메뉴 건너뛰기




Volumn 580, Issue 14, 2006, Pages 3344-3352

Mycobacterial adenylyl cyclases: Biochemical diversity and structural plasticity

Author keywords

Biochemistry; cAMP; Comparative genomics; Crystal structure; Mutational analysis; Phylogeny

Indexed keywords

ADENYLATE CYCLASE; BACTERIAL ENZYME; CYCLIC AMP; ENZYME MA1120; ENZYME ML1399; ENZYME RV0386; ENZYME RV0891C; ENZYME RV1120C; ENZYME RV1264; ENZYME RV1318C; ENZYME RV1319C; ENZYME RV1320C; ENZYME RV1358; ENZYME RV1359; ENZYME RV1625C; ENZYME RV1647; ENZYME RV1900C; ENZYME RV2212; ENZYME RV2435C; ENZYME RV2488C; ENZYME RV3645; UNCLASSIFIED DRUG;

EID: 33646921482     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2006.05.034     Document Type: Short Survey
Times cited : (52)

References (45)
  • 1
    • 0028317640 scopus 로고
    • Adenylyl cyclases: a heterogeneous class of ATP-utilizing enzymes
    • Barzu O., and Danchin A. Adenylyl cyclases: a heterogeneous class of ATP-utilizing enzymes. Prog. Nucleic Acid Res. Mol. Biol. 49 (1994) 241-283
    • (1994) Prog. Nucleic Acid Res. Mol. Biol. , vol.49 , pp. 241-283
    • Barzu, O.1    Danchin, A.2
  • 2
    • 0042076040 scopus 로고    scopus 로고
    • The catalytic domains of thiamine triphosphatase and CyaB-like adenylyl cyclase define a novel superfamily of domains that bind organic phosphates
    • Iyer L.M., and Aravind L. The catalytic domains of thiamine triphosphatase and CyaB-like adenylyl cyclase define a novel superfamily of domains that bind organic phosphates. BMC Genom. 3 (2002) 33
    • (2002) BMC Genom. , vol.3 , pp. 33
    • Iyer, L.M.1    Aravind, L.2
  • 3
    • 1542298264 scopus 로고    scopus 로고
    • Class III nucleotide cyclases in bacteria and archaebacteria: lineage-specific expansion of adenylyl cyclases and a dearth of guanylyl cyclases
    • Shenoy A.R., and Visweswariah S.S. Class III nucleotide cyclases in bacteria and archaebacteria: lineage-specific expansion of adenylyl cyclases and a dearth of guanylyl cyclases. FEBS Lett. 561 (2004) 11-21
    • (2004) FEBS Lett. , vol.561 , pp. 11-21
    • Shenoy, A.R.1    Visweswariah, S.S.2
  • 4
    • 0032412405 scopus 로고    scopus 로고
    • The structure, catalytic mechanism and regulation of adenylyl cyclase
    • Tesmer J.J., and Sprang S.R. The structure, catalytic mechanism and regulation of adenylyl cyclase. Curr. Opin. Struct. Biol. 8 (1998) 713-719
    • (1998) Curr. Opin. Struct. Biol. , vol.8 , pp. 713-719
    • Tesmer, J.J.1    Sprang, S.R.2
  • 5
    • 0031820874 scopus 로고    scopus 로고
    • Catalytic mechanism and regulation of mammalian adenylyl cyclases
    • Tang W.J., and Hurley J.H. Catalytic mechanism and regulation of mammalian adenylyl cyclases. Mol. Pharmacol. 54 (1998) 231-240
    • (1998) Mol. Pharmacol. , vol.54 , pp. 231-240
    • Tang, W.J.1    Hurley, J.H.2
  • 6
    • 2942566606 scopus 로고    scopus 로고
    • Structure, function and evolution of microbial adenylyl and guanylyl cyclases
    • Baker D.A., and Kelly J.M. Structure, function and evolution of microbial adenylyl and guanylyl cyclases. Mol. Microbiol. 52 (2004) 1229-1242
    • (2004) Mol. Microbiol. , vol.52 , pp. 1229-1242
    • Baker, D.A.1    Kelly, J.M.2
  • 7
    • 0142122328 scopus 로고    scopus 로고
    • The class III adenylyl cyclases: multi-purpose signalling modules
    • Linder J.U., and Schultz J.E. The class III adenylyl cyclases: multi-purpose signalling modules. Cell Signal. 15 (2003) 1081-1089
    • (2003) Cell Signal. , vol.15 , pp. 1081-1089
    • Linder, J.U.1    Schultz, J.E.2
  • 8
    • 0035898614 scopus 로고    scopus 로고
    • Adenylyl cyclase Rv1625c of Mycobacterium tuberculosis: a progenitor of mammalian adenylyl cyclases
    • Guo Y.L., Seebacher T., Kurz U., Linder J.U., and Schultz J.E. Adenylyl cyclase Rv1625c of Mycobacterium tuberculosis: a progenitor of mammalian adenylyl cyclases. EMBO J. 20 (2001) 3667-3675
    • (2001) EMBO J. , vol.20 , pp. 3667-3675
    • Guo, Y.L.1    Seebacher, T.2    Kurz, U.3    Linder, J.U.4    Schultz, J.E.5
  • 9
    • 0038201922 scopus 로고    scopus 로고
    • Mutational analysis of the Mycobacterium tuberculosis Rv1625c adenylyl cyclase: residues that confer nucleotide specificity contribute to dimerization
    • Shenoy A.R., Srinivasan N., Subramaniam M., and Visweswariah S.S. Mutational analysis of the Mycobacterium tuberculosis Rv1625c adenylyl cyclase: residues that confer nucleotide specificity contribute to dimerization. FEBS Lett. 545 (2003) 253-259
    • (2003) FEBS Lett. , vol.545 , pp. 253-259
    • Shenoy, A.R.1    Srinivasan, N.2    Subramaniam, M.3    Visweswariah, S.S.4
  • 10
    • 0035860799 scopus 로고    scopus 로고
    • Eukaryotic-like adenylyl cyclases in Mycobacterium tuberculosis H37Rv: cloning and characterization
    • Reddy S.K., Kamireddi M., Dhanireddy K., Young L., Davis A., and Reddy P.T. Eukaryotic-like adenylyl cyclases in Mycobacterium tuberculosis H37Rv: cloning and characterization. J. Biol. Chem. 276 (2001) 35141-35149
    • (2001) J. Biol. Chem. , vol.276 , pp. 35141-35149
    • Reddy, S.K.1    Kamireddi, M.2    Dhanireddy, K.3    Young, L.4    Davis, A.5    Reddy, P.T.6
  • 11
    • 31344432952 scopus 로고    scopus 로고
    • A structural basis for the role of nucleotide specifying residues in regulating the oligomerization of the Rv1625c adenylyl cyclase from M. tuberculosis
    • Ketkar A.D., Shenoy A.R., Ramagopal U.A., Visweswariah S.S., and Suguna K. A structural basis for the role of nucleotide specifying residues in regulating the oligomerization of the Rv1625c adenylyl cyclase from M. tuberculosis. J. Mol. Biol. 356 (2006) 904-916
    • (2006) J. Mol. Biol. , vol.356 , pp. 904-916
    • Ketkar, A.D.1    Shenoy, A.R.2    Ramagopal, U.A.3    Visweswariah, S.S.4    Suguna, K.5
  • 12
    • 0037013276 scopus 로고    scopus 로고
    • Adenylyl cyclase Rv1264 from Mycobacterium tuberculosis has an autoinhibitory N-terminal domain
    • Linder J.U., Schultz A., and Schultz J.E. Adenylyl cyclase Rv1264 from Mycobacterium tuberculosis has an autoinhibitory N-terminal domain. J. Biol. Chem. 277 (2002) 15271-15276
    • (2002) J. Biol. Chem. , vol.277 , pp. 15271-15276
    • Linder, J.U.1    Schultz, A.2    Schultz, J.E.3
  • 13
    • 18644372238 scopus 로고    scopus 로고
    • The structure of a pH sensing Mycobacterial adenylyl cyclase holoenzyme
    • Tews I., Findeisen F., Sinning I., Schultz A., Schultz J.E., and Linder J.U. The structure of a pH sensing Mycobacterial adenylyl cyclase holoenzyme. Science 308 (2005) 1020-1023
    • (2005) Science , vol.308 , pp. 1020-1023
    • Tews, I.1    Findeisen, F.2    Sinning, I.3    Schultz, A.4    Schultz, J.E.5    Linder, J.U.6
  • 14
    • 15444376813 scopus 로고    scopus 로고
    • Origin of asymmetry in adenylyl cyclases: structures of Mycobacterium tuberculosis Rv1900c
    • Sinha S.C., Wetterer M., Sprang S.R., Schultz J.E., and Linder J.U. Origin of asymmetry in adenylyl cyclases: structures of Mycobacterium tuberculosis Rv1900c. EMBO J. 24 (2005) 663-673
    • (2005) EMBO J. , vol.24 , pp. 663-673
    • Sinha, S.C.1    Wetterer, M.2    Sprang, S.R.3    Schultz, J.E.4    Linder, J.U.5
  • 15
    • 15444374437 scopus 로고    scopus 로고
    • Characterization of phylogenetically distant members of the adenylyl cyclase family from mycobacteria: Rv1647 from M. tuberculosis and its ortholog ML1399 from M. leprae
    • Shenoy A.R., Sreenath N.P., Mahalingam M., and Visweswariah S.S. Characterization of phylogenetically distant members of the adenylyl cyclase family from mycobacteria: Rv1647 from M. tuberculosis and its ortholog ML1399 from M. leprae. Biochem J. 387 (2005) 541-551
    • (2005) Biochem J. , vol.387 , pp. 541-551
    • Shenoy, A.R.1    Sreenath, N.P.2    Mahalingam, M.3    Visweswariah, S.S.4
  • 16
    • 21344433227 scopus 로고    scopus 로고
    • Adenylyl cyclase Rv0386 from Mycobacterium tuberculosis H37Rv uses a novel mode for substrate selection
    • Castro L.I., Hermsen C., Schultz J.E., and Linder J.U. Adenylyl cyclase Rv0386 from Mycobacterium tuberculosis H37Rv uses a novel mode for substrate selection. FEBS J. 272 (2005) 3085-3092
    • (2005) FEBS J. , vol.272 , pp. 3085-3092
    • Castro, L.I.1    Hermsen, C.2    Schultz, J.E.3    Linder, J.U.4
  • 17
    • 0036777599 scopus 로고    scopus 로고
    • Whole-genome comparison of Mycobacterium tuberculosis clinical and laboratory strains
    • Fleischmann R.D., et al. Whole-genome comparison of Mycobacterium tuberculosis clinical and laboratory strains. J. Bacteriol. 184 (2002) 5479-5490
    • (2002) J. Bacteriol. , vol.184 , pp. 5479-5490
    • Fleischmann, R.D.1
  • 18
    • 0032508046 scopus 로고    scopus 로고
    • Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence
    • Cole S.T., et al. Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. Nature 393 (1998) 537-544
    • (1998) Nature , vol.393 , pp. 537-544
    • Cole, S.T.1
  • 19
    • 1542334336 scopus 로고    scopus 로고
    • A survey of nucleotide cyclases in Actinobacteria: unique domain organization and expansion of the class III cyclase family in Mycobacterium tuberculosis
    • Shenoy A.R., Sivakumar K., Krupa A., Srinivasan N., and Visweswariah S.S. A survey of nucleotide cyclases in Actinobacteria: unique domain organization and expansion of the class III cyclase family in Mycobacterium tuberculosis. Comp. Funct. Genom. 5 (2004) 17-38
    • (2004) Comp. Funct. Genom. , vol.5 , pp. 17-38
    • Shenoy, A.R.1    Sivakumar, K.2    Krupa, A.3    Srinivasan, N.4    Visweswariah, S.S.5
  • 20
    • 2942598083 scopus 로고    scopus 로고
    • Functional chimeras between the catalytic domains of the mycobacterial adenylyl cyclase Rv1625c and a Paramecium guanylyl cyclase
    • Linder J.U., Castro L.I., Guo Y.L., and Schultz J.E. Functional chimeras between the catalytic domains of the mycobacterial adenylyl cyclase Rv1625c and a Paramecium guanylyl cyclase. FEBS Lett. 568 (2004) 151-154
    • (2004) FEBS Lett. , vol.568 , pp. 151-154
    • Linder, J.U.1    Castro, L.I.2    Guo, Y.L.3    Schultz, J.E.4
  • 22
    • 0031719202 scopus 로고    scopus 로고
    • Pleiotropic effects of cAMP on germination, antibiotic biosynthesis and morphological development in Streptomyces coelicolor
    • Susstrunk U., Pidoux J., Taubert S., Ullmann A., and Thompson C.J. Pleiotropic effects of cAMP on germination, antibiotic biosynthesis and morphological development in Streptomyces coelicolor. Mol. Microbiol. 30 (1998) 33-46
    • (1998) Mol. Microbiol. , vol.30 , pp. 33-46
    • Susstrunk, U.1    Pidoux, J.2    Taubert, S.3    Ullmann, A.4    Thompson, C.J.5
  • 23
    • 0035845587 scopus 로고    scopus 로고
    • Novel domains of the prokaryotic two-component signal transduction systems
    • Galperin M.Y., Nikolskaya A.N., and Koonin E.V. Novel domains of the prokaryotic two-component signal transduction systems. FEMS Microbiol. Lett. 203 (2001) 11-21
    • (2001) FEMS Microbiol. Lett. , vol.203 , pp. 11-21
    • Galperin, M.Y.1    Nikolskaya, A.N.2    Koonin, E.V.3
  • 24
    • 3042516998 scopus 로고    scopus 로고
    • The effect of HAMP domains on class IIIb adenylyl cyclases from Mycobacterium tuberculosis
    • Linder J.U., Hammer A., and Schultz J.E. The effect of HAMP domains on class IIIb adenylyl cyclases from Mycobacterium tuberculosis. Eur. J. Biochem. 271 (2004) 2446-2451
    • (2004) Eur. J. Biochem. , vol.271 , pp. 2446-2451
    • Linder, J.U.1    Hammer, A.2    Schultz, J.E.3
  • 25
    • 0041315748 scopus 로고    scopus 로고
    • A defined subset of adenylyl cyclases is regulated by bicarbonate ion
    • Cann M.J., Hammer A., Zhou J., and Kanacher T. A defined subset of adenylyl cyclases is regulated by bicarbonate ion. J. Biol. Chem. 278 (2003) 35033-35038
    • (2003) J. Biol. Chem. , vol.278 , pp. 35033-35038
    • Cann, M.J.1    Hammer, A.2    Zhou, J.3    Kanacher, T.4
  • 26
    • 10344257246 scopus 로고    scopus 로고
    • Bicarbonate stimulated adenylyl cyclases
    • Cann M. Bicarbonate stimulated adenylyl cyclases. IUBMB Life 56 (2004) 529-534
    • (2004) IUBMB Life , vol.56 , pp. 529-534
    • Cann, M.1
  • 27
    • 11444256177 scopus 로고    scopus 로고
    • Bicarbonate activation of adenylyl cyclase via promotion of catalytic active site closure and metal recruitment
    • Steegborn C., Litvin T.N., Levin L.R., Buck J., and Wu H. Bicarbonate activation of adenylyl cyclase via promotion of catalytic active site closure and metal recruitment. Nat. Struct. Mol. Biol. 12 (2005) 32-37
    • (2005) Nat. Struct. Mol. Biol. , vol.12 , pp. 32-37
    • Steegborn, C.1    Litvin, T.N.2    Levin, L.R.3    Buck, J.4    Wu, H.5
  • 28
    • 30344471805 scopus 로고    scopus 로고
    • Substrate selection by class III adenylyl cyclases and guanylyl cyclases
    • Linder J.U. Substrate selection by class III adenylyl cyclases and guanylyl cyclases. IUBMB Life 57 (2005) 797-803
    • (2005) IUBMB Life , vol.57 , pp. 797-803
    • Linder, J.U.1
  • 29
    • 20144363828 scopus 로고    scopus 로고
    • An adenylyl cyclase pseudogene in Mycobacterium tuberculosis has a functional ortholog in Mycobacterium avium
    • Shenoy A.R., Srinivas A., Mahalingam M., and Visweswariah S.S. An adenylyl cyclase pseudogene in Mycobacterium tuberculosis has a functional ortholog in Mycobacterium avium. Biochimie 87 (2005) 557-563
    • (2005) Biochimie , vol.87 , pp. 557-563
    • Shenoy, A.R.1    Srinivas, A.2    Mahalingam, M.3    Visweswariah, S.S.4
  • 30
    • 0035448545 scopus 로고    scopus 로고
    • The evolution of mycobacterial pathogenicity: clues from comparative genomics
    • Brosch R., Pym A.S., Gordon S.V., and Cole S.T. The evolution of mycobacterial pathogenicity: clues from comparative genomics. Trends Microbiol. 9 (2001) 452-458
    • (2001) Trends Microbiol. , vol.9 , pp. 452-458
    • Brosch, R.1    Pym, A.S.2    Gordon, S.V.3    Cole, S.T.4
  • 31
    • 12344261833 scopus 로고    scopus 로고
    • The relationship between domain duplication and recombination
    • Vogel C., Teichmann S.A., and Pereira-Leal J. The relationship between domain duplication and recombination. J. Mol. Biol. 346 (2005) 355-365
    • (2005) J. Mol. Biol. , vol.346 , pp. 355-365
    • Vogel, C.1    Teichmann, S.A.2    Pereira-Leal, J.3
  • 32
    • 0036307754 scopus 로고    scopus 로고
    • The geometry of domain combination in proteins
    • Bashton M., and Chothia C. The geometry of domain combination in proteins. J. Mol. Biol. 315 (2002) 927-939
    • (2002) J. Mol. Biol. , vol.315 , pp. 927-939
    • Bashton, M.1    Chothia, C.2
  • 33
  • 34
    • 0016808761 scopus 로고
    • Mycobacterium microti may protect itself from intracellular destruction by releasing cyclic AMP into phagosomes
    • Lowrie D.B., Jackett P.S., and Ratcliffe N.A. Mycobacterium microti may protect itself from intracellular destruction by releasing cyclic AMP into phagosomes. Nature 254 (1975) 600-602
    • (1975) Nature , vol.254 , pp. 600-602
    • Lowrie, D.B.1    Jackett, P.S.2    Ratcliffe, N.A.3
  • 35
    • 0034005701 scopus 로고    scopus 로고
    • Functional classification of cNMP-binding proteins and nucleotide cyclases with implications for novel regulatory pathways in Mycobacterium tuberculosis
    • McCue L.A., McDonough K.A., and Lawrence C.E. Functional classification of cNMP-binding proteins and nucleotide cyclases with implications for novel regulatory pathways in Mycobacterium tuberculosis. Genome Res. 10 (2000) 204-219
    • (2000) Genome Res. , vol.10 , pp. 204-219
    • McCue, L.A.1    McDonough, K.A.2    Lawrence, C.E.3
  • 36
    • 28544433399 scopus 로고    scopus 로고
    • The Rv0805 gene from Mycobacterium tuberculosis encodes a 3′,5′-cyclic nucleotide phosphodiesterase: biochemical and mutational analysis
    • Shenoy A.R., Sreenath N.P., Podobnik M., Kovacevic M., and Visweswariah S.S. The Rv0805 gene from Mycobacterium tuberculosis encodes a 3′,5′-cyclic nucleotide phosphodiesterase: biochemical and mutational analysis. Biochemistry 44 (2005) 15695-15704
    • (2005) Biochemistry , vol.44 , pp. 15695-15704
    • Shenoy, A.R.1    Sreenath, N.P.2    Podobnik, M.3    Kovacevic, M.4    Visweswariah, S.S.5
  • 37
    • 19944418509 scopus 로고    scopus 로고
    • A member of the cAMP receptor protein family of transcription regulators in Mycobacterium tuberculosis is required for virulence in mice and controls transcription of the rpfA gene coding for a resuscitation promoting factor
    • Rickman L., et al. A member of the cAMP receptor protein family of transcription regulators in Mycobacterium tuberculosis is required for virulence in mice and controls transcription of the rpfA gene coding for a resuscitation promoting factor. Mol. Microbiol. 56 (2005) 1274-1286
    • (2005) Mol. Microbiol. , vol.56 , pp. 1274-1286
    • Rickman, L.1
  • 38
    • 14044254213 scopus 로고    scopus 로고
    • Point mutations in the DNA- and cNMP-binding domains of the homologue of the cAMP receptor protein (CRP) in Mycobacterium bovis BCG: implications for the inactivation of a global regulator and strain attenuation
    • Spreadbury C.L., Pallen M.J., Overton T., Behr M.A., Mostowy S., Spiro S., Busby S.J., and Cole J.A. Point mutations in the DNA- and cNMP-binding domains of the homologue of the cAMP receptor protein (CRP) in Mycobacterium bovis BCG: implications for the inactivation of a global regulator and strain attenuation. Microbiology 151 (2005) 547-556
    • (2005) Microbiology , vol.151 , pp. 547-556
    • Spreadbury, C.L.1    Pallen, M.J.2    Overton, T.3    Behr, M.A.4    Mostowy, S.5    Spiro, S.6    Busby, S.J.7    Cole, J.A.8
  • 39
    • 27744449032 scopus 로고    scopus 로고
    • Characterization of Mycobacterium tuberculosis Rv3676 (CRPMt), a cyclic AMP receptor protein-like DNA binding protein
    • Bai G., McCue L.A., and McDonough K.A. Characterization of Mycobacterium tuberculosis Rv3676 (CRPMt), a cyclic AMP receptor protein-like DNA binding protein. J. Bacteriol. 187 (2005) 7795-7804
    • (2005) J. Bacteriol. , vol.187 , pp. 7795-7804
    • Bai, G.1    McCue, L.A.2    McDonough, K.A.3
  • 40
    • 16844377887 scopus 로고    scopus 로고
    • Identification of cyclic AMP-regulated genes in Mycobacterium tuberculosis complex bacteria under low-oxygen conditions
    • Gazdik M.A., and McDonough K.A. Identification of cyclic AMP-regulated genes in Mycobacterium tuberculosis complex bacteria under low-oxygen conditions. J. Bacteriol. 187 (2005) 2681-2692
    • (2005) J. Bacteriol. , vol.187 , pp. 2681-2692
    • Gazdik, M.A.1    McDonough, K.A.2
  • 41
    • 0028943622 scopus 로고
    • Role of cyclic adenosine monophosphate in phospholipid synthesis in Mycobacterium smegmatis ATCC 607
    • Kaur H., and Khuller G.K. Role of cyclic adenosine monophosphate in phospholipid synthesis in Mycobacterium smegmatis ATCC 607. Lipids 30 (1995) 345-349
    • (1995) Lipids , vol.30 , pp. 345-349
    • Kaur, H.1    Khuller, G.K.2
  • 42
    • 0031695464 scopus 로고    scopus 로고
    • Glutamate and cyclic AMP regulate the expression of galactokinase in Mycobacterium smegmatis
    • Raychaudhuri S., Basu M., and Mandal N.C. Glutamate and cyclic AMP regulate the expression of galactokinase in Mycobacterium smegmatis. Microbiology 144 (1998) 2131-2140
    • (1998) Microbiology , vol.144 , pp. 2131-2140
    • Raychaudhuri, S.1    Basu, M.2    Mandal, N.C.3
  • 43
    • 22644446852 scopus 로고    scopus 로고
    • Interaction of Rv1625c, a mycobacterial class IIIa adenylyl cyclase, with a mammalian congener
    • Guo Y.L., et al. Interaction of Rv1625c, a mycobacterial class IIIa adenylyl cyclase, with a mammalian congener. Mol. Microbiol. 57 (2005) 667-677
    • (2005) Mol. Microbiol. , vol.57 , pp. 667-677
    • Guo, Y.L.1
  • 44
    • 3042666256 scopus 로고    scopus 로고
    • MUSCLE: multiple sequence alignment with high accuracy and high throughput
    • Edgar R.C. MUSCLE: multiple sequence alignment with high accuracy and high throughput. Nucleic Acids Res. 32 (2004) 1792-1797
    • (2004) Nucleic Acids Res. , vol.32 , pp. 1792-1797
    • Edgar, R.C.1
  • 45
    • 3242810318 scopus 로고    scopus 로고
    • MEGA3: integrated software for molecular evolutionary genetics analysis and sequence alignment
    • Kumar S., Tamura K., and Nei M. MEGA3: integrated software for molecular evolutionary genetics analysis and sequence alignment. Brief Bioinform. 5 (2004) 150-163
    • (2004) Brief Bioinform. , vol.5 , pp. 150-163
    • Kumar, S.1    Tamura, K.2    Nei, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.