subunit ofprotein phosphatase 1 that interact with phosphorylase a, glycogenand protein phosphatase 1. Biochem. J., 1998, 336, 699-704.
    • (1998) Biochem. J , vol.336 , pp. 699-704
    • Armstrong, C.G.1    Doherty, M.J.2    Cohen, P.T.W.3
  • 161
    • 0028788805 scopus 로고
    • Amino acid sequence and expression of the hepatic glycogen-binding (GL)-subunit of protein phosphatase-1
    • Doherty, M. J.; Moorhead, G.; Morrice, N.; Cohen, P.; Cohen, P. T.W. Amino acid sequence and expression of the hepatic glycogen-binding (GL)-subunit of protein phosphatase-1. FEBS Lett., 1995,375(2), 294-298.
    • (1995) FEBS Lett , vol.375 , Issue.2 , pp. 294-298
    • Doherty, M.J.1    Moorhead, G.2    Morrice, N.3    Cohen, P.4    Cohen, P.T.W.5
  • 162
    • 64849099553 scopus 로고    scopus 로고
    • Disruption of theallosteric phosphorylase a regulation of the hepatic glycogen-targeted protein phosphatase 1 improves glucose tolerance in vivo
    • Kelsall, I. R.; Rosenzweig, D.; Cohen, P. T. W. Disruption of theallosteric phosphorylase a regulation of the hepatic glycogen-targeted protein phosphatase 1 improves glucose tolerance in vivo. Cell. Signal., 2009, 21(7), 1123-1134.
    • (2009) Cell. Signal , vol.21 , Issue.7 , pp. 1123-1134
    • Kelsall, I.R.1    Rosenzweig, D.2    Cohen, P.T.W.3
  • 163
    • 34548697097 scopus 로고    scopus 로고
    • The hepatic PP1 glycogen-targeting subunit interactionwith phosphorylase a can be blocked by C-terminal tyrosine dele-tion or an indole drug
    • Kelsall, I. R.; Munro, S.; Hallyburton, I.; Treadway, J. L.; Cohen, P.T.W. The hepatic PP1 glycogen-targeting subunit interactionwith phosphorylase a can be blocked by C-terminal tyrosine dele-tion or an indole drug. FEBS Lett., 2007, 581(24), 4749-4753.
    • (2007) FEBS Lett , vol.581 , Issue.24 , pp. 4749-4753
    • Kelsall, I.R.1    Munro, S.2    Hallyburton, I.3    Treadway, J.L.4    Cohen, P.T.W.5
  • 164
    • 44449170938 scopus 로고    scopus 로고
    • Inhibitionof the interaction between protein phosphatase 1 glycogen-targeting subunit and glycogen phosphorylase increases glycogensynthesis in primary rat hepatocytes
    • Zibrova, D.; Grempler, R.; Streicher, R.; Kauschke, S. G. Inhibitionof the interaction between protein phosphatase 1 glycogen-targeting subunit and glycogen phosphorylase increases glycogensynthesis in primary rat hepatocytes. Biochem. J., 2008, 412(2),359-366.
    • (2008) Biochem. J , vol.412 , Issue.2 , pp. 359-366
    • Zibrova, D.1    Grempler, R.2    Streicher, R.3    Kauschke, S.G.4
  • 165
    • 44049096537 scopus 로고    scopus 로고
    • Molecular Recognition of the Protein Phosphatase 1Glycogen Targeting Subunit by Glycogen Phosphorylase
    • Pautsch, A.; Stadler, N.; Wissdorf, O.; Langkopf, E.; Moreth, W.; Streicher, R. Molecular Recognition of the Protein Phosphatase 1Glycogen Targeting Subunit by Glycogen Phosphorylase. J. Biol.Chem., 2008, 283, 8913-8918.
    • (2008) J. Biol.Chem , vol.283 , pp. 8913-8918
    • Pautsch, A.1    Stadler, N.2    Wissdorf, O.3    Langkopf, E.4    Moreth, W.5    Streicher, R.6
  • 166
    • 67649786881 scopus 로고    scopus 로고
    • Synthesis of new modified truncated peptides and inhibition of gly-cogen phosphorylase
    • Schweiker, S. S.; Loughlin, W. A.; Brown, C. L.; Pierens, G. K. Synthesis of new modified truncated peptides and inhibition of gly-cogen phosphorylase. J. Pept. Sci., 2009, 15(6), 442-450.
    • (2009) J. Pept. Sci , vol.15 , Issue.6 , pp. 442-450
    • Schweiker, S.S.1    Loughlin, W.A.2    Brown, C.L.3    Pierens, G.K.4
  • 167
    • 78549286088 scopus 로고    scopus 로고
    • Preparation of newsubstituted arylsulphonylglycines as inhibitors of the interactionbetween glycogen phosphorylase and GL subunit of glycogen -associated protein phosphatase 1 and their pharmaceutical compo-sitions useful for treating diabetes
    • WO2009127723
    • Langkopf, E.; Himmelsbach, F.; Mack, J.; Pautsch, A.; Schoelch, C.; Schuler-Metz, A.; Streicher, R.; Wagner, H. Preparation of newsubstituted arylsulphonylglycines as inhibitors of the interactionbetween glycogen phosphorylase and GL subunit of glycogen -associated protein phosphatase 1 and their pharmaceutical compo-sitions useful for treating diabetes. PCT. Int. Appl.; WO2009127723, 2009.
    • (2009) PCT. Int. Appl
    • Langkopf, E.1    Himmelsbach, F.2    Mack, J.3    Pautsch, A.4    Schoelch, C.5    Schuler-Metz, A.6    Streicher, R.7    Wagner, H.8
  • 168
    • 78549279894 scopus 로고    scopus 로고
    • Substituted N-heterocyclic aryl-sulfonylaminomethylphosphonic acid derivatives as medicamentsfor treatment of Type I and II Diabetes mellitus and process fortheir preparation
    • WO 2009016119
    • Wagner, H.; Langkopf, E.; Eckhardt, M.; Streicher, R.; Schoelch, C.; Schuler-Metz, A.; Pautsch, A. Substituted N-heterocyclic aryl-sulfonylaminomethylphosphonic acid derivatives as medicamentsfor treatment of Type I and II Diabetes mellitus and process fortheir preparation. PCT. Int. Appl.; WO 2009016119, 2009.
    • (2009) PCT. Int. Appl
    • Wagner, H.1    Langkopf, E.2    Eckhardt, M.3    Streicher, R.4    Schoelch, C.5    Schuler-Metz, A.6    Pautsch, A.7
  • 169
    • 78549259810 scopus 로고    scopus 로고
    • Substituted N-heterocyclic aryl-sulfonylaminomethylphosphonic acid derivatives as medicamentsfor treatment of Type I and II Diabetes mellitus and process fortheir preparation
    • DE 102007035334 Ger. Offen
    • Wagner, H.; Langkopf, E.; Eckhardt, M.; Streicher, R.; Schoelch, C.; Schuler-Metz, A.; Pautsch, A. Substituted N-heterocyclic aryl-sulfonylaminomethylphosphonic acid derivatives as medicamentsfor treatment of Type I and II Diabetes mellitus and process fortheir preparation. Ger. Offen.; DE 102007035334 Ger. Offen. 2009.
    • (2009) Ger. Offen
    • Wagner, H.1    Langkopf, E.2    Eckhardt, M.3    Streicher, R.4    Schoelch, C.5    Schuler-Metz, A.6    Pautsch, A.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.