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Volumn 22, Issue 4, 2012, Pages 492-503

Production of active human glucocerebrosidase in seeds of Arabidopsis thaliana complex-glycan-deficient (cgl) plants

Author keywords

Arabidopsis cgl mutant; Gaucher disease; human glucocerebrosidase; mannose terminated N glycans; N glycosylation

Indexed keywords

AMINO ACID DERIVATIVE; CHAPERONE; FUCOSE; GLUCOSYLCERAMIDASE; GLYCAN; IMIGLUCERASE; ISOFAGOMINE; MANNOSE; N ACETYLGLUCOSAMINYLTRANSFERASE; N ACETYLGLUCOSAMINYLTRANSFERASE I; RECOMBINANT ENZYME; UNCLASSIFIED DRUG; XYLOSE;

EID: 84863398445     PISSN: 09596658     EISSN: 14602423     Source Type: Journal    
DOI: 10.1093/glycob/cwr157     Document Type: Article
Times cited : (40)

References (67)
  • 3
    • 0027179238 scopus 로고
    • Human acid β-glucosidase. N-glycosylation site occupancy and the effect of glycosylation on enzymatic activity
    • Berg-Fussman A, Grace ME, Ioannou Y, Grabowski GA. 1993. Human acid beta-glucosidase. N-glycosylation site occupancy and the effect of glycosylation on enzymatic activity. J Biol Chem. 268:14861-14866. (Pubitemid 23206631)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.20 , pp. 14861-14866
    • Berg-Fussman, A.1    Grace, M.E.2    Ioannou, Y.3    Grabowski, G.A.4
  • 4
    • 0024542617 scopus 로고
    • Posttranslational processing of human lysosomal acid β-glucosidase: A continuum of defects in Gaucher disease type 1 and type 2 fibroblasts
    • Bergmann JE, Grabowski GA. 1989. Posttranslational processing of human lysosomal acid beta-glucosidase: a continuum of defects in Gaucher disease type 1 and type 2 fibroblasts. Am J Hum Genet. 44:741-750. (Pubitemid 19119987)
    • (1989) American Journal of Human Genetics , vol.44 , Issue.5 , pp. 741-750
    • Bergmann, J.E.1    Grabowski, G.A.2
  • 6
    • 0029664406 scopus 로고    scopus 로고
    • Quantitative analysis of the targeting of mannose-terminal glucocerebrosidase. Predominant uptake by liver endothelial cells
    • Bijsterbosch MK, Donker W, van de Bilt H, van Weely S, van Berkel TJ, Aerts JM. 1996. Quantitative analysis of the targeting of mannose-terminal glucocerebrosidase. Predominant uptake by liver endothelial cells. Eur J Biochem. 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
  • 10
    • 0024342687 scopus 로고
    • Purification of lysosomal membrane-bound glucocerebrosidase from human cultured fibroblasts using high-performance liquid chromatography
    • DOI 10.1016/0003-2697(89)90135-8
    • Choy FYM. 1989. Purification of lysosomal membrane-bound glucocerebrosidase from human cultured fibroblasts using high-performance liquid chromatography. Anal Biochem. 179:312-318. (Pubitemid 19153839)
    • (1989) Analytical Biochemistry , vol.179 , Issue.2 , pp. 312-318
    • Choy, F.Y.M.1
  • 11
    • 0032447801 scopus 로고    scopus 로고
    • Floral dip: A simplified method for Agrobacterium-mediated transformation of Arabidopsis thaliana
    • Clough SJ, Bent AF. 1998. Floral dip: a simplified method for Agrobacterium-mediated transformation of Arabidopsis thaliana. Plant J. 16:735-743.
    • (1998) Plant J , vol.16 , pp. 735-743
    • Clough, S.J.1    Bent, A.F.2
  • 13
    • 84863407073 scopus 로고
    • A bifunctional fusion between β-glucuronidase and neomycin phosphotransferase: A broad-spectrum marker enzyme for plants
    • Datla RSS, Hammerlindl JK, Panchuk B, Pelcher LE, Keller W. 1991. A bifunctional fusion between β-glucuronidase and neomycin phosphotransferase: a broad-spectrum marker enzyme for plants. Gene. 122:383-384.
    • (1991) Gene , vol.122 , pp. 383-384
    • Datla, R.S.S.1    Hammerlindl, J.K.2    Panchuk, B.3    Pelcher, L.E.4    Keller, W.5
  • 14
    • 0036901291 scopus 로고    scopus 로고
    • Boosting heterologous protein production in transgenic dicotyledonous seeds using Phaseolus vulgaris regulatory sequences
    • DOI 10.1038/nbt755
    • De Jaeger G, Scheffer S, Jacobs A, Zambre M, Zobell O, Goossens A, Depicker A, Angenon G. 2002. Boosting heterologous protein production in transgenic dicotyledonous seeds using Phaseolus vulgaris regulatory sequences. Nat Biotechnol. 20:1265-1268. (Pubitemid 35462494)
    • (2002) Nature Biotechnology , vol.20 , Issue.12 , pp. 1265-1268
    • De Jaeger, G.1    Scheffer, S.2    Jacobs, A.3    Zambre, M.4    Zobell, O.5    Goossens, A.6    Depicker, A.7    Angenon, G.8
  • 16
    • 33846104366 scopus 로고    scopus 로고
    • Post-transcriptional factors are important for high-level expression of the human α-l-iduronidase gene in Arabidopsis cgl (complex-glycan- deficient) seeds
    • DOI 10.1016/j.plantsci.2006.09.007, PII S016894520600255X
    • Downing WL, Hu X, Kermode AR. 2007. Post-transcriptional factors are important for high-level expression of the human α-L-iduronidase gene in Arabidopsis cgl (complex glycan-deficient) seeds. Plant Sci. 172:327-334. (Pubitemid 46073272)
    • (2007) Plant Science , vol.172 , Issue.2 , pp. 327-334
    • Downing, W.L.1    Hu, X.2    Kermode, A.R.3
  • 17
    • 57749115778 scopus 로고    scopus 로고
    • Comparative analyses of Arabidopsis complex glycan1 mutants and genetic interaction with staurosporin and temperature sensitive3a
    • DOI 10.1104/pp.108.127027
    • Frank J, Kaulfürst-Soboll H, Rips S, Koiwa H, von Schaewen A. 2008. Comparative analyses of Arabidopsis complex glycan 1 mutants and genetic interaction with staurosporin and temperature sensitive3a. Plant Physiol. 148:1354-1367. (Pubitemid 352847501)
    • (2008) Plant Physiology , vol.148 , Issue.3 , pp. 1354-1367
    • Frank, J.1    Kaulfurst-Soboll, H.2    Rips, S.3    Koiwa, H.4    Von Schaewen, A.5
  • 18
    • 0033134795 scopus 로고    scopus 로고
    • A comparison of the pharmacological properties of carbohydrate remodeled recombinant and placental-derived β-glucocerebrosidase: Implications for clinical efficacy in treatment of Gaucher disease
    • Friedman B, Vaddi K, Preston C, Mahon E, Cataldo JR, McPherson JM. 1999. A comparison of the pharmacological properties of carbohydrate remodeled recombinant and placental-derived beta-glucocerebrosidase: implications for clinical efficacy in treatment of Gaucher disease. Blood 93:2807-2816. (Pubitemid 29200770)
    • (1999) Blood , vol.93 , Issue.9 , pp. 2807-2816
    • Friedman, B.1    Vaddi, K.2    Preston, C.3    Mahon, E.4    Cataldo, J.R.5    McPherson, J.M.6
  • 19
    • 0017708011 scopus 로고
    • Enzyme replacement therapy in Gaucher's disease: large-scale purification of glucocerebrosidase suitable for human administration
    • DOI 10.1073/pnas.74.8.3560
    • Furbish FS, Blair HE, Shiloach J, Pentchev PG, Brady RO. 1977. Enzyme replacement therapy in Gaucher's disease: large-scale purification of glucocerebrosidase suitable for human administration. Proc Natl Acad Sci USA. 74:3560-3563. (Pubitemid 8180245)
    • (1977) Proceedings of the National Academy of Sciences of the United States of America , vol.74 , Issue.8 , pp. 3560-3563
    • Furbish, F.S.1    Blair, H.E.2    Shiloach, J.3
  • 20
    • 0019475525 scopus 로고
    • Uptake and distribution of placental glucocerebrosidase in rat hepatic cells and effects of sequential deglycosylation
    • Furbish FS, Steer CJ, Krett NL, Barranger JA. 1981. Uptake and distribution of placental glucocerebrosidase in rat hepatic cells and effects of sequential deglycosylation. Biochim Biophys Acta. 673:425-434. (Pubitemid 11103742)
    • (1981) Biochimica et Biophysica Acta , vol.673 , Issue.4 , pp. 425-434
    • Furbish, F.S.1    Steer, C.J.2    Krett, N.L.3    Barranger, J.A.4
  • 21
    • 1542291118 scopus 로고    scopus 로고
    • Posttranslational modification of therapeutic proteins in plants
    • DOI 10.1016/j.pbi.2004.01.015, PII S1369526604000184
    • Gomord V, Faye L. 2004. Posttranslational modification of therapeutic proteins in plants. Curr Opin Plant Biol. 7:171-181. (Pubitemid 38308053)
    • (2004) Current Opinion in Plant Biology , vol.7 , Issue.2 , pp. 171-181
    • Gomord, V.1    Faye, L.2
  • 23
    • 0033179948 scopus 로고    scopus 로고
    • The arcelin-5 gene of Phaseolus vulgaris directs high seed-specific expression in transgenic Phaseolus acutifolius and Arabidopsis plants
    • Goossens A, Dillen W, De Clercq J, Van Montagu M, Angenon G. 1999. The arcelin-5 gene of Phaseolus vulgaris directs high seed-specific expression in transgenic Phaseolus acutifolius and Arabidopsis plants. Plant Physiol. 120:1095-1104. (Pubitemid 29411897)
    • (1999) Plant Physiology , vol.120 , Issue.4 , pp. 1095-1104
    • Goossens, A.1    Dillen, W.2    De Clercq, J.3    Van Montagu, M.4    Angenon, G.5
  • 24
    • 0031292176 scopus 로고    scopus 로고
    • Gaucher disease: Gene frequencies and genotype/phenotype correlations
    • Grabowski GA. 1997. Gaucher disease: Gene frequencies and genotype/phenotype correlations. Genet Test. 1:5-12. (Pubitemid 127526931)
    • (1997) Genetic Testing , vol.1 , Issue.1 , pp. 5-12
    • Grabowski, G.A.1
  • 25
    • 53049096591 scopus 로고    scopus 로고
    • Phenotype, diagnosis, and treatment of Gaucher's disease
    • Grabowski GA. 2008. Phenotype, diagnosis, and treatment of Gaucher's disease. Lancet. 372:1263-1271.
    • (2008) Lancet , vol.372 , pp. 1263-1271
    • Grabowski, G.A.1
  • 27
    • 0021859754 scopus 로고
    • Genetic heterogeneity in Gaucher disease: Physicokinetic and immunologic studies of the residual enzyme in cultured fibroblasts from non-neuronopathic and neuronopathic patients
    • DOI 10.1002/ajmg.1320210316
    • Grabowski GA, Goldblatt J, Dinur T, Kruse J, Svennerholm L, Gatt S, Desnick RJ. 1985. Genetic heterogeneity in Gaucher disease: physicokinetic and immunologic studies of the residual enzyme in cultured fibroblasts from non-neuronopathic and neuronpathic patients. Am J Med Genet. 21:529-549. (Pubitemid 15051177)
    • (1985) American Journal of Medical Genetics , vol.21 , Issue.3 , pp. 529-549
    • Grabowski, G.A.1    Goldblatt, J.2    Dinur, T.3
  • 28
    • 0028012014 scopus 로고
    • Mice lacking N-acetylglucosaminyltransferase i activity die at mid-gestation, revealing an essential role for complex or hybrid N-linked carbohydrates
    • Ioffe E, Stanley P. 1994. Mice lacking N-acetylglucosaminyltransferase I activity die at mid-gestation, revealing an essential role for complex or hybrid N-linked carbohydrates. Proc Natl Acad Sci USA. 91:728-732.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 728-732
    • Ioffe, E.1    Stanley, P.2
  • 29
    • 0023099774 scopus 로고
    • Biosynthesis and maturation of glucocerebrosidase in Gaucher fibroblasts
    • DOI 10.1111/j.1432-1033.1987.tb11008.x
    • Jonsson LM, Murray GJ, Sorrell SH, Strijland A, Aerts JF, Ginns EI, Barranger JA, Tager JM, Schram AW. 1987. Biosynthesis and maturation of glucocerebrosidase in Gaucher fibroblasts. Eur J Biochem. 164:171-179. (Pubitemid 17053681)
    • (1987) European Journal of Biochemistry , vol.164 , Issue.1 , pp. 171-179
    • Jonsson, L.M.V.1    Murray, G.J.2    Sorrell, S.H.3
  • 31
    • 0000360614 scopus 로고    scopus 로고
    • Mechanisms of intracellular protein transport and targeting in plant cells
    • Kermode AR. 1996. Mechanisms of intracellular protein transport and targeting. Crit Rev Plant Sci. 15:285-423. (Pubitemid 126485693)
    • (1996) Critical Reviews in Plant Sciences , vol.15 , Issue.4 , pp. 285-423
    • Kermode, A.R.1
  • 32
    • 33748171144 scopus 로고    scopus 로고
    • Plants as factories for production of biopharmaceutical and bioindustrial proteins: Lessons from cell biology
    • DOI 10.1139/B06-069
    • Kermode AR. 2006. Plants as factories for production of biopharmaceutical and bioindustrial proteins: lessons from cell biology. Can J Bot. 84:679-694. (Pubitemid 44310421)
    • (2006) Canadian Journal of Botany , vol.84 , Issue.4 , pp. 679-694
    • Kermode, A.R.1
  • 34
    • 33947095458 scopus 로고    scopus 로고
    • Ectopic expression of a conifer Abscisic Acid Insensitive3 transcription factor induces high-level synthesis of recombinant human α-L-iduronidase in transgenic tobacco leaves
    • DOI 10.1007/s11103-006-9122-y
    • Kermode AR, Zeng Y, Hu X, Lauson S, Abrams SR, He X. 2007. Ectopic expression of a conifer Abscisic Acid Insensitive3 transcription factor induces high-level synthesis of recombinant human α-L-iduronidase in transgenic tobacco leaves. Plant Mol Biol. 63:763-776. (Pubitemid 46399168)
    • (2007) Plant Molecular Biology , vol.63 , Issue.6 , pp. 763-776
    • Kermode, A.R.1    Zeng, Y.2    Hu, X.3    Lauson, S.4    Abrams, S.R.5    He, X.6
  • 35
    • 0034307511 scopus 로고    scopus 로고
    • N-Glycan analysis by matrix-assisted laser desorption/ionization mass spectrometry of electrophoretically separated nonmammalian proteins: Application to peanut allergen Ara h 1 and olive pollen allergen Ole e 1
    • Kolarich D, Altmann F. 2000. N-Glycan analysis by matrix-assisted laser desorption/ionization mass spectrometry of electrophoretically separated nonmammalian proteins: application to peanut allergen Ara h 1 and olive pollen allergen Ole e 1. Anal Biochem. 285:64-75.
    • (2000) Anal Biochem , vol.285 , pp. 64-75
    • Kolarich, D.1    Altmann, F.2
  • 36
    • 0001200134 scopus 로고
    • The promoter of TL-DNA gene 5 controls the tissuespecific expression of chimaeric genes carried by a novel type of Agrobacterium binary vector
    • Koncz C, Schell J. 1986. The promoter of TL-DNA gene 5 controls the tissuespecific expression of chimaeric genes carried by a novel type of Agrobacterium binary vector. Mol Gen Genet. 204:383-396.
    • (1986) Mol Gen Genet , vol.204 , pp. 383-396
    • Koncz, C.1    Schell, J.2
  • 39
    • 70349778691 scopus 로고    scopus 로고
    • Plant seeds as bioreactors for recombinant protein production
    • Lau OS, Sun SSM. 2009. Plant seeds as bioreactors for recombinant protein production. Biotechnol Adv. 27:1015-1022.
    • (2009) Biotechnol Adv , vol.27 , pp. 1015-1022
    • Lau, O.S.1    Sun, S.S.M.2
  • 40
    • 0000406542 scopus 로고
    • Characterization of a xylose-specific antiserum that reacts with the complex asparagine-linked glycans of extracellular and vacuolar glycoproteins
    • Lauriere M, Lauriere C, Chrispeels MJ, Johnson KD, Sturm A. 1989. Characterization of a xylose-specific antiserum that reacts with the complex asparagine-linked glycans of extracellular and vacuolar glycoproteins. Plant Physiol. 90:1182-1188.
    • (1989) Plant Physiol , vol.90 , pp. 1182-1188
    • Lauriere, M.1    Lauriere, C.2    Chrispeels, M.J.3    Johnson, K.D.4    Sturm, A.5
  • 42
    • 16544370449 scopus 로고    scopus 로고
    • A genetic and structural analysis of the N-glycosylation capabilities of rice and other monocotyledons
    • DOI 10.1007/s11103-004-1558-3
    • Leonard R, Kolarich D, Paschinger K, Altmann F, Wilson IB. 2004. A genetic and structural analysis of the N-glycosylation capabilities of rice and other monocotyledons. Plant Mol Biol. 55:631-644. (Pubitemid 40660253)
    • (2004) Plant Molecular Biology , vol.55 , Issue.5 , pp. 631-644
    • Leonard, R.1    Kolarich, D.2    Paschinger, K.3    Altmann, F.4    Wilson, I.B.H.5
  • 43
    • 0032169762 scopus 로고    scopus 로고
    • N-glycosylation of recombinant pharmaceutical glycoproteins produced in transgenic plants: Towards an humanisation of plant N-glycans
    • Lerouge P, Cabanes-Macheteau M, Rayon C, Fischette-Lainé AC, Gomord V, Faye L. 1998. N-glycosylation of recombinant pharmaceutical glycoproteins produced in transgenic plants: towards an humanisation of plant N-glycans. Plant Mol Biol. 38:31-48.
    • (1998) Plant Mol Biol , vol.38 , pp. 31-48
    • Lerouge, P.1    Cabanes-Macheteau, M.2    Rayon, C.3    Fischette-Lainé, A.C.4    Gomord, V.5    Faye, L.6
  • 46
    • 0025840612 scopus 로고
    • A short C-terminal sequence is necessary and sufficient for the targeting of chitinases to the plant vacuole
    • Neuhaus JM, Sticher L, Meins FJ, Boller T. 1991. A short C-terminal sequence is necessary and sufficient for the targeting of chitinases to the plant vacuole. Proc Natl Acad Sci USA 88:362-366.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 362-366
    • Neuhaus, J.M.1    Sticher, L.2    Meins, F.J.3    Boller, T.4
  • 47
    • 36048935960 scopus 로고    scopus 로고
    • LIMP-2 Is a Receptor for Lysosomal Mannose-6-Phosphate-Independent Targeting of β-Glucocerebrosidase
    • DOI 10.1016/j.cell.2007.10.018, PII S0092867407012901
    • Reczek D, Schwake M, Schröder J, Hughes H, Blanz J, Jin X, Brondyk W, Van Patten S, Edmunds T, Saftig P. 2007. LIMP-2 is a receptor for lysosomal mannose-6-phosphate-independent targeting of beta-glucocerebrosidase. Cell. 131:770-783. (Pubitemid 350087202)
    • (2007) Cell , vol.131 , Issue.4 , pp. 770-783
    • Reczek, D.1    Schwake, M.2    Schroder, J.3    Hughes, H.4    Blanz, J.5    Jin, X.6    Brondyk, W.7    Van Patten, S.8    Edmunds, T.9    Saftig, P.10
  • 48
    • 17844368369 scopus 로고    scopus 로고
    • Recombinant human acid β-glucosidase stored in tobacco seed is stable, active and taken up by human fibroblasts
    • DOI 10.1007/s11103-004-6832-x
    • Reggi S, Marchetti S, Patti T, De Amicis F, Cariati R, Bembi B, Fogher C. 2005. Recombinant human acid β-glucosidase stored in tobacco seed is stable, active and taken up by human fibroblasts. Plant Mol Biol. 57:101-113. (Pubitemid 40580444)
    • (2005) Plant Molecular Biology , vol.57 , Issue.1 , pp. 101-113
    • Reggi, S.1    Marchetti, S.2    Patti, T.3    De Amicis, F.4    Cariati, R.5    Bembi, B.6    Fogher, C.7
  • 49
    • 34250346068 scopus 로고    scopus 로고
    • From planta to pharma with glycosylation in the toolbox
    • DOI 10.1016/j.tibtech.2007.04.008, PII S0167779907001126
    • Saint-Jore-Dupas C, Faye L, Gomord V. 2007. From planta to pharma with glycosylation in the toolbox. Trends Biotechnol. 25:317-323. (Pubitemid 46908836)
    • (2007) Trends in Biotechnology , vol.25 , Issue.7 , pp. 317-323
    • Saint-Jore-Dupas, C.1    Faye, L.2    Gomord, V.3
  • 52
    • 33947504524 scopus 로고    scopus 로고
    • Therapy of adult Gaucher disease
    • DOI 10.3324/haematol.11193
    • Schmitz J, Poll LW, vom Dahl S. 2007. Therapy of adult Gaucher disease. Hematol J. 92:148-152. (Pubitemid 46852414)
    • (2007) Haematologica , vol.92 , Issue.2 , pp. 148-152
    • Schmitz, J.1    Poll, L.W.2    Vom Dahl, S.3
  • 54
    • 0036425270 scopus 로고    scopus 로고
    • Synonymous codon usage bias and the expression of human glucocerebrosidase in the methylotrophic yeast, Pichia pastoris
    • DOI 10.1016/S1046-5928(02)00526-0, PII S1046592802005260
    • Sinclair G, Choy FY. 2002. Synonymous codon usage bias and the expression of human glucocerebrosidase in the methylotrophic yeast. Protein Exp Purif. 26:96-105. (Pubitemid 35307492)
    • (2002) Protein Expression and Purification , vol.26 , Issue.1 , pp. 96-105
    • Sinclair, G.1    Choy, F.Y.M.2
  • 55
    • 33846223535 scopus 로고    scopus 로고
    • Generation of a conditional knockout of murine glucocerebrosidase: Utility for the study of Gaucher disease
    • DOI 10.1016/j.ymgme.2006.09.008, PII S1096719206003015
    • Sinclair GB, Jevon G, Colobong KE, Randall DR, Choy FYM, Clarke LA. 2007. Generation of a conditional knockout of murine glucocerebrosidase: Utility for the study of Gaucher disease. Mol Genet Metab. 90:148-156. (Pubitemid 46108614)
    • (2007) Molecular Genetics and Metabolism , vol.90 , Issue.2 , pp. 148-156
    • Sinclair, G.B.1    Jevon, G.2    Colobong, K.E.3    Randall, D.R.4    Choy, F.Y.M.5    Clarke, L.A.6
  • 57
    • 17044406723 scopus 로고    scopus 로고
    • Sowing the seeds of success: Pharmaceutical proteins from plants
    • Stoger E, Ma JK. 2005. Sowing the seeds of success: Pharmaceutical proteins from plants. Curr Opin Biotechnol. 16:167-173.
    • (2005) Curr Opin Biotechnol , vol.16 , pp. 167-173
    • Stoger, E.1    Ma, J.K.2
  • 59
    • 17644423487 scopus 로고    scopus 로고
    • Molecular basis of N-acetylglucosaminyltransferase I deficiency in Arabidopsis thaliana plants lacking complex N-glycans
    • DOI 10.1042/BJ20041686
    • Strasser R, Stadlmann J, Svoboda B, Altmann F, Glössl J, Mach L. 2005. Molecular basis of N-acetylglucosaminyltransferase I deficiency in Arabidopsis thaliana plants lacking complex N-glycans. Biochem J. 387:385-391. (Pubitemid 40571224)
    • (2005) Biochemical Journal , vol.387 , Issue.2 , pp. 385-391
    • Strasser, R.1    Stadlmann, J.2    Svoboda, B.3    Altmann, F.4    Glossl, J.5    Mach, L.6
  • 60
    • 59449109683 scopus 로고    scopus 로고
    • Identification of pharmacological chaperones for Gaucher disease and characterization of their effects on beta-glucocerebrosidase by hydrogen/deuterium exchange mass spectrometry
    • Tropak MB, Kornhaber GJ, Rigat BA, Maegawa GH, Buttner JD, Blanchard JE, Murphy C, Tuske SJ, Coales SJ, Hamuro Y, et al. 2008. Identification of pharmacological chaperones for Gaucher disease and characterization of their effects on beta-glucocerebrosidase by hydrogen/deuterium exchange mass spectrometry. Chembiochem. 9:2650-2662.
    • (2008) Chembiochem , vol.9 , pp. 2650-2662
    • Tropak, M.B.1    Kornhaber, G.J.2    Rigat, B.A.3    Maegawa, G.H.4    Buttner, J.D.5    Blanchard, J.E.6    Murphy, C.7    Tuske, S.J.8    Coales, S.J.9    Hamuro, Y.10
  • 61
    • 1542370795 scopus 로고    scopus 로고
    • Identification of multivesicular bodies as prevacuolar compartments in Nicotiana tabacum BY-2 cells
    • DOI 10.1105/tpc.019703
    • Tse YC, Mo B, Hillmer S, Zhao M, Lo SW, Robinson DG, Jiang L. 2004. Identification of multivesicular bodies as prevacuolar compartments in Nicotiana tabacum BY-2 cells. Plant Cell. 16:672-693. (Pubitemid 38335278)
    • (2004) Plant Cell , vol.16 , Issue.3 , pp. 672-693
    • Tse, Y.C.1    Mo, B.2    Hillmer, S.3    Zhao, M.4    Lo, S.W.5    Robinson, D.G.6    Jiang, L.7
  • 62
    • 0242475327 scopus 로고    scopus 로고
    • Molecular farming in plants: Host systems and expression technology
    • DOI 10.1016/j.tibtech.2003.10.002
    • Twyman RM, Stoger E, Schillberg S, Christou P, Fischer R. 2003. Molecular farming in plants: Host systems and expression technology. Trends Biotechnol. 21:570-578. (Pubitemid 37415010)
    • (2003) Trends in Biotechnology , vol.21 , Issue.12 , pp. 570-578
    • Twyman, R.M.1    Stoger, E.2    Schillberg, S.3    Christou, P.4    Fischer, R.5
  • 65
    • 0027640147 scopus 로고
    • Isolation of a mutant Arabidopsis plant that lacks N-acetyl glucosaminyl transferase i and is unable to synthesize Golgi-mediated complex N-linked glycans
    • von Schaewen A, Sturm A, O'Neill J, Chrispeels MJ. 1993. Isolation of a mutant Arabidopsis plant that lacks N-acetyl glucosaminyl transferase I and is unable to synthesize Golgi-mediated complex N-linked glycans. Plant Physiol. 102:1109-1118.
    • (1993) Plant Physiol , vol.102 , pp. 1109-1118
    • Von Schaewen, A.1    Sturm, A.2    O'Neill, J.3    Chrispeels, M.J.4
  • 66
    • 0031596341 scopus 로고    scopus 로고
    • Core α1,3-fucose is a key part of the epitope recognized by antibodies reacting against plant N-linked oligosaccharides and is present in a wide variety of plant extracts
    • DOI 10.1093/glycob/8.7.651
    • Wilson IBH, Harthill JE, Mullin N, Ashford D, Altmann F. 1998. Core α1,3-fucose is a key part of the epitope recognized by antibodies reacting against plant N-linked oligosaccharides and is present in a wide variety of plant extracts. Glycobiology. 8:651-661. (Pubitemid 28331441)
    • (1998) Glycobiology , vol.8 , Issue.7 , pp. 651-661
    • Wilson, I.B.H.1    Harthill, J.E.2    Mullin, N.P.3    Ashford, D.A.4    Altmann, F.5
  • 67
    • 0036874367 scopus 로고    scopus 로고
    • Sequential analysis of N- and O-linked glycosylation of 2D-PAGE separated glycoproteins
    • DOI 10.1021/pr025538d
    • Wilson NL, Schulz BL, Karlsson NG, Packer NH. 2002. Sequential analysis of N-and O-linked glycosylation of 2D-PAGE separated glycoproteins. J Proteome Res. 1:521-529. (Pubitemid 36395851)
    • (2002) Journal of Proteome Research , vol.1 , Issue.6 , pp. 521-529
    • Wilson, N.L.1    Schulz, B.L.2    Karlsson, N.G.3    Packer, N.H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.