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Volumn 75, Issue 2, 2011, Pages 469-479

Effects of Clostridium difficile Toxin A on the proteome of colonocytes studied by differential 2D electrophoresis

Author keywords

2D DIGE; Caco 2; Clostridium difficile; Proteome map; Toxin A

Indexed keywords

BETA ACTIN; CLOSTRIDIUM DIFFICILE TOXIN A; EZRIN; GLUCOSYLTRANSFERASE; UBIQUITIN;

EID: 82355173202     PISSN: 18743919     EISSN: 18767737     Source Type: Journal    
DOI: 10.1016/j.jprot.2011.08.012     Document Type: Article
Times cited : (13)

References (50)
  • 1
    • 55249105923 scopus 로고    scopus 로고
    • Clostridium difficile-more difficult than ever
    • Kelly C.P., LaMont J.T. Clostridium difficile-more difficult than ever. N Engl J Med 2008, 359:1932-1940.
    • (2008) N Engl J Med , vol.359 , pp. 1932-1940
    • Kelly, C.P.1    LaMont, J.T.2
  • 5
    • 34548472183 scopus 로고    scopus 로고
    • Auto-catalytic cleavage of Clostridium difficile toxins A and B depends on cysteine protease activity
    • Egerer M., Giesemann T., Jank T., Satchell K.J., Aktories K. Auto-catalytic cleavage of Clostridium difficile toxins A and B depends on cysteine protease activity. J Biol Chem 2007, 282:25314-25321.
    • (2007) J Biol Chem , vol.282 , pp. 25314-25321
    • Egerer, M.1    Giesemann, T.2    Jank, T.3    Satchell, K.J.4    Aktories, K.5
  • 7
    • 39649088950 scopus 로고    scopus 로고
    • Clostridium difficile toxins: More than mere inhibitors of Rho proteins
    • Genth H., Dreger S.C., Huelsenbeck J., Just I. Clostridium difficile toxins: More than mere inhibitors of Rho proteins. Int J Biochem Cell Biol 2008, 40:592-597.
    • (2008) Int J Biochem Cell Biol , vol.40 , pp. 592-597
    • Genth, H.1    Dreger, S.C.2    Huelsenbeck, J.3    Just, I.4
  • 8
    • 33846807241 scopus 로고    scopus 로고
    • Difference in the cytotoxic effects of toxin B from Clostridium difficile strain VPI 10463 and toxin B from variant Clostridium difficile strain 1470
    • Huelsenbeck J., Dreger S., Gerhard R., Barth H., Just I., Genth H. Difference in the cytotoxic effects of toxin B from Clostridium difficile strain VPI 10463 and toxin B from variant Clostridium difficile strain 1470. Infect Immun 2006, 75(2):801-809.
    • (2006) Infect Immun , vol.75 , Issue.2 , pp. 801-809
    • Huelsenbeck, J.1    Dreger, S.2    Gerhard, R.3    Barth, H.4    Just, I.5    Genth, H.6
  • 9
    • 34250821092 scopus 로고    scopus 로고
    • Clostridium difficile toxin A-induced apoptosis is p53-independent but depends on glucosylation of Rho GTPases
    • Nottrott S., Schoentaube J., Genth H., Just I., Gerhard R. Clostridium difficile toxin A-induced apoptosis is p53-independent but depends on glucosylation of Rho GTPases. Apoptosis 2007, 12(8):1443-1453.
    • (2007) Apoptosis , vol.12 , Issue.8 , pp. 1443-1453
    • Nottrott, S.1    Schoentaube, J.2    Genth, H.3    Just, I.4    Gerhard, R.5
  • 10
    • 33749257130 scopus 로고    scopus 로고
    • Application of mutated Clostridium difficile toxin A for determination of glucosyltransferase-dependent effects
    • Teichert M., Tatge H., Schoentaube J., Just I., Gerhard R. Application of mutated Clostridium difficile toxin A for determination of glucosyltransferase-dependent effects. Infect Immun 2006, 74(10):6006-6010.
    • (2006) Infect Immun , vol.74 , Issue.10 , pp. 6006-6010
    • Teichert, M.1    Tatge, H.2    Schoentaube, J.3    Just, I.4    Gerhard, R.5
  • 11
    • 0037040188 scopus 로고    scopus 로고
    • Protein kinase C signaling regulates ZO-1 translocation and increased paracellular flux of T84 colonocytes exposed to Clostridium difficile toxin A
    • Chen M.L., Pothoulakis C., LaMont J.T. Protein kinase C signaling regulates ZO-1 translocation and increased paracellular flux of T84 colonocytes exposed to Clostridium difficile toxin A. J Biol Chem 2002, 277:4247-4254.
    • (2002) J Biol Chem , vol.277 , pp. 4247-4254
    • Chen, M.L.1    Pothoulakis, C.2    LaMont, J.T.3
  • 12
    • 0036207579 scopus 로고    scopus 로고
    • Clostridium difficile toxin A triggers human colonocyte IL-8 release via mitochondrial oxygen radical generation
    • He D., Sougioultzis S., Hagen S., Liu J., Keates S., Keates A.C., et al. Clostridium difficile toxin A triggers human colonocyte IL-8 release via mitochondrial oxygen radical generation. Gastroenterology 2002, 122:1048-1057.
    • (2002) Gastroenterology , vol.122 , pp. 1048-1057
    • He, D.1    Sougioultzis, S.2    Hagen, S.3    Liu, J.4    Keates, S.5    Keates, A.C.6
  • 13
    • 28844442756 scopus 로고    scopus 로고
    • Clostridium difficile toxin A-induced colonocyte apoptosis involves p53-dependent p21(WAF1/CIP1) induction via p38 mitogen-activated protein kinase
    • Kim H., Kokkotou E., Na X., Rhee S.H., Moyer M.P., Pothoulakis C., et al. Clostridium difficile toxin A-induced colonocyte apoptosis involves p53-dependent p21(WAF1/CIP1) induction via p38 mitogen-activated protein kinase. Gastroenterology 2005, 129:1875-1888.
    • (2005) Gastroenterology , vol.129 , pp. 1875-1888
    • Kim, H.1    Kokkotou, E.2    Na, X.3    Rhee, S.H.4    Moyer, M.P.5    Pothoulakis, C.6
  • 14
    • 0034234809 scopus 로고    scopus 로고
    • Clostridium difficile toxin A causes early damage to mitochondria in cultured cells
    • He D., Hagen S.J., Pothoulakis C., Chen M., Medina N.D., Warny M., et al. Clostridium difficile toxin A causes early damage to mitochondria in cultured cells. Gastroenterology 2000, 119(1):139-150.
    • (2000) Gastroenterology , vol.119 , Issue.1 , pp. 139-150
    • He, D.1    Hagen, S.J.2    Pothoulakis, C.3    Chen, M.4    Medina, N.D.5    Warny, M.6
  • 15
    • 34247889959 scopus 로고    scopus 로고
    • Clostridium difficile toxin B causes apoptosis in epithelial cells by thrilling mitochondria. Involvement of ATP-sensitive mitochondrial potassium channels
    • Matarrese P., Falzano L., Fabbri A., Gambardella L., Frank C., Geny B., et al. Clostridium difficile toxin B causes apoptosis in epithelial cells by thrilling mitochondria. Involvement of ATP-sensitive mitochondrial potassium channels. J Biol Chem 2007, 282:9029-9041.
    • (2007) J Biol Chem , vol.282 , pp. 9029-9041
    • Matarrese, P.1    Falzano, L.2    Fabbri, A.3    Gambardella, L.4    Frank, C.5    Geny, B.6
  • 16
    • 0041670743 scopus 로고    scopus 로고
    • Expression of recombinant Clostridium difficile toxin A using the Bacillus megaterium system
    • Burger S., Tatge H., Hofmann F., Genth H., Just I., Gerhard R. Expression of recombinant Clostridium difficile toxin A using the Bacillus megaterium system. Biochem Biophys Res Commun 2003, 307:584-588.
    • (2003) Biochem Biophys Res Commun , vol.307 , pp. 584-588
    • Burger, S.1    Tatge, H.2    Hofmann, F.3    Genth, H.4    Just, I.5    Gerhard, R.6
  • 17
    • 34547697437 scopus 로고    scopus 로고
    • Emergence and control of fluoroquinolone-resistant, toxin A-negative, toxin B-positive Clostridium difficile
    • Drudy D., Harnedy N., Fanning S., Hannan M., Kyne L. Emergence and control of fluoroquinolone-resistant, toxin A-negative, toxin B-positive Clostridium difficile. Infect Control Hosp Epidemiol 2007, 28(8):932-940.
    • (2007) Infect Control Hosp Epidemiol , vol.28 , Issue.8 , pp. 932-940
    • Drudy, D.1    Harnedy, N.2    Fanning, S.3    Hannan, M.4    Kyne, L.5
  • 19
  • 20
    • 0022646133 scopus 로고
    • Effect of toxin A and B of Clostridium difficile on rabbit ileum and colon
    • Mitchell T.J., Ketley J.M., Haslam S.C., Stephen J., Burdon D.W., Candy D.C., et al. Effect of toxin A and B of Clostridium difficile on rabbit ileum and colon. Gut 1986, 27(1):78-85.
    • (1986) Gut , vol.27 , Issue.1 , pp. 78-85
    • Mitchell, T.J.1    Ketley, J.M.2    Haslam, S.C.3    Stephen, J.4    Burdon, D.W.5    Candy, D.C.6
  • 21
    • 0023223849 scopus 로고
    • Biological mode of action of Clostridium difficile toxin A: a novel enterotoxin
    • Mitchell T.J., Ketley J.M., Burdon D.W., Candy D.C., Stephen J. Biological mode of action of Clostridium difficile toxin A: a novel enterotoxin. J Med Microbiol 1987, 23(3):211-219.
    • (1987) J Med Microbiol , vol.23 , Issue.3 , pp. 211-219
    • Mitchell, T.J.1    Ketley, J.M.2    Burdon, D.W.3    Candy, D.C.4    Stephen, J.5
  • 22
    • 0021995801 scopus 로고
    • Effects of Clostridium difficile toxins given intragastrically to animals
    • Lyerly D.M., Saum K.E., MacDonald D.K., Wilkins T.D. Effects of Clostridium difficile toxins given intragastrically to animals. Infect Immun 1985, 47:349-352.
    • (1985) Infect Immun , vol.47 , pp. 349-352
    • Lyerly, D.M.1    Saum, K.E.2    MacDonald, D.K.3    Wilkins, T.D.4
  • 23
    • 12544256902 scopus 로고    scopus 로고
    • Clostridium difficile toxin A induces expression of the stress-induced early gene product RhoB
    • Gerhard R., Tatge H., Genth H., Thum T., Borlak J., Fritz G., et al. Clostridium difficile toxin A induces expression of the stress-induced early gene product RhoB. J Biol Chem 2005, 280(2):1499-1505.
    • (2005) J Biol Chem , vol.280 , Issue.2 , pp. 1499-1505
    • Gerhard, R.1    Tatge, H.2    Genth, H.3    Thum, T.4    Borlak, J.5    Fritz, G.6
  • 24
    • 45249093628 scopus 로고    scopus 로고
    • Glucosylation of Rho GTPases by Clostridium difficile toxin A triggers apoptosis in intestinal epithelial cells
    • Gerhard R., Nottrott S., Schoentaube J., Tatge H., Olling A., Just I. Glucosylation of Rho GTPases by Clostridium difficile toxin A triggers apoptosis in intestinal epithelial cells. J Med Microbiol 2008, 57:765-770.
    • (2008) J Med Microbiol , vol.57 , pp. 765-770
    • Gerhard, R.1    Nottrott, S.2    Schoentaube, J.3    Tatge, H.4    Olling, A.5    Just, I.6
  • 25
    • 0017184389 scopus 로고
    • A rapid and sensitive for the quantitation of microgram quantitites of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive for the quantitation of microgram quantitites of protein utilizing the principle of protein-dye binding. Anal Biochem 1976, 72:248-254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 26
    • 33646942752 scopus 로고    scopus 로고
    • Cellular stability of Rho-GTPases glucosylated by Clostridium difficile toxin B
    • Genth H., Huelsenbeck J., Hartmann B., Hofmann F., Just I., Gerhard R. Cellular stability of Rho-GTPases glucosylated by Clostridium difficile toxin B. FEBS Lett 2006, 580:3565-3569.
    • (2006) FEBS Lett , vol.580 , pp. 3565-3569
    • Genth, H.1    Huelsenbeck, J.2    Hartmann, B.3    Hofmann, F.4    Just, I.5    Gerhard, R.6
  • 27
    • 0037253267 scopus 로고    scopus 로고
    • A novel experimental design for comparative two-dimensional gel analysis: two-dimensional difference gel electrophoresis incorporating a pooled internal standard
    • Alban A., David S.O., Bjorkesten L., Andersson C., Sloge E., Lewis S., et al. A novel experimental design for comparative two-dimensional gel analysis: two-dimensional difference gel electrophoresis incorporating a pooled internal standard. Proteomics 2003, 3(1):36-44.
    • (2003) Proteomics , vol.3 , Issue.1 , pp. 36-44
    • Alban, A.1    David, S.O.2    Bjorkesten, L.3    Andersson, C.4    Sloge, E.5    Lewis, S.6
  • 28
    • 34247889959 scopus 로고    scopus 로고
    • Clostridium difficile toxin B causes apoptosis in epithelial cells by thrilling mitochondria. Involvement of ATP-sensitive mitochondrial potassium channels
    • Matarrese P., Falzano L., Fabbri A., Gambardella L., Frank C., Geny B., et al. Clostridium difficile toxin B causes apoptosis in epithelial cells by thrilling mitochondria. Involvement of ATP-sensitive mitochondrial potassium channels. J Biol Chem 2007, 282:9029-9041.
    • (2007) J Biol Chem , vol.282 , pp. 9029-9041
    • Matarrese, P.1    Falzano, L.2    Fabbri, A.3    Gambardella, L.4    Frank, C.5    Geny, B.6
  • 29
    • 34250372908 scopus 로고    scopus 로고
    • Stable isotope labeling by amino acids in cell culture for quantitative proteomics
    • Ong S.E., Mann M. Stable isotope labeling by amino acids in cell culture for quantitative proteomics. Methods Mol Biol 2007, 359:37-52.
    • (2007) Methods Mol Biol , vol.359 , pp. 37-52
    • Ong, S.E.1    Mann, M.2
  • 30
    • 79959424627 scopus 로고    scopus 로고
    • Quantitative, high-resolution proteomics for data-driven systems biology
    • Cox J., Mann M. Quantitative, high-resolution proteomics for data-driven systems biology. Annu Rev Biochem 2011, 80:273-299.
    • (2011) Annu Rev Biochem , vol.80 , pp. 273-299
    • Cox, J.1    Mann, M.2
  • 31
    • 0026802046 scopus 로고
    • A gene family consisting of ezrin, radixin and moesin. Its specific localization at actin filament/plasma membrane association sites
    • Sato N., Funayama N., Nagafuchi A., Yonemura S., Tsukita S., Tsukita S. A gene family consisting of ezrin, radixin and moesin. Its specific localization at actin filament/plasma membrane association sites. J Cell Sci 1992, 103:131-143.
    • (1992) J Cell Sci , vol.103 , pp. 131-143
    • Sato, N.1    Funayama, N.2    Nagafuchi, A.3    Yonemura, S.4    Tsukita, S.5    Tsukita, S.6
  • 32
    • 0031081475 scopus 로고    scopus 로고
    • ERM proteins: head-to-tail regulation of actin-plasma membrane interaction
    • Tsukita S., Yonemura S., Tsukita S. ERM proteins: head-to-tail regulation of actin-plasma membrane interaction. Trends Biochem Sci 1997, 22:53-58.
    • (1997) Trends Biochem Sci , vol.22 , pp. 53-58
    • Tsukita, S.1    Yonemura, S.2    Tsukita, S.3
  • 33
    • 0032498528 scopus 로고    scopus 로고
    • Rho-kinase phosphorylates COOH-terminal threonines of ezrin/radixin/moesin (ERM) proteins and regulates their head-to-tail association
    • Matsui T., Maeda M., Doi Y., Yonemura S., Amano M., Kaibuchi K., et al. Rho-kinase phosphorylates COOH-terminal threonines of ezrin/radixin/moesin (ERM) proteins and regulates their head-to-tail association. J Cell Biol 1998, 140:647-657.
    • (1998) J Cell Biol , vol.140 , pp. 647-657
    • Matsui, T.1    Maeda, M.2    Doi, Y.3    Yonemura, S.4    Amano, M.5    Kaibuchi, K.6
  • 34
    • 0029795488 scopus 로고    scopus 로고
    • Regulation mechanism of ERM (Ezrin/Radixin/Moesin) protein/plasma membrane association: possible involvement of phosphatidylinositol turnover and Rho-dependent signaling pathway
    • Hirao M., Sato N., Kondo T., Yonemura S., Monden M., Sasaki T., et al. Regulation mechanism of ERM (Ezrin/Radixin/Moesin) protein/plasma membrane association: possible involvement of phosphatidylinositol turnover and Rho-dependent signaling pathway. J Cell Biol 1996, 135(1):37-51.
    • (1996) J Cell Biol , vol.135 , Issue.1 , pp. 37-51
    • Hirao, M.1    Sato, N.2    Kondo, T.3    Yonemura, S.4    Monden, M.5    Sasaki, T.6
  • 35
    • 52749086539 scopus 로고    scopus 로고
    • Comparative study of ezrin phosphorylation among different tissues: more is good; too much is bad
    • Zhu L., Hatakeyama J., Chen C., Shastri A., Poon K., Forte J.G. Comparative study of ezrin phosphorylation among different tissues: more is good; too much is bad. Am J Physiol Cell Physiol 2008, 295(1):192-202.
    • (2008) Am J Physiol Cell Physiol , vol.295 , Issue.1 , pp. 192-202
    • Zhu, L.1    Hatakeyama, J.2    Chen, C.3    Shastri, A.4    Poon, K.5    Forte, J.G.6
  • 37
    • 0024472054 scopus 로고
    • Effects of Clostridium difficile toxins A and B on cytoskeleton organization in HEp-2 cells: a comparative morphological study
    • Fiorentini C., Arancia G., Paradisi S., Donelli G., Giuliano M., Piemonte F., et al. Effects of Clostridium difficile toxins A and B on cytoskeleton organization in HEp-2 cells: a comparative morphological study. Toxicon 1989, 27(11):1209-1218.
    • (1989) Toxicon , vol.27 , Issue.11 , pp. 1209-1218
    • Fiorentini, C.1    Arancia, G.2    Paradisi, S.3    Donelli, G.4    Giuliano, M.5    Piemonte, F.6
  • 38
    • 0025367873 scopus 로고
    • Interaction of Clostridium difficile toxin A with cultured cells: cytoskeletal changes and nuclear polarization
    • Fiorentini C., Malorni W., Paradisi S., Giuliano M., Mastrantonio P., Donelli G. Interaction of Clostridium difficile toxin A with cultured cells: cytoskeletal changes and nuclear polarization. Infect Immun 1990, 58(7):2329-2336.
    • (1990) Infect Immun , vol.58 , Issue.7 , pp. 2329-2336
    • Fiorentini, C.1    Malorni, W.2    Paradisi, S.3    Giuliano, M.4    Mastrantonio, P.5    Donelli, G.6
  • 39
    • 21144458164 scopus 로고    scopus 로고
    • Immunoaffinity profiling of tyrosine phosphorylation in cancer cells
    • Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., et al. Immunoaffinity profiling of tyrosine phosphorylation in cancer cells. Nat Biotechnol 2005, 23:94-101.
    • (2005) Nat Biotechnol , vol.23 , pp. 94-101
    • Rush, J.1    Moritz, A.2    Lee, K.A.3    Guo, A.4    Goss, V.L.5    Spek, E.J.6
  • 41
    • 26844559000 scopus 로고    scopus 로고
    • Exponentially modified protein abundance index (emPAI) for estimation of absolute protein amount in proteomics by the number of sequenced peptides per protein
    • Ishihama Y., Oda Y., Tabata T., Sato T., Nagasu T., Rappsilber J., et al. Exponentially modified protein abundance index (emPAI) for estimation of absolute protein amount in proteomics by the number of sequenced peptides per protein. Mol Cell Proteomics 2005, 4(9):1265-1272.
    • (2005) Mol Cell Proteomics , vol.4 , Issue.9 , pp. 1265-1272
    • Ishihama, Y.1    Oda, Y.2    Tabata, T.3    Sato, T.4    Nagasu, T.5    Rappsilber, J.6
  • 43
    • 0025369062 scopus 로고
    • Mapping enteroendocrine cell populations in transgenic mice reveals an unexpected degree of complexity in cellular differentiation within the gastrointestinal tract
    • Roth K.A., Hertz J.M., Gordon J.I. Mapping enteroendocrine cell populations in transgenic mice reveals an unexpected degree of complexity in cellular differentiation within the gastrointestinal tract. J Cell Biol 1990, 110:1791-1801.
    • (1990) J Cell Biol , vol.110 , pp. 1791-1801
    • Roth, K.A.1    Hertz, J.M.2    Gordon, J.I.3
  • 44
    • 0024097375 scopus 로고
    • Mechanisms underlying generation of gradients in gene expression within the intestine: an analysis using transgenic mice containing fatty acid binding protein-human growth hormone fusion genes
    • Sweetser D.A., Birkenmeier E.H., Hoppe P.C., McKeel D.W., Gordon J.I. Mechanisms underlying generation of gradients in gene expression within the intestine: an analysis using transgenic mice containing fatty acid binding protein-human growth hormone fusion genes. Genes Dev 1988, 2:1318-1332.
    • (1988) Genes Dev , vol.2 , pp. 1318-1332
    • Sweetser, D.A.1    Birkenmeier, E.H.2    Hoppe, P.C.3    McKeel, D.W.4    Gordon, J.I.5
  • 45
    • 33846475428 scopus 로고    scopus 로고
    • Role of cytosolic liver fatty acid binding protein in hepatocellular oxidative stress: effect of dexamethasone and clofibrate treatment
    • Rajaraman G., Wang G.Q., Yan J., Jiang P., Gong Y., Burczynski F.J. Role of cytosolic liver fatty acid binding protein in hepatocellular oxidative stress: effect of dexamethasone and clofibrate treatment. Mol Cell Biochem 2007, 295(1-2):27-34.
    • (2007) Mol Cell Biochem , vol.295 , Issue.1-2 , pp. 27-34
    • Rajaraman, G.1    Wang, G.Q.2    Yan, J.3    Jiang, P.4    Gong, Y.5    Burczynski, F.J.6
  • 46
    • 34248590374 scopus 로고    scopus 로고
    • Developmental biology: a chordate with a difference
    • Holland L.Z. Developmental biology: a chordate with a difference. Nature 2007, 447:153-155.
    • (2007) Nature , vol.447 , pp. 153-155
    • Holland, L.Z.1
  • 47
    • 77349124965 scopus 로고    scopus 로고
    • Retinoic acid protects human breast cancer cells against etoposide-induced apoptosis by NF-kappaB-dependent but cIAP2-independent mechanisms
    • Jiménez-Lara A.M., Aranda A., Gronemeyer H. Retinoic acid protects human breast cancer cells against etoposide-induced apoptosis by NF-kappaB-dependent but cIAP2-independent mechanisms. Mol Cancer 2010, 9:15.
    • (2010) Mol Cancer , vol.9 , pp. 15
    • Jiménez-Lara, A.M.1    Aranda, A.2    Gronemeyer, H.3
  • 49
    • 0028206551 scopus 로고
    • A sequence-specific, single-strand binding protein activates the far upstream element of c-myc and defines a new DNA-binding motif
    • Duncan R., Bazar L., Michelotti G., Tomonaga T., Krutzsch H., Avigan M., et al. A sequence-specific, single-strand binding protein activates the far upstream element of c-myc and defines a new DNA-binding motif. Genes Dev 1994, 8(4):465-480.
    • (1994) Genes Dev , vol.8 , Issue.4 , pp. 465-480
    • Duncan, R.1    Bazar, L.2    Michelotti, G.3    Tomonaga, T.4    Krutzsch, H.5    Avigan, M.6
  • 50
    • 35248831220 scopus 로고    scopus 로고
    • Pluripotency redux-advances in stem-cell research
    • Gearhart J., Pashos E.E., Prasad M.K. Pluripotency redux-advances in stem-cell research. N Engl J Med 2007, 357(15):1469-1472.
    • (2007) N Engl J Med , vol.357 , Issue.15 , pp. 1469-1472
    • Gearhart, J.1    Pashos, E.E.2    Prasad, M.K.3


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