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Volumn 110, Issue 5, 1997, Pages 557-567

A mutation in a highly conserved region in brush-border sucrase-isomaltase and lysosomal α-glucosidase results in Golgi retention

Author keywords

ERGIC; Intestine; Quality control; SI deficiency; Trafficking

Indexed keywords

ALPHA GLUCOSIDASE; LYSOSOME ENZYME; OLIGO 1,6 GLUCOSIDASE; SUCRASE;

EID: 0031003841     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (31)

References (50)
  • 1
    • 0025913946 scopus 로고
    • A single amino acid change in the cytoplasmic domain alters the polarized delivery of influenza virus hemagglutinin
    • Brewer, C. B. and Roth, M. G. (1991). A single amino acid change in the cytoplasmic domain alters the polarized delivery of influenza virus hemagglutinin. J. Cell Biol. 114, 413-421.
    • (1991) J. Cell Biol. , vol.114 , pp. 413-421
    • Brewer, C.B.1    Roth, M.G.2
  • 3
    • 0014235959 scopus 로고
    • Assay of intestinal disaccharidases
    • Dahlqvist, A. (1968). Assay of intestinal disaccharidases. Anal. Biochem. 22, 99-107.
    • (1968) Anal. Biochem. , vol.22 , pp. 99-107
    • Dahlqvist, A.1
  • 4
    • 0027157736 scopus 로고
    • Folding and assembly of viral membrane proteins
    • Doms, R. W., Lamb, R. A., Rose, J. K. and Helenius, A. (1993). Folding and assembly of viral membrane proteins. Virology 193, 545-562.
    • (1993) Virology , vol.193 , pp. 545-562
    • Doms, R.W.1    Lamb, R.A.2    Rose, J.K.3    Helenius, A.4
  • 5
    • 0022255353 scopus 로고
    • Immuno-electronmicroscopical localization of a microvillus membrane disaccharidase in the human small-intestinal epithelium with monoclonal antibodies
    • Fransen, J. A., Ginsel, L. A., Hauri, H. P., Sterchi, E. and Blok, J. (1985). Immuno-electronmicroscopical localization of a microvillus membrane disaccharidase in the human small-intestinal epithelium with monoclonal antibodies. Eur. J. Cell Biol. 38, 6-15.
    • (1985) Eur. J. Cell Biol. , vol.38 , pp. 6-15
    • Fransen, J.A.1    Ginsel, L.A.2    Hauri, H.P.3    Sterchi, E.4    Blok, J.5
  • 6
    • 0026042569 scopus 로고
    • Naturally occurring mutations in intestinal sucrase-isomaltase provide evidence for the existence of an intracellular sorting signal in the isomaltase subunit
    • published erratum appears in J. Cell Biol. 115 (5), following 1473
    • Fransen, J. A., Hauri, H. P., Ginsel, L. A. and Naim, H. Y. (1991). Naturally occurring mutations in intestinal sucrase-isomaltase provide evidence for the existence of an intracellular sorting signal in the isomaltase subunit [published erratum appears in J. Cell Biol. 115 (5), following 1473]. J. Cell Biol. 115, 45-57.
    • (1991) J. Cell Biol. , vol.115 , pp. 45-57
    • Fransen, J.A.1    Hauri, H.P.2    Ginsel, L.A.3    Naim, H.Y.4
  • 7
    • 0024603788 scopus 로고
    • Role of protein disulphide-isomerase in the expression of native proteins
    • Freedman, R. B., Bulleid, N. J., Hawkins, H. C. and Paver, J. L. (1989). Role of protein disulphide-isomerase in the expression of native proteins. Biochem. Soc. Symp. 55, 167-192.
    • (1989) Biochem. Soc. Symp. , vol.55 , pp. 167-192
    • Freedman, R.B.1    Bulleid, N.J.2    Hawkins, H.C.3    Paver, J.L.4
  • 8
    • 0024838247 scopus 로고
    • Protein folding and intracellular transport: Evaluation of conformational changes in nascent exocytotic proteins
    • Gething, M. J., McCammon, K. and Sambrook, J. (1989). Protein folding and intracellular transport: evaluation of conformational changes in nascent exocytotic proteins. Meth. Cell Biol. 32, 185-206.
    • (1989) Meth. Cell Biol. , vol.32 , pp. 185-206
    • Gething, M.J.1    McCammon, K.2    Sambrook, J.3
  • 9
    • 0026584271 scopus 로고
    • Protein folding in the cell
    • Gething, M. J. and Sambrook, J. (1992). Protein folding in the cell. Nature 355, 33-45.
    • (1992) Nature , vol.355 , pp. 33-45
    • Gething, M.J.1    Sambrook, J.2
  • 10
    • 0024283936 scopus 로고
    • A versatile in vivo eukaryotic expression vector for protein engineering
    • Green, S., Isseman, I. and Sheer, E. (1988). A versatile in vivo eukaryotic expression vector for protein engineering. Nucl. Acids Res. 16, 369.
    • (1988) Nucl. Acids Res. , vol.16 , pp. 369
    • Green, S.1    Isseman, I.2    Sheer, E.3
  • 11
    • 0021078994 scopus 로고
    • Plasmid-encoded hygromycin B resistance: The sequence of hygromycin B phosphotransferase gene and its expression in Escherichia coli and Saccharomyces cerevisiae
    • Gritz, L. and Davies, J. (1983). Plasmid-encoded hygromycin B resistance: the sequence of hygromycin B phosphotransferase gene and its expression in Escherichia coli and Saccharomyces cerevisiae. Gene 25, 179-188.
    • (1983) Gene , vol.25 , pp. 179-188
    • Gritz, L.1    Davies, J.2
  • 12
    • 0028103695 scopus 로고
    • Role of N-linked oligosaccharide recognition, glucose trimming, and calnexin in glycoprotein folding and quality control
    • Hammond, C., Braakman, I. and Helenius, A. (1994). Role of N-linked oligosaccharide recognition, glucose trimming, and calnexin in glycoprotein folding and quality control. Proc. Nat. Acad. Sci. USA 91, 913-917.
    • (1994) Proc. Nat. Acad. Sci. USA , vol.91 , pp. 913-917
    • Hammond, C.1    Braakman, I.2    Helenius, A.3
  • 13
    • 0028339518 scopus 로고
    • Quality control in the secretory pathway: Retention of a misfolded viral membrane glycoprotein involves cycling between the ER, intermediate compartment, and Golgi apparatus
    • Hammond, C. and Helenius, A. (1994). Quality control in the secretory pathway: retention of a misfolded viral membrane glycoprotein involves cycling between the ER, intermediate compartment, and Golgi apparatus. J. Cell Biol. 126, 41-52.
    • (1994) J. Cell Biol. , vol.126 , pp. 41-52
    • Hammond, C.1    Helenius, A.2
  • 14
    • 0022181709 scopus 로고
    • Expression and intracellular transport of microvillus membrane hydrolases in human intestinal epithelial cells
    • Hauri, H. P., Sterchi, E. E., Bienz, D., Fransen, J. A. and Marxer, A. (1985). Expression and intracellular transport of microvillus membrane hydrolases in human intestinal epithelial cells. J. Cell Biol. 101, 838-851.
    • (1985) J. Cell Biol. , vol.101 , pp. 838-851
    • Hauri, H.P.1    Sterchi, E.E.2    Bienz, D.3    Fransen, J.A.4    Marxer, A.5
  • 15
    • 0026063240 scopus 로고
    • A 58-kDa resident protein of the cis Golgi cisterna is not terminally glycosylated
    • Hendricks, L. C., Gabel, C. A., Suh, K. and Farquhar, M. G. (1991). A 58-kDa resident protein of the cis Golgi cisterna is not terminally glycosylated. J. Biol. Chem. 266, 17559-17565.
    • (1991) J. Biol. Chem. , vol.266 , pp. 17559-17565
    • Hendricks, L.C.1    Gabel, C.A.2    Suh, K.3    Farquhar, M.G.4
  • 17
    • 0024026526 scopus 로고
    • Primary structure and processing of lysosomal alpha-glucosidase; homology with the intestinal sucrase-isomaltase complex
    • Hoefsloot, L. H., Hoogeveen Westerveld, M., Kroos, M. A., van Beeumen, J., Reuser, A. J. and Oostra, B. A. (1988). Primary structure and processing of lysosomal alpha-glucosidase; homology with the intestinal sucrase-isomaltase complex. EMBO J. 7, 1697-1704.
    • (1988) EMBO J. , vol.7 , pp. 1697-1704
    • Hoefsloot, L.H.1    Hoogeveen Westerveld, M.2    Kroos, M.A.3    Van Beeumen, J.4    Reuser, A.J.5    Oostra, B.A.6
  • 19
    • 0027580922 scopus 로고
    • Protein trafficking along the exocytic pathway
    • Hong, W. and Tang, B. L. (1993). Protein trafficking along the exocytic pathway. BioEssays 15, 231-238.
    • (1993) BioEssays , vol.15 , pp. 231-238
    • Hong, W.1    Tang, B.L.2
  • 20
    • 0024461745 scopus 로고
    • Protein oligomerization in the endoplasmic reticulum
    • Hurtley, S. M. and Helenius, A. (1989). Protein oligomerization in the endoplasmic reticulum. Annu. Rev. Cell Biol. 5, 277-307.
    • (1989) Annu. Rev. Cell Biol. , vol.5 , pp. 277-307
    • Hurtley, S.M.1    Helenius, A.2
  • 21
    • 0025853058 scopus 로고
    • Oligomerization and intracellular protein transport: Dimerization of intestinal dipeptidylpeptidase IV occurs in the Golgi apparatus
    • Jascur, T., Matter, K. and Hauri, H. P. (1991). Oligomerization and intracellular protein transport: dimerization of intestinal dipeptidylpeptidase IV occurs in the Golgi apparatus. Biochemistry 30, 1908-1915.
    • (1991) Biochemistry , vol.30 , pp. 1908-1915
    • Jascur, T.1    Matter, K.2    Hauri, H.P.3
  • 22
    • 0025877148 scopus 로고
    • Intracellular localization and endocytosis of brush border enzymes in the enterocyte-like cell line Caco-2
    • Klumperman, J., Boekestijn, J. C., Mulder, A. M., Fransen, J. A. and Ginsel, L. A. (1991). Intracellular localization and endocytosis of brush border enzymes in the enterocyte-like cell line Caco-2. Eur. J. Cell Biol. 54, 76-84.
    • (1991) Eur. J. Cell Biol. , vol.54 , pp. 76-84
    • Klumperman, J.1    Boekestijn, J.C.2    Mulder, A.M.3    Fransen, J.A.4    Ginsel, L.A.5
  • 23
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970). Cleavage of structural proteins during assembly of the head of bacteriophage T4. Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 24
    • 0024276904 scopus 로고
    • A single amino acid change in the cytoplasmic domain allows the influenza virus hemagglutinin to be endocytosed through coated pits
    • Lazarovits, J. and Roth, M. (1988). A single amino acid change in the cytoplasmic domain allows the influenza virus hemagglutinin to be endocytosed through coated pits. Cell 53, 743-752.
    • (1988) Cell , vol.53 , pp. 743-752
    • Lazarovits, J.1    Roth, M.2
  • 25
    • 0030034568 scopus 로고    scopus 로고
    • Oligomerization supports transport of a mutant secretory protein out of the endoplasmic reticulum
    • Lösch, A. K., Henkel, K., Wagner, M., Urban, J. and Koch-Brandt, C. (1996). Oligomerization supports transport of a mutant secretory protein out of the endoplasmic reticulum. Eur. J. Cell Biol. 69, 107-115.
    • (1996) Eur. J. Cell Biol. , vol.69 , pp. 107-115
    • Lösch, A.K.1    Henkel, K.2    Wagner, M.3    Urban, J.4    Koch-Brandt, C.5
  • 26
    • 0025805273 scopus 로고
    • Intracellular transport and conformational maturation of intestinal brush border hydrolases
    • Matter, K. and Hauri, H. P. (1991). Intracellular transport and conformational maturation of intestinal brush border hydrolases. Biochemistry 30, 1916-1923.
    • (1991) Biochemistry , vol.30 , pp. 1916-1923
    • Matter, K.1    Hauri, H.P.2
  • 27
    • 0023088808 scopus 로고
    • Biosynthesis and maturation of lactase-phlorizin hydrolase in the human small intestinal epithelial cells
    • Naim, H. Y., Sterchi, E. E. and Lentze, M. J. (1987). Biosynthesis and maturation of lactase-phlorizin hydrolase in the human small intestinal epithelial cells. Biochem. J. 241, 427-434.
    • (1987) Biochem. J. , vol.241 , pp. 427-434
    • Naim, H.Y.1    Sterchi, E.E.2    Lentze, M.J.3
  • 28
    • 0023783489 scopus 로고
    • Sucrase-isomaltase deficiency in humans. Different mutations disrupt intracellular transport, processing, and function of an intestinal brush border enzyme
    • Naim, H. Y., Roth, J., Sterchi, E. E., Lentze, M., Milla, P., Schmitz, J. and Hauri, H. P. (1988a). Sucrase-isomaltase deficiency in humans. Different mutations disrupt intracellular transport, processing, and function of an intestinal brush border enzyme. J. Clin. Invest. 82, 667-679.
    • (1988) J. Clin. Invest. , vol.82 , pp. 667-679
    • Naim, H.Y.1    Roth, J.2    Sterchi, E.E.3    Lentze, M.4    Milla, P.5    Schmitz, J.6    Hauri, H.P.7
  • 29
    • 0023923020 scopus 로고
    • Biosynthesis of the human sucrase-isomaltase complex. Differential O-glycosylation of the sucrase subunit correlates with its position within the enzyme complex
    • Naim, H. Y., Sterchi, E. E. and Lentze, M. J. (1988b). Biosynthesis of the human sucrase-isomaltase complex. Differential O-glycosylation of the sucrase subunit correlates with its position within the enzyme complex. J. Biol. Chem. 263, 7242-7253.
    • (1988) J. Biol. Chem. , vol.263 , pp. 7242-7253
    • Naim, H.Y.1    Sterchi, E.E.2    Lentze, M.J.3
  • 30
    • 0024268345 scopus 로고
    • Structure, biosynthesis, and glycosylation of human small intestinal maltase-glucoamylase
    • Naim, H. Y., Sterchi, E. E. and Lentze, M. J. (1988c). Structure, biosynthesis, and glycosylation of human small intestinal maltase-glucoamylase. J. Biol. Chem. 263, 19709-19717.
    • (1988) J. Biol. Chem. , vol.263 , pp. 19709-19717
    • Naim, H.Y.1    Sterchi, E.E.2    Lentze, M.J.3
  • 31
    • 0025823166 scopus 로고
    • Expression of a full-length cDNa coding for human intestinal lactase-phlorizin hydrolase reveals an uncleaved, enzymatically active, and transport-competent protein
    • Naim, H. Y., Lacey, S. W., Sambrook, J. F. and Gething, M. J. (1991a). Expression of a full-length cDNA coding for human intestinal lactase-phlorizin hydrolase reveals an uncleaved, enzymatically active, and transport-competent protein. J. Biol. Chem. 266, 12313-12320.
    • (1991) J. Biol. Chem. , vol.266 , pp. 12313-12320
    • Naim, H.Y.1    Lacey, S.W.2    Sambrook, J.F.3    Gething, M.J.4
  • 32
    • 0026041607 scopus 로고
    • Striking structural and functional similarities suggest that intestinal sucrase-isomaltase, human lysosomal alpha-glucosidase and Schwanniomyces occidentalis glucoamylase are derived from a common ancestral gene
    • Naim, H. Y., Niermann, T., Kleinhans, U., Hollenberg, C. P. and Strasser, A. W. (1991b). Striking structural and functional similarities suggest that intestinal sucrase-isomaltase, human lysosomal alpha-glucosidase and Schwanniomyces occidentalis glucoamylase are derived from a common ancestral gene. FEBS Lett. 294, 109-112.
    • (1991) FEBS Lett. , vol.294 , pp. 109-112
    • Naim, H.Y.1    Niermann, T.2    Kleinhans, U.3    Hollenberg, C.P.4    Strasser, A.W.5
  • 33
    • 0026491215 scopus 로고
    • Impact of O-glycosylation on the function of human intestinal lactase-phlorizin hydrolase. Characterization of glycoforms varying in enzyme activity and localization of O-glycoside addition
    • Naim, H. Y. and Lentze, M. J. (1992). Impact of O-glycosylation on the function of human intestinal lactase-phlorizin hydrolase. Characterization of glycoforms varying in enzyme activity and localization of O-glycoside addition. J. Biol. Chem. 267, 25494-25504.
    • (1992) J. Biol. Chem. , vol.267 , pp. 25494-25504
    • Naim, H.Y.1    Lentze, M.J.2
  • 34
    • 0028148546 scopus 로고
    • The pro region of human intestinal lactase-phlorizin hydrolase
    • Naim, H. Y., Jacob, R., Naim, H., Sambrook, J. F. and Gething, M. J. (1994). The pro region of human intestinal lactase-phlorizin hydrolase. J. Biol. Chem. 269, 26933-26943.
    • (1994) J. Biol. Chem. , vol.269 , pp. 26933-26943
    • Naim, H.Y.1    Jacob, R.2    Naim, H.3    Sambrook, J.F.4    Gething, M.J.5
  • 35
    • 0027497114 scopus 로고
    • The pro sequence of lactase-phlorizin hydrolase is required for the enzyme to reach the plasma membrane. An intramolecular chaperone?
    • Oberholzer, T., Mantei, N. and Semenza, G. (1993). The pro sequence of lactase-phlorizin hydrolase is required for the enzyme to reach the plasma membrane. An intramolecular chaperone? FEBS Lett. 333, 127-131.
    • (1993) FEBS Lett. , vol.333 , pp. 127-131
    • Oberholzer, T.1    Mantei, N.2    Semenza, G.3
  • 36
    • 0027295871 scopus 로고
    • Association of folding intermediates of glycoproteins with calnexin during protein maturation
    • Ou, W. J., Cameron, P. H., Thomas, D. Y. and Bergeron, J. J. (1993). Association of folding intermediates of glycoproteins with calnexin during protein maturation. Nature 364, 771-776.
    • (1993) Nature , vol.364 , pp. 771-776
    • Ou, W.J.1    Cameron, P.H.2    Thomas, D.Y.3    Bergeron, J.J.4
  • 37
    • 0030062178 scopus 로고    scopus 로고
    • Congenital sucrase-isomaltase deficiency. Identification of a glutamine to proline substitution that leads to a transport block of sucrase-isomaltase in a pre-Golgi compartment
    • Ouwendijk, J., Moolenaar, C. E., Peters, W. J., Hollenberg, C. P., Ginsel, L. A., Fransen, J. A. and Naim, H. Y. (1996). Congenital sucrase-isomaltase deficiency. Identification of a glutamine to proline substitution that leads to a transport block of sucrase-isomaltase in a pre-Golgi compartment. J. Clin. Invest. 97, 633-641.
    • (1996) J. Clin. Invest. , vol.97 , pp. 633-641
    • Ouwendijk, J.1    Moolenaar, C.E.2    Peters, W.J.3    Hollenberg, C.P.4    Ginsel, L.A.5    Fransen, J.A.6    Naim, H.Y.7
  • 38
    • 0024427039 scopus 로고
    • Control of protein exit from the endoplasmic reticulum
    • Pelham, H. R. (1989). Control of protein exit from the endoplasmic reticulum. Annu. Rev. Cell Biol. 5, 1-23.
    • (1989) Annu. Rev. Cell Biol. , vol.5 , pp. 1-23
    • Pelham, H.R.1
  • 39
    • 0027489133 scopus 로고
    • Sorting of membrane proteins in the secretory pathway
    • Pelham, H. R. and Munro, S. (1993). Sorting of membrane proteins in the secretory pathway. Cell 75, 603-605.
    • (1993) Cell , vol.75 , pp. 603-605
    • Pelham, H.R.1    Munro, S.2
  • 40
    • 0023077578 scopus 로고
    • Biosynthetic protein transport and sorting by the endoplasmic reticulum and Golgi
    • Pfeffer, S. R. and Rothman, J. E. (1987). Biosynthetic protein transport and sorting by the endoplasmic reticulum and Golgi. Annu. Rev. Biochem. 56, 829-852.
    • (1987) Annu. Rev. Biochem. , vol.56 , pp. 829-852
    • Pfeffer, S.R.1    Rothman, J.E.2
  • 41
    • 0029564918 scopus 로고
    • Misfolded major histocompatibility complex class I molecules accumulate in an expanded ER-Golgi intermediate compartment
    • Raposo, G., van Santen, H. M., Leijendekker, R., Geuze, H. J. and Ploegh, H. L. (1995). Misfolded major histocompatibility complex class I molecules accumulate in an expanded ER-Golgi intermediate compartment. J. Cell Biol. 131, 1403-1419.
    • (1995) J. Cell Biol. , vol.131 , pp. 1403-1419
    • Raposo, G.1    Van Santen, H.M.2    Leijendekker, R.3    Geuze, H.J.4    Ploegh, H.L.5
  • 42
    • 0022256691 scopus 로고
    • Defects in synthesis, phosphorylation, and maturation of acid alpha-glucosidase in glycogenosis type II
    • Reuser, A. J., Kroos, M., Oude Elferink, R. P. and Tager, J. M. (1985). Defects in synthesis, phosphorylation, and maturation of acid alpha-glucosidase in glycogenosis type II. J. Biol. Chem. 260, 8336-8341.
    • (1985) J. Biol. Chem. , vol.260 , pp. 8336-8341
    • Reuser, A.J.1    Kroos, M.2    Oude Elferink, R.P.3    Tager, J.M.4
  • 43
    • 0023239008 scopus 로고
    • Clinical diversity in glycogenosis type II. Biosynthesis and in situ localization of acid alpha-glucosidase in mutant fibroblasts
    • Reuser, A. J., Kroos, M., Willemsen, R., Swallow, D., Tager, J. M. and Galjaard, H. (1987). Clinical diversity in glycogenosis type II. Biosynthesis and in situ localization of acid alpha-glucosidase in mutant fibroblasts. J. Clin. Invest. 79, 1689-1699.
    • (1987) J. Clin. Invest. , vol.79 , pp. 1689-1699
    • Reuser, A.J.1    Kroos, M.2    Willemsen, R.3    Swallow, D.4    Tager, J.M.5    Galjaard, H.6
  • 44
    • 0026555196 scopus 로고
    • Molecular dissection of the secretory pathway
    • Rothman, J. E. and Orci, L. (1992). Molecular dissection of the secretory pathway. Nature 355, 409-415.
    • (1992) Nature , vol.355 , pp. 409-415
    • Rothman, J.E.1    Orci, L.2
  • 45
    • 0029670289 scopus 로고    scopus 로고
    • Protein sorting by transport vesicles
    • Rothman, J. E. and Wieland, F.T. (1996). Protein sorting by transport vesicles. Science 272, 227-234.
    • (1996) Science , vol.272 , pp. 227-234
    • Rothman, J.E.1    Wieland, F.T.2
  • 46
    • 0028171843 scopus 로고
    • The pro-peptide of the pro beta-polypeptide chain of human beta-hexosaminidase is necessary for proper protein folding and exit from the endoplasmic reticulum
    • Sagherian, C., Thorner, P. and Mahuran, D. (1994). The pro-peptide of the pro beta-polypeptide chain of human beta-hexosaminidase is necessary for proper protein folding and exit from the endoplasmic reticulum. Biochem. Biophys. Res. Commun. 204, 135-141.
    • (1994) Biochem. Biophys. Res. Commun. , vol.204 , pp. 135-141
    • Sagherian, C.1    Thorner, P.2    Mahuran, D.3
  • 47
    • 0023733211 scopus 로고
    • Identification, by a monoclonal antibody, of a 53-kD protein associated with a tubulo-vesicular compartment at the cis-side of the Golgi apparatus
    • Schweizer, A., Fransen, J. A., Bachi, T., Ginsel, L. and Hauri, H. P. (1988). Identification, by a monoclonal antibody, of a 53-kD protein associated with a tubulo-vesicular compartment at the cis-side of the Golgi apparatus. J. Cell Biol. 107, 1643-1653.
    • (1988) J. Cell Biol. , vol.107 , pp. 1643-1653
    • Schweizer, A.1    Fransen, J.A.2    Bachi, T.3    Ginsel, L.4    Hauri, H.P.5
  • 48
    • 0023694659 scopus 로고
    • Dissection of the asynchronous transport of intestinal microvillar hydrolases to the cell surface
    • Stieger, B., Matter, K., Baur, B., Bucher, K., Hochli, M. and Hauri, H. P. (1988). Dissection of the asynchronous transport of intestinal microvillar hydrolases to the cell surface. J. Cell Biol. 106, 1853-1861.
    • (1988) J. Cell Biol. , vol.106 , pp. 1853-1861
    • Stieger, B.1    Matter, K.2    Baur, B.3    Bucher, K.4    Hochli, M.5    Hauri, H.P.6
  • 49
    • 0028906029 scopus 로고
    • Folding and oligomerization of influenza hemagglutinin in the ER and the intermediate compartment
    • Tatu, U., Hammond, C. and Helenius, A. (1995). Folding and oligomerization of influenza hemagglutinin in the ER and the intermediate compartment. EMBO J. 14, 1340-1348.
    • (1995) EMBO J. , vol.14 , pp. 1340-1348
    • Tatu, U.1    Hammond, C.2    Helenius, A.3
  • 50
    • 0027392113 scopus 로고
    • Structural and functional changes of lysosomal acid alpha-glucosidase during intracellular transport and maturation
    • Wisselaar, H. A., Kroos, M. A., Hermans, M. M., van Beeumen, J. and Reuser, A. J. (1993). Structural and functional changes of lysosomal acid alpha-glucosidase during intracellular transport and maturation. J. Biol. Chem. 268, 2223-2231.
    • (1993) J. Biol. Chem. , vol.268 , pp. 2223-2231
    • Wisselaar, H.A.1    Kroos, M.A.2    Hermans, M.M.3    Van Beeumen, J.4    Reuser, A.J.5


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