메뉴 건너뛰기




Volumn 70, Issue 3, 1996, Pages 198-208

Dimerization of lactase-phlorizin hydrolase occurs in the endoplasmic reticulum, involves the putative membrane spanning domain and is required for an efficient transport of the enzyme to the cell surface

Author keywords

Dimerization; ER; Lactase phlorizin hydrolase; Transmembrane domain

Indexed keywords

ENZYME PRECURSOR; GLYCOSYLCERAMIDASE; HYDROLASE; LACTASE; MANNOSE; MEMBRANE ENZYME; MUTANT PROTEIN;

EID: 0029884290     PISSN: 01719335     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (26)

References (59)
  • 1
    • 0022834188 scopus 로고
    • ATP-coupled transport of vesicular stomatitis virus G protein. Functional boundaries of secretory compartments
    • Balch, W. E., D. S. Keller: ATP-coupled transport of vesicular stomatitis virus G protein. Functional boundaries of secretory compartments. J. Biol. Chem. 261, 14690-14696 (1986).
    • (1986) J. Biol. Chem. , vol.261 , pp. 14690-14696
    • Balch, W.E.1    Keller, D.S.2
  • 2
    • 0026694442 scopus 로고
    • Intermembrane helix-helix association in oligomerization and transmembrane signaling
    • Bormann, B. J., D. M. Engelman: Intermembrane helix-helix association in oligomerization and transmembrane signaling. Annu. Rev. Biophys. Biomol. Struct. 21, 223-242 (1992).
    • (1992) Annu. Rev. Biophys. Biomol. Struct. , vol.21 , pp. 223-242
    • Bormann, B.J.1    Engelman, D.M.2
  • 3
    • 0023657227 scopus 로고
    • Biosynthesis, glycosylation, and intracellular transport of intestinal lactase-phlorizin hydrolase in rat
    • Büller, H. A., R. K. Montgomery, W. V. Sasak, R. J. Grand: Biosynthesis, glycosylation, and intracellular transport of intestinal lactase-phlorizin hydrolase in rat. J. Biol. Chem. 262, 17206-17211 (1987).
    • (1987) J. Biol. Chem. , vol.262 , pp. 17206-17211
    • Büller, H.A.1    Montgomery, R.K.2    Sasak, W.V.3    Grand, R.J.4
  • 4
    • 0024294338 scopus 로고
    • Folding, trimerization, and transport are sequential events in the biogenesis of influenza hemagglutinin
    • Copeland, C. S., K.-P. Zimmer, K. R. Wagner, G. A. Healey, I. Mellman, A. Helenius: Folding, trimerization, and transport are sequential events in the biogenesis of influenza hemagglutinin. Cell 53, 197-209 (1988).
    • (1988) Cell , vol.53 , pp. 197-209
    • Copeland, C.S.1    Zimmer, K.-P.2    Wagner, K.R.3    Healey, G.A.4    Mellman, I.5    Helenius, A.6
  • 5
    • 0022456221 scopus 로고
    • Topology and quaternary structure of prosucrase-isomaltase and final-form sucrase-isomaltase
    • Cowell, G. M., J. Tranum-Jensen, H. Sjöström, H. O. Norén: Topology and quaternary structure of prosucrase-isomaltase and final-form sucrase-isomaltase. Biochem. J. 237, 455-461 (1986).
    • (1986) Biochem. J. , vol.237 , pp. 455-461
    • Cowell, G.M.1    Tranum-Jensen, J.2    Sjöström, H.3    Norén, H.O.4
  • 6
    • 0014235959 scopus 로고
    • Assay of intestinal disaccharidases
    • Dahlqvist, A.: Assay of intestinal disaccharidases. Anal. Biochem. 22, 99-107 (1968).
    • (1968) Anal. Biochem. , vol.22 , pp. 99-107
    • Dahlqvist, A.1
  • 7
    • 0021282020 scopus 로고
    • Biosynthesis of intestinal microvillar proteins. Intracellular processing of lactase-phlorizin hydrolase
    • Danielsen, E. M., H. Skovbjerg, O. Norén, H. Sjöström: Biosynthesis of intestinal microvillar proteins. Intracellular processing of lactase-phlorizin hydrolase. Biochem. Biophys. Res. Commun. 122, 82-90 (1984).
    • (1984) Biochem. Biophys. Res. Commun. , vol.122 , pp. 82-90
    • Danielsen, E.M.1    Skovbjerg, H.2    Norén, O.3    Sjöström, H.4
  • 8
    • 0025169919 scopus 로고
    • Biosynthesis of intestinal microvillar proteins. Dimerization of aminopeptidase N and lactase-phlorizin hydrolase
    • Danielsen, E. M.: Biosynthesis of intestinal microvillar proteins. Dimerization of aminopeptidase N and lactase-phlorizin hydrolase. Biochemistry 29, 305-308 (1990).
    • (1990) Biochemistry , vol.29 , pp. 305-308
    • Danielsen, E.M.1
  • 9
    • 0023788652 scopus 로고
    • Different effects of mutations in three domains on folding, trimerization and intracellular transport of VSV G protein trimers
    • Doms, R. W., A. Ruusala, C. Machamer, J. Helenius, A. Helenius, J K. Rose: Different effects of mutations in three domains on folding, trimerization and intracellular transport of VSV G protein trimers. J. Cell Biol. 107, 89-99 (1988).
    • (1988) J. Cell Biol. , vol.107 , pp. 89-99
    • Doms, R.W.1    Ruusala, A.2    Machamer, C.3    Helenius, J.4    Helenius, A.5    Rose, J.K.6
  • 10
    • 0023014134 scopus 로고
    • Analysis of progressive deletions of the transmembrane and cytoplasmic domains of influenza virus
    • Doyle, C., J. Sambrook, M. J. Gething: Analysis of progressive deletions of the transmembrane and cytoplasmic domains of influenza virus. J. Cell Biol. 103, 1193-1204 (1986).
    • (1986) J. Cell Biol. , vol.103 , pp. 1193-1204
    • Doyle, C.1    Sambrook, J.2    Gething, M.J.3
  • 11
    • 0023068446 scopus 로고
    • Genetics of lactose digestion in humans
    • H. Harris, K. Hirschborn (eds.): Plenum Press, New York
    • Flatz, G.: Genetics of lactose digestion in humans. In: H. Harris, K. Hirschborn (eds.): Advances in Human Genetics. Vol. 16. pp. 1-77. Plenum Press, New York 1987.
    • (1987) Advances in Human Genetics , vol.16 , pp. 1-77
    • Flatz, G.1
  • 12
    • 0022552149 scopus 로고
    • Expression of wild type and mutant forms of influenza hemagglutinin: The role of folding in intracellular transport
    • Gething, M. J., K. McCammon, J. Sambrook: Expression of wild type and mutant forms of influenza hemagglutinin: the role of folding in intracellular transport. Cell 46, 939-950 (1986).
    • (1986) Cell , vol.46 , pp. 939-950
    • Gething, M.J.1    McCammon, K.2    Sambrook, J.3
  • 13
    • 0026584271 scopus 로고
    • Protein folding in the cell
    • Gething, M. J., J. Sambrook: Protein folding in the cell. Nature 355, 33-45 (1992).
    • (1992) Nature , vol.355 , pp. 33-45
    • Gething, M.J.1    Sambrook, J.2
  • 14
    • 0026619708 scopus 로고
    • Proteolytic processing of human intestinal lactase-phlorizin hydrolase precursor is not a prerequisite for correct sorting in Madin-Darby canine kidney (MDCK) cells
    • Grünberg, J., U. Luginbühl, E. E. Sterchi: Proteolytic processing of human intestinal lactase-phlorizin hydrolase precursor is not a prerequisite for correct sorting in Madin-Darby canine kidney (MDCK) cells. FEBS Lett. 314, 224-228 (1992).
    • (1992) FEBS Lett. , vol.314 , pp. 224-228
    • Grünberg, J.1    Luginbühl, U.2    Sterchi, E.E.3
  • 15
    • 0023718134 scopus 로고
    • Biogenesis and intracellular transport of intestinal brush border membrane hydrolases
    • Hauri, H. P.: Biogenesis and intracellular transport of intestinal brush border membrane hydrolases. Subcell. Biochem. 12, 155-219 (1988).
    • (1988) Subcell. Biochem. , vol.12 , pp. 155-219
    • Hauri, H.P.1
  • 16
    • 0022181709 scopus 로고
    • Expression and intracellular transport of microvillis membrane hydrolases in human small intestinal epithelial cells
    • Hauri, H. P., E. E. Sterchi, D. Bienz, J. A. M. Fransen, A. Marxer: Expression and intracellular transport of microvillis membrane hydrolases in human small intestinal epithelial cells. J. Cell Biol. 101, 838-851 (1985).
    • (1985) J. Cell Biol. , vol.101 , pp. 838-851
    • Hauri, H.P.1    Sterchi, E.E.2    Bienz, D.3    Fransen, J.A.M.4    Marxer, A.5
  • 17
    • 0019520970 scopus 로고
    • Postnatal development: Coordination of feeding, digestion and metabolism
    • Henning, S. J.: Postnatal development: Coordination of feeding, digestion and metabolism. Am. J. Physiol. 241, G199-G214 (1981).
    • (1981) Am. J. Physiol. , vol.241
    • Henning, S.J.1
  • 18
    • 0023431536 scopus 로고
    • Pig kidney angiotensin converting enzyme. Purification and characterization of amphipathic and hydrophilic forms of the enzyme establishes C-terminal anchorage to the plasma membrane
    • Hooper, N. M., J. Keen, D. J. Pappin, A. J. Turner: Pig kidney angiotensin converting enzyme. Purification and characterization of amphipathic and hydrophilic forms of the enzyme establishes C-terminal anchorage to the plasma membrane. Biochem. J. 247, 85-93 (1987).
    • (1987) Biochem. J. , vol.247 , pp. 85-93
    • Hooper, N.M.1    Keen, J.2    Pappin, D.J.3    Turner, A.J.4
  • 19
    • 0022504432 scopus 로고
    • The sucrase-isomaltase primary structure, membrane orientation and evolution of a stalked, intrinsic brush border protein
    • Hunziker, W., M. Spiess, G. Semenza, H. F. Lodish: The sucrase-isomaltase primary structure, membrane orientation and evolution of a stalked, intrinsic brush border protein. Cell 46, 227-234 (1986).
    • (1986) Cell , vol.46 , pp. 227-234
    • Hunziker, W.1    Spiess, M.2    Semenza, G.3    Lodish, H.F.4
  • 20
    • 0024461745 scopus 로고
    • Protein oligomerization in the endoplasmic reticulum
    • Hurtley, S. M., A. Helenius: Protein oligomerization in the endoplasmic reticulum. Annu. Rev. Cell Biol. 5, 277-307 (1989).
    • (1989) Annu. Rev. Cell Biol. , vol.5 , pp. 277-307
    • Hurtley, S.M.1    Helenius, A.2
  • 21
    • 0029155988 scopus 로고
    • Folding of human intestinal lactase-phlorizin hydrolase
    • Jacob, R., N. J. Bulleid, H. Y. Naim: Folding of human intestinal lactase-phlorizin hydrolase. J. Biol. Chem. 270, 18678-18684 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 18678-18684
    • Jacob, R.1    Bulleid, N.J.2    Naim, H.Y.3
  • 22
    • 0027936702 scopus 로고
    • Transport, function and sorting of lactase-phlorizin hydrolase in Madin-Darby canine kidney cells
    • Jacob, R., C. Brewer, J. A. M. Fransen, H. Y. Naim: Transport, function and sorting of lactase-phlorizin hydrolase in Madin-Darby canine kidney cells. J. Biol. Chem. 269, 2712-2721 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 2712-2721
    • Jacob, R.1    Brewer, C.2    Fransen, J.A.M.3    Naim, H.Y.4
  • 23
    • 0025853058 scopus 로고
    • Oligomerization and intracellular protein transport: Dimerization of intestinal dipeptidylpeptidase IV occurs in the Golgi apparatus
    • Jascur, T., K. Matter, H.-P. Hauri: Oligomerization and intracellular protein transport: dimerization of intestinal dipeptidylpeptidase IV occurs in the Golgi apparatus. Biochemistry 30, 1908-1915 (1991).
    • (1991) Biochemistry , vol.30 , pp. 1908-1915
    • Jascur, T.1    Matter, K.2    Hauri, H.-P.3
  • 24
    • 0020007911 scopus 로고
    • Topology of microvillar membrane hydrolases of kidney and intestine
    • Kenny, A. J., S. Maroux: Topology of microvillar membrane hydrolases of kidney and intestine. Physiol. Rev. 62, 91-128 (1982).
    • (1982) Physiol. Rev. , vol.62 , pp. 91-128
    • Kenny, A.J.1    Maroux, S.2
  • 25
    • 0015172807 scopus 로고
    • Memorial lecture: Lactose and lactase - A historical perspective
    • Kretchmer, N.: Memorial lecture: lactose and lactase - A historical perspective. Gastroenterology 61, 805-813 (1971).
    • (1971) Gastroenterology , vol.61 , pp. 805-813
    • Kretchmer, N.1
  • 26
    • 0021891884 scopus 로고
    • Assembly of asparagine-linked oligosaccharides
    • Kornfeld, R., S. Kornfeld: Assembly of asparagine-linked oligosaccharides. Annu. Rev. Biochem. 54, 631-664 (1985).
    • (1985) Annu. Rev. Biochem. , vol.54 , pp. 631-664
    • Kornfeld, R.1    Kornfeld, S.2
  • 27
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.: Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685 (1970).
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.1
  • 28
    • 0023644634 scopus 로고
    • The chicken receptor for endocytosis of glycoproteins contains a cluster of N-acetylglucosamine-binding sites
    • Loeb, J. A., K. Drickamer: The chicken receptor for endocytosis of glycoproteins contains a cluster of N-acetylglucosamine-binding sites. J. Biol. Chem. 262, 3022-3029 (1987).
    • (1987) J. Biol. Chem. , vol.262 , pp. 3022-3029
    • Loeb, J.A.1    Drickamer, K.2
  • 30
    • 0024076253 scopus 로고
    • Complete primary structure of human and rabbit lactase-phlorizin hydrolase: Implications for biosynthesis, membrane anchoring and evolution of the enzyme
    • Mantei, N., M. Villa, T. Enzler, H. Wacker, W. Boll, P. James, W. Hunziker, G. Semenza: Complete primary structure of human and rabbit lactase-phlorizin hydrolase: implications for biosynthesis, membrane anchoring and evolution of the enzyme. EMBO J. 7, 2705-2713 (1988).
    • (1988) EMBO J. , vol.7 , pp. 2705-2713
    • Mantei, N.1    Villa, M.2    Enzler, T.3    Wacker, H.4    Boll, W.5    James, P.6    Hunziker, W.7    Semenza, G.8
  • 32
    • 0025876183 scopus 로고
    • Lactose intolerance and the genetic regulation of intestinal lactase-phlorizin hydrolase
    • Montgomery, R. K., H. A. Büller, E. H. H. M. Rings, R. J. Grand: Lactose intolerance and the genetic regulation of intestinal lactase-phlorizin hydrolase. FASEB J. 13, 2824-2832 (1991).
    • (1991) FASEB J. , vol.13 , pp. 2824-2832
    • Montgomery, R.K.1    Büller, H.A.2    Rings, E.H.H.M.3    Grand, R.J.4
  • 33
    • 0028148546 scopus 로고
    • The pro region of human intestinal lactase-phlorizin hydrolase
    • Naim, H. Y., R. Jacob, H. Naim, J. F. Sambrook, M. J. H. Gething: The pro region of human intestinal lactase-phlorizin hydrolase. J. Biol. Chem. 269, 26933-26943 (1994).
    • (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.H.5
  • 34
    • 0027748177 scopus 로고
    • Human small intestinal angiotensin-converting enzyme: Intracellular transport, secretion and glycosylation
    • Naim, H. Y.: Human small intestinal angiotensin-converting enzyme: intracellular transport, secretion and glycosylation. Biochem. J. 296, 607-615 (1993).
    • (1993) Biochem. J. , vol.296 , pp. 607-615
    • Naim, H.Y.1
  • 35
    • 0027194751 scopus 로고
    • Basis for selective incorporation of glycoproteins into the influenza virus envelope
    • Naim, H. Y., M. G. Roth: Basis for selective incorporation of glycoproteins into the influenza virus envelope. J. Virol. 67, 4831-4841 (1993).
    • (1993) J. Virol. , vol.67 , pp. 4831-4841
    • Naim, H.Y.1    Roth, M.G.2
  • 36
    • 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., M. J. Lentze: 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).
    • (1992) J. Biol. Chem. , vol.267 , pp. 25494-25504
    • Naim, H.Y.1    Lentze, M.J.2
  • 37
    • 0026808767 scopus 로고
    • Angiotensin-converting enzyme of the human small intestine. Subunit and quaternary structure, biosynthesis and membrane association
    • Naim, H. Y.: Angiotensin-converting enzyme of the human small intestine. Subunit and quaternary structure, biosynthesis and membrane association. Biochem. J. 286, 451-457 (1992).
    • (1992) Biochem. J. , vol.286 , pp. 451-457
    • Naim, H.Y.1
  • 38
    • 0026639133 scopus 로고
    • Processing of human pro-lactase-phlorizin hydrolase at reduced temperatures: Cleavage is preceded by complex glycosylation
    • Naim, H. Y.: Processing of human pro-lactase-phlorizin hydrolase at reduced temperatures: cleavage is preceded by complex glycosylation. Biochem. J. 285, 13-16 (1992).
    • (1992) Biochem. J. , vol.285 , pp. 13-16
    • Naim, H.Y.1
  • 39
    • 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., S. Lacey, J. F. Sambrook, M. J. H. Gething: 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).
    • (1991) J. Biol. Chem. , vol.266 , pp. 12313-12320
    • Naim, H.Y.1    Lacey, S.2    Sambrook, J.F.3    Gething, M.J.H.4
  • 40
    • 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., E. E. Sterchi, M. J. Lentze: 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).
    • (1988) J. Biol. Chem. , vol.263 , pp. 7242-7253
    • Naim, H.Y.1    Sterchi, E.E.2    Lentze, M.J.3
  • 41
    • 0024268345 scopus 로고
    • Structure, biosynthesis, and glycosylation of human small intestinal maltase-glucoamylase
    • Naim, H. Y., E. E. Sterchi, M. J. Lentze: Structure, biosynthesis, and glycosylation of human small intestinal maltase-glucoamylase. J. Biol. Chem. 263, 19709-19717 (1988).
    • (1988) J. Biol. Chem. , vol.263 , pp. 19709-19717
    • Naim, H.Y.1    Sterchi, E.E.2    Lentze, M.J.3
  • 42
    • 0023088808 scopus 로고
    • Biosynthesis and maturation of lactase-phlorizin hydrolase in the human small intestinal epithelial cells
    • Naim, H. Y., E. E. Sterchi, M. J. Lentze: Biosynthesis and maturation of lactase-phlorizin hydrolase in the human small intestinal epithelial cells. Biochem. J. 241, 427-434 (1987).
    • (1987) Biochem. J. , vol.241 , pp. 427-434
    • Naim, H.Y.1    Sterchi, E.E.2    Lentze, M.J.3
  • 43
    • 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., N. Mantei, G. Semenza: 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).
    • (1993) FEBS Lett. , vol.333 , pp. 127-131
    • Oberholzer, T.1    Mantei, N.2    Semenza, G.3
  • 45
    • 0024997068 scopus 로고
    • Intestinal lactase. Shift in intracellular processing to altered, inactive species in the adult rat
    • Quan, R., N. A. Santiago, K. K. Tsuboi, G. M. Gray: Intestinal lactase. Shift in intracellular processing to altered, inactive species in the adult rat. J. Biol. Chem. 265, 15882-15888 (1990).
    • (1990) J. Biol. Chem. , vol.265 , pp. 15882-15888
    • Quan, R.1    Santiago, N.A.2    Tsuboi, K.K.3    Gray, G.M.4
  • 46
    • 0024149621 scopus 로고
    • Regulation of protein export from the endoplasmic reticulum
    • Rose, J. K., R. W. Doms: Regulation of protein export from the endoplasmic reticulum. Annu. Rev. Cell Biol. 4, 257-288 (1988).
    • (1988) Annu. Rev. Cell Biol. , vol.4 , pp. 257-288
    • Rose, J.K.1    Doms, R.W.2
  • 47
    • 0023024475 scopus 로고
    • Temperature-sensitive steps in the transport of secretory proteins through the Golgi complex in exocrine pancreatic cells
    • Saraste, J., G. E. Palade, M. G. Farquhar: Temperature-sensitive steps in the transport of secretory proteins through the Golgi complex in exocrine pancreatic cells. Proc. Natl. Acad. Sci. USA 83, 6425-6429 (1986).
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 6425-6429
    • Saraste, J.1    Palade, G.E.2    Farquhar, M.G.3
  • 49
    • 0022854871 scopus 로고
    • Anchoring and biosynthesis of stalked brush border membrane glycosidases and peptidases of enterocytes and renal tubuli
    • Semenza, G.: Anchoring and biosynthesis of stalked brush border membrane glycosidases and peptidases of enterocytes and renal tubuli. Annu. Rev. Cell Biol. 2, 255-313 (1986).
    • (1986) Annu. Rev. Cell Biol. , vol.2 , pp. 255-313
    • Semenza, G.1
  • 50
    • 0026531034 scopus 로고
    • Alterations to influenza virus hemagglutinin cytoplasmic tail modulate virus infectivity
    • Simpson, D. A., R. A. Lamb: Alterations to influenza virus hemagglutinin cytoplasmic tail modulate virus infectivity. J. Virol. 66, 790-803 (1992).
    • (1992) J. Virol. , vol.66 , pp. 790-803
    • Simpson, D.A.1    Lamb, R.A.2
  • 51
    • 0019545313 scopus 로고
    • Purification and characterization of amphiphilic lactase/phlorizin hydrolase from human small intestine
    • Skovbjerg, H., H. Sjöström, O. Norén: Purification and characterization of amphiphilic lactase/phlorizin hydrolase from human small intestine. Eur. J. Biochem. 114, 653-661 (1981).
    • (1981) Eur. J. Biochem. , vol.114 , pp. 653-661
    • Skovbjerg, H.1    Sjöström, H.2    Norén, O.3
  • 53
    • 0023677695 scopus 로고
    • Biosynthesis of N-benzoyl-L-tyrosyl-p-aminobenzoic acid hydrolase: Disulfide-linked dimers are formed at the site of synthesis in the rough endoplasmic reticulum
    • Sterchi, E. E., H. Y. Naim, M. J. Lentze: Biosynthesis of N-benzoyl-L-tyrosyl-p-aminobenzoic acid hydrolase: disulfide-linked dimers are formed at the site of synthesis in the rough endoplasmic reticulum. Arch. Biochem. Biophys. 265, 119-127 (1988).
    • (1988) Arch. Biochem. Biophys. , vol.265 , pp. 119-127
    • Sterchi, E.E.1    Naim, H.Y.2    Lentze, M.J.3
  • 54
    • 0021272399 scopus 로고
    • Golgi/granule processing of peptide hormone and neuropeptide precursors a minireview
    • Steiner, D. F., K. Docherty, R. Carroll: Golgi/granule processing of peptide hormone and neuropeptide precursors: a minireview. J. Cell. Biochem. 24, 121-130 (1984).
    • (1984) J. Cell. Biochem. , vol.24 , pp. 121-130
    • Steiner, D.F.1    Docherty, K.2    Carroll, R.3
  • 55
    • 0022745592 scopus 로고
    • Temperature and energy dependence of secretory protein transport in the exocrine pancreas
    • Tartakoff, A. M.: Temperature and energy dependence of secretory protein transport in the exocrine pancreas. EMBO J. 5, 1477-1482 (1986).
    • (1986) EMBO J. , vol.5 , pp. 1477-1482
    • Tartakoff, A.M.1
  • 56
    • 0025835629 scopus 로고
    • Gp160, the envelope glycoprotein of human immunodeficiency virus type I, is a dimer of 125-kilodalton subunits stabilized through interactions between their gp41 domains
    • Thomas, D. J., J. S. Wall, J. F. Hainfeld, M. Kaczorek, F. P Booy, B. L. Trus, F. A. Eiserling, A. C. Steven: gp160, the envelope glycoprotein of human immunodeficiency virus type I, is a dimer of 125-kilodalton subunits stabilized through interactions between their gp41 domains. J. Virol. 65, 3797-3803 (1991).
    • (1991) J. Virol. , vol.65 , pp. 3797-3803
    • Thomas, D.J.1    Wall, J.S.2    Hainfeld, J.F.3    Kaczorek, M.4    Booy, F.P.5    Trus, B.L.6    Eiserling, F.A.7    Steven, A.C.8
  • 57
    • 0021324851 scopus 로고
    • Promoter-regulatory region of the major immediate early gene of human cytomegalovirus
    • Thomsen, D. R., R. M. Stenberg, W. F. Goins, M. F. Stinski: Promoter-regulatory region of the major immediate early gene of human cytomegalovirus. Proc. Natl. Acad. Sci. USA 81, 659-663 (1984).
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 659-663
    • Thomsen, D.R.1    Stenberg, R.M.2    Goins, W.F.3    Stinski, M.F.4
  • 58
    • 0017123985 scopus 로고
    • Organ-culture methods in the study of gastrointestinal-mucosal function and development
    • Trier, J. S.: Organ-culture methods in the study of gastrointestinal-mucosal function and development. N. Engl. J. Med. 295, 150-155 (1976).
    • (1976) N. Engl. J. Med. , vol.295 , pp. 150-155
    • Trier, J.S.1
  • 59
    • 0025886259 scopus 로고
    • Posttranslational cleavage of rat intestinal lactase occurs at the luminal side of the brush border membrane
    • Yeh, K.-Y., M. Yeh, P.-C. Pan, P. R. Holt: Posttranslational cleavage of rat intestinal lactase occurs at the luminal side of the brush border membrane. Gastroenterology 101, 312-318 (1991).
    • (1991) Gastroenterology , vol.101 , pp. 312-318
    • Yeh, K.-Y.1    Yeh, M.2    Pan, P.-C.3    Holt, P.R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.