메뉴 건너뛰기




Volumn 33, Issue 2, 2004, Pages 274-287

Expression, purification, and characterization of avian Thy-1 from Lec1 mammalian and Tn5 insect cells

Author keywords

Fourier transform ion cyclotron resonance; FT ICR; Glycoform homogeneity; MALDI; Mass spectrometry; Recombinant glycoprotein; Thy 1

Indexed keywords

AVES; GALLUS GALLUS; INSECTA; MAMMALIA;

EID: 0842267067     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2003.10.011     Document Type: Article
Times cited : (4)

References (54)
  • 1
    • 0027318961 scopus 로고
    • Biological roles of oligosaccharides: All of the theories are correct
    • A. Varki, Biological roles of oligosaccharides: all of the theories are correct, Glycobiology 3 (1993) 97-130.
    • (1993) Glycobiology , vol.3 , pp. 97-130
    • Varki, A.1
  • 2
    • 0025945169 scopus 로고
    • Oligosaccharides at each glycosylation site make structure-dependent contributions to biological properties of human tissue plasminogen activator
    • S.C. Howard, A.J. Wittwer, J.K. Welply, Oligosaccharides at each glycosylation site make structure-dependent contributions to biological properties of human tissue plasminogen activator, Glycobiology 1 (1991) 411-417.
    • (1991) Glycobiology , vol.1 , pp. 411-417
    • Howard, S.C.1    Wittwer, A.J.2    Welply, J.K.3
  • 3
    • 0021891884 scopus 로고
    • Assembly of asparagine-linked oligosaccharides
    • R. Kornfeld, S. Kornfeld, Assembly of asparagine-linked oligosaccharides, Annu. Rev. Biochem. 54 (1985) 631-664.
    • (1985) Annu. Rev. Biochem. , vol.54 , pp. 631-664
    • Kornfeld, R.1    Kornfeld, S.2
  • 4
    • 0024355330 scopus 로고
    • Glycoproteins - What are the sugar chains for?
    • J.C. Paulson, Glycoproteins - What are the sugar chains for?, Trends Biochem. Sci. 14 (1989) 272-276.
    • (1989) Trends Biochem. Sci. , vol.14 , pp. 272-276
    • Paulson, J.C.1
  • 5
    • 0034442818 scopus 로고    scopus 로고
    • A journey to the world of glycobiology
    • A. Kobata, A journey to the world of glycobiology, Glycoconj. J. 17 (2000) 443-464.
    • (2000) Glycoconj. J. , vol.17 , pp. 443-464
    • Kobata, A.1
  • 7
    • 0024559003 scopus 로고
    • Chinese hamster ovary cell mutants with multiple glycosylation defects for production of glycoproteins with minimal carbohydrate heterogeneity
    • P. Stanley, Chinese hamster ovary cell mutants with multiple glycosylation defects for production of glycoproteins with minimal carbohydrate heterogeneity, Mol. Cell. Biol. 9 (1989) 377-383.
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 377-383
    • Stanley, P.1
  • 8
    • 0025193736 scopus 로고
    • The oligosaccharides of influenza virus hemagglutinin expressed in insect cells by a baculovirus vector
    • K. Kuroda, H. Geyer, R. Geyer, W. Doerfler, H.D. Klenk, The oligosaccharides of influenza virus hemagglutinin expressed in insect cells by a baculovirus vector, Virology 174 (1990) 418-429.
    • (1990) Virology , vol.174 , pp. 418-429
    • Kuroda, K.1    Geyer, H.2    Geyer, R.3    Doerfler, W.4    Klenk, H.D.5
  • 11
    • 0020771155 scopus 로고
    • Purification and characterization of the mouse thymocyte Thy-1 glycoprotein
    • S.R. Carlsson, T.I. Stigbrand, Purification and characterization of the mouse thymocyte Thy-1 glycoprotein, Biochem. J. 211 (1983) 641-647.
    • (1983) Biochem. J. , vol.211 , pp. 641-647
    • Carlsson, S.R.1    Stigbrand, T.I.2
  • 12
    • 0019795504 scopus 로고
    • Biochemical characterization including amino-acid and carbohydrate compositions of canine and human-brain Thy-1 antigen
    • J.L. McKenzie, A.K. Allen, J.W. Fabre, Biochemical characterization including amino-acid and carbohydrate compositions of canine and human-brain Thy-1 antigen, Biochem. J. 197 (1981) 629-636.
    • (1981) Biochem. J. , vol.197 , pp. 629-636
    • McKenzie, J.L.1    Allen, A.K.2    Fabre, J.W.3
  • 13
    • 0023338172 scopus 로고
    • Tissue-specific N-glycosylation, site-specific oligosaccharide patterns and lentil lectin recognition of rat Thy-1
    • R.B. Parekh, A.G.D. Tse, R.A. Dwek, A.F. Williams, T.W. Rademacher, Tissue-specific N-glycosylation, site-specific oligosaccharide patterns and lentil lectin recognition of rat Thy-1, EMBO J. 6 (1987) 1233-1244.
    • (1987) EMBO J. , vol.6 , pp. 1233-1244
    • Parekh, R.B.1    Tse, A.G.D.2    Dwek, R.A.3    Williams, A.F.4    Rademacher, T.W.5
  • 14
    • 0027295706 scopus 로고
    • Comparative analysis of the N-glycans of rat, mouse, and human Thy-1. Site-specific oligosaccharide patterns of neural Thy-1, a member of the immunoglobulin superfamily
    • A.F. Williams, R.B. Parekh, D.R. Wing, A.C. Willis, A.N. Barclay, R. Dalchau, R.A. Dwek, T.W. Rademacher, Comparative analysis of the N-glycans of rat, mouse, and human Thy-1. Site-specific oligosaccharide patterns of neural Thy-1, a member of the immunoglobulin superfamily, Glycobiology 3 (1993) 339-348.
    • (1993) Glycobiology , vol.3 , pp. 339-348
    • Williams, A.F.1    Parekh, R.B.2    Wing, D.R.3    Willis, A.C.4    Barclay, A.N.5    Dalchau, R.6    Dwek, R.A.7    Rademacher, T.W.8
  • 15
    • 0000188544 scopus 로고
    • Akr thymic antigen: Its distribution in leukemias and nervous tissues
    • A.E. Reif, J.M.V. Allen, Akr thymic antigen: its distribution in leukemias and nervous tissues, J. Exp. Med. 120 (1964) 413-417.
    • (1964) J. Exp. Med. , vol.120 , pp. 413-417
    • Reif, A.E.1    Allen, J.M.V.2
  • 17
    • 0026605289 scopus 로고
    • Thy-1 involvement in neurite outgrowth-perturbation by antibodies, phospholipase-C, and mutation
    • N.K. Mahanthappa, P.H. Patterson, Thy-1 involvement in neurite outgrowth-perturbation by antibodies, phospholipase-C, and mutation, Dev. Biol. 150 (1992) 47-59.
    • (1992) Dev. Biol. , vol.150 , pp. 47-59
    • Mahanthappa, N.K.1    Patterson, P.H.2
  • 18
    • 0035838390 scopus 로고    scopus 로고
    • Thy-1 binds to integrin beta(3) on astrocytes and triggers formation of focal contact sites
    • L. Leyton, P. Schneider, C.V. Labra, C. Ruegg, C.A. Hetz, A.F. Quest, C. Bron, Thy-1 binds to integrin beta(3) on astrocytes and triggers formation of focal contact sites, Curr. Biol. 11 (2001) 1028-1038.
    • (2001) Curr. Biol. , vol.11 , pp. 1028-1038
    • Leyton, L.1    Schneider, P.2    Labra, C.V.3    Ruegg, C.4    Hetz, C.A.5    Quest, A.F.6    Bron, C.7
  • 20
    • 0026100208 scopus 로고
    • Enhanced secretion from insect cells of a foreign protein fused to honeybee melittin signal peptide
    • D.C. Tessier, D.Y. Thomas, H.E. Khouri, F. Laliberte, T. Vernet, Enhanced secretion from insect cells of a foreign protein fused to honeybee melittin signal peptide, Gene 98 (1991) 177-183.
    • (1991) Gene , vol.98 , pp. 177-183
    • Tessier, D.C.1    Thomas, D.Y.2    Khouri, H.E.3    Laliberte, F.4    Vernet, T.5
  • 21
    • 7344238492 scopus 로고    scopus 로고
    • Histone acetylation is required to maintain the unfolded nucleosome structure associated with transcribing DNA
    • H. Walia, H.Y. Chen, J.M. Sun, L.T. Holth, J.R. Davie, Histone acetylation is required to maintain the unfolded nucleosome structure associated with transcribing DNA, J. Biol. Chem. 273 (1998) 14516-14522.
    • (1998) J. Biol. Chem. , vol.273 , pp. 14516-14522
    • Walia, H.1    Chen, H.Y.2    Sun, J.M.3    Holth, L.T.4    Davie, J.R.5
  • 22
    • 0034073382 scopus 로고    scopus 로고
    • Transcriptional repression by blimp-1 (PRDI-BF1) involves recruitment of histone deacetylase
    • J. Yu, C. Angelin-Duclos, J. Greenwood, J. Liao, K. Calame, Transcriptional repression by blimp-1 (PRDI-BF1) involves recruitment of histone deacetylase, Mol. Cell. Biol. 20 (2000) 2592-2603.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 2592-2603
    • Yu, J.1    Angelin-Duclos, C.2    Greenwood, J.3    Liao, J.4    Calame, K.5
  • 23
    • 0024448151 scopus 로고
    • Calculation of protein extinction coefficients from amino acid sequence data
    • S.C. Gill, P.H. von Hippel, Calculation of protein extinction coefficients from amino acid sequence data, Anal. Biochem. 182 (1989) 319-326.
    • (1989) Anal. Biochem. , vol.182 , pp. 319-326
    • Gill, S.C.1    Von Hippel, P.H.2
  • 24
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • H. Towbin, T. Staehelin, J. Gordon, Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications, Proc. Natl. Acad. Sci. USA 76 (1979) 4350-4354.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 25
    • 0034672325 scopus 로고    scopus 로고
    • Estimation of protein secondary structure from circular dichroism spectra: Comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set
    • N. Sreerama, R.W. Woody, Estimation of protein secondary structure from circular dichroism spectra: Comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set, Anal. Biochem. 287 (2000) 252-260.
    • (2000) Anal. Biochem. , vol.287 , pp. 252-260
    • Sreerama, N.1    Woody, R.W.2
  • 26
    • 0000178042 scopus 로고
    • Micro-electrospray mass-spectrometry-ultra-high-sensitivity analysis of peptides and proteins
    • M.R. Emmett, R.M. Caprioli, Micro-electrospray mass-spectrometry-ultra- high-sensitivity analysis of peptides and proteins, J. Am. Soc. Mass Spectrom. 5 (1994) 605-613.
    • (1994) J. Am. Soc. Mass Spectrom. , vol.5 , pp. 605-613
    • Emmett, M.R.1    Caprioli, R.M.2
  • 28
    • 0031239787 scopus 로고    scopus 로고
    • External accumulation of ions for enhanced electrospray ionization Fourier transform ion cyclotron resonance mass spectrometry
    • M.W. Senko, C.L. Hendrickson, M.R. Emmett, S.D.H. Shi, A.G. Marshall, External accumulation of ions for enhanced electrospray ionization Fourier transform ion cyclotron resonance mass spectrometry, J. Am. Soc. Mass Spectrom. 8 (1997) 970-976.
    • (1997) J. Am. Soc. Mass Spectrom. , vol.8 , pp. 970-976
    • Senko, M.W.1    Hendrickson, C.L.2    Emmett, M.R.3    Shi, S.D.H.4    Marshall, A.G.5
  • 30
    • 0030481735 scopus 로고    scopus 로고
    • A high-performance modular data system for Fourier transform ion cyclotron resonance mass spectrometry
    • M.W. Senko, J.D. Canterbury, S.H. Guan, A.G. Marshall, A high-performance modular data system for Fourier transform ion cyclotron resonance mass spectrometry, Rapid Commun. Mass Spectrom. 10 (1996) 1839-1844.
    • (1996) Rapid Commun. Mass Spectrom. , vol.10 , pp. 1839-1844
    • Senko, M.W.1    Canterbury, J.D.2    Guan, S.H.3    Marshall, A.G.4
  • 31
    • 0021705942 scopus 로고
    • Space charge effects in Fourier transform mass spectrometry: Mass calibration
    • E.B. Ledford Jr., D.L. Rempel, M.L. Gross, Space charge effects in Fourier transform mass spectrometry: mass calibration, Anal. Chem. 56 (1984) 2744-2748.
    • (1984) Anal. Chem. , vol.56 , pp. 2744-2748
    • Ledford Jr., E.B.1    Rempel, D.L.2    Gross, M.L.3
  • 32
    • 0034695360 scopus 로고    scopus 로고
    • Comparison and interconversion of the two most common frequency-to-mass calibration functions for Fourier transform ion cyclotron resonance mass spectrometry
    • S.D.-H. Shi, J.J. Drader, M.A. Freitas, C.L. Hendrickson, A.G. Marshall, Comparison and interconversion of the two most common frequency-to-mass calibration functions for Fourier transform ion cyclotron resonance mass spectrometry, Int. J. Mass Spectrom. 196 (2000) 591-598.
    • (2000) Int. J. Mass Spectrom. , vol.196 , pp. 591-598
    • Shi, S.D.-H.1    Drader, J.J.2    Freitas, M.A.3    Hendrickson, C.L.4    Marshall, A.G.5
  • 33
    • 0035884155 scopus 로고    scopus 로고
    • Electron capture dissociation and infrared multiphoton dissociation MS/ MS of an N-glycosylated tryptic peptide to yield complementary sequence information
    • K. Håkansson, H.J. Cooper, M.R. Emmett, C.E. Costello, A.G. Marshall, C.L. Nilsson, Electron capture dissociation and infrared multiphoton dissociation MS/MS of an N-glycosylated tryptic peptide to yield complementary sequence information, Anal. Chem. 73 (2001) 4530-4536.
    • (2001) Anal. Chem. , vol.73 , pp. 4530-4536
    • Håkansson, K.1    Cooper, H.J.2    Emmett, M.R.3    Costello, C.E.4    Marshall, A.G.5    Nilsson, C.L.6
  • 34
    • 0027997748 scopus 로고
    • Infrared multiphoton dissociation of large multiply-charged ions for biomolecule sequencing
    • D.P. Little, J.P. Speir, M.W. Senko, P.B. Oconnor, F.W. McLafferty, Infrared multiphoton dissociation of large multiply-charged ions for biomolecule sequencing, Anal. Chem. 66 (1994) 2809-2815.
    • (1994) Anal. Chem. , vol.66 , pp. 2809-2815
    • Little, D.P.1    Speir, J.P.2    Senko, M.W.3    Oconnor, P.B.4    McLafferty, F.W.5
  • 35
    • 0032964297 scopus 로고    scopus 로고
    • Blast 2 Sequences, a new tool for comparing protein and nucleotide sequences
    • T.A. Tatusova, T.L. Madden, BLAST 2 SEQUENCES, a new tool for comparing protein and nucleotide sequences, FEMS Microbiol. Lett. 174 (1999) 247-250.
    • (1999) FEMS Microbiol. Lett. , vol.174 , pp. 247-250
    • Tatusova, T.A.1    Madden, T.L.2
  • 37
    • 0035261661 scopus 로고    scopus 로고
    • GlycoMod - A software tool for determining glycosylation compositions from mass spectrometric data
    • C.A. Cooper, E. Gasteiger, N.H. Packer, GlycoMod - a software tool for determining glycosylation compositions from mass spectrometric data, Proteomics 1 (2001) 340-349.
    • (2001) Proteomics , vol.1 , pp. 340-349
    • Cooper, C.A.1    Gasteiger, E.2    Packer, N.H.3
  • 38
    • 0021957779 scopus 로고
    • A hydrophopbic transmembrane segment at the carboxy terminus of Thy-1
    • T. Seki, H.-C. Chang, T. Moriuchi, R. Denome, H. Ploegh, J. Silver, A hydrophopbic transmembrane segment at the carboxy terminus of Thy-1, Science 227 (1985) 649-651.
    • (1985) Science , vol.227 , pp. 649-651
    • Seki, T.1    Chang, H.-C.2    Moriuchi, T.3    Denome, R.4    Ploegh, H.5    Silver, J.6
  • 40
    • 11944265249 scopus 로고
    • High-level expression of tissue inhibitor of metalloproteinase in Chinese hamster ovary cells using glutamine synthetase gene amplification
    • M.I. Crockett, C.R. Bebbington, G.T. Yarranton, High-level expression of tissue inhibitor of metalloproteinase in Chinese hamster ovary cells using glutamine synthetase gene amplification, Biotechnology 8 (1990) 662-667.
    • (1990) Biotechnology , vol.8 , pp. 662-667
    • Crockett, M.I.1    Bebbington, C.R.2    Yarranton, G.T.3
  • 42
    • 0022971228 scopus 로고
    • Partial characterization of chicken Thy-1 glycoprotein by monoclonal antibodies
    • P.W. French, P.L. Jeffrey, Partial characterization of chicken Thy-1 glycoprotein by monoclonal antibodies, J. Neurosci. Res. 16 (1986) 479-489.
    • (1986) J. Neurosci. Res. , vol.16 , pp. 479-489
    • French, P.W.1    Jeffrey, P.L.2
  • 43
    • 0032506222 scopus 로고    scopus 로고
    • Dynamics of fluorescence fluctuations in green fluorescent protein observed by fluorescence correlation spectroscopy
    • U. Haupts, S. Maiti, P. Schwille, W.W. Webb, Dynamics of fluorescence fluctuations in green fluorescent protein observed by fluorescence correlation spectroscopy, Proc. Natl. Acad. Sci. USA 95 (1998) 13573-13578.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 13573-13578
    • Haupts, U.1    Maiti, S.2    Schwille, P.3    Webb, W.W.4
  • 44
    • 0018635676 scopus 로고
    • Structural similarities between Thy-1 antigen from rat-brain and immunoglobulin
    • D.G. Campbell, A.F. Williams, P.M. Bayley, K.B.M. Reid, Structural similarities between Thy-1 antigen from rat-brain and immunoglobulin, Nature 282 (1979) 341-342.
    • (1979) Nature , vol.282 , pp. 341-342
    • Campbell, D.G.1    Williams, A.F.2    Bayley, P.M.3    Reid, K.B.M.4
  • 45
    • 0020787175 scopus 로고
    • The purification and characterization of a Thy-1-like glycoprotein from chicken brain
    • J.A.P. Rostas, T.A. Shevenan, C.M. Sinclair, P.L. Jeffrey, The purification and characterization of a Thy-1-like glycoprotein from chicken brain, Biochem. J. 213 (1983) 143-152.
    • (1983) Biochem. J. , vol.213 , pp. 143-152
    • Rostas, J.A.P.1    Shevenan, T.A.2    Sinclair, C.M.3    Jeffrey, P.L.4
  • 46
    • 0025984862 scopus 로고
    • Fragmentation of proteins by S. aureus strain V8 protease. Ammonium bicarbonate strongly inhibits the enzyme but does not improve the selectivity for glutamic acid
    • S.B. Sorensen, T.L. Sorensen, K. Breddam, Fragmentation of proteins by S. aureus strain V8 protease. Ammonium bicarbonate strongly inhibits the enzyme but does not improve the selectivity for glutamic acid, FEBS Lett. 294 (1991) 195-197.
    • (1991) FEBS Lett. , vol.294 , pp. 195-197
    • Sorensen, S.B.1    Sorensen, T.L.2    Breddam, K.3
  • 47
    • 33845379336 scopus 로고
    • Taillored excitation for Fourier transform ion cyclotron resonance mass spectrometry
    • A.G. Marshall, T.-C.L. Wang, T.L. Ricca, Taillored excitation for Fourier transform ion cyclotron resonance mass spectrometry, J. Am. Chem. Soc. 107 (1985) 7893-7897.
    • (1985) J. Am. Chem. Soc. , vol.107 , pp. 7893-7897
    • Marshall, A.G.1    Wang, T.-C.L.2    Ricca, T.L.3
  • 48
    • 4243270417 scopus 로고    scopus 로고
    • Stored waveform inverse Fourier transform (SWIFT) ion excitation in trapped-ion mass spectrometry: Theory and applications
    • S. Guan, A.G. Marshall, Stored waveform inverse Fourier transform (SWIFT) ion excitation in trapped-ion mass spectrometry: theory and applications, Int. J. Mass Spectrom. Ion Process. 158 (1996) 5-37.
    • (1996) Int. J. Mass Spectrom. Ion Process. , vol.158 , pp. 5-37
    • Guan, S.1    Marshall, A.G.2
  • 49
    • 0022623648 scopus 로고
    • The mouse Thy-1.2 glycoprotein gene - Complete sequence and identification of an unusual promoter
    • H.A. Ingraham, G.M. Lawless, G.A. Evans, The mouse Thy-1.2 glycoprotein gene - complete sequence and identification of an unusual promoter, J. Immunol. 136 (1986) 1482-1489.
    • (1986) J. Immunol. , vol.136 , pp. 1482-1489
    • Ingraham, H.A.1    Lawless, G.M.2    Evans, G.A.3
  • 50
    • 0019505815 scopus 로고
    • Analysis of structural similarities between brain Thy-1 antigen and immunoglobulin domains, Evidence for an evolutionary relationship and a hypothesis for its functional significance
    • F.E. Cohen, J. Novotny, M.J.E. Sternberg, D.G. Campbell, A.F. Williams, Analysis of structural similarities between brain Thy-1 antigen and immunoglobulin domains, Evidence for an evolutionary relationship and a hypothesis for its functional significance, Biochem. J. 195 (1981) 31-40.
    • (1981) Biochem. J. , vol.195 , pp. 31-40
    • Cohen, F.E.1    Novotny, J.2    Sternberg, M.J.E.3    Campbell, D.G.4    Williams, A.F.5
  • 51
    • 0032485869 scopus 로고    scopus 로고
    • Overexpression of a cytosolic chaperone to improve solubility and secretion of a recombinant IgG protein in insect cells
    • E. Ailor, M.J. Betenbaugh, Overexpression of a cytosolic chaperone to improve solubility and secretion of a recombinant IgG protein in insect cells, Biotechnol. Bioeng. 58 (1998) 196-203.
    • (1998) Biotechnol. Bioeng. , vol.58 , pp. 196-203
    • Ailor, E.1    Betenbaugh, M.J.2
  • 52
    • 0030151987 scopus 로고    scopus 로고
    • Rescue of immunoglobulins from insolubility is facilitated by PDI in the baculovirus expression system
    • T.A. Hsu, S. Watson, J.J. Eiden, M.J. Betenbaugh, Rescue of immunoglobulins from insolubility is facilitated by PDI in the baculovirus expression system, Protein Expr. Purif. 7 (1996) 281-288.
    • (1996) Protein Expr. Purif. , vol.7 , pp. 281-288
    • Hsu, T.A.1    Watson, S.2    Eiden, J.J.3    Betenbaugh, M.J.4
  • 53
    • 0033008021 scopus 로고    scopus 로고
    • Oligosaccharide analysis and molecular modeling of soluble forms of glycoproteins belonging to the Ly-6, scavenger receptor, and immunoglobulin superfamilies expressed in Chinese hamster ovary cells
    • P.M. Rudd, M.R. Wormald, D.J. Harvey, M. Devasahayam, M.S.B. McAlister, M.H. Brown, S.J. Davis, A.N. Barclay, R.A. Dwek, Oligosaccharide analysis and molecular modeling of soluble forms of glycoproteins belonging to the Ly-6, scavenger receptor, and immunoglobulin superfamilies expressed in Chinese hamster ovary cells, Glycobiology 9 (1999) 443-458.
    • (1999) Glycobiology , vol.9 , pp. 443-458
    • Rudd, P.M.1    Wormald, M.R.2    Harvey, D.J.3    Devasahayam, M.4    McAlister, M.S.B.5    Brown, M.H.6    Davis, S.J.7    Barclay, A.N.8    Dwek, R.A.9
  • 54
    • 0028588549 scopus 로고
    • Core fucosylation of high-mannose-type oligosaccharides in GlcNAc transferase I-deficient (Lec1) CHO cells
    • A.I. Lin, G.A. Philipsberg, R.S. Haltiwanger, Core fucosylation of high-mannose-type oligosaccharides in GlcNAc transferase I-deficient (Lec1) CHO cells, Glycobiology 4 (1994) 895-901.
    • (1994) Glycobiology , vol.4 , pp. 895-901
    • Lin, A.I.1    Philipsberg, G.A.2    Haltiwanger, R.S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.