메뉴 건너뛰기




Volumn 80, Issue 1, 1998, Pages 59-68

'Glyco-deglyco' processes during the synthesis of N-glycoproteins

Author keywords

Endoplasmic reticulum; Lipid intermediates; N glycosylation; Oligomannoside trafficking

Indexed keywords

ALPHA GLUCOSIDASE; GLYCOPROTEIN; MANNOSIDASE; OLIGOSACCHARIDE; PYROPHOSPHATE;

EID: 0031899212     PISSN: 03009084     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0300-9084(98)80057-6     Document Type: Article
Times cited : (25)

References (52)
  • 1
    • 0021891884 scopus 로고
    • Assembly of asparagine-linked oligosaccharides
    • 1 Kornfeld R, Kornfeld S (1985) Assembly of asparagine-linked oligosaccharides. Annu Rev Biochem 54, 631-664
    • (1985) Annu Rev Biochem , vol.54 , pp. 631-664
    • Kornfeld, R.1    Kornfeld, S.2
  • 2
    • 0018946112 scopus 로고
    • Fate of oligosaccharide-lipid intermediates synthetised by resting rat-spleen lymphocytes
    • 2 Cacan R, Hoflack B, Verben A (1980) Fate of oligosaccharide-lipid intermediates synthetised by resting rat-spleen lymphocytes. Eur J Biochem 106, 473-479
    • (1980) Eur J Biochem , vol.106 , pp. 473-479
    • Cacan, R.1    Hoflack, B.2    Verben, A.3
  • 3
    • 0016254329 scopus 로고
    • The role of a dolichol-oligosaccharide as an intermediate in glycoprotein biosynthesis
    • 3 Hsu AF, Baynes JW, Heath EC (1974) The role of a dolichol-oligosaccharide as an intermediate in glycoprotein biosynthesis. Proc Natl Acad Sci USA 71, 2391-2395
    • (1974) Proc Natl Acad Sci USA , vol.71 , pp. 2391-2395
    • Hsu, A.F.1    Baynes, J.W.2    Heath, E.C.3
  • 4
    • 0016685618 scopus 로고
    • The mannosylation of dolichol-diphosphate oligosaccharides in relation to the formation of oligosaccharides and glycoproteins in pig liver endoplasmic reticulum
    • 4 Oliver GJA, Harrison J, Hemming FW (1975) The mannosylation of dolichol-diphosphate oligosaccharides in relation to the formation of oligosaccharides and glycoproteins in pig liver endoplasmic reticulum. Eur J Biochem 58, 223-229
    • (1975) Eur J Biochem , vol.58 , pp. 223-229
    • Oliver, G.J.A.1    Harrison, J.2    Hemming, F.W.3
  • 5
    • 0018186610 scopus 로고
    • Study of nuclear mannosyltransferase: Lipids intermediates
    • 5 Richard M, Tytgat F, Louisot P (1978) Study of nuclear mannosyltransferase: lipids intermediates. Biochimie 60, 593-599
    • (1978) Biochimie , vol.60 , pp. 593-599
    • Richard, M.1    Tytgat, F.2    Louisot, P.3
  • 6
    • 0025317473 scopus 로고
    • Permeabilized cells as a way of gaining access to intracellular organelles: An approach to glycosylation reactions
    • 6 Lepers A, Cacan R, Verbert A (1990) Permeabilized cells as a way of gaining access to intracellular organelles: an approach to glycosylation reactions. Biochimie 72, 1-5
    • (1990) Biochimie , vol.72 , pp. 1-5
    • Lepers, A.1    Cacan, R.2    Verbert, A.3
  • 7
    • 0025761657 scopus 로고
    • Cytosolic pore-forming proteins and peptides: Is there a common structural motif?
    • 7 Ojcius DM, Young JDE (1991) Cytosolic pore-forming proteins and peptides: is there a common structural motif? TIBS 16, 225-229
    • (1991) TIBS , vol.16 , pp. 225-229
    • Ojcius, D.M.1    Young, J.D.E.2
  • 9
    • 0023821862 scopus 로고
    • Characterization of an oligosaccharide-pyrophosphodolichol pyrophosphatase in yeast
    • 9 Bélard M, Cacan R, Verbert A (1988) Characterization of an oligosaccharide-pyrophosphodolichol pyrophosphatase in yeast. Biochem J 255, 235-242
    • (1988) Biochem J , vol.255 , pp. 235-242
    • Bélard, M.1    Cacan, R.2    Verbert, A.3
  • 10
    • 0019154119 scopus 로고
    • Enzymatic activities in cultured human lymphocytes that dephosphorylate dolichol pyrophosphate in dolichol phosphate
    • 10 Wedgwood JF, Strominger JL (1980) Enzymatic activities in cultured human lymphocytes that dephosphorylate dolichol pyrophosphate in dolichol phosphate. J Biol Chem 255, 1120-1123
    • (1980) J Biol Chem , vol.255 , pp. 1120-1123
    • Wedgwood, J.F.1    Strominger, J.L.2
  • 11
    • 0019483754 scopus 로고
    • Dolichol pathway in lymphocytes from rat spleen: Influence of the glucosylation on the cleavage of dolichol diphosphate oligosaccharides into phospho-oligosaccharides
    • 11 Hoflack B, Cacan R, Verbert A (1981) Dolichol pathway in lymphocytes from rat spleen: influence of the glucosylation on the cleavage of dolichol diphosphate oligosaccharides into phospho-oligosaccharides. Eur J Biochem 117, 285-290
    • (1981) Eur J Biochem , vol.117 , pp. 285-290
    • Hoflack, B.1    Cacan, R.2    Verbert, A.3
  • 12
    • 0023655478 scopus 로고
    • Catabolic pathway of oligosaccharide-diphosphodolichol: Study of the fate of the oligosaccharidic moiety in mouse splenocytes
    • 12 Cacan R, Cecchelli R, Verbert A (1987) Catabolic pathway of oligosaccharide-diphosphodolichol: study of the fate of the oligosaccharidic moiety in mouse splenocytes. Eur J Biochem 166, 469-474
    • (1987) Eur J Biochem , vol.166 , pp. 469-474
    • Cacan, R.1    Cecchelli, R.2    Verbert, A.3
  • 14
    • 0021255868 scopus 로고
    • Transmembrane movement of oligosaccharide-lipids during glycoprotein synthesis
    • 14 Snider MD, Rogers OC (1984) Transmembrane movement of oligosaccharide-lipids during glycoprotein synthesis. Cell 36, 753-761
    • (1984) Cell , vol.36 , pp. 753-761
    • Snider, M.D.1    Rogers, O.C.2
  • 15
    • 0019631138 scopus 로고
    • Transmembrane assembly of membrane and secretory glycoproteins
    • 15 Hanover JA, Lennarz J (1981) Transmembrane assembly of membrane and secretory glycoproteins. Arch Biochem Biophys 211, 1-19
    • (1981) Arch Biochem Biophys , vol.211 , pp. 1-19
    • Hanover, J.A.1    Lennarz, J.2
  • 16
    • 0020490406 scopus 로고
    • Transmembrane assembly of N-linked glycoproteins
    • 16 Hanover JA, Lennarz J (1982) Transmembrane assembly of N-linked glycoproteins. J Biol Chem 257, 2787-2794
    • (1982) J Biol Chem , vol.257 , pp. 2787-2794
    • Hanover, J.A.1    Lennarz, J.2
  • 17
    • 0021015788 scopus 로고
    • Release of glucose-containing polymannose oligosaccharides during glycoprotein biosynthesis
    • 17 Anumula KR, Spiro RG (1983) Release of glucose-containing polymannose oligosaccharides during glycoprotein biosynthesis. J Biol Chem 258, 15274-15282
    • (1983) J Biol Chem , vol.258 , pp. 15274-15282
    • Anumula, K.R.1    Spiro, R.G.2
  • 18
    • 0024456160 scopus 로고
    • Catabolic pathway of oligosaccharide-diphosphodolichol: Subcellular sites of the degradation of the oligomannoside moiety
    • 18 Cacan R, Lepers A, Bélard M, Verbert A (1989) Catabolic pathway of oligosaccharide-diphosphodolichol: subcellular sites of the degradation of the oligomannoside moiety. Eur J Biochem 185, 173-179
    • (1989) Eur J Biochem , vol.185 , pp. 173-179
    • Cacan, R.1    Lepers, A.2    Bélard, M.3    Verbert, A.4
  • 19
    • 0028335370 scopus 로고
    • Itracellular compartmentalization and degradation of free polymannose oligosaccharides released during glycoprotein biosynthesis
    • 19 Moore SEH, Spiro RG (1994) Itracellular compartmentalization and degradation of free polymannose oligosaccharides released during glycoprotein biosynthesis. J Biol Chem 269, 12715-12721
    • (1994) J Biol Chem , vol.269 , pp. 12715-12721
    • Moore, S.E.H.1    Spiro, R.G.2
  • 20
    • 0028827570 scopus 로고
    • Endoplasmic reticulum to cytosol transport of free polymannose oligosaccharides in pernieabilized HepG2 cells
    • 20 Moore SEH, Bauvy C, Codogno P (1995) Endoplasmic reticulum to cytosol transport of free polymannose oligosaccharides in pernieabilized HepG2 cells. EMBO J 14, 6034-6042
    • (1995) EMBO J , vol.14 , pp. 6034-6042
    • Moore, S.E.H.1    Bauvy, C.2    Codogno, P.3
  • 21
    • 0031030663 scopus 로고    scopus 로고
    • Transfer of free polymannose type oligosaccharides from the cytosol to lysosomes in cultured human hepatocellular carcinoma HepG2 cells
    • 21 Saint-Pol A, Bauvy C, Codogno P, Moore SEH (1997) Transfer of free polymannose type oligosaccharides from the cytosol to lysosomes in cultured human hepatocellular carcinoma HepG2 cells. J Cell Biol 136, 45-59
    • (1997) J Cell Biol , vol.136 , pp. 45-59
    • Saint-Pol, A.1    Bauvy, C.2    Codogno, P.3    Moore, S.E.H.4
  • 22
    • 0025762343 scopus 로고
    • Potential regulation of N-glycosylation precuror through oligosaccharide-lipid hydrolase action and glucosyltransferase-glucosidase shuttle
    • 22 Spiro MJ, Spiro RG (1991) Potential regulation of N-glycosylation precuror 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
  • 23
    • 0028084472 scopus 로고
    • Release of oligomannoside-type glycans as a marker of the degradation of newly synthesized glycoprotein
    • 23 Villers C, Cacan R, Mir AM, Labiau O, Verbert A (1994) Release of oligomannoside-type glycans as a marker of the degradation of newly synthesized glycoprotein. Biochem J 298, 135-142
    • (1994) Biochem J , vol.298 , pp. 135-142
    • Villers, C.1    Cacan, R.2    Mir, A.M.3    Labiau, O.4    Verbert, A.5
  • 24
    • 0020957538 scopus 로고
    • 2 in calf thyroid cells: A possible recognition signal in the processing of glycoproteins
    • 2 in calf thyroid cells: a possible recognition signal in the processing of glycoproteins. J Biol Chem 258, 8260-8265
    • (1983) J Biol Chem , vol.258 , pp. 8260-8265
    • Parodi, A.J.1    Mendelzon, D.H.2    Lederkremer, G.Z.3
  • 25
    • 0024468302 scopus 로고
    • Glucosylation of glycoproteins by mammalian, plant, fungal and trypanosomatid protozoa microsomal membranes
    • 25 Trombetta ES, Bosch M, Parodi AJ (1989) Glucosylation of glycoproteins by mammalian, plant, fungal and trypanosomatid protozoa microsomal membranes. Biochemistry 28, 8108-8116
    • (1989) Biochemistry , vol.28 , pp. 8108-8116
    • Trombetta, E.S.1    Bosch, M.2    Parodi, A.J.3
  • 26
    • 0040232798 scopus 로고    scopus 로고
    • The interaction of the UDP-Glc:Glycoprotein glucosyltransferase with the acceptor glycoprotein
    • 26 Sousa MC, Parodi AJ (1996) The interaction of the UDP-Glc:glycoprotein glucosyltransferase with the acceptor glycoprotein. Cell Mol Biol 42, 609-616
    • (1996) Cell Mol Biol , vol.42 , pp. 609-616
    • Sousa, M.C.1    Parodi, A.J.2
  • 27
    • 0029024748 scopus 로고
    • Glucose trimming and reglucosylation determine glycoprotein association with calnexin in the endoplasmic reticulum
    • 27 Hebert DN, Foellmer B, Helenius A (1995) Glucose trimming and reglucosylation determine glycoprotein association with calnexin in the endoplasmic reticulum. Cell 81, 425-433
    • (1995) Cell , vol.81 , pp. 425-433
    • Hebert, D.N.1    Foellmer, B.2    Helenius, A.3
  • 28
    • 0029934119 scopus 로고    scopus 로고
    • Calnexin and calreticulin promote folding, delay oligomerization and suppress degradation of influenza hemagglutinin in microsomes
    • 28 Hebert DN, Foellmer B, Helenius A (1996) Calnexin and calreticulin promote folding, delay oligomerization and suppress degradation of influenza hemagglutinin in microsomes. EMBO J 15, 2961-2968
    • (1996) EMBO J , vol.15 , pp. 2961-2968
    • Hebert, D.N.1    Foellmer, B.2    Helenius, A.3
  • 29
    • 0030449989 scopus 로고    scopus 로고
    • N-linked oligosaccharides are necessary and sufficient for association of glycosylated forms of bovine RNase with calnexin and calreticulin
    • 29 Rodan AR, Simons JF, Trombetta ES, Helenius A (1996) N-linked oligosaccharides are necessary and sufficient for association of glycosylated forms of bovine RNase with calnexin and calreticulin. EMBO J 15, 6921-6930
    • (1996) EMBO J , vol.15 , pp. 6921-6930
    • Rodan, A.R.1    Simons, J.F.2    Trombetta, E.S.3    Helenius, A.4
  • 30
    • 21344440110 scopus 로고    scopus 로고
    • The UDP-Glc:Glycoprotein glucosyltransferase and the quality control of glycoprotein folding in the endoplasmic reticulum
    • 30 Parodi AJ (1996) The UDP-Glc:glycoprotein glucosyltransferase and the quality control of glycoprotein folding in the endoplasmic reticulum. TIGS 8, 1-12
    • (1996) TIGS , vol.8 , pp. 1-12
    • Parodi, A.J.1
  • 31
    • 15844386822 scopus 로고    scopus 로고
    • Definition of the lectin-like properties of the molecular chaperone calreticulin and demonstration of its copurification with endomannosidase from rat liver Golgi
    • 31 Spiro RG, Zhu Q, Bhoyroo V, Söling HD (1996) Definition of the lectin-like properties of the molecular chaperone calreticulin and demonstration of its copurification with endomannosidase from rat liver Golgi. J Biol Chem 271, 11588-11594
    • (1996) J Biol Chem , vol.271 , pp. 11588-11594
    • Spiro, R.G.1    Zhu, Q.2    Bhoyroo, V.3    Söling, H.D.4
  • 32
    • 0030033862 scopus 로고    scopus 로고
    • Occurrence of a cytosolic neutral chitobiase activity involved in oligomannoside degradation: A study with Madin-Darby Bovin Kidney (MDBK) cells
    • 32 Cacan R, Dengremont C, Labiau O, Kmiécik D, Mir AM, Verbert A (1996) Occurrence of a cytosolic neutral chitobiase activity involved in oligomannoside degradation: a study with Madin-Darby Bovin Kidney (MDBK) cells. Biochem J 313, 597-602
    • (1996) Biochem J , vol.313 , pp. 597-602
    • Cacan, R.1    Dengremont, C.2    Labiau, O.3    Kmiécik, D.4    Mir, A.M.5    Verbert, A.6
  • 33
    • 0018791725 scopus 로고
    • Cytosolic location of an endoN-acetyl-β-D-glucosaminidase activity in rat liver and kidney
    • 33 Pierce RJ, Spik G, Montreuil J (1979) Cytosolic location of an endoN-acetyl-β-D-glucosaminidase activity in rat liver and kidney. Biochem J 180, 673-676
    • (1979) Biochem J , vol.180 , pp. 673-676
    • Pierce, R.J.1    Spik, G.2    Montreuil, J.3
  • 34
    • 0018841512 scopus 로고
    • Demonstration and cytosolic location of an endo-N-acetyl-β-D-glucosaminidase activity towards an asialo-N-acetyl-lactosaminic-type substrat in rat liver
    • 34 Pierce RJ, Spik G, Montreuil J (1980) Demonstration and cytosolic location of an endo-N-acetyl-β-D-glucosaminidase activity towards an asialo-N-acetyl-lactosaminic-type substrat in rat liver. Biochem J 185, 261-264
    • (1980) Biochem J , vol.185 , pp. 261-264
    • Pierce, R.J.1    Spik, G.2    Montreuil, J.3
  • 35
    • 0021990870 scopus 로고
    • Use of an active site-directed inhibitor to study in situ degradation of glycoproteins by the perfused rat liver
    • 35 Kuranda MJ, Aronson NN Jr (1985) Use of an active site-directed inhibitor to study in situ degradation of glycoproteins by the perfused rat liver. J Biol Chem 260, 1858-1866
    • (1985) J Biol Chem , vol.260 , pp. 1858-1866
    • Kuranda, M.J.1    Aronson N.N., Jr.2
  • 36
    • 0023025334 scopus 로고
    • A di-N-acetylchitobiase activity is involved in the lysosomal catabolism of asparagine-linked glycoprotein in rat liver
    • 36 Kuranda MJ, Aronson NN Jr (1986) A di-N-acetylchitobiase activity is involved in the lysosomal catabolism of asparagine-linked glycoprotein in rat liver. J Biol Chem 261, 5803-5809
    • (1986) J Biol Chem , vol.261 , pp. 5803-5809
    • Kuranda, M.J.1    Aronson N.N., Jr.2
  • 37
    • 0028362217 scopus 로고
    • Purification and enzymatic properties of petide-N-glycanase from C3H mouse-derived L-929 fibroblast cells, possible widespread occurrence of post-translational remodification of proteins by N-deglycosylation
    • 37 Suzuki T, Seko A, Kitajima K, Inoue Y, Inoue S (1994) Purification and enzymatic properties of petide-N-glycanase from C3H mouse-derived L-929 fibroblast cells, possible widespread occurrence of post-translational remodification of proteins by N-deglycosylation. J Biol Chem 269, 17611-17618
    • (1994) J Biol Chem , vol.269 , pp. 17611-17618
    • Suzuki, T.1    Seko, A.2    Kitajima, K.3    Inoue, Y.4    Inoue, S.5
  • 38
    • 0031042905 scopus 로고    scopus 로고
    • Demonstration of a peptide: N-glycosidase in the endoplasmic reticulum of rat liver
    • 38 Weng S, Spiro RG (1997) Demonstration of a peptide: N-glycosidase in the endoplasmic reticulum of rat liver. Biochem J 322, 655-661
    • (1997) Biochem J , vol.322 , pp. 655-661
    • Weng, S.1    Spiro, R.G.2
  • 39
    • 0344434423 scopus 로고    scopus 로고
    • De-N-glycosylation system does occur ubiquitously in animal cells!
    • 39 Suzuki T (1996) De-N-glycosylation system does occur ubiquitously in animal cells! TIGS 8, 367-368
    • (1996) TIGS , vol.8 , pp. 367-368
    • Suzuki, T.1
  • 40
    • 0023749075 scopus 로고
    • Degradation from endoplasmic reticulum: Disposing of newly synthesized glycoproteins
    • 40 Lippincott-Schwartz J, Bonifacino JS, Yuan LC, Klausner RD (1988) Degradation from endoplasmic reticulum: disposing of newly synthesized glycoproteins. Cell 54, 209-220
    • (1988) Cell , vol.54 , pp. 209-220
    • Lippincott-Schwartz, J.1    Bonifacino, J.S.2    Yuan, L.C.3    Klausner, R.D.4
  • 41
    • 0025041029 scopus 로고
    • Protein degradation in the endoplasmic reticulum
    • 41 Klausner RD, Sitia R (1990) Protein degradation in the endoplasmic reticulum Cell 62, 610-614
    • (1990) Cell , vol.62 , pp. 610-614
    • Klausner, R.D.1    Sitia, R.2
  • 43
    • 0025720479 scopus 로고
    • A permeabilized cell system identifies the endoplasmic reticulum as a site of protein degradation
    • 43 Stafford FJ, Bonifacino JS (1991) A permeabilized cell system identifies the endoplasmic reticulum as a site of protein degradation. J Cell Biol 115, 1225-1236
    • (1991) J Cell Biol , vol.115 , pp. 1225-1236
    • Stafford, F.J.1    Bonifacino, J.S.2
  • 44
    • 0029915568 scopus 로고    scopus 로고
    • The human cytomegalovirus USII gene product dislocates MHC class I heavy chains from the endoplasmic reticulum to the cytosol
    • 44 Wiertz EJHJ, Jones TR, Sun L, Bogyo M, Geuze HJ, Ploegh HL (1996) The human cytomegalovirus USII gene product dislocates MHC class I heavy chains from the endoplasmic reticulum to the cytosol. Cell 84, 769-779
    • (1996) Cell , vol.84 , pp. 769-779
    • Wiertz, E.J.H.J.1    Jones, T.R.2    Sun, L.3    Bogyo, M.4    Geuze, H.J.5    Ploegh, H.L.6
  • 45
  • 46
    • 0029852685 scopus 로고    scopus 로고
    • Reversal of fortune for nascent proteins
    • 46 Bonifacino JS (1996) Reversal of fortune for nascent proteins. Nature 384, 405-406
    • (1996) Nature , vol.384 , pp. 405-406
    • Bonifacino, J.S.1
  • 47
    • 0028840915 scopus 로고
    • Degradation of CFTR by the ubiquitin-proteasome pathway
    • 47 Ward CL, Omura S, Kopito RR (1995) Degradation of CFTR by the ubiquitin-proteasome pathway. Cell 83, 121-127
    • (1995) Cell , vol.83 , pp. 121-127
    • Ward, C.L.1    Omura, S.2    Kopito, R.R.3
  • 48
    • 0029788023 scopus 로고    scopus 로고
    • 1-anlitrypsin Z, in the endoplasmic reticulum requires proteasome activity
    • 1-anlitrypsin Z, in the endoplasmic reticulum requires proteasome activity. J Biol Chem 271, 22791-22795
    • (1996) J Biol Chem , vol.271 , pp. 22791-22795
    • Qu, D.1    Teckman, J.H.2    Omura, S.3    Perlmutter, D.H.4
  • 49
    • 0031051852 scopus 로고    scopus 로고
    • Misfolded major histocompatibility complex class I heavy chains are translocated into the cytoplasm and degraded into the proteasome
    • 49 Hughes EA, Hammond C, Cresswell P (1997) Misfolded major histocompatibility complex class I heavy chains are translocated into the cytoplasm and degraded into the proteasome. Proc Natl Acad Sci USA 94, 1896-1901
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 1896-1901
    • Hughes, E.A.1    Hammond, C.2    Cresswell, P.3
  • 50
    • 0031516167 scopus 로고    scopus 로고
    • Transglysosylation activity of endogycosidases and its application
    • 50 Yamamoto K, Takegawa K (1997) Transglysosylation activity of endogycosidases and its application. TIGS 9, 339-353
    • (1997) TIGS , vol.9 , pp. 339-353
    • Yamamoto, K.1    Takegawa, K.2
  • 51
    • 0027295871 scopus 로고
    • Association of folding intermediates of glycoproteins with calnexin during protein maturation
    • 51 Ou WJ, Carneron PH, Thomas DY, Bergeron JJM (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    Carneron, P.H.2    Thomas, D.Y.3    Bergeron, J.J.M.4
  • 52
    • 0028926420 scopus 로고
    • ERGIC-53, a membrane protein of the endoplasmic reticulum-Golgi intermediate compartment, is identical to MR60 an intracellular mannose-specific lectin of myelomonocytic cells
    • 52 Arar C, Carpentier V, Le Caer JP, Monsigny M, Roche AC (1995) ERGIC-53, a membrane protein of the endoplasmic reticulum-Golgi intermediate compartment, is identical to MR60 an intracellular mannose-specific lectin of myelomonocytic cells. J Biol Chem 270, 3551-3553
    • (1995) J Biol Chem , vol.270 , pp. 3551-3553
    • Arar, C.1    Carpentier, V.2    Le Caer, J.P.3    Monsigny, M.4    Roche, A.C.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.