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Volumn 8, Issue 6, 2011, Pages 2390-2397

Therapeutic strategies for Gaucher disease: Miglustat (NB-DNJ) as a pharmacological chaperone for glucocerebrosidase and the different thermostability of velaglucerase alfa and imiglucerase

Author keywords

calorimetry; Gaucher disease; imiglucerase; NB DNJ; velaglucerase alfa

Indexed keywords

CHAPERONE; GLUCOSYLCERAMIDASE; IMIGLUCERASE; MIGLUSTAT; VELAGLUCERASE ALFA;

EID: 82955173021     PISSN: 15438384     EISSN: 15438392     Source Type: Journal    
DOI: 10.1021/mp200313e     Document Type: Article
Times cited : (42)

References (65)
  • 1
    • 50549198437 scopus 로고
    • Metabolism of glucocerebrosides. II. Evidence of an enzymatic deficiency in Gaucher's disease
    • Brady, R. O.; Kanfer, J. N.; Shapiro, D. Metabolism of glucocerebrosides. II. Evidence of an enzymatic deficiency in Gaucher's disease Biochem. Biophys. Res. Commun. 1965, 18, 221-225
    • (1965) Biochem. Biophys. Res. Commun. , vol.18 , pp. 221-225
    • Brady, R.O.1    Kanfer, J.N.2    Shapiro, D.3
  • 2
    • 0000216808 scopus 로고    scopus 로고
    • Gaucher disease
    • 8 th ed. Scriver, C. R. Beaudet, A. L. Sly, W. S. Valle, D. McGraw-Hill: New York
    • Beutler, E.; Grabowski, G. A. Gaucher disease. In The metabolic and molecular bases of inherited diseases, 8 th ed.; Scriver, C. R.; Beaudet, A. L.; Sly, W. S.; Valle, D., Eds.; McGraw-Hill: New York, 2001; pp 3635-3668.
    • (2001) The Metabolic and Molecular Bases of Inherited Diseases , pp. 3635-3668
    • Beutler, E.1    Grabowski, G.A.2
  • 4
    • 33745293617 scopus 로고    scopus 로고
    • Therapeutic strategies to ameliorate lysosomal storage disorders - A focus on Gaucher disease
    • DOI 10.1007/s00018-005-5437-0
    • Sawkar, A. R.; D'Haeze, W.; Kelly, J. W. Therapeutic strategies to ameliorate lysosomal storage disorders - a focus on Gaucher disease Cell. Mol. Life Sci. 2006, 63, 1179-1192 (Pubitemid 43939004)
    • (2006) Cellular and Molecular Life Sciences , vol.63 , Issue.10 , pp. 1179-1192
    • Sawkar, A.R.1    D'Haeze, W.2    Kelly, J.W.3
  • 5
    • 0031844267 scopus 로고    scopus 로고
    • Therapy for the sphingolipidoses
    • DOI 10.1001/archneur.55.8.1055
    • Brady, R. O. Therapy for the sphingolipidoses Arch. Neurol. 1998, 55, 1055-1056 (Pubitemid 28367229)
    • (1998) Archives of Neurology , vol.55 , Issue.8 , pp. 1055-1056
    • Brady, R.O.1
  • 6
    • 0029664406 scopus 로고    scopus 로고
    • Quantitative analysis of the targeting of mannose-terminal glucocerebrosidase. Predominant uptake by liver endothelial cells
    • Bijsterbosch, M. K.; Donker, W.; van de Bilt, H.; van Weely, S.; van Berkel, T. J.; Aerts, J. M. Quantitative analysis of the targeting of mannose-terminal glucocerebrosidase. Predominant uptake by liver endothelial cells Eur. J. Biochem. 1996, 237, 344-349
    • (1996) Eur. J. Biochem. , vol.237 , pp. 344-349
    • Bijsterbosch, M.K.1    Donker, W.2    Van De Bilt, H.3    Van Weely, S.4    Van Berkel, T.J.5    Aerts, J.M.6
  • 7
    • 0029845416 scopus 로고    scopus 로고
    • Therapeutic delivery of proteins to macrophages: Implications for treatment of Gaucher's disease
    • DOI 10.1016/S0140-6736(96)04451-0
    • Mistry, P. K.; Wraight, E. P.; Cox, T. M. Therapeutic delivery of proteins to macrophages: implications for treatment of Gaucher's disease Lancet 1996, 348, 1555-1559 (Pubitemid 26411655)
    • (1996) Lancet , vol.348 , Issue.9041 , pp. 1555-1559
    • Mistry, P.K.1    Wraight, E.P.2    Cox, T.M.3
  • 8
    • 34248504877 scopus 로고    scopus 로고
    • A pharmacokinetic analysis of a novel enzyme replacement therapy with Gene-Activated human glucocerebrosidase (GA-GCB) in patients with type 1 Gaucher disease
    • DOI 10.1016/j.bcmd.2007.02.008, PII S1079979607000319
    • Zimran, A.; Loveday, K.; Fratazzi, C.; Elstein, D. A pharmacokinetic analysis of a novel enzyme replacement therapy with Gene-Activated human glucocerebrosidase (GA-GCB) in patients with type 1 Gaucher disease Blood Cells, Mol., Dis. 2007, 39, 115-118 (Pubitemid 46754922)
    • (2007) Blood Cells, Molecules, and Diseases , vol.39 , Issue.1 , pp. 115-118
    • Zimran, A.1    Loveday, K.2    Fratazzi, C.3    Elstein, D.4
  • 9
    • 0025869216 scopus 로고
    • Replacement therapy for inherited enzyme deficiency - Macrophage-targeted glucocerebrosidase for Gaucher's disease
    • Barton, N. W.; Brady, R. O.; Dambrosia, J. M.; Di Bisceglie, A. M.; Doppelt, S. H.; Hill, S. C. Replacement therapy for inherited enzyme deficiency - macrophage-targeted glucocerebrosidase for Gaucher's disease N. Engl. J. Med. 1991, 324, 1464-1470
    • (1991) N. Engl. J. Med. , vol.324 , pp. 1464-1470
    • Barton, N.W.1    Brady, R.O.2    Dambrosia, J.M.3    Di Bisceglie, A.M.4    Doppelt, S.H.5    Hill, S.C.6
  • 12
    • 32944476769 scopus 로고    scopus 로고
    • Enzyme replacement for lysosomal diseases
    • DOI 10.1146/annurev.med.57.110104.115650
    • Brady, R. O. Enzyme replacement for lysosomal diseases Annu. Rev. Med. 2006, 57, 283-296 (Pubitemid 43261992)
    • (2006) Annual Review of Medicine , vol.57 , pp. 283-296
    • Brady, R.O.1
  • 13
    • 0031868229 scopus 로고    scopus 로고
    • Enzyme therapy for Gaucher disease: The first 5 years
    • DOI 10.1016/S0268-960X(98)90023-6
    • Grabowski, G. A.; Leslie, N.; Wenstrup, R. Enzyme therapy for Gaucher disease: the first 5 years Blood Rev. 1998, 12, 115-133 (Pubitemid 28327418)
    • (1998) Blood Reviews , vol.12 , Issue.2 , pp. 115-133
    • Grabowski, G.A.1    Leslie, N.2    Wenstrup, R.3
  • 15
    • 33745506072 scopus 로고    scopus 로고
    • Lysosomal storage diseases: Natural history and ethical and economic aspects
    • DOI 10.1016/j.ymgme.2006.01.010, PII S109671920600028X
    • Beutler, E. Lysosomal storage diseases: natural history and ethical and economic aspects Mol. Genet. Metab. 2006, 88, 208-215 (Pubitemid 43963435)
    • (2006) Molecular Genetics and Metabolism , vol.88 , Issue.3 , pp. 208-215
    • Beutler, E.1
  • 17
    • 0038206527 scopus 로고    scopus 로고
    • Miglustat. Oxford GlycoSciences/Actelion
    • Lachmann, R. H. Miglustat. Oxford GlycoSciences/Actelion Curr. Opin. Invest. Drugs 2003, 4, 472-479
    • (2003) Curr. Opin. Invest. Drugs , vol.4 , pp. 472-479
    • Lachmann, R.H.1
  • 21
    • 34948880765 scopus 로고    scopus 로고
    • Oral maintenance clinical trial with miglustat for type I Gaucher disease: Switch from or combination with intravenous enzyme replacement
    • DOI 10.1182/blood-2007-02-075960
    • Elstein, D.; Dweck, A.; Attias, D.; Hadas-Halpern, I.; Zevin, S.; Altarescu, G. Oral maintenance clinical trial with miglustat for type I Gaucher disease: switch from or combination with intravenous enzyme replacement Blood 2007, 110, 2296-2301 (Pubitemid 47523147)
    • (2007) Blood , vol.110 , Issue.7 , pp. 2296-2301
    • Elstein, D.1    Dweck, A.2    Attias, D.3    Hadas-Halpern, I.4    Zevin, S.5    Altarescu, G.6    Aerts, J.F.M.G.7    Van Weely, S.8    Zimran, A.9
  • 22
    • 34848916343 scopus 로고    scopus 로고
    • Effect of Miglustat on Bone Disease in Adults with Type 1 Gaucher Disease: A Pooled Analysis of Three Multinational, Open-Label Studies
    • DOI 10.1016/j.clinthera.2007.08.006, PII S014929180700241X
    • Pastores, G. M.; Elstein, D.; Hrebícek, M.; Zimran, A. Effect of miglustat on bone disease in adults with type 1 Gaucher disease: a pooled analysis of three multinational, open-label studies Clin. Ther. 2007, 29, 1645-1654 (Pubitemid 47494543)
    • (2007) Clinical Therapeutics , vol.29 , Issue.8 , pp. 1645-1654
    • Pastores, G.M.1    Elstein, D.2    Hrebicek, M.3    Zimran, A.4
  • 23
    • 73049101383 scopus 로고    scopus 로고
    • Real-world clinical experience with long-term miglustat maintenance therapy in type 1 Gaucher disease: The ZAGAL project
    • Giraldo, P.; Alfonso, P.; Atutxa, K.; Fernández-Galán, M. A.; Barez, A.; Franco, R. Real-world clinical experience with long-term miglustat maintenance therapy in type 1 Gaucher disease: the ZAGAL project Haematologica 2009, 94, 1771-1775
    • (2009) Haematologica , vol.94 , pp. 1771-1775
    • Giraldo, P.1    Alfonso, P.2    Atutxa, K.3    Fernández-Galán, M.A.4    Barez, A.5    Franco, R.6
  • 24
    • 0033018496 scopus 로고    scopus 로고
    • Accelerated transport and maturation of lysosomal α-galactosidase A in fabry lymphoblasts by an enzyme inhibitor
    • DOI 10.1038/4801
    • Fan, J. Q.; Ishii, S.; Asano, N.; Suzuki, Y. Accelerated transport and maturation of lysosomal alpha-galactosidase A in Fabry lymphoblasts by an enzyme inhibitor Nat. Med. 1999, 5, 112-115 (Pubitemid 29051008)
    • (1999) Nature Medicine , vol.5 , Issue.1 , pp. 112-115
    • Fan, J.-Q.1    Ishii, S.2    Asano, N.3    Suzuki, Y.4
  • 25
    • 7244253015 scopus 로고    scopus 로고
    • Pharmacologic rescue of conformationally-defective proteins: Implications for the treatment of human disease
    • DOI 10.1111/j.1600-0854.2004.00232.x
    • Ulloa-Aguirre, A.; Janovick, J. A.; Brothers, S. P.; Conn, P. M. Pharmacologic rescue of conformationally-defective proteins: implications for the treatment of human disease Traffic 2004, 5, 821-837 (Pubitemid 39433553)
    • (2004) Traffic , vol.5 , Issue.11 , pp. 821-837
    • Ulloa-Aguirre, A.1    Janovick, J.A.2    Brothers, S.P.3    Conn, P.M.4
  • 26
    • 33846020543 scopus 로고    scopus 로고
    • Small molecule pharmacological chaperones: From thermodynamic stabilization to pharmaceutical drugs
    • DOI 10.1016/j.bbapap.2006.08.012, PII S157096390600286X
    • Arakawa, T.; Ejima, D.; Kita, Y.; Tsumoto, K. Small molecule pharmacological chaperones: From thermodynamic stabilization to pharmaceutical drugs Biochim. Biophys. Acta 2006, 1764, 1677-1687 (Pubitemid 46053854)
    • (2006) Biochimica et Biophysica Acta - Proteins and Proteomics , vol.1764 , Issue.11 , pp. 1677-1687
    • Arakawa, T.1    Ejima, D.2    Kita, Y.3    Tsumoto, K.4
  • 27
    • 50149112642 scopus 로고    scopus 로고
    • Protein misfolding in conformational disorders: Rescue of folding defects and chemical chaperoning
    • Leandro, P.; Gomes, C. M. Protein misfolding in conformational disorders: rescue of folding defects and chemical chaperoning Mini-Rev. Med. Chem. 2008, 8, 901-11
    • (2008) Mini-Rev. Med. Chem. , vol.8 , pp. 901-11
    • Leandro, P.1    Gomes, C.M.2
  • 28
    • 0033521072 scopus 로고    scopus 로고
    • Setting the standards: Quality control in the secretory pathway
    • Ellgaard, L.; Molinari, M.; Helenius, A. Setting the standards: quality control in the secretory pathway Science 1999, 286, 1882-1888 (Pubitemid 129515888)
    • (1999) Science , vol.286 , Issue.5446 , pp. 1882-1888
    • Ellgaard, L.1    Molinari, M.2    Helenius, A.3
  • 29
    • 0037336295 scopus 로고    scopus 로고
    • Quality control in the endoplasmic reticulum
    • DOI 10.1038/nrm1052
    • Ellgaard, L.; Helenius, A. Quality control in the endoplasmic reticulum Nat. Rev. Mol. Cell Biol. 2003, 4, 181-191 (Pubitemid 36288040)
    • (2003) Nature Reviews Molecular Cell Biology , vol.4 , Issue.3 , pp. 181-191
    • Ellgaard, L.1    Helenius, A.2
  • 30
    • 33845240108 scopus 로고    scopus 로고
    • Clinical chaperones and permissive temperatures alter localization of Gaucher disease associated glucocerebrosidase variants
    • Sawkar, A. R.; Schmitz, M.; Zimmer, K. P.; Reczek, D.; Edmunds, T.; Balch, W. E. Clinical chaperones and permissive temperatures alter localization of Gaucher disease associated glucocerebrosidase variants ACS Chem. Biol. 2006, 1, 235-251
    • (2006) ACS Chem. Biol. , vol.1 , pp. 235-251
    • Sawkar, A.R.1    Schmitz, M.2    Zimmer, K.P.3    Reczek, D.4    Edmunds, T.5    Balch, W.E.6
  • 31
    • 0023841862 scopus 로고
    • A view of acidic intracellular compartments
    • Anderson, R. G.; Orci, L. A view of acidic intracellular compartments J. Cell Biol. 1988, 106, 539-543 (Pubitemid 18089954)
    • (1988) Journal of Cell Biology , vol.106 , Issue.3 , pp. 539-543
    • Anderson, R.G.W.1    Orci, L.2
  • 33
    • 24644490499 scopus 로고    scopus 로고
    • Miglustat (NB-DNJ) works as a chaperone for mutated acid β-glucosidase in cells transfected with several Gaucher disease mutations
    • DOI 10.1016/j.bcmd.2005.05.007, PII S1079979605000689
    • Alfonso, P.; Pampín, S.; Estrada, J.; Rodríguez-Rey, J. C.; Giraldo, P.; Sancho, J. Miglustat (NB-DNJ) works as a chaperone for mutated acid beta-glucosidase in cells transfected with several Gaucher disease mutations Blood Cells, Mol., Dis. 2005, 35, 268-276 (Pubitemid 41267059)
    • (2005) Blood Cells, Molecules, and Diseases , vol.35 , Issue.2 , pp. 268-276
    • Alfonso, P.1    Pampin, S.2    Estrada, J.3    Rodriguez-Rey, J.C.4    Giraldo, P.5    Sancho, J.6    Pocovi, M.7
  • 34
    • 27744459735 scopus 로고    scopus 로고
    • Gaucher disease-associated glucocerebrosidases show mutation-dependent chemical chaperoning profiles
    • DOI 10.1016/j.chembiol.2005.09.007, PII S1074552105002978
    • Sawkar, A. R.; Adamski-Werner, S. L.; Cheng, W. C.; Wong, C. H.; Beutler, E.; Zimmer, K. P. Gaucher disease-associated glucocerebrosidases show mutation-dependent chemical chaperoning profiles Chem. Biol. 2005, 12, 1235-1244 (Pubitemid 41628259)
    • (2005) Chemistry and Biology , vol.12 , Issue.11 , pp. 1235-1244
    • Sawkar, A.R.1    Adamski-Werner, S.L.2    Cheng, W.-C.3    Wong, C.-H.4    Beutler, E.5    Zimmer, K.-P.6    Kelly, J.W.7
  • 36
    • 67349151270 scopus 로고    scopus 로고
    • The pharmacological chaperone 1-deoxygalactonojirimycin increases alpha-galactosidase A levels in Fabry patient cell lines
    • Benjamin, E. R.; Flanagan, J. J.; Schilling, A.; Chang, H. H.; Agarwal, L.; Katz, E. The pharmacological chaperone 1-deoxygalactonojirimycin increases alpha-galactosidase A levels in Fabry patient cell lines J. Inherited Metab. Dis. 2009, 32, 424-440
    • (2009) J. Inherited Metab. Dis. , vol.32 , pp. 424-440
    • Benjamin, E.R.1    Flanagan, J.J.2    Schilling, A.3    Chang, H.H.4    Agarwal, L.5    Katz, E.6
  • 37
    • 77953127358 scopus 로고    scopus 로고
    • 2,5-Dideoxy-2,5-imino-d-altritol as a new class of pharmacological chaperone for Fabry disease
    • Kato, A.; Yamashita, Y.; Nakagawa, S.; Koike, Y.; Adachi, I.; Hollinshead, J. 2,5-Dideoxy-2,5-imino-d-altritol as a new class of pharmacological chaperone for Fabry disease Bioorg. Med. Chem. 2010, 18, 3790-3794
    • (2010) Bioorg. Med. Chem. , vol.18 , pp. 3790-3794
    • Kato, A.1    Yamashita, Y.2    Nakagawa, S.3    Koike, Y.4    Adachi, I.5    Hollinshead, J.6
  • 40
    • 41349085850 scopus 로고    scopus 로고
    • Treatment perspectives for the lysosomal storage diseases
    • DOI 10.1517/14728214.13.1.197
    • Grabowski, G. A. Treatment perspectives for the lysosomal storage diseases Expert Opin. Emerging Drugs 2008, 13, 197-211 (Pubitemid 351448710)
    • (2008) Expert Opinion on Emerging Drugs , vol.13 , Issue.1 , pp. 197-211
    • Grabowski, G.A.1
  • 41
    • 41249093218 scopus 로고    scopus 로고
    • Isofagomine increases lysosomal delivery of exogenous glucocerebrosidase
    • Shen, J. S.; Edwards, N. J.; Hong, Y. B.; Murray, G. J. Isofagomine increases lysosomal delivery of exogenous glucocerebrosidase Biochem. Biophys. Res. Commun. 2008, 369, 1071-1075
    • (2008) Biochem. Biophys. Res. Commun. , vol.369 , pp. 1071-1075
    • Shen, J.S.1    Edwards, N.J.2    Hong, Y.B.3    Murray, G.J.4
  • 44
    • 0042354624 scopus 로고    scopus 로고
    • X-ray structure of human acid-β-glucosidase, the defective enzyme in Gaucher disease
    • DOI 10.1038/sj.embor.embor873
    • Dvir, H.; Harel, M.; McCarthy, A. A.; Toker, L.; Silman, I.; Futerman, A. H. X-ray structure of human acid-beta-glucosidase, the defective enzyme in Gaucher disease EMBO Rep. 2003, 4, 704-709 (Pubitemid 36974756)
    • (2003) EMBO Reports , vol.4 , Issue.7 , pp. 704-709
    • Dvir, H.1    Harel, M.2    McCarthy, A.A.3    Toker, L.4    Silman, I.5    Futerman, A.H.6    Sussman, J.L.7
  • 45
    • 35348989145 scopus 로고    scopus 로고
    • Crystal structures of complexes of N-butyl- and N-nonyl-deoxynojirimycin bound to acid β-glucosidase: Insights into the mechanism of chemical chaperone action in Gaucher disease
    • DOI 10.1074/jbc.M705005200
    • Brumshtein, B.; Greenblatt, H. M.; Butters, T. D.; Shaaltiel, Y.; Aviezer, D.; Silman, I Crystal structures of complexes of N-butyl- and N-nonyl-deoxynojirimycin bound to acid beta-glucosidase: insights into the mechanism of chemical chaperone action in Gaucher disease J. Biol. Chem. 2007, 282, 29052-29058 (Pubitemid 47606022)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.39 , pp. 29052-29058
    • Brumshtein, B.1    Greenblatt, H.M.2    Butters, T.D.3    Shaaltiel, Y.4    Aviezer, D.5    Silman, I.6    Futerman, A.H.7    Sussman, J.L.8
  • 46
    • 70849126444 scopus 로고    scopus 로고
    • Characterization of gene-activated human acid-beta-glucosidase: Crystal structure, glycan composition, and internalization into macrophages
    • Brumshtein, B.; Salinas, P.; Peterson, B.; Chan, V.; Silman, I.; Sussman, J. L. Characterization of gene-activated human acid-beta-glucosidase: crystal structure, glycan composition, and internalization into macrophages Glycobiology 2010, 20, 24-32
    • (2010) Glycobiology , vol.20 , pp. 24-32
    • Brumshtein, B.1    Salinas, P.2    Peterson, B.3    Chan, V.4    Silman, I.5    Sussman, J.L.6
  • 48
    • 0030030138 scopus 로고    scopus 로고
    • Turnover and distribution of intravenously administered mannose-terminated human acid β-glucosidase in murine and human tissues
    • Xu, Y. H.; Ponce, E.; Sun, Y.; Leonova, T.; Bove, K.; Witte, D. Turnover and distribution of intravenously administered mannose-terminated human acid beta-glucosidase in murine and human tissues Pediatr. Res. 1996, 39, 313-322 (Pubitemid 26039557)
    • (1996) Pediatric Research , vol.39 , Issue.2 , pp. 313-322
    • Xu, Y.-H.1    Ponce, E.2    Sun, Y.3    Leonova, T.4    Bove, K.5    Witte, D.6    Grabowski, G.A.7
  • 49
    • 33751206186 scopus 로고    scopus 로고
    • Delivery of lysosomal enzymes for therapeutic use: Glucocerebrosidase as an example
    • DOI 10.1517/17425247.3.6.771
    • Grabowski, G. A. Delivery of lysosomal enzymes for therapeutic use: glucocerebrosidase as an example Expert Opin. Drug Delivery 2006, 3, 771-782 (Pubitemid 44781849)
    • (2006) Expert Opinion on Drug Delivery , vol.3 , Issue.6 , pp. 771-782
    • Grabowski, G.A.1
  • 50
    • 66649137718 scopus 로고    scopus 로고
    • Effects of pH and iminosugar pharmacological chaperones on lysosomal glycosidase structure and stability
    • Lieberman, R. L.; D́aquino, J. A.; Ringe, D.; Petsko, G. A. Effects of pH and iminosugar pharmacological chaperones on lysosomal glycosidase structure and stability Biochemistry 2009, 48, 4816-4827
    • (2009) Biochemistry , vol.48 , pp. 4816-4827
    • Lieberman, R.L.1    D́aquino, J.A.2    Ringe, D.3    Petsko, G.A.4
  • 51
    • 16344382388 scopus 로고    scopus 로고
    • Thermodynamic stability of carbonic anhydrase: Measurements of binding affinity and stoichiometry using thermofluor
    • DOI 10.1021/bi048135v
    • Matulis, D.; Kranz, J. K.; Salemme, F. R.; Todd, M. J. Thermodynamic stability of carbonic anhydrase: measurements of binding affinity and stoichiometry using ThermoFluor Biochemistry 2005, 44, 5258-5266 (Pubitemid 40471238)
    • (2005) Biochemistry , vol.44 , Issue.13 , pp. 5258-5266
    • Matulis, D.1    Kranz, J.K.2    Salemme, F.R.3    Todd, M.J.4
  • 52
    • 0022392671 scopus 로고
    • Characterization of the activation of rat liver β-glucosidase by sialosylgangliotetraosylceramide
    • Basu, A.; Glew, R. H. Characterization of the activation of rat liver beta-glucosidase sialosylgangliotetraosylceramide J. Biol. Chem. 1985, 260, 13067-13073 (Pubitemid 16209777)
    • (1985) Journal of Biological Chemistry , vol.260 , Issue.24 , pp. 13067-13073
    • Basu, A.1    Glew, R.H.2
  • 53
    • 0022485729 scopus 로고
    • In situ radiation-inactivation size of fibroblast membrane-bound acid β-glucosidase in Gaucher type 1, type 2 and type 3 disease
    • DOI 10.1016/0167-4838(86)90010-5
    • Choy, F. Y; Woo, M.; Potier, M. In situ radiation-inactivation size of fibroblast membrane-bound acid beta-glucosidase in Gaucher type 1, type 2 and type 3 disease Biochim. Biophys. Acta 1986, 870, 76-81 (Pubitemid 16073488)
    • (1986) Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology , vol.870 , Issue.1 , pp. 76-81
    • Choy, F.Y.M.1    Woo, M.2    Potier, M.3
  • 54
    • 0038412819 scopus 로고    scopus 로고
    • Transient expression of wild-type and mutant glucocerebrosidases in hybrid vaccinia expression system
    • Hodanová, K.; Melková, Z.; Horowitz, M.; Hrebízek, M. Transient expression of wild-type and mutant glucocerebrosidases in hybrid vaccinia expression system Eur. J. Hum. Genet. 2003, 11, 369-374
    • (2003) Eur. J. Hum. Genet. , vol.11 , pp. 369-374
    • Hodanová, K.1    Melková, Z.2    Horowitz, M.3    Hrebízek, M.4
  • 55
    • 0020480481 scopus 로고
    • Anilinonaphthalene sulfonate as a probe of membrane composition and function
    • Slavik, J. Anilinonaphthalene sulfonate as a probe of membrane composition and function Biochim. Biophys. Acta 1982, 694, 1-25
    • (1982) Biochim. Biophys. Acta , vol.694 , pp. 1-25
    • Slavik, J.1
  • 60
    • 78649898944 scopus 로고    scopus 로고
    • Conformational stability of hepatitis C virus NS3 protease
    • Abian, O.; Vega, S.; Neira, J. L.; Velazquez-Campoy, A. Conformational stability of hepatitis C virus NS3 protease Biophys. J. 2010, 99, 3811-3820
    • (2010) Biophys. J. , vol.99 , pp. 3811-3820
    • Abian, O.1    Vega, S.2    Neira, J.L.3    Velazquez-Campoy, A.4
  • 61
    • 79955404357 scopus 로고    scopus 로고
    • Isofagomine in vivo effects in a neuronopathic Gaucher disease mouse
    • Sun, Y.; Ran, H.; Liou, B.; Quinn, B.; Zamzow, M.; Zhang, W. Isofagomine in vivo effects in a neuronopathic Gaucher disease mouse PLoS One 2011, 6, e19037
    • (2011) PLoS One , vol.6 , pp. 19037
    • Sun, Y.1    Ran, H.2    Liou, B.3    Quinn, B.4    Zamzow, M.5    Zhang, W.6
  • 63
    • 67349206148 scopus 로고    scopus 로고
    • The pharmacological chaperone N-butyldeoxynojirimycin enhances enzyme replacement therapy in Pompe disease fibroblasts
    • Porto, C; Cardone, M.; Fontana, F.; Rossi, B.; Tuzzi, M. R.; Tarallo, A. The pharmacological chaperone N-butyldeoxynojirimycin enhances enzyme replacement therapy in Pompe disease fibroblasts Mol. Ther. 2009, 17, 964-971
    • (2009) Mol. Ther. , vol.17 , pp. 964-971
    • Porto, C.1    Cardone, M.2    Fontana, F.3    Rossi, B.4    Tuzzi, M.R.5    Tarallo, A.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.