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Volumn 48, Issue 6, 2005, Pages 2036-2044

Biological properties of D- and L-1-deoxyazasugars

Author keywords

[No Author keywords available]

Indexed keywords

1 DEOXYALLONOJIRIMYCIN; 1 DEOXYALTRONOJIRIMYCIN; 1 DEOXYGALACTONOJIRIMYCIN; 1 DEOXYGULUNOJIRIMYCIN; 1 DEOXYMANNONOJIRIMYCIN; 1 DEOXYNOJIRIMYCIN; ALPHA GALACTOSIDASE; ALPHA GLUCOSIDASE; ALPHA LEVO FUCOSIDASE; ALPHA MANNOSIDASE; GLYCOSIDASE INHIBITOR; UNCLASSIFIED DRUG;

EID: 20144382745     PISSN: 00222623     EISSN: None     Source Type: Journal    
DOI: 10.1021/jm0495881     Document Type: Article
Times cited : (180)

References (58)
  • 2
    • 0034607947 scopus 로고    scopus 로고
    • Sugar-mimic glycosidase inhibitors: Natural occurrence, biological activity and prospects for therapeutic application
    • Asano, N.; Nash, R. J.; Molyneux, R. J.; Fleet, G. W. J. Sugar-mimic glycosidase inhibitors: natural occurrence, biological activity and prospects for therapeutic application. Tetrahedron Asymmetry 2000, 11, 1645-1680.
    • (2000) Tetrahedron Asymmetry , vol.11 , pp. 1645-1680
    • Asano, N.1    Nash, R.J.2    Molyneux, R.J.3    Fleet, G.W.J.4
  • 3
    • 0035925104 scopus 로고    scopus 로고
    • Polyhydroxylated alkaloids-natural occurrence and therapeutic applications
    • Watson, A. A.; Fleet, G. W. J.; Asano, N.; Molyneux, R. J.; Nash, R. J. Polyhydroxylated alkaloids-natural occurrence and therapeutic applications. Phytochemistry 2001, 56, 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
  • 4
    • 0141804127 scopus 로고    scopus 로고
    • Iminosugars: Recent Insights into their Bioactivity and Potential as Therapeutic Agents
    • Martin, O. R., Compain, P., Eds. Iminosugars: Recent Insights into their Bioactivity and Potential as Therapeutic Agents. Curr. Top. Med. Chem. 2003, 3 (5).
    • (2003) Curr. Top. Med. Chem. , vol.3 , Issue.5
    • Martin, O.R.1    Compain, P.2
  • 5
    • 0242287992 scopus 로고    scopus 로고
    • Glycosidase inhibitors: Update and perspectives on practical use
    • Asano, N. Glycosidase inhibitors: update and perspectives on practical use. Glycobiology 2003, 13, 93R-104R.
    • (2003) Glycobiology , vol.13
    • Asano, N.1
  • 6
    • 0031820774 scopus 로고    scopus 로고
    • Long-term effectiveness of a new α-glucosidase inhibitor (BAY m1099-miglitol) in insulin-treated type 2 diabetes mellitus
    • Mitrakou, A.; Tountas, N.; Raptis, A. E.; Bauer, R. J.; Schulz, H.; Raptis, S. A. Long-term effectiveness of a new α-glucosidase inhibitor (BAY m1099-miglitol) in insulin-treated type 2 diabetes mellitus. Diab. Med. 1998, 15, 657-660.
    • (1998) Diab. Med. , vol.15 , pp. 657-660
    • Mitrakou, A.1    Tountas, N.2    Raptis, A.E.3    Bauer, R.J.4    Schulz, H.5    Raptis, S.A.6
  • 7
    • 0038170055 scopus 로고    scopus 로고
    • Therapeutic applications of imino sugars in lysosomal storage disorders
    • Butters, T. D.; Dwek, R. A.; Platt, F. M. Therapeutic applications of imino sugars in lysosomal storage disorders. Curr. Top. Med. Chem. 2003, 3, 561-574.
    • (2003) Curr. Top. Med. Chem. , vol.3 , pp. 561-574
    • Butters, T.D.1    Dwek, R.A.2    Platt, F.M.3
  • 8
    • 0034512968 scopus 로고    scopus 로고
    • Inhibition of glycosphingolipid biosynthesis: Application to lysosomal storage disorders
    • Butters, T. D.; Dwek, A.; Platt, F. M. Inhibition of glycosphingolipid biosynthesis: application to lysosomal storage disorders. Chem. Rev. 2000, 100, 4683-4696.
    • (2000) Chem. Rev. , vol.100 , pp. 4683-4696
    • Butters, T.D.1    Dwek, A.2    Platt, F.M.3
  • 10
    • 0033018496 scopus 로고
    • Accelerated transport and maturation of lysosomal α-galactosidase A in Fabry lymphoblasts by an enzyme inhibitor
    • Fan, J.-Q.; Ishii, S.; Asano, N.; Suzuki, Y. Accelerated transport and maturation of lysosomal α-galactosidase A in Fabry lymphoblasts by an enzyme inhibitor. Nat. Med. 1909, 5, 112-115.
    • (1909) Nat. Med. , vol.5 , pp. 112-115
    • Fan, J.-Q.1    Ishii, S.2    Asano, N.3    Suzuki, Y.4
  • 11
    • 0033936361 scopus 로고    scopus 로고
    • In vitro inhibition and intracellular enhancement of lysosomal α-galactosidase A activity in Fabry lymphoblasts by 1- deoxygalactonojirimycin and its derivatives
    • Asano, N.; Ishii, S.; Kizu, H.; Ikeda, K.; Yasuda, K.; Kato, A.; Martin, O. R.; Fan, J.-Q. In vitro inhibition and intracellular enhancement of lysosomal α-galactosidase A activity in Fabry lymphoblasts by 1- deoxygalactonojirimycin and its derivatives. Eur. J. Biochem. 2000, 267, 4179-4186.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 4179-4186
    • Asano, N.1    Ishii, S.2    Kizu, H.3    Ikeda, K.4    Yasuda, K.5    Kato, A.6    Martin, O.R.7    Fan, J.-Q.8
  • 12
    • 0037180511 scopus 로고    scopus 로고
    • Chemical chaperones increase the cellular activity of N370S β-glucosidase: A therapeutic strategy for Gaucher disease
    • Sawkar, A. R.; Cheng, W.-C.; Beutler, E.; Wong, C.-H.; Balch, W. E.; Kelly, J. W. Chemical chaperones increase the cellular activity of N370S β-glucosidase: a therapeutic strategy for Gaucher disease. Proc. Natl. Acad. Sci. U.S.A. 2002, 99, 15428-15433.
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 15428-15433
    • Sawkar, A.R.1    Cheng, W.-C.2    Beutler, E.3    Wong, C.-H.4    Balch, W.E.5    Kelly, J.W.6
  • 14
    • 0030154323 scopus 로고    scopus 로고
    • Influence of molecular and chemical chaperones on protein folding
    • Welch, W. J.; Brown, C. R. Influence of molecular and chemical chaperones on protein folding. Cell Stress Chaperones 1996, 1, 109-115.
    • (1996) Cell Stress Chaperones , vol.1 , pp. 109-115
    • Welch, W.J.1    Brown, C.R.2
  • 15
    • 0043235841 scopus 로고    scopus 로고
    • A contradictory treatment for lysosomal storage disorders: Inhibitors enhance mutant enzyme activity
    • Fan, J.-Q. A contradictory treatment for lysosomal storage disorders: inhibitors enhance mutant enzyme activity. Trends Pharmacol. Sci. 2003, 24, 355-360.
    • (2003) Trends Pharmacol. Sci. , vol.24 , pp. 355-360
    • Fan, J.-Q.1
  • 18
    • 0034354913 scopus 로고    scopus 로고
    • Modification of glycosylation as a therapeutic strategy
    • Winchester, B.; Fleet, G. W. J. Modification of glycosylation as a therapeutic strategy. J. Carbohydr. Chem. 2000, 19, 471-483.
    • (2000) J. Carbohydr. Chem. , vol.19 , pp. 471-483
    • Winchester, B.1    Fleet, G.W.J.2
  • 19
    • 15444365464 scopus 로고    scopus 로고
    • Azaglycomimetics: Synthesis and chemical biology
    • Fraser-Reid, B. O., Tatsuta, K., Thiem, J., Eds.; Springer-Verlag: Berlin, Heidelberg
    • Asano, N.; Hashimoto, H. Azaglycomimetics: synthesis and chemical biology. Glycoscience: Chemistry and Chemical Biology III; Fraser-Reid, B. O., Tatsuta, K., Thiem, J., Eds.; Springer-Verlag: Berlin, Heidelberg, 2001; pp 2541-2594.
    • (2001) Glycoscience: Chemistry and Chemical Biology III , pp. 2541-2594
    • Asano, N.1    Hashimoto, H.2
  • 20
    • 0023159808 scopus 로고
    • Inhibitors of the biosynthesis and processing of N-linked oligosaccharide chains
    • Elbein, A. D. Inhibitors of the biosynthesis and processing of N-linked oligosaccharide chains. Annu. Rev. Biochem. 1987, 56, 497-534.
    • (1987) Annu. Rev. Biochem. , vol.56 , pp. 497-534
    • Elbein, A.D.1
  • 21
    • 0026317511 scopus 로고
    • Glycosidase inhibitors: Inhibitors of N-linked oligosaccharide processing
    • Elbein, A. D. Glycosidase inhibitors: inhibitors of N-linked oligosaccharide processing. FASEB J. 1991, 5, 3055-3063.
    • (1991) FASEB J. , vol.5 , pp. 3055-3063
    • Elbein, A.D.1
  • 22
    • 0026654870 scopus 로고
    • Amino-sugar glycosidase inhibitors: Versatile tools for glycobiologists
    • Winchester, B.; Fleet, G. W. J. Amino-sugar glycosidase inhibitors: versatile tools for glycobiologists. Glycobiology 1992, 2, 199-210.
    • (1992) Glycobiology , vol.2 , pp. 199-210
    • Winchester, B.1    Fleet, G.W.J.2
  • 23
    • 0141519631 scopus 로고    scopus 로고
    • Concise and highly stereocontrolled synthesis of 1- deoxygalactonojirimycin and its congeners using dioxanylpiperidene, a promising chiral building block
    • Takahata, H.; Banba, Y.; Ouchi, H.; Nemoto, H. Concise and highly stereocontrolled synthesis of 1-deoxygalactonojirimycin and its congeners using dioxanylpiperidene, a promising chiral building block. Org. Lett. 2003, 5, 2527-2529.
    • (2003) Org. Lett. , vol.5 , pp. 2527-2529
    • Takahata, H.1    Banba, Y.2    Ouchi, H.3    Nemoto, H.4
  • 24
    • 85027844179 scopus 로고    scopus 로고
    • Synthesis of 1,1-dimethylethyl (S)-4-formyl-2,2-dimethyl-3- oxazolidinecarboxylate by oxidation of the alcohol
    • Dondoni, A.; Perrome, D. Synthesis of 1,1-dimethylethyl (S)-4-formyl-2,2-dimethyl-3-oxazolidinecarboxylate by oxidation of the alcohol. Org. Synth. 1999, 77, 64-77.
    • (1999) Org. Synth. , vol.77 , pp. 64-77
    • Dondoni, A.1    Perrome, D.2
  • 25
    • 0023684709 scopus 로고
    • A stereodivergent synthesis of D-erythro-sphingosine and D-threo-sphingosine from L-serine
    • Garner, P.; Park, J. M.; Malecki, E. A stereodivergent synthesis of D-erythro-sphingosine and D-threo-sphingosine from L-serine. J. Org. Chem. 1988, 53, 4395-4398.
    • (1988) J. Org. Chem. , vol.53 , pp. 4395-4398
    • Garner, P.1    Park, J.M.2    Malecki, E.3
  • 26
    • 0023838180 scopus 로고
    • Synthesis of D-erythro- and D-threo-sphingosine derivatives from L-serine
    • Herold, P. Synthesis of D-erythro- and D-threo-sphingosine derivatives from L-serine. Helv. Chim. Acta 1988, 71, 354-363.
    • (1988) Helv. Chim. Acta , vol.71 , pp. 354-363
    • Herold, P.1
  • 27
    • 0032580376 scopus 로고    scopus 로고
    • Recent advances on olefin metathesis and its application in organic synthesis
    • Grubbs, R. H.; Chang, S. Recent advances on olefin metathesis and its application in organic synthesis. Tetrahedron 1998, 54, 4413-4450.
    • (1998) Tetrahedron , vol.54 , pp. 4413-4450
    • Grubbs, R.H.1    Chang, S.2
  • 28
    • 4143147593 scopus 로고    scopus 로고
    • Asymmetric synthesis of 1-deoxynojirimycin and its congeners from a common chiral building block
    • Takahata, H.; Banba, Y.; Sasatani, M.; Nemoto, H.; Kato, A.; Adachi, I. Asymmetric synthesis of 1-deoxynojirimycin and its congeners from a common chiral building block. Tetrahedron 2004, 60, 8199-8205.
    • (2004) Tetrahedron , vol.60 , pp. 8199-8205
    • Takahata, H.1    Banba, Y.2    Sasatani, M.3    Nemoto, H.4    Kato, A.5    Adachi, I.6
  • 32
    • 0001214733 scopus 로고
    • Glycosidase inhibition by plant alkaloids which are structural analogues of monosaccharides
    • Evans, S. V.; Fellows, L. E.; Shing, T. K. M.; Fleet, G. W. J. Glycosidase inhibition by plant alkaloids which are structural analogues of monosaccharides. Phytochemistry 1985, 24, 1953-1955.
    • (1985) Phytochemistry , vol.24 , pp. 1953-1955
    • Evans, S.V.1    Fellows, L.E.2    Shing, T.K.M.3    Fleet, G.W.J.4
  • 34
    • 0022447786 scopus 로고
    • Inhibition of mammalian digestive disaccharidases by polyhydroxy alkaloids
    • Scofield, A. M.; Fellows, L. E.; Nash, R. J.; Fleet, G. W. J. Inhibition of mammalian digestive disaccharidases by polyhydroxy alkaloids. Life Sci. 1886, 39, 645-650.
    • (1886) Life Sci. , vol.39 , pp. 645-650
    • Scofield, A.M.1    Fellows, L.E.2    Nash, R.J.3    Fleet, G.W.J.4
  • 35
    • 0028127346 scopus 로고
    • Nitrogen-in-the-ring pyranose and furanoses: Structural basis of inhibition of mammalian glycosidases
    • Asano, N.; Oseki, K.; Kizu, H.; Matsui, K. Nitrogen-in-the-ring pyranose and furanoses: structural basis of inhibition of mammalian glycosidases. J. Med. Chem. 1994, 37, 3701-3706.
    • (1994) J. Med. Chem. , vol.37 , pp. 3701-3706
    • Asano, N.1    Oseki, K.2    Kizu, H.3    Matsui, K.4
  • 36
    • 0022814210 scopus 로고
    • Synthesis of 5-amino-5-deoxy-D-galactopyranose and 1,5-dideoxy-1,5-imino- D-galactitol, and their inhibition of α- and β-D-galactosidase
    • Legler, G.; Pohl, S. Synthesis of 5-amino-5-deoxy-D-galactopyranose and 1,5-dideoxy-1,5-imino-D-galactitol, and their inhibition of α- and β-D-galactosidase. Carbohydr. Res. 1986, 155, 119-129.
    • (1986) Carbohydr. Res. , vol.155 , pp. 119-129
    • Legler, G.1    Pohl, S.2
  • 37
    • 0027551956 scopus 로고
    • A chemoenzymic synthesis of 1,5-dideoxy-1,5-imino-L-mannitol and -L-rhamnitol and investigation of their effects on glycosidases
    • Zhou, P.; Salleh, H. M.; Chan, P. C. M.; Lajoie, G.; Honek, J. F.; Nambiar, P. T. C.; Ward, O. P. A chemoenzymic synthesis of 1,5-dideoxy-1,5- imino-L-mannitol and -L-rhamnitol and investigation of their effects on glycosidases. Carbohydr. Res. 1993, 155-166.
    • (1993) Carbohydr. Res. , pp. 155-166
    • Zhou, P.1    Salleh, H.M.2    Chan, P.C.M.3    Lajoie, G.4    Honek, J.F.5    Nambiar, P.T.C.6    Ward, O.P.7
  • 38
    • 37049097621 scopus 로고
    • Synthesis from D-glucose of 1,5-dideoxy-1,5-imino-L-fucitol, a potent α-L-fucosidase inhibitor
    • Fleet, G. W. J.; Shaw, A. N.; Evans, S. V.; Fellows, L. E. Synthesis from D-glucose of 1,5-dideoxy-1,5-imino-L-fucitol, a potent α-L-fucosidase inhibitor. J. Chem. Soc., Chem. Commun. 1985, 841-842.
    • (1985) J. Chem. Soc., Chem. Commun. , pp. 841-842
    • Fleet, G.W.J.1    Shaw, A.N.2    Evans, S.V.3    Fellows, L.E.4
  • 39
    • 0024347053 scopus 로고
    • Iminoheptitols as glycosidase inhibitors: Synthesis and specific α-L-fucosidase inhibition by β-L-homofuconojirimycin and 1-β-C-substituted deoxymannojirimycin
    • Fleet, G. W. J.; Namgoong, S. K.; Barker, C.; Baines, S.; Jacob, G. S.; Winchester, B. Iminoheptitols as glycosidase inhibitors: synthesis and specific α-L-fucosidase inhibition by β-L-homofuconojirimycin and 1-β-C-substituted deoxymannojirimycin. Tetrahedron Lett. 1989, 30, 4439-4442.
    • (1989) Tetrahedron Lett. , vol.30 , pp. 4439-4442
    • Fleet, G.W.J.1    Namgoong, S.K.2    Barker, C.3    Baines, S.4    Jacob, G.S.5    Winchester, B.6
  • 40
    • 0025063976 scopus 로고
    • Inhibition of α-L-fucosidase by derivatives of deoxyfuconojirimycin and deoxymannojirimycin
    • Winchester, B.; Barker, C.; Baines, S.; Jacob, G. S.; Namgoong, S. K.; Fleet, G. W. J. Inhibition of α-L-fucosidase by derivatives of deoxyfuconojirimycin and deoxymannojirimycin. Biochem. J. 1990, 265, 277-282.
    • (1990) Biochem. J. , vol.265 , pp. 277-282
    • Winchester, B.1    Barker, C.2    Baines, S.3    Jacob, G.S.4    Namgoong, S.K.5    Fleet, G.W.J.6
  • 42
    • 0024461745 scopus 로고
    • A protein oligomerization in the endoplasmic reticulum
    • Hurtley, S. M.; Helenius, A. A protein oligomerization in the endoplasmic reticulum. Annu. Rev. Cell Biol. 1989, 5, 277-307.
    • (1989) Annu. Rev. Cell Biol. , vol.5 , pp. 277-307
    • Hurtley, S.M.1    Helenius, A.2
  • 43
    • 0026584271 scopus 로고
    • Protein folding in the cells
    • Gething, M.-J.; Sambrook, J. Protein folding in the cells. Nature 1992, 355, 33-45.
    • (1992) Nature , vol.355 , pp. 33-45
    • Gething, M.-J.1    Sambrook, J.2
  • 44
    • 0026659680 scopus 로고
    • The endoplasmic reticulum as a protein folding compartment
    • Helenius, A.; Marquardt, T.; Braakmann, I. The endoplasmic reticulum as a protein folding compartment. Trends Cell Biol. 1992, 2, 227-231.
    • (1992) Trends Cell Biol. , vol.2 , pp. 227-231
    • Helenius, A.1    Marquardt, T.2    Braakmann, I.3
  • 45
    • 0028859841 scopus 로고
    • Folding intermediates are involved in genetic diseases?
    • Bychova, V. E.; Ptitsyn, O. B. Folding intermediates are involved in genetic diseases? FEBS Lett. 1995, 359, 6-8.
    • (1995) FEBS Lett. , vol.359 , pp. 6-8
    • Bychova, V.E.1    Ptitsyn, O.B.2
  • 46
    • 0030154323 scopus 로고    scopus 로고
    • Influence of molecular and chemical chaperones on protein folding
    • Welch, W. J.; Brown, C. R. Influence of molecular and chemical chaperones on protein folding. Cell Stress Cap. 1996, 1, 109-115.
    • (1996) Cell Stress Cap. , vol.1 , pp. 109-115
    • Welch, W.J.1    Brown, C.R.2
  • 48
    • 0029940208 scopus 로고    scopus 로고
    • Aggregation of the inactive form of human α-galactosidase in the endoplasmic reticulum
    • Ishii, S.; Kase, R.; Okumiya, T.; Sakuraba, H.; Suzuki, Y. Aggregation of the inactive form of human α-galactosidase in the endoplasmic reticulum. Biochem. Biophys. Res. Commun. 1996, 220, 812-815.
    • (1996) Biochem. Biophys. Res. Commun. , vol.220 , pp. 812-815
    • Ishii, S.1    Kase, R.2    Okumiya, T.3    Sakuraba, H.4    Suzuki, Y.5
  • 49
    • 0021280849 scopus 로고
    • Glucose removal from N-linked oligosaccharides is required for efficient maturation of certain secretory glycoproteins from the rough endoplasmic reticulum to the Golgi complex
    • Lodish, H. F.; Kong, N. Glucose removal from N-linked oligosaccharides is required for efficient maturation of certain secretory glycoproteins from the rough endoplasmic reticulum to the Golgi complex. J. Cell Biol. 1984, 98, 1720-1729.
    • (1984) J. Cell Biol. , vol.98 , pp. 1720-1729
    • Lodish, H.F.1    Kong, N.2
  • 50
    • 0034897590 scopus 로고    scopus 로고
    • Galactonojirimycin derivatives restore mutant human β-galactosidase activities expressed in fibroblasts from enzyme-deficient knockout mouse
    • Tominaga, L.; Ogawa, Y.; Taniguchi, M.; Ohno, K.; Matsuda, J.; Oshima, A.; Suzuki, Y.; Nanba, E. Galactonojirimycin derivatives restore mutant human β-galactosidase activities expressed in fibroblasts from enzyme-deficient knockout mouse. Brain Dev. 2001, 23, 284-287.
    • (2001) Brain Dev. , vol.23 , pp. 284-287
    • Tominaga, L.1    Ogawa, Y.2    Taniguchi, M.3    Ohno, K.4    Matsuda, J.5    Oshima, A.6    Suzuki, Y.7    Nanba, E.8
  • 51
    • 0028213490 scopus 로고
    • Glycosidases of the asparagines-linked oligosaccharide processing pathway
    • Moremen, K. W.; Trimble, A.; Herscovics, A. Glycosidases of the asparagines-linked oligosaccharide processing pathway. Glycobiology 1994, 4, 113-125.
    • (1994) Glycobiology , vol.4 , pp. 113-125
    • Moremen, K.W.1    Trimble, A.2    Herscovics, A.3
  • 52
    • 0028172714 scopus 로고
    • Mammalian α-mannosidases: Multiple forms but a common purpose?
    • Daniel, P. F.; Winchester, B.; Warren, C. D. Mammalian α-mannosidases: multiple forms but a common purpose? Glycobiology 1904, 4, 551-566.
    • (1904) Glycobiology , vol.4 , pp. 551-566
    • Daniel, P.F.1    Winchester, B.2    Warren, C.D.3
  • 53
    • 0034731519 scopus 로고    scopus 로고
    • Structural basis for catalysis and inhibition of N-glycan processing class I α1,2-mannosidases
    • Vallée, F.; Karaveg, K.; Herscovics, A.; Moremen, K. W. Howell, P. L. Structural basis for catalysis and inhibition of N-glycan processing class I α1,2-mannosidases. J. Biol. Chem. 2000, 275, 41287-41298.
    • (2000) J. Biol. Chem. , vol.275 , pp. 41287-41298
    • Vallée, F.1    Karaveg, K.2    Herscovics, A.3    Moremen, K.W.4    Howell, P.L.5
  • 54
    • 0020965173 scopus 로고
    • The uptake of swainsonine, a specific inhibitor of α-mannosidase, into normal human fibroblasts in culture
    • Chotai, K.; Jennings, C.; Winchester, B.; Dorling, P. The uptake of swainsonine, a specific inhibitor of α-mannosidase, into normal human fibroblasts in culture. J. Cell Biochem. 1983, 21, 107-117.
    • (1983) J. Cell Biochem. , vol.21 , pp. 107-117
    • Chotai, K.1    Jennings, C.2    Winchester, B.3    Dorling, P.4
  • 55
    • 0346219045 scopus 로고    scopus 로고
    • Alkaloids from the poisonous plant Ipomoea carnea: Effects on intracellular lysosomal glycosidase activities in human lymphoblast cultures
    • Ikeda, K.; Kato, A.; Adachi, I.; Haraguchi, M.; Asano, N. Alkaloids from the poisonous plant Ipomoea carnea: effects on intracellular lysosomal glycosidase activities in human lymphoblast cultures. J. Agric. Food Chem. 2003, 51, 7642-7646.
    • (2003) J. Agric. Food Chem. , vol.51 , pp. 7642-7646
    • Ikeda, K.1    Kato, A.2    Adachi, I.3    Haraguchi, M.4    Asano, N.5
  • 56
    • 0026666613 scopus 로고
    • Rat epididymal luminal fluid acid β-D-galactosidase optimally hydrolyses glycoprotein substrate at neutral pH
    • Skudlarek, M. D.; Tulsiani, D. R. P.; Orgebin-Crist, M.-C. Rat epididymal luminal fluid acid β-D-galactosidase optimally hydrolyses glycoprotein substrate at neutral pH. Biochem. J. 1992, 286, 907-914.
    • (1992) Biochem. J. , vol.286 , pp. 907-914
    • Skudlarek, M.D.1    Tulsiani, D.R.P.2    Orgebin-Crist, M.-C.3
  • 57
    • 0017913374 scopus 로고
    • A modified procedure for the rapid preparation of efficiently transporting vesicles from small intestinal brush border membranes. Their use in investigating some properties of D-glucose and choline transport system
    • Kessler, M.; Acuto, O.; Strelli, C.; Murer, H.; Semenza, G. A. A modified procedure for the rapid preparation of efficiently transporting vesicles from small intestinal brush border membranes. Their use in investigating some properties of D-glucose and choline transport system. Biochim. Biophys. Acta 1978, 506, 136-154.
    • (1978) Biochim. Biophys. Acta , vol.506 , pp. 136-154
    • Kessler, M.1    Acuto, O.2    Strelli, C.3    Murer, H.4    Semenza, G.A.5


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