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Volumn 34, Issue 11, 2010, Pages 1170-1174

Molecular cloning, characterization and expression analysis of cathepsin C gene involved in the antibacterial response in Chinese mitten crab, Eriocheir sinensis

Author keywords

Cathepsin C; Chinese mitten crab; Eriocheir sinensis; Infection; Quantitative real time PCR

Indexed keywords

AMINO ACID DERIVATIVE; COMPLEMENTARY DNA; DIPEPTIDYL PEPTIDASE I; MESSENGER RNA;

EID: 77956402985     PISSN: 0145305X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.dci.2010.06.011     Document Type: Article
Times cited : (18)

References (52)
  • 1
    • 1642422727 scopus 로고    scopus 로고
    • Insights into the anti-microbial defense of marine invertebrates: the penaeid shrimps and the oyster Crassostrea gigas
    • Bachere E., Gueguen Y., Gonzalez M., de Lorgeril J., Garnier J., Romestand B. Insights into the anti-microbial defense of marine invertebrates: the penaeid shrimps and the oyster Crassostrea gigas. Immunol. Rev. 2004, 198:149-168.
    • (2004) Immunol. Rev. , vol.198 , pp. 149-168
    • Bachere, E.1    Gueguen, Y.2    Gonzalez, M.3    de Lorgeril, J.4    Garnier, J.5    Romestand, B.6
  • 2
    • 0034930561 scopus 로고    scopus 로고
    • Evolutionary lines of cysteine peptidases
    • Barrett A.J., Rawlings N.D. Evolutionary lines of cysteine peptidases. J. Biol. Chem. 2001, 382:727-733.
    • (2001) J. Biol. Chem. , vol.382 , pp. 727-733
    • Barrett, A.J.1    Rawlings, N.D.2
  • 3
    • 0028923541 scopus 로고
    • Alignment/phylogeny of the papain superfamily of cysteine proteases
    • Berti P.J., Storer A.C. Alignment/phylogeny of the papain superfamily of cysteine proteases. J. Mol. Biol. 1995, 246:273-283.
    • (1995) J. Mol. Biol. , vol.246 , pp. 273-283
    • Berti, P.J.1    Storer, A.C.2
  • 4
    • 0019363396 scopus 로고
    • Organization and expression of eukaryotic split genes coding for proteins
    • Breathnach R., Chambon P. Organization and expression of eukaryotic split genes coding for proteins. Annu. Rev. Biochem. 1981, 50:349-383.
    • (1981) Annu. Rev. Biochem. , vol.50 , pp. 349-383
    • Breathnach, R.1    Chambon, P.2
  • 5
    • 0030783009 scopus 로고    scopus 로고
    • Dense core lysosomes can fuse withlate endosomesand are re-formed fromthe resultant hybrid organelles
    • Bright N.A., Reaves B.J., Mullock B.M., Luzio J.P. Dense core lysosomes can fuse withlate endosomesand are re-formed fromthe resultant hybrid organelles. J. Cell Sci. 1997, 110:2027-2040.
    • (1997) J. Cell Sci. , vol.110 , pp. 2027-2040
    • Bright, N.A.1    Reaves, B.J.2    Mullock, B.M.3    Luzio, J.P.4
  • 7
    • 0033587689 scopus 로고    scopus 로고
    • Dipeptidyl peptidase I is required for the processing and activation of granzymes A and B in vivo
    • Christine T.N., Pham, Timothy J.L. Dipeptidyl peptidase I is required for the processing and activation of granzymes A and B in vivo. Proc. Natl. Acad. Sci. U.S.A. 1999, 96:8627-8632.
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 8627-8632
    • Christine, T.N.1    Pham2    Timothy, J.L.3
  • 8
    • 0040043343 scopus 로고    scopus 로고
    • Stoichiometry and heterogeneity of the pro-region chain in tetrameric human cathepsin C
    • Cigicó B., Krizaj I., Kralj B., Turk V., Pain R.H. Stoichiometry and heterogeneity of the pro-region chain in tetrameric human cathepsin C. Biochim. Biophys. Acta 1998, 1382:143-150.
    • (1998) Biochim. Biophys. Acta , vol.1382 , pp. 143-150
    • Cigicó, B.1    Krizaj, I.2    Kralj, B.3    Turk, V.4    Pain, R.H.5
  • 9
    • 0034633884 scopus 로고    scopus 로고
    • The residual pro-part of cathepsin C fulfills the criteria required for an intramolecular chaperone in folding and stabilizing the human proenzyme
    • Cigicó B., Dahl S.W., Pain R.H. The residual pro-part of cathepsin C fulfills the criteria required for an intramolecular chaperone in folding and stabilizing the human proenzyme. Biochemistry 2000, 39:12382-12390.
    • (2000) Biochemistry , vol.39 , pp. 12382-12390
    • Cigicó, B.1    Dahl, S.W.2    Pain, R.H.3
  • 11
    • 0035852855 scopus 로고    scopus 로고
    • Human recombinant pro-dipeptidyl peptidase I (cathepsin C) can be activated by cathepsins L and S but not by autocatalytic processing
    • Dahl S.W., Halkier T., Lauritzen C., Dolenc I., Pedersen J., Turk V., Turk B. Human recombinant pro-dipeptidyl peptidase I (cathepsin C) can be activated by cathepsins L and S but not by autocatalytic processing. Biochemistry 2001, 40:1671-1678.
    • (2001) Biochemistry , vol.40 , pp. 1671-1678
    • Dahl, S.W.1    Halkier, T.2    Lauritzen, C.3    Dolenc, I.4    Pedersen, J.5    Turk, V.6    Turk, B.7
  • 12
    • 0033178886 scopus 로고    scopus 로고
    • Intron-exon structures of eukaryotic model organisms
    • Deutsch M., Long M. Intron-exon structures of eukaryotic model organisms. Nucleic Acids Res. 1999, 27:3219-3228.
    • (1999) Nucleic Acids Res. , vol.27 , pp. 3219-3228
    • Deutsch, M.1    Long, M.2
  • 14
    • 0029163155 scopus 로고
    • Oligomeric structure and substrate induced inhibition of human cathepsin C
    • Dolenc I., Turk B., Pungercic G., Ritonja A., Turk V. Oligomeric structure and substrate induced inhibition of human cathepsin C. J. Biol. Chem. 1995, 270:21626-21631.
    • (1995) J. Biol. Chem. , vol.270 , pp. 21626-21631
    • Dolenc, I.1    Turk, B.2    Pungercic, G.3    Ritonja, A.4    Turk, V.5
  • 15
    • 0023576201 scopus 로고
    • Cell growth and substrate effects on characteristics of a lysosomal enzyme (cathepsin C) in Duchenne muscular dystrophy fibroblasts
    • Doughty M.J., Gruenstein E.I. Cell growth and substrate effects on characteristics of a lysosomal enzyme (cathepsin C) in Duchenne muscular dystrophy fibroblasts. Biochem. Cell Biol. 1987, 65:617-625.
    • (1987) Biochem. Cell Biol. , vol.65 , pp. 617-625
    • Doughty, M.J.1    Gruenstein, E.I.2
  • 16
    • 0034697980 scopus 로고    scopus 로고
    • Predicting subcellular localization of proteins based on their N-terminal amino acids sequence
    • Emanuelsson O., Nielsen H., Brunak S., Von Heijne G. Predicting subcellular localization of proteins based on their N-terminal amino acids sequence. J. Mol. Biol. 2000, 300:1005-1016.
    • (2000) J. Mol. Biol. , vol.300 , pp. 1005-1016
    • Emanuelsson, O.1    Nielsen, H.2    Brunak, S.3    Von Heijne, G.4
  • 17
    • 0242713072 scopus 로고    scopus 로고
    • Neutrophil granules and secretory vesicles in inflammation
    • Faurschou M., Borregaard N. Neutrophil granules and secretory vesicles in inflammation. Microbes Infect. 2003, 5:1317-1327.
    • (2003) Microbes Infect. , vol.5 , pp. 1317-1327
    • Faurschou, M.1    Borregaard, N.2
  • 18
    • 45849113987 scopus 로고    scopus 로고
    • N-glycosylation modulates the cell-surface expression and catalytic activity of corin
    • Gladysheva I.P., King S.M., Houng A.K. N-glycosylation modulates the cell-surface expression and catalytic activity of corin. Biochem. Biophys. Res. Commun. 2008, 373:130-135.
    • (2008) Biochem. Biophys. Res. Commun. , vol.373 , pp. 130-135
    • Gladysheva, I.P.1    King, S.M.2    Houng, A.K.3
  • 19
    • 0034927549 scopus 로고    scopus 로고
    • Immune gene discovery by expressed sequence tag analysis of hemocytes and hepatopancreas in the Pacific White Shrimp, Litopenaeus vannamei, and the Atlantic White Shrimp, L. setiferus
    • Gross P.S., Bartlett T.C., Browdy C.L., Chapman R.W., Warr G.W. Immune gene discovery by expressed sequence tag analysis of hemocytes and hepatopancreas in the Pacific White Shrimp, Litopenaeus vannamei, and the Atlantic White Shrimp, L. setiferus. Dev. Comp. Immunol. 2001, 25:565-577.
    • (2001) Dev. Comp. Immunol. , vol.25 , pp. 565-577
    • Gross, P.S.1    Bartlett, T.C.2    Browdy, C.L.3    Chapman, R.W.4    Warr, G.W.5
  • 21
    • 0035258424 scopus 로고    scopus 로고
    • Response of haemocyte lysosomes to bacterial inoculation in the oysters Ostrea edulis L. and Crassostrea gigas (Thunberg) and the scallop Pecten maximus (L.)
    • Hauton C., Hawkins L.E., Hutchson S. Response of haemocyte lysosomes to bacterial inoculation in the oysters Ostrea edulis L. and Crassostrea gigas (Thunberg) and the scallop Pecten maximus (L.). Fish Shellfish Immunol. 2001, 11:143-153.
    • (2001) Fish Shellfish Immunol. , vol.11 , pp. 143-153
    • Hauton, C.1    Hawkins, L.E.2    Hutchson, S.3
  • 22
    • 3943059566 scopus 로고    scopus 로고
    • Roles of N-linked glycans in the endoplasmic reticulum
    • Helenius A., Aebi M. Roles of N-linked glycans in the endoplasmic reticulum. Annu. Rev. Biochem. 2004, 73:1019-1049.
    • (2004) Annu. Rev. Biochem. , vol.73 , pp. 1019-1049
    • Helenius, A.1    Aebi, M.2
  • 23
    • 0028126073 scopus 로고
    • Evidence for retrograde traffic between terminal lysosomes and the prelysosomal/late endosome compartment
    • Jahraus A., Storrie B., Griffiths G., Desjardins M. Evidence for retrograde traffic between terminal lysosomes and the prelysosomal/late endosome compartment. J. Cell Sci. 1994, 107:145-157.
    • (1994) J. Cell Sci. , vol.107 , pp. 145-157
    • Jahraus, A.1    Storrie, B.2    Griffiths, G.3    Desjardins, M.4
  • 24
    • 63449091251 scopus 로고    scopus 로고
    • Functional annotation and analysis of expressed sequence tags from the hepatopancreas of mitten crab (Eriocheir sinensis)
    • Jiang H., Cai Y.M., Chen L.Q., Zhang X.W., Hu S.N., Wang Q. Functional annotation and analysis of expressed sequence tags from the hepatopancreas of mitten crab (Eriocheir sinensis). Mar. Biotechnol. 2009, 11:317-326.
    • (2009) Mar. Biotechnol. , vol.11 , pp. 317-326
    • Jiang, H.1    Cai, Y.M.2    Chen, L.Q.3    Zhang, X.W.4    Hu, S.N.5    Wang, Q.6
  • 26
    • 0027373715 scopus 로고
    • Vacuolar/lysosomal proteolysis: proteases, substrates mechanisms
    • Knop M., Schiffer H.H., Rupp S., Wolf D.H. Vacuolar/lysosomal proteolysis: proteases, substrates mechanisms. Curr. Opin. Cell Biol. 1993, 5:990-996.
    • (1993) Curr. Opin. Cell Biol. , vol.5 , pp. 990-996
    • Knop, M.1    Schiffer, H.H.2    Rupp, S.3    Wolf, D.H.4
  • 27
    • 23944468031 scopus 로고    scopus 로고
    • Up-regulation of cathepsin X in Helicobacter pylorigastritis and gastric cancer
    • Krueger S., Kalinski T., Hundertmark T., Wex T., Kuster D., Peitz U. Up-regulation of cathepsin X in Helicobacter pylorigastritis and gastric cancer. J. Pathol. 2005, 207:32-42.
    • (2005) J. Pathol. , vol.207 , pp. 32-42
    • Krueger, S.1    Kalinski, T.2    Hundertmark, T.3    Wex, T.4    Kuster, D.5    Peitz, U.6
  • 28
    • 19344371274 scopus 로고    scopus 로고
    • Interactions between human colon carcinoma cells, fibroblasts and monocytic cells in coculture-regulation of cathepsin B expression and invasiveness
    • Krueger S., Kalinski T., Wolf H., Kellner U., Roessner A. Interactions between human colon carcinoma cells, fibroblasts and monocytic cells in coculture-regulation of cathepsin B expression and invasiveness. Cancer Lett. 2005, 223:313-322.
    • (2005) Cancer Lett. , vol.223 , pp. 313-322
    • Krueger, S.1    Kalinski, T.2    Wolf, H.3    Kellner, U.4    Roessner, A.5
  • 29
    • 0036882393 scopus 로고    scopus 로고
    • Human and parasitic papain-like cysteine proteases: their role in physiology and pathology and recent developments in inhibitor design
    • Lecaille F., Kaleta J., Brömme D. Human and parasitic papain-like cysteine proteases: their role in physiology and pathology and recent developments in inhibitor design. Chem. Rev. 2002, 102:4459-4488.
    • (2002) Chem. Rev. , vol.102 , pp. 4459-4488
    • Lecaille, F.1    Kaleta, J.2    Brömme, D.3
  • 30
    • 0036076660 scopus 로고    scopus 로고
    • Early events in crustacean innate immunity
    • Lee S.Y., Soderhall K. Early events in crustacean innate immunity. Fish Shellfish Immunol. 2002, 12:421-437.
    • (2002) Fish Shellfish Immunol. , vol.12 , pp. 421-437
    • Lee, S.Y.1    Soderhall, K.2
  • 31
    • 0035710746 scopus 로고    scopus 로고
    • Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) Method
    • Livak K.J., Schmittgen T.D. Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) Method. Methods 2001, 25:402-408.
    • (2001) Methods , vol.25 , pp. 402-408
    • Livak, K.J.1    Schmittgen, T.D.2
  • 32
    • 0029752791 scopus 로고    scopus 로고
    • Endocytosis and molecular sorting
    • Mellman I. Endocytosis and molecular sorting. Annu. Rev. Cell Dev. Biol. 1996, 12:575-625.
    • (1996) Annu. Rev. Cell Dev. Biol. , vol.12 , pp. 575-625
    • Mellman, I.1
  • 33
    • 71649106554 scopus 로고    scopus 로고
    • The role of asparagine-linked glycosylation site on the catalytic domain of matriptase in its zymogen activation
    • Miyake Y., Tsuzuki S., Mochida S., Fushiki T., Inouye K. The role of asparagine-linked glycosylation site on the catalytic domain of matriptase in its zymogen activation. Biochim. Biophys. Acta 2010, 1804:156-165.
    • (2010) Biochim. Biophys. Acta , vol.1804 , pp. 156-165
    • Miyake, Y.1    Tsuzuki, S.2    Mochida, S.3    Fushiki, T.4    Inouye, K.5
  • 34
    • 0031240609 scopus 로고    scopus 로고
    • A neural network method for identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites
    • Nielsen H., Engelbrecht J., Brunak S., Von Heijne G. A neural network method for identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites. Int. J. Neural Syst. 1997, 10:581-599.
    • (1997) Int. J. Neural Syst. , vol.10 , pp. 581-599
    • Nielsen, H.1    Engelbrecht, J.2    Brunak, S.3    Von Heijne, G.4
  • 35
    • 0030586280 scopus 로고    scopus 로고
    • The size differences among mammalian introns are due to the accumulation of small deletions
    • Ogata H., Fujibuchi W., Kanehisa M. The size differences among mammalian introns are due to the accumulation of small deletions. FEBS Lett. 1996, 390:99-103.
    • (1996) FEBS Lett. , vol.390 , pp. 99-103
    • Ogata, H.1    Fujibuchi, W.2    Kanehisa, M.3
  • 36
    • 0002704375 scopus 로고
    • Deux cas de keratodermie palmaire et plantaire symetrique familiale (maladie de Meleda) chez le frere et la soeur Coexistence dans les deux cas dalterations dentaires graves
    • Papillon M.M., Lefeevre P. Deux cas de keratodermie palmaire et plantaire symetrique familiale (maladie de Meleda) chez le frere et la soeur Coexistence dans les deux cas dalterations dentaires graves. Bull. Soc. Fr. Dermatol. Syphiligr. 1924, 31:82-87.
    • (1924) Bull. Soc. Fr. Dermatol. Syphiligr. , vol.31 , pp. 82-87
    • Papillon, M.M.1    Lefeevre, P.2
  • 38
    • 0030888065 scopus 로고    scopus 로고
    • Molecular cloning, chromosomal localization, and expression of murine dipeptidyl peptidase I
    • Pham C.T.N., Armstrong R.J., Zimonjic D.B., Popescu N.C., Payan D.G., Ley T.J. Molecular cloning, chromosomal localization, and expression of murine dipeptidyl peptidase I. J. Biol. Chem. 1997, 272:10695-10703.
    • (1997) J. Biol. Chem. , vol.272 , pp. 10695-10703
    • Pham, C.T.N.1    Armstrong, R.J.2    Zimonjic, D.B.3    Popescu, N.C.4    Payan, D.G.5    Ley, T.J.6
  • 39
    • 11844285654 scopus 로고    scopus 로고
    • C transcripts are differentially expressed in the final stages of oocyte maturation in kuruma prawn Marsupenaeus japonicus
    • Qiu G.F., Yamanoa K., Unuma K., Cathepsin C transcripts are differentially expressed in the final stages of oocyte maturation in kuruma prawn Marsupenaeus japonicus. Comp. Biochem. Physiol. 2005, 140:171-181.
    • (2005) Comp. Biochem. Physiol. , vol.140 , pp. 171-181
    • Qiu, G.F.1    Yamanoa, K.2    Unuma, K.3    Cathepsin4
  • 40
    • 44749086356 scopus 로고    scopus 로고
    • Molecular cloning and mRNA expression of cathepsin C gene in black tiger shrimp (Penaeus monodon)
    • Qiu L.H., Jiang S.G., Huang J.H., Wang W.F., Zhang D.C., Wu Q., Yang K. Molecular cloning and mRNA expression of cathepsin C gene in black tiger shrimp (Penaeus monodon). Comp. Biochem. Physiol. 2008, 180:320-325.
    • (2008) Comp. Biochem. Physiol. , vol.180 , pp. 320-325
    • Qiu, L.H.1    Jiang, S.G.2    Huang, J.H.3    Wang, W.F.4    Zhang, D.C.5    Wu, Q.6    Yang, K.7
  • 43
    • 0000810322 scopus 로고    scopus 로고
    • Intrahaemocytic activity of lysosomal enzymes in Penaeus monodon and Macrobrachium rosenbergii
    • Sung H.H., Sun R. Intrahaemocytic activity of lysosomal enzymes in Penaeus monodon and Macrobrachium rosenbergii. Fish Shellfish Immunol. 1999, 9:505-508.
    • (1999) Fish Shellfish Immunol. , vol.9 , pp. 505-508
    • Sung, H.H.1    Sun, R.2
  • 44
    • 0030918546 scopus 로고    scopus 로고
    • Structural and functional aspects of papain-like cysteine proteinases and their protein inhibitors
    • Turk B., Turk V., Turk D. Structural and functional aspects of papain-like cysteine proteinases and their protein inhibitors. Biol. Chem. 1997, 378:141-150.
    • (1997) Biol. Chem. , vol.378 , pp. 141-150
    • Turk, B.1    Turk, V.2    Turk, D.3
  • 45
    • 0037060717 scopus 로고    scopus 로고
    • Rickettsia-like organism associated with tremor disease and mortality of the Chinese mitten crab Eriocheir sinensis
    • Wang W., Gu Z. Rickettsia-like organism associated with tremor disease and mortality of the Chinese mitten crab Eriocheir sinensis. Dis. Aquat. Org. 2002, 48:149-153.
    • (2002) Dis. Aquat. Org. , vol.48 , pp. 149-153
    • Wang, W.1    Gu, Z.2
  • 46
    • 0035881830 scopus 로고    scopus 로고
    • Human cathepsin W, a cysteine protease predominantly expressed in NK cells, is mainly localized in the endoplasmic reticulum
    • Wex T., Buhling F., Wex H., Gunther D., Malfertheiner P., Weber E. Human cathepsin W, a cysteine protease predominantly expressed in NK cells, is mainly localized in the endoplasmic reticulum. J. Immunol. 2001, 167:2172-2178.
    • (2001) J. Immunol. , vol.167 , pp. 2172-2178
    • Wex, T.1    Buhling, F.2    Wex, H.3    Gunther, D.4    Malfertheiner, P.5    Weber, E.6
  • 48
    • 0032546934 scopus 로고    scopus 로고
    • Regulated expression, processing, and secretion of dog mast cell dipeptidyl peptidase I
    • Wolters P.J., Raymond W.W., Blount J.L., Caughey G.H. Regulated expression, processing, and secretion of dog mast cell dipeptidyl peptidase I. J. Biol. Chem. 1998, 273:15514-15520.
    • (1998) J. Biol. Chem. , vol.273 , pp. 15514-15520
    • Wolters, P.J.1    Raymond, W.W.2    Blount, J.L.3    Caughey, G.H.4
  • 49
    • 0033030776 scopus 로고    scopus 로고
    • Localization of rat cathepsin K in osteoclasts and resorption pits: inhibition of bone resorption and cathepsin K-activity by peptidyl vinyl sulfones
    • Xia L., Kilb J., Wex H., Li Z., Lipyansky A., Breuil V. Localization of rat cathepsin K in osteoclasts and resorption pits: inhibition of bone resorption and cathepsin K-activity by peptidyl vinyl sulfones. Biol. Chem. 1999, 380:679-687.
    • (1999) Biol. Chem. , vol.380 , pp. 679-687
    • Xia, L.1    Kilb, J.2    Wex, H.3    Li, Z.4    Lipyansky, A.5    Breuil, V.6
  • 50
    • 2542498171 scopus 로고    scopus 로고
    • Identification of Vibrio parahaemolyticus isolated from cultured Eriocheir sinensis and pathogenicity of its extracellular products
    • Xu H.S., Shu M.A., Zhan X.A., Wang S.X. Identification of Vibrio parahaemolyticus isolated from cultured Eriocheir sinensis and pathogenicity of its extracellular products. J. Fish China 2002, 26:357-362.
    • (2002) J. Fish China , vol.26 , pp. 357-362
    • Xu, H.S.1    Shu, M.A.2    Zhan, X.A.3    Wang, S.X.4
  • 51
    • 36248948251 scopus 로고    scopus 로고
    • Current trends of aquaculture production and sustainable development of Chinese mitten crab Eriocheir sinensis
    • (in Chinese with English abstract)
    • Yang W.L., Zhang G.H. Current trends of aquaculture production and sustainable development of Chinese mitten crab Eriocheir sinensis. Chin. J. Freshwater Fish 2005, vol. 35:62-64. (in Chinese with English abstract).
    • (2005) Chin. J. Freshwater Fish , vol.35 , pp. 62-64
    • Yang, W.L.1    Zhang, G.H.2
  • 52
    • 49749088896 scopus 로고    scopus 로고
    • The lysosome and lysozyme response in Chinese shrimp Fenneropenaeus chinensis to Vibrio anguillarum and laminarin stimulation
    • Yao C.L., Wu C.G., Xiang J.H., Li F.H., Wang Z.Y., Han H.Z. The lysosome and lysozyme response in Chinese shrimp Fenneropenaeus chinensis to Vibrio anguillarum and laminarin stimulation. J. Exp. Mar. Biol. Ecol. 2008, 363:124-129.
    • (2008) J. Exp. Mar. Biol. Ecol. , vol.363 , pp. 124-129
    • Yao, C.L.1    Wu, C.G.2    Xiang, J.H.3    Li, F.H.4    Wang, Z.Y.5    Han, H.Z.6


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