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Volumn 54, Issue 1, 2007, Pages 63-73

Cloning and analysis of a novel conserved membrane zinc-metalloprotease family from Solanum surattense

Author keywords

Bioinformatics; Cyanobacteria; G protein coupled receptors; Peptidase; Solanum surattense; Zinc metalloprotease

Indexed keywords

ARABIDOPSIS; ARABIDOPSIS THALIANA; BACTERIA (MICROORGANISMS); CHLOROPHYTA; CYANOBACTERIA; ESCHERICHIA COLI; EUKARYOTA; GOSSYPIUM HIRSUTUM; HORDEUM VULGARE SUBSP. VULGARE; LYCOPERSICON ESCULENTUM; PROKARYOTA; SOLANUM; SOLANUM TUBEROSUM; SOLANUM VIRGINIANUM;

EID: 33846072886     PISSN: 10214437     EISSN: None     Source Type: Journal    
DOI: 10.1134/S1021443707010104     Document Type: Article
Times cited : (3)

References (46)
  • 1
    • 0344668824 scopus 로고    scopus 로고
    • Characterization of a Novel Zinc Metalloprotease Involved in Degrading Targeting Peptides in Mitochondria and Chloroplasts
    • Moberg, P., Stahl, A., Bhushan, S., Wright, S.J., Eriksson, A., Bruce, B.D., and Glaser, E., Characterization of a Novel Zinc Metalloprotease Involved in Degrading Targeting Peptides in Mitochondria and Chloroplasts, Plant J., 2003, vol. 36, pp. 616-628.
    • (2003) Plant J , vol.36 , pp. 616-628
    • Moberg, P.1    Stahl, A.2    Bhushan, S.3    Wright, S.J.4    Eriksson, A.5    Bruce, B.D.6    Glaser, E.7
  • 2
    • 0036882394 scopus 로고    scopus 로고
    • Serine Protease Mechanism and Specificity
    • Hedstrom, L., Serine Protease Mechanism and Specificity, Chem. Rev., 2002, vol. 102, pp. 4501-4523.
    • (2002) Chem. Rev , vol.102 , pp. 4501-4523
    • Hedstrom, L.1
  • 3
    • 0035398526 scopus 로고    scopus 로고
    • A Genomic Perspective on Human Proteases as Drug Targets
    • Southan, C., A Genomic Perspective on Human Proteases as Drug Targets, Drug Discov. Today, 2001, vol. 6, pp. 681-688.
    • (2001) Drug Discov. Today , vol.6 , pp. 681-688
    • Southan, C.1
  • 4
    • 0347445722 scopus 로고    scopus 로고
    • A Genomic Analysis of Rat Proteases and Protease Inhibitors
    • Puente, X.S. and Lopez-Otin, C., A Genomic Analysis of Rat Proteases and Protease Inhibitors, Genome Res., 2004, vol. 14, pp. 609-622.
    • (2004) Genome Res , vol.14 , pp. 609-622
    • Puente, X.S.1    Lopez-Otin, C.2
  • 6
    • 11844252119 scopus 로고    scopus 로고
    • A Cut above the Rest: The Regulatory Function of Plant Proteases
    • Schaller, A., A Cut above the Rest: The Regulatory Function of Plant Proteases, Planta, 2004, vol. 220, pp. 183-197.
    • (2004) Planta , vol.220 , pp. 183-197
    • Schaller, A.1
  • 7
    • 0038019916 scopus 로고    scopus 로고
    • Structural Aspects of the Metzincin Clan of Metalloendopeptidases
    • Gomis-Ruth, F.X., Structural Aspects of the Metzincin Clan of Metalloendopeptidases, Mol. Biotechnol., 2003, vol. 24, pp. 157-202.
    • (2003) Mol. Biotechnol , vol.24 , pp. 157-202
    • Gomis-Ruth, F.X.1
  • 8
    • 0035831262 scopus 로고    scopus 로고
    • A Proteolytic Transmembrane Signaling Pathway and Resistance to beta-Lactams in Staphylococci
    • Zhang, H.Z., Hackbarth, C.J., Chansky, K.M., and Chambers, H.F., A Proteolytic Transmembrane Signaling Pathway and Resistance to beta-Lactams in Staphylococci, Science, 2001, vol. 291, pp. 1962-1965.
    • (2001) Science , vol.291 , pp. 1962-1965
    • Zhang, H.Z.1    Hackbarth, C.J.2    Chansky, K.M.3    Chambers, H.F.4
  • 9
    • 0036007414 scopus 로고    scopus 로고
    • Shedding Light on Sheddases: Role in Growth and Development
    • Kheradmand, F. and Werb, Z., Shedding Light on Sheddases: Role in Growth and Development, BioEssay, 2002, vol. 24, pp. 8-12.
    • (2002) BioEssay , vol.24 , pp. 8-12
    • Kheradmand, F.1    Werb, Z.2
  • 10
    • 0029036451 scopus 로고
    • Evolutionary Families of Metallopeptidases
    • Abelson, J.N, Simon, M.I, and Barrett, A.J, Eds, San Diego: Academic
    • Rawlings, N.D. and Barrett, A.J., Evolutionary Families of Metallopeptidases, Proteolytic Enzymes: Aspartic and Metallo Peptidases, Abelson, J.N., Simon, M.I., and Barrett, A.J., Eds., San Diego: Academic, 1995, pp. 183-228.
    • (1995) Proteolytic Enzymes: Aspartic and Metallo Peptidases , pp. 183-228
    • Rawlings, N.D.1    Barrett, A.J.2
  • 13
    • 0025272240 scopus 로고
    • Rapid and Sensitive Sequence Comparison with Fastp and Fasta
    • Pearson, W.R., Rapid and Sensitive Sequence Comparison with Fastp and Fasta, Nucleic Acids Res., 1990, vol. 183, pp. 63-98.
    • (1990) Nucleic Acids Res , vol.183 , pp. 63-98
    • Pearson, W.R.1
  • 14
    • 0027968068 scopus 로고
    • Clustal-W - Improving the Sensitivity of Progressive Multiple Sequence Alignment through Sequence Weighting, Position-Specific Gap Penalties and Weight Matrix Choice
    • Thompson, J.D., Higgins, D.G., and Gibson, T.J., Clustal-W - Improving the Sensitivity of Progressive Multiple Sequence Alignment through Sequence Weighting, Position-Specific Gap Penalties and Weight Matrix Choice, Nucleic Acids Res., 1994, vol. 22, pp. 4673-4680.
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 15
    • 0027105007 scopus 로고
    • A Knowledge Base for Predicting Protein Localization Sites in Eukaryotic Cells
    • Nakai, K. and Kanehisa, M., A Knowledge Base for Predicting Protein Localization Sites in Eukaryotic Cells, Genomics, 1992, vol. 14, pp. 897-911.
    • (1992) Genomics , vol.14 , pp. 897-911
    • Nakai, K.1    Kanehisa, M.2
  • 16
    • 0036187913 scopus 로고    scopus 로고
    • Extensive Feature Detection of N-Terminal Protein Sorting Signals
    • Bannai, H., Tamada, Y., Maruyama, O., Nakai, K., and Miyano, S., Extensive Feature Detection of N-Terminal Protein Sorting Signals, Nucleic Acids Res., 2002, vol. 18, pp. 298-305.
    • (2002) Nucleic Acids Res , vol.18 , pp. 298-305
    • Bannai, H.1    Tamada, Y.2    Maruyama, O.3    Nakai, K.4    Miyano, S.5
  • 17
    • 0034697980 scopus 로고    scopus 로고
    • Predicting Subcellular Localization of Proteins Based on Their N-Terminal Amino Acid Sequence
    • Emanuelsson, O., Nielsen, H., Brunak, S., and von Heijne, G., Predicting Subcellular Localization of Proteins Based on Their N-Terminal Amino Acid Sequence, Nucleic Acids Res., 2000, vol. 300, pp. 1005-1016.
    • (2000) Nucleic Acids Res , vol.300 , pp. 1005-1016
    • Emanuelsson, O.1    Nielsen, H.2    Brunak, S.3    von Heijne, G.4
  • 19
    • 0032935861 scopus 로고    scopus 로고
    • ChloroP, a Neural Network-Based Method for Predicting Chloroplast Transit Peptides and Their Cleavage Sites
    • Emanuelsson, O., Nielsen, H., and von Heijne, G., ChloroP, a Neural Network-Based Method for Predicting Chloroplast Transit Peptides and Their Cleavage Sites, Protein Sci., 1999, vol. 8, pp. 978-984.
    • (1999) Protein Sci , vol.8 , pp. 978-984
    • Emanuelsson, O.1    Nielsen, H.2    von Heijne, G.3
  • 20
    • 0029915525 scopus 로고    scopus 로고
    • Computational Method to Predict Mitochondrially Imported Proteins and Their Targeting Sequences
    • Claros, M.G. and Vincens, P., Computational Method to Predict Mitochondrially Imported Proteins and Their Targeting Sequences, Eur. J. Biochem., 1996, vol. 241, pp. 779-786.
    • (1996) Eur. J. Biochem , vol.241 , pp. 779-786
    • Claros, M.G.1    Vincens, P.2
  • 21
    • 0035910270 scopus 로고    scopus 로고
    • Predicting Transmembrane Protein Topology with a Hidden Markov Model: Application to Complete Genomes
    • Krogh, A., Larsson, B., von Heijne, G., and Sonnhammer, E.L.L., Predicting Transmembrane Protein Topology with a Hidden Markov Model: Application to Complete Genomes, Nucleic Acids Res., 2001, vol. 305, pp. 567-580.
    • (2001) Nucleic Acids Res , vol.305 , pp. 567-580
    • Krogh, A.1    Larsson, B.2    von Heijne, G.3    Sonnhammer, E.L.L.4
  • 23
    • 0033579464 scopus 로고    scopus 로고
    • Sequence and Structure-Based Prediction of Eukaryotic Protein Phosphorylation Sites
    • Blom, N., Gammeltoft, S., and Brunak, S., Sequence and Structure-Based Prediction of Eukaryotic Protein Phosphorylation Sites, J. Mol. Biol., 1999, vol. 294, pp. 1351-1362.
    • (1999) J. Mol. Biol , vol.294 , pp. 1351-1362
    • Blom, N.1    Gammeltoft, S.2    Brunak, S.3
  • 25
    • 0032568655 scopus 로고    scopus 로고
    • SMART, a Simple Modular Architecture Research Tool: Identification of Signaling Domains
    • Schultz, J., Milpetz, F., Bork, P., and Ponting, C.P., SMART, a Simple Modular Architecture Research Tool: Identification of Signaling Domains, Proc. Natl. Acad. Sci. USA, 1998, vol. 95, pp. 5857-5864.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 5857-5864
    • Schultz, J.1    Milpetz, F.2    Bork, P.3    Ponting, C.P.4
  • 26
    • 3242887157 scopus 로고    scopus 로고
    • CD-Search: Protein Domain Annotations on the Fly
    • Marchler-Bauer, A. and Bryant, S.H., CD-Search: Protein Domain Annotations on the Fly, Nucleic Acids Res., 2004, vol. 32, pp. W327-W331.
    • (2004) Nucleic Acids Res , vol.32
    • Marchler-Bauer, A.1    Bryant, S.H.2
  • 28
    • 0030614169 scopus 로고    scopus 로고
    • Salicylic Acid and Disease Resistance in Plants
    • Durner, J., Shah, J., and Kessig, D.F., Salicylic Acid and Disease Resistance in Plants, Trends Plant Sci., 1997, vol. 2, pp. 266-274.
    • (1997) Trends Plant Sci , vol.2 , pp. 266-274
    • Durner, J.1    Shah, J.2    Kessig, D.F.3
  • 29
    • 0032129686 scopus 로고    scopus 로고
    • Ethylene, and Disease in Plants
    • Dong, X., SA, JA, Ethylene, and Disease in Plants, Curr. Opin. Plant Biol., 1998, vol. 1, pp. 316-323.
    • (1998) Curr. Opin. Plant Biol , vol.1 , pp. 316-323
    • Dong, X.1    JA, S.A.2
  • 30
    • 0037624063 scopus 로고    scopus 로고
    • Kikuchi, S, Satoh, K, Nagata, T, Kawagashira, N, Doi, K, Kishimoto, N, Yazaki, J, Ishikawa, M, Yamada, H, Ooka, H, Hotta, I, Kojima, K, Namiki, T, Ohneda, E, Yahagi, W, Suzuki, K, Li, C.J, Ohtsuki, K, Shishiki, T, Otomo, Y, Murakami, K, Iida, Y, Sugano, S, Fujimura, T, Suzuki, Y, Tsunoda, Y, Kurosaki, T, Kodama, T, Masuda, H, Kobayashi, M, Xie, Q.H, Lu, M, Narikawa, R, Sugiyama, A, Mizuno, K, Yokomizo, S, Niikura, J, Ikeda, R, Ishibiki, J, Kawamata, M, Yoshimura, A, Miura, J, Kusumegi, T, Oka, M, Ryu, R, Ueda, M, Matsubara, K, Kawai, J, Carninci, P, Adachi, J, Aizawa, K, Arakawa, T, Fukuda, S, Hara, A, Hashizume, W, Hayatsu, N, Imotani, K, Ishii, Y, Itoh, M, Kagawa, I, Kondo, S, Konno, H, Miyazaki, A, Osato, N, Ota, Y, Saito, R, Sasaki, D, Sato, K, Shibata, K, Shinagawa, A, Shiraki, T, Yoshino, M, Hayashizaki, Y, and Yasunishi, A, Collection, Mapping, and Annotation of over 28,000 cDNA Clones from Japonica Rice
    • Kikuchi, S., Satoh, K., Nagata, T., Kawagashira, N., Doi, K., Kishimoto, N., Yazaki, J., Ishikawa, M., Yamada, H., Ooka, H., Hotta, I., Kojima, K., Namiki, T., Ohneda, E., Yahagi, W., Suzuki, K., Li, C.J., Ohtsuki, K., Shishiki, T., Otomo, Y., Murakami, K., Iida, Y., Sugano, S., Fujimura, T., Suzuki, Y., Tsunoda, Y., Kurosaki, T., Kodama, T., Masuda, H., Kobayashi, M., Xie, Q.H., Lu, M., Narikawa, R., Sugiyama, A., Mizuno, K., Yokomizo, S., Niikura, J., Ikeda, R., Ishibiki, J., Kawamata, M., Yoshimura, A., Miura, J., Kusumegi, T., Oka, M., Ryu, R., Ueda, M., Matsubara, K., Kawai, J., Carninci, P., Adachi, J., Aizawa, K., Arakawa, T., Fukuda, S., Hara, A., Hashizume, W., Hayatsu, N., Imotani, K., Ishii, Y., Itoh, M., Kagawa, I., Kondo, S., Konno, H., Miyazaki, A., Osato, N., Ota, Y., Saito, R., Sasaki, D., Sato, K., Shibata, K., Shinagawa, A., Shiraki, T., Yoshino, M., Hayashizaki, Y., and Yasunishi, A., Collection, Mapping, and Annotation of over 28,000 cDNA Clones from Japonica Rice, Science, 2003, vol. 301, pp. 376-379.
  • 32
    • 33846066448 scopus 로고    scopus 로고
    • Sporulation Factor SpoIVFB
    • Barrett, A, Rawlings, N, and Woessner, J, Eds, London: Elsevier
    • Dong, T. and Cutting, S., Sporulation Factor SpoIVFB, Handbook of Proteolytic Enzymes, Barrett, A., Rawlings, N., and Woessner, J., Eds., London: Elsevier, 2004, pp. 989-991.
    • (2004) Handbook of Proteolytic Enzymes , pp. 989-991
    • Dong, T.1    Cutting, S.2
  • 33
    • 0034035286 scopus 로고    scopus 로고
    • Evidence that SpoIVFB Is a Novel Type of Membrane Metalloprotease Governing Intercompartmental Communication during Bacillus subtilis Sporulation
    • Yu, Y.T.N. and Kroos, L., Evidence that SpoIVFB Is a Novel Type of Membrane Metalloprotease Governing Intercompartmental Communication during Bacillus subtilis Sporulation, J. Bacteriol., 2000, vol. 182, pp. 3305-3309.
    • (2000) J. Bacteriol , vol.182 , pp. 3305-3309
    • Yu, Y.T.N.1    Kroos, L.2
  • 34
    • 0027263747 scopus 로고
    • Identification of Glutamate-169 as the 3rd Zinc-Binding Residue in Proteinase-111, a Member of the Family of Insulin-Degrading Enzymes
    • Becker, A.B. and Roth, R.A., Identification of Glutamate-169 as the 3rd Zinc-Binding Residue in Proteinase-111, a Member of the Family of Insulin-Degrading Enzymes, Biochem. J., 1993, vol. 292, pp. 137-142.
    • (1993) Biochem. J , vol.292 , pp. 137-142
    • Becker, A.B.1    Roth, R.A.2
  • 35
    • 0027454093 scopus 로고
    • Functional Analysis of Conserved Residues in the Active Site of Insulin-Degrading Enzyme
    • Perlman, R.K., Gehm, B.D., Kuo, W.L., and Rosner, M.R., Functional Analysis of Conserved Residues in the Active Site of Insulin-Degrading Enzyme, J. Biol. Chem., 1993, vol. 268, pp. 21538-21544.
    • (1993) J. Biol. Chem , vol.268 , pp. 21538-21544
    • Perlman, R.K.1    Gehm, B.D.2    Kuo, W.L.3    Rosner, M.R.4
  • 36
    • 0028587344 scopus 로고
    • Identification of Zinc Ligands of the Insulin-Degrading Enzyme
    • Perlman, R.K. and Rosner, M.R., Identification of Zinc Ligands of the Insulin-Degrading Enzyme, J. Biol. Chem., 1994, vol. 269, pp. 33140-33145.
    • (1994) J. Biol. Chem , vol.269 , pp. 33140-33145
    • Perlman, R.K.1    Rosner, M.R.2
  • 37
    • 0032508046 scopus 로고    scopus 로고
    • Cole, S.T., Brosch, R., Parkhill, J., Garnier, T., Churcher, C., Harris, D., Gordon, S.V., Eiglmeier, K., Gas, S., Barry, C.E. III, Tekaia, F., Badcock, K., Basham, D., Brown, D., Chillingworth, T., Connor, R., Davies, R., Devlin, K., Feltwell, T., Gentles, S., Hamlin, N., Holroyd, S., Hornsby, T., Jagels, K., Krogh, A., McLean, J., Moule, S., Murphy, L., Oliver, K., Osborne, J., Quail, M.A., Rajandream, M.-A., Rogers, J., Rutter, S., Seeger, K., Skelton, J., Squares, R., Squares, S., Sulston, J.E., Taylor, K., Whitehead, S., and Barrell, B.G., Deciphering the Biology of Mycobacterium tuberculosis from the Complete Genome Sequence, Nature, 1998, 393, pp. 537-544.
    • Cole, S.T., Brosch, R., Parkhill, J., Garnier, T., Churcher, C., Harris, D., Gordon, S.V., Eiglmeier, K., Gas, S., Barry, C.E. III, Tekaia, F., Badcock, K., Basham, D., Brown, D., Chillingworth, T., Connor, R., Davies, R., Devlin, K., Feltwell, T., Gentles, S., Hamlin, N., Holroyd, S., Hornsby, T., Jagels, K., Krogh, A., McLean, J., Moule, S., Murphy, L., Oliver, K., Osborne, J., Quail, M.A., Rajandream, M.-A., Rogers, J., Rutter, S., Seeger, K., Skelton, J., Squares, R., Squares, S., Sulston, J.E., Taylor, K., Whitehead, S., and Barrell, B.G., Deciphering the Biology of Mycobacterium tuberculosis from the Complete Genome Sequence, Nature, 1998, vol. 393, pp. 537-544.
  • 38
    • 0026071908 scopus 로고
    • Structure-Function Relationship of Proteins Belonging to the Family of Receptors Coupled to GTP-Binding Proteins
    • Strosberg, A.D., Structure-Function Relationship of Proteins Belonging to the Family of Receptors Coupled to GTP-Binding Proteins, Eur. J. Biochem., 1991, vol. 196, pp. 1-10.
    • (1991) Eur. J. Biochem , vol.196 , pp. 1-10
    • Strosberg, A.D.1
  • 40
    • 0036078874 scopus 로고    scopus 로고
    • Mutagenesis and Peptide Analysis of the DRY Motif in the Alpha 2A Adrenergic Receptor: Evidence for Alternate Mechanisms in G Protein-Coupled Receptors
    • Chung, D.A., Wade, S.M., Fowler, C.B., Woods, D.D., Abada, P.B., Mosberg, H.L., and Neubig, R.R., Mutagenesis and Peptide Analysis of the DRY Motif in the Alpha 2A Adrenergic Receptor: Evidence for Alternate Mechanisms in G Protein-Coupled Receptors, Biochem. Biophys. Res. Commun., 2002, vol. 293, pp. 1233-1241.
    • (2002) Biochem. Biophys. Res. Commun , vol.293 , pp. 1233-1241
    • Chung, D.A.1    Wade, S.M.2    Fowler, C.B.3    Woods, D.D.4    Abada, P.B.5    Mosberg, H.L.6    Neubig, R.R.7
  • 41
    • 0034112037 scopus 로고    scopus 로고
    • The Effect of Mutations in the DRY Motif on the Constitutive Activity and Structural Instability of the Histamine H-2 Receptor
    • Alewijnse, A.E., Timmerman, H., Jacobs, E.H., Smit, M.J., Roovers, E., Cotecchia, S., and Leurs, R., The Effect of Mutations in the DRY Motif on the Constitutive Activity and Structural Instability of the Histamine H-2 Receptor, Mol. Pharmacol., 2000, vol. 57, pp. 890-898.
    • (2000) Mol. Pharmacol , vol.57 , pp. 890-898
    • Alewijnse, A.E.1    Timmerman, H.2    Jacobs, E.H.3    Smit, M.J.4    Roovers, E.5    Cotecchia, S.6    Leurs, R.7
  • 42
    • 0033049565 scopus 로고    scopus 로고
    • Constitutively Active alpha-1b Adrenergic Receptor Mutants Display Different Phosphorylation and Internalization Features
    • Mhaouty-Kodja, S., Barak, L.S., Scheer, A., Abuin, L., Diviani, D., Caron, M.G., and Cotecchia, S., Constitutively Active alpha-1b Adrenergic Receptor Mutants Display Different Phosphorylation and Internalization Features, Mol. Pharmacol., 1999, vol. 55, pp. 339-347.
    • (1999) Mol. Pharmacol , vol.55 , pp. 339-347
    • Mhaouty-Kodja, S.1    Barak, L.S.2    Scheer, A.3    Abuin, L.4    Diviani, D.5    Caron, M.G.6    Cotecchia, S.7
  • 44
    • 0032510320 scopus 로고    scopus 로고
    • A Higher Plant Seven-Transmembrane Receptor That Influences Sensitivity to Cytokinins
    • Plakidou-Dymock, S., Dymock, D., and Hooley, R., A Higher Plant Seven-Transmembrane Receptor That Influences Sensitivity to Cytokinins, Curr. Biol., 1998, vol. 8, pp. 315-324.
    • (1998) Curr. Biol , vol.8 , pp. 315-324
    • Plakidou-Dymock, S.1    Dymock, D.2    Hooley, R.3
  • 45
    • 0030701839 scopus 로고    scopus 로고
    • Cloning of a Putative G-Protein-Coupled Receptor from Arabidopsis thaliana
    • Josefsson, L.G. and Rask, L., Cloning of a Putative G-Protein-Coupled Receptor from Arabidopsis thaliana, Eur. J. Biochem., 1997, vol. 249, pp. 415-420.
    • (1997) Eur. J. Biochem , vol.249 , pp. 415-420
    • Josefsson, L.G.1    Rask, L.2
  • 46
    • 0037007028 scopus 로고    scopus 로고
    • GCR1, the Putative Arabidopsis G Protein-Coupled Receptor Gene Is Cell Cycle-Regulated, and Its Overexpression Abolishes Seed Dormancy and Shortens Time to Flowering
    • Colucci, G., Apone, F., Alyeshmerni, N., Chalmers, D., and Chrispeels, M.J., GCR1, the Putative Arabidopsis G Protein-Coupled Receptor Gene Is Cell Cycle-Regulated, and Its Overexpression Abolishes Seed Dormancy and Shortens Time to Flowering, Proc. Natl. Acad. Sci. USA, 2002, vol. 99, pp. 4736-4741.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 4736-4741
    • Colucci, G.1    Apone, F.2    Alyeshmerni, N.3    Chalmers, D.4    Chrispeels, M.J.5


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