메뉴 건너뛰기




Volumn 50, Issue 1, 1996, Pages 73-90

A modeling framework for the study of protein glycosylation

Author keywords

glycosylation site occupancy; modeling; N linked glycoproteins; oligosaccharyltransferase

Indexed keywords

CELL CULTURE; GROWTH KINETICS; MATHEMATICAL MODELS; SYNTHESIS (CHEMICAL);

EID: 0030570080     PISSN: 00063592     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0290(19960405)50:1<73::AID-BIT9>3.0.CO;2-Z     Document Type: Article
Times cited : (47)

References (45)
  • 1
    • 0019579733 scopus 로고
    • The role of the hydroxy amino acid in the triplet sequence Asn-Xaa-Thr(Ser) for the N-glycosylation step during glycoprotein biosynthesis
    • Bause, E., Legler, G. 1981. The role of the hydroxy amino acid in the triplet sequence Asn-Xaa-Thr(Ser) for the N-glycosylation step during glycoprotein biosynthesis. Biochem. J. 195: 639-644.
    • (1981) Biochem. J. , vol.195 , pp. 639-644
    • Bause, E.1    Legler, G.2
  • 2
    • 0018181456 scopus 로고
    • Temporal relationship of translation and glycosylation of immunoglobulin heavy and light chains
    • Bergman, L. W., Kuehl, W. M. 1978. Temporal relationship of translation and glycosylation of immunoglobulin heavy and light chains. Biochemistry 17: 5174-5180.
    • (1978) Biochemistry , vol.17 , pp. 5174-5180
    • Bergman, L.W.1    Kuehl, W.M.2
  • 3
    • 0018613233 scopus 로고
    • A kinetic model of protein synthesis: Application to hemoglobin synthesis and translational control
    • Bergmann, J. E., Lodish, H. F. 1979. A kinetic model of protein synthesis: application to hemoglobin synthesis and translational control. J. Biol. Chem. 254: 11927-11937.
    • (1979) J. Biol. Chem. , vol.254 , pp. 11927-11937
    • Bergmann, J.E.1    Lodish, H.F.2
  • 4
    • 0026688551 scopus 로고
    • Cell-free synthesis of enzymatically active tissue-type plasminogen activator: Protein folding determines the extent of N-linked glycosylation
    • Bulleid, N. J., Bassel-Duby, R. S., Freedman, R. B., et al. 1992. Cell-free synthesis of enzymatically active tissue-type plasminogen activator: protein folding determines the extent of N-linked glycosylation. Biochem. J. 286: 275-280.
    • (1992) Biochem. J. , vol.286 , pp. 275-280
    • Bulleid, N.J.1    Bassel-Duby, R.S.2    Freedman, R.B.3
  • 5
    • 0027203025 scopus 로고
    • Effect of cell attachment and growth on the synthesis and fate of dolichol-linked oligosaccharides in Chinese hamster ovary cells
    • Cacan, R., Labiau, O., Mir, A., et al. 1993. Effect of cell attachment and growth on the synthesis and fate of dolichol-linked oligosaccharides in Chinese hamster ovary cells. Eur. J. Biochem. 215: 873-881.
    • (1993) Eur. J. Biochem. , vol.215 , pp. 873-881
    • Cacan, R.1    Labiau, O.2    Mir, A.3
  • 6
    • 0023790731 scopus 로고
    • Effect of phospholipids on thyroid oligosaccharyltransferase activity and orientation: Evaluation of structural determinants for stimulation of N-glycosylation
    • Chalifour, R. J., Spiro, R. G. 1988. Effect of phospholipids on thyroid oligosaccharyltransferase activity and orientation: evaluation of structural determinants for stimulation of N-glycosylation. J. Biol. Chem. 263: 15673-15680.
    • (1988) J. Biol. Chem. , vol.263 , pp. 15673-15680
    • Chalifour, R.J.1    Spiro, R.G.2
  • 7
    • 0023861015 scopus 로고
    • Effects of glucose starvation and puromycin treatment on lipid-linked oligosaccharide precursors and biosynthetic enzymes in Chinese Hamster Ovary cells in vivo and in vitro
    • Chapman, A. E, Calhoun IV, J. C. 1988. Effects of glucose starvation and puromycin treatment on lipid-linked oligosaccharide precursors and biosynthetic enzymes in Chinese Hamster Ovary cells in vivo and in vitro. Arch. Biochem. Biophys. 260: 320-333.
    • (1988) Arch. Biochem. Biophys. , vol.260 , pp. 320-333
    • Chapman, A.E.1    Calhoun IV, J.C.2
  • 8
    • 0026536874 scopus 로고
    • Pause transfer a topogenic sequence in apolipoprotein B mediates stopping and restarting of transtocation
    • Chuck, S. L., Lingappa, V. R. 1992. Pause transfer a topogenic sequence in apolipoprotein B mediates stopping and restarting of transtocation. Cell 68: 9-21.
    • (1992) Cell , vol.68 , pp. 9-21
    • Chuck, S.L.1    Lingappa, V.R.2
  • 9
    • 0025981417 scopus 로고
    • Glycosylation of recombinant protein therapeutics: Control and functional implications
    • Cumming, D. A. 1991. Glycosylation of recombinant protein therapeutics: control and functional implications. Glycobiology 1: 115-130.
    • (1991) Glycobiology , vol.1 , pp. 115-130
    • Cumming, D.A.1
  • 10
    • 0025367812 scopus 로고
    • Sequence differences between glycosylated and non-glycosylated Asn-X-Thr/Ser acceptor sites: Implications for protein engineering
    • Gavel, Y., von Heijne, G. 1990. Sequence differences between glycosylated and non-glycosylated Asn-X-Thr/Ser acceptor sites: implications for protein engineering. Protein Eng. 3: 433-442.
    • (1990) Protein Eng. , vol.3 , pp. 433-442
    • Gavel, Y.1    Von Heijne, G.2
  • 11
    • 0000623424 scopus 로고
    • The oligosaccharides of glycoproteins: Factors affecting their synthesis and their influence on glycoprotein properties
    • P. Todd, S. K. Sikdar, and M. Bier (eds.), American Chemical Society, Washington, DC
    • Goochee, C. F., Gramer, M. J., Andersen, D. C., et al. 1992. The oligosaccharides of glycoproteins: factors affecting their synthesis and their influence on glycoprotein properties, pp. 199-240. In: P. Todd, S. K. Sikdar, and M. Bier (eds.), Frontiers in bioprocessing II. American Chemical Society, Washington, DC.
    • (1992) Frontiers in Bioprocessing II , pp. 199-240
    • Goochee, C.F.1    Gramer, M.J.2    Andersen, D.C.3
  • 12
    • 0021104696 scopus 로고
    • Relationship between oligosaccharide-lipid synthesis and protein synthesis in mouse LM cells
    • Grant, S. R., Lennarz, W. J. 1983. Relationship between oligosaccharide-lipid synthesis and protein synthesis in mouse LM cells. Eur. J. Biochem. 134: 575-583.
    • (1983) Eur. J. Biochem. , vol.134 , pp. 575-583
    • Grant, S.R.1    Lennarz, W.J.2
  • 13
    • 0027112084 scopus 로고
    • Glucose-limited chemostat culture of Chinese Hamster Ovary cells producing recombinant human interferon-γ
    • Hayter, P. M., Curling, E. M. A., Baines, A. J., et al. 1992. Glucose-limited chemostat culture of Chinese Hamster Ovary cells producing recombinant human interferon-γ. Biotechnol. Bioeng. 39: 327-335.
    • (1992) Biotechnol. Bioeng. , vol.39 , pp. 327-335
    • Hayter, P.M.1    Curling, E.M.A.2    Baines, A.J.3
  • 14
    • 0019296388 scopus 로고
    • Synthesis of the N-linked oligosaccharides of glycoproteins: Assembly of the lipid-linked precursor oligosaccharide and its relation to protein synthesis in-vivo
    • Hubbard, S. C. 1980. Synthesis of the N-linked oligosaccharides of glycoproteins: assembly of the lipid-linked precursor oligosaccharide and its relation to protein synthesis in-vivo. J. Biol. Chem. 255: 11782-11793.
    • (1980) J. Biol. Chem. , vol.255 , pp. 11782-11793
    • Hubbard, S.C.1
  • 15
    • 0025787462 scopus 로고
    • Differences between Asn-Xaa-Thr-containing peptides: A comparison of solution conformation and substrate behavior with oligosaccharyltransferase
    • Imperiali, B., Shannon, K. L. 1991. Differences between Asn-Xaa-Thr-containing peptides: a comparison of solution conformation and substrate behavior with oligosaccharyltransferase. Biochemistry 30: 4374-4380.
    • (1991) Biochemistry , vol.30 , pp. 4374-4380
    • Imperiali, B.1    Shannon, K.L.2
  • 16
    • 0001523706 scopus 로고
    • A mechanistic proposal for asparagine-linked glycosylation
    • Imperiali, B., Shannon, K. L., Unno, M., et al. 1992. A mechanistic proposal for asparagine-linked glycosylation. J. Am. Chem. Soc. 114: 7945-7946.
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 7945-7946
    • Imperiali, B.1    Shannon, K.L.2    Unno, M.3
  • 17
    • 0028224656 scopus 로고
    • Glycosylation of recombinant proteins: Problems and prospects
    • Jenkins, N., Curling, E. M. A. 1994. Glycosylation of recombinant proteins: problems and prospects. Enzyme Microb. Technol. 16: 354-364.
    • (1994) Enzyme Microb. Technol. , vol.16 , pp. 354-364
    • Jenkins, N.1    Curling, E.M.A.2
  • 18
    • 0027749370 scopus 로고
    • Formation of a molten globule intermediate early in the kinetic pathway of apomyoglobin
    • Jennings, P. A., Wright, P. E. 1993. Formation of a molten globule intermediate early in the kinetic pathway of apomyoglobin. Science 262: 892-896.
    • (1993) Science , vol.262 , pp. 892-896
    • Jennings, P.A.1    Wright, P.E.2
  • 19
    • 0026716017 scopus 로고
    • Oligosaccharyltransferase activity is associated with a protein complex composed of ribophorins I and II and a 48 kD protein
    • Kelleher, D. J., Kreibich, G., Gilmore, R. 1992. Oligosaccharyltransferase activity is associated with a protein complex composed of ribophorins I and II and a 48 kD protein. Cell 69: 55-65.
    • (1992) Cell , vol.69 , pp. 55-65
    • Kelleher, D.J.1    Kreibich, G.2    Gilmore, R.3
  • 20
    • 0028361344 scopus 로고
    • Regulation of N-glycosylation: Long term effect of cyclic AMP mediates enhanced synthesis of the dolichol pyrophosphate core oligosaccharide
    • Konrad, M., Merz, W. E. 1994. Regulation of N-glycosylation: long term effect of cyclic AMP mediates enhanced synthesis of the dolichol pyrophosphate core oligosaccharide. J. Biol. Chem. 269: 8659-8666.
    • (1994) J. Biol. Chem. , vol.269 , pp. 8659-8666
    • Konrad, M.1    Merz, W.E.2
  • 21
    • 0021013021 scopus 로고
    • Substrate recognition by oligosaccharyl transferase: Inhibition of cotranslational glycosylation by acceptor peptides
    • Lau, J. T. Y., Welply, J. K., Shenbagamurthi, P., et al. 1983. Substrate recognition by oligosaccharyl transferase: inhibition of cotranslational glycosylation by acceptor peptides. J. Biol. Chem. 258: 15255-15260.
    • (1983) J. Biol. Chem. , vol.258 , pp. 15255-15260
    • Lau, J.T.Y.1    Welply, J.K.2    Shenbagamurthi, P.3
  • 22
    • 0014245158 scopus 로고
    • Kinetics of biopolymerization on nucleic acid templates
    • MacDonald, C. T., Gibbs, J. H., Pipkin, A. C. 1968. Kinetics of biopolymerization on nucleic acid templates. Biopolymers 6: 1-25.
    • (1968) Biopolymers , vol.6 , pp. 1-25
    • MacDonald, C.T.1    Gibbs, J.H.2    Pipkin, A.C.3
  • 23
    • 13344291923 scopus 로고
    • The binomial probability distribution
    • Dellen Publishing Co., San Francisco, CA
    • Mendenhall, W., Sincich, T. 1992. The binomial probability distribution, pp. 124-131. In: Statistics for engineering and the sciences. Dellen Publishing Co., San Francisco, CA.
    • (1992) Statistics for Engineering and the Sciences , pp. 124-131
    • Mendenhall, W.1    Sincich, T.2
  • 24
    • 0027417476 scopus 로고
    • Determination of the distance between the oligosaccharyltransferase active site and the endoplasmic reticulum membrane
    • Nilsson, I., von Heijne, G. 1993. Determination of the distance between the oligosaccharyltransferase active site and the endoplasmic reticulum membrane. J. Biol. Chem. 268: 5798-5801.
    • (1993) J. Biol. Chem. , vol.268 , pp. 5798-5801
    • Nilsson, I.1    Von Heijne, G.2
  • 25
    • 0022001849 scopus 로고
    • Decreased transfer of oligosaccharide from oligosaccharide-lipid to protein acceptors in regenerating rat liver
    • Oda-Tamai, S., Kato, S., Hara, S., et al. 1985. Decreased transfer of oligosaccharide from oligosaccharide-lipid to protein acceptors in regenerating rat liver. J. Biol. Chem. 260: 57-63.
    • (1985) J. Biol. Chem. , vol.260 , pp. 57-63
    • Oda-Tamai, S.1    Kato, S.2    Hara, S.3
  • 26
    • 0026644816 scopus 로고
    • Bidirectional movement of a nascent polypeptide across microsomal membranes reveals requirements for vectorial translocation of proteins
    • Ooi, C. E., Weiss, J. 1992. Bidirectional movement of a nascent polypeptide across microsomal membranes reveals requirements for vectorial translocation of proteins. Cell 71: 87-96.
    • (1992) Cell , vol.71 , pp. 87-96
    • Ooi, C.E.1    Weiss, J.2
  • 27
    • 0025055357 scopus 로고
    • Different pathways of secretion for glycosylated and nonglycosylated human prolactin
    • Pellegrini, I., Gunz, G., Grisoli, F., et al. 1990. Different pathways of secretion for glycosylated and nonglycosylated human prolactin. Endocrinology 126: 1087-1095.
    • (1990) Endocrinology , vol.126 , pp. 1087-1095
    • Pellegrini, I.1    Gunz, G.2    Grisoli, F.3
  • 28
    • 0017594823 scopus 로고
    • Enzymatic conversion of proteins to glycoproteins
    • Pless, D. D., Lennarz, W. J. 1977. Enzymatic conversion of proteins to glycoproteins. Proc. Natl. Acad. Sci. USA 74: 134-138.
    • (1977) Proc. Natl. Acad. Sci. USA , vol.74 , pp. 134-138
    • Pless, D.D.1    Lennarz, W.J.2
  • 29
    • 0024672126 scopus 로고
    • Structural requirements for protein N-glycosylation: Influence of acceptor peptides on cotranslational glycosylation of yeast invertase and site-directed mutagenesis around a sequon sequence
    • Roitsch, T., Lehle, L. 1989. Structural requirements for protein N-glycosylation: influence of acceptor peptides on cotranslational glycosylation of yeast invertase and site-directed mutagenesis around a sequon sequence. Eur. J. Biochem. 181: 525-529.
    • (1989) Eur. J. Biochem. , vol.181 , pp. 525-529
    • Roitsch, T.1    Lehle, L.2
  • 30
    • 0024456399 scopus 로고
    • Polypeptide chain binding proteins: Catalysts of protein folding and related processes in cells
    • Rothman, J. E. 1989. Polypeptide chain binding proteins: catalysts of protein folding and related processes in cells. Cell 59: 591-601.
    • (1989) Cell , vol.59 , pp. 591-601
    • Rothman, J.E.1
  • 31
    • 0017753965 scopus 로고
    • Synchronised transmembrane insertion and glycosylation of a nascent membrane protein
    • Rothman, J. E., Lodish, H. F. 1977. Synchronised transmembrane insertion and glycosylation of a nascent membrane protein. Nature 269: 775-780.
    • (1977) Nature , vol.269 , pp. 775-780
    • Rothman, J.E.1    Lodish, H.F.2
  • 32
    • 0018610487 scopus 로고
    • Inhibition of protein synthesis also inhibits synthesis of lipid-linked oligosaccharides
    • Schmitt, J. W., Elbein, A. D. 1979. Inhibition of protein synthesis also inhibits synthesis of lipid-linked oligosaccharides. J. Biol. Chem. 254: 12291-12294.
    • (1979) J. Biol. Chem. , vol.254 , pp. 12291-12294
    • Schmitt, J.W.1    Elbein, A.D.2
  • 33
    • 0027383275 scopus 로고
    • Efficiency of N-linked core glycosylation at asparagine-319 of rabies virus glycoprotein is altered by deletions C-terminal to the glycosylation sequon
    • Shakin-Eshleman, S. H., Wunner, W. H., Spitalnik, S. L. 1993. Efficiency of N-linked core glycosylation at asparagine-319 of rabies virus glycoprotein is altered by deletions C-terminal to the glycosylation sequon. Biochemistry 32: 9465-9472.
    • (1993) Biochemistry , vol.32 , pp. 9465-9472
    • Shakin-Eshleman, S.H.1    Wunner, W.H.2    Spitalnik, S.L.3
  • 34
    • 0019570379 scopus 로고
    • N-glycosylation of yeast proteins: Characterization of the solubilized oligosaccharyl transferase
    • Sharma, C. B., Lehle, L., Tanner, W. 1981. N-glycosylation of yeast proteins: characterization of the solubilized oligosaccharyl transferase. Eur. J. Biochem. 116: 101-108.
    • (1981) Eur. J. Biochem. , vol.116 , pp. 101-108
    • Sharma, C.B.1    Lehle, L.2    Tanner, W.3
  • 35
    • 0028707616 scopus 로고
    • The effect of protein synthesis inhibitors on the glycosylation site occupancy of recombinant human prolactin
    • Shelikoff, M., Sinskey, A. J., Stephanopoulos, G. 1994. The effect of protein synthesis inhibitors on the glycosylation site occupancy of recombinant human prolactin. Cytotechnology 15: 195-208.
    • (1994) Cytotechnology , vol.15 , pp. 195-208
    • Shelikoff, M.1    Sinskey, A.J.2    Stephanopoulos, G.3
  • 37
    • 0023112116 scopus 로고
    • Intramolecular disulfide loop formation in a peptide containing two cysteines
    • Snyder, G. H. 1987. Intramolecular disulfide loop formation in a peptide containing two cysteines. Biochemistry 26: 688-694.
    • (1987) Biochemistry , vol.26 , pp. 688-694
    • Snyder, G.H.1
  • 38
    • 0003086056 scopus 로고
    • Regulation of elongation rate
    • H. Trachsel (ed.), CRC Press, Boca Raton, FL
    • Spirin, A. S., Ryazanov, A. G. 1991. Regulation of elongation rate, pp. 325-350. In: H. Trachsel (ed.), Translation in eukaryotes. CRC Press, Boca Raton, FL.
    • (1991) Translation in Eukaryotes , pp. 325-350
    • Spirin, A.S.1    Ryazanov, A.G.2
  • 39
    • 0022853029 scopus 로고
    • Control of N-linked carbohydrate unit synthesis in thyroid endoplasmic reticulum by membrane organization and dolichol phosphate availability
    • Spiro, M. J., Spiro, R. G. 1986. Control of N-linked carbohydrate unit synthesis in thyroid endoplasmic reticulum by membrane organization and dolichol phosphate availability. J. Biol. Chem. 261: 14725-14732.
    • (1986) J. Biol. Chem. , vol.261 , pp. 14725-14732
    • Spiro, M.J.1    Spiro, R.G.2
  • 40
    • 0025762343 scopus 로고
    • Potential regutation of N-glycosylation precursor through oligosaccharide-lipid hydrolase action and glucosyltransferase-glucosidase shuttle
    • Spiro, M. J., Spiro, R. G. 1991. Potential regutation of N-glycosylation precursor through oligosaccharide-lipid hydrolase action and glucosyltransferase-glucosidase shuttle. J. Biol. Chem. 266: 5311-5317.
    • (1991) J. Biol. Chem. , vol.266 , pp. 5311-5317
    • Spiro, M.J.1    Spiro, R.G.2
  • 41
    • 0004155427 scopus 로고
    • W. H. Freeman and Co., New York
    • Stryer, L. 1988. Biochemistry. W. H. Freeman and Co., New York.
    • (1988) Biochemistry
    • Stryer, L.1
  • 42
    • 0027510252 scopus 로고
    • Yeast Wbp1p and Swp1p from a protein complex essential for oligosaccharyl transferase activity
    • te Heesen, S., Knauer, R., Lehle, L., et al 1993. Yeast Wbp1p and Swp1p from a protein complex essential for oligosaccharyl transferase activity. EMBO J. 12: 279-284.
    • (1993) EMBO J. , vol.12 , pp. 279-284
    • Te Heesen, S.1    Knauer, R.2    Lehle, L.3
  • 44
    • 13344265604 scopus 로고
    • Complex kinetics and cooperativity
    • Wiley, New York
    • Wharton, C. W., Eisenthal, R. 1981. Complex kinetics and cooperativity, pp. 169-203. In: Molecular enzymology. Wiley, New York.
    • (1981) Molecular Enzymology , pp. 169-203
    • Wharton, C.W.1    Eisenthal, R.2
  • 45
    • 0024817509 scopus 로고
    • Signal recognition particle mediates a transient elongation arrest of preprolactin in reticulocyte lysate
    • Wolin, S. L., Walter, P. 1989. Signal recognition particle mediates a transient elongation arrest of preprolactin in reticulocyte lysate. J. Cell Biol. 109: 2617-2622.
    • (1989) J. Cell Biol. , vol.109 , pp. 2617-2622
    • Wolin, S.L.1    Walter, P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.