메뉴 건너뛰기




Volumn 59, Issue 4, 2006, Pages 1341-1356

Predicting metals sensed by ArsR-SmtB repressors: Allosteric interference by a non-effector metal

Author keywords

[No Author keywords available]

Indexed keywords

ANTIMONY DERIVATIVE; ARSENIC TRIOXIDE; BACTERIAL PROTEIN; CUPRIC ION; DNA; DNA BINDING PROTEIN; GENE PRODUCT; PROTEIN ARSR SMTB REPRESSOR; PROTEIN ASER; PROTEIN CZRA; THIOL DERIVATIVE; UNCLASSIFIED DRUG; ZINC;

EID: 33645049326     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/j.1365-2958.2006.05029.x     Document Type: Article
Times cited : (37)

References (58)
  • 1
    • 0037465337 scopus 로고    scopus 로고
    • Understanding copper trafficking in bacteria: Interaction between the copper transport protein CopZ and the N-terminal domain of the copper ATPase CopA from Bacillus subtilis
    • Banci L. Bertini I. Ciofi-Baffoni S. Del-Conte R. Gionnelli L. 2003 Understanding copper trafficking in bacteria: interaction between the copper transport protein CopZ and the N-terminal domain of the copper ATPase CopA from Bacillus subtilis Biochemistry 42 1939 1949
    • (2003) Biochemistry , vol.42 , pp. 1939-1949
    • Banci, L.1    Bertini, I.2    Ciofi-Baffoni, S.3    Del-Conte, R.4    Gionnelli, L.5
  • 2
    • 3042551157 scopus 로고    scopus 로고
    • Solution structures of a cyanobacterial metallochaperone: Insight into an atypical copper-binding motif
    • Banci L. Bertini I. Ciofi-Baffoni S. Su XC. Borrelly GPM. Robinson NJ. 2004 Solution structures of a cyanobacterial metallochaperone: insight into an atypical copper-binding motif J Biol Chem 279 27502 27510
    • (2004) J Biol Chem , vol.279 , pp. 27502-27510
    • Banci, L.1    Bertini, I.2    Ciofi-Baffoni, S.3    Su, X.C.4    Borrelly, G.P.M.5    Robinson, N.J.6
  • 5
    • 3142632027 scopus 로고    scopus 로고
    • 1-type ATPases and their transcriptional regulators: Contributions of a cytosolic amino-terminal domain to metal-specificity
    • 1-type ATPases and their transcriptional regulators: contributions of a cytosolic amino-terminal domain to metal-specificity Mol Microbiol 53 217 227
    • (2004) Mol Microbiol , vol.53 , pp. 217-227
    • Borrelly, G.P.M.1    Rondet, S.A.2    Tottey, S.3    Robinson, N.J.4
  • 7
    • 0036301096 scopus 로고    scopus 로고
    • Elucidation of the primary (α3N) and vestigial (α5) heavy metal binding sites in Staphylococcus aureus pI258 CadC: Evolutionary implications for metal ion selectivity of ArsR/SmtB metal sensor proteins
    • Busenlehner LS. Weng T-C. Penner-Hahn JE. Giedroc DP. 2002 Elucidation of the primary (α3N) and vestigial (α5) heavy metal binding sites in Staphylococcus aureus pI258 CadC: evolutionary implications for metal ion selectivity of ArsR/SmtB metal sensor proteins J Mol Biol 319 685 701
    • (2002) J Mol Biol , vol.319 , pp. 685-701
    • Busenlehner, L.S.1    Weng, T.-C.2    Penner-Hahn, J.E.3    Giedroc, D.P.4
  • 8
    • 0037565104 scopus 로고    scopus 로고
    • The SmtB/ArsR family of metalloregulatory transcriptional repressors: Structural insights into prokaryotic metal resistance
    • Busenlehner LS. Pennella MA. Giedroc DP. 2003 The SmtB/ArsR family of metalloregulatory transcriptional repressors: structural insights into prokaryotic metal resistance FEMS Microbiol Rev 27 131 143
    • (2003) FEMS Microbiol Rev , vol.27 , pp. 131-143
    • Busenlehner, L.S.1    Pennella, M.A.2    Giedroc, D.P.3
  • 9
    • 0037064122 scopus 로고    scopus 로고
    • A nickel-cobalt sensing ArsR-SmtB family repressor: Contributions of cytosol and effector binding sites to metal selectivity
    • Cavet JS. Meng W. Pennella MA. Appelhoff RJ. Giedroc DP. Robinson NJ. 2002 A nickel-cobalt sensing ArsR-SmtB family repressor: contributions of cytosol and effector binding sites to metal selectivity J Biol Chem 277 38441 38448
    • (2002) J Biol Chem , vol.277 , pp. 38441-38448
    • Cavet, J.S.1    Meng, W.2    Pennella, M.A.3    Appelhoff, R.J.4    Giedroc, D.P.5    Robinson, N.J.6
  • 10
    • 0242582330 scopus 로고    scopus 로고
    • A cadmium-lead sensing ArsR-SmtB repressor with novel sensory sites: Complementary metal-discrimination by NmtR and CmtR in a common cytosol
    • Cavet JS. Graham AI. Meng W. Robinson NJ. 2003 A cadmium-lead sensing ArsR-SmtB repressor with novel sensory sites: complementary metal-discrimination by NmtR and CmtR in a common cytosol J Biol Chem 278 44560 44566
    • (2003) J Biol Chem , vol.278 , pp. 44560-44566
    • Cavet, J.S.1    Graham, A.I.2    Meng, W.3    Robinson, N.J.4
  • 13
    • 0032536158 scopus 로고    scopus 로고
    • Crystal structure of the cyanobacterial metallothionein repressor SmtB: A model for metalloregulatory proteins
    • Cook WJ. Kar SR. Taylor KB. Hall LM. 1998 Crystal structure of the cyanobacterial metallothionein repressor SmtB: a model for metalloregulatory proteins J Mol Biol 275 337 347
    • (1998) J Mol Biol , vol.275 , pp. 337-347
    • Cook, W.J.1    Kar, S.R.2    Taylor, K.B.3    Hall, L.M.4
  • 15
    • 0029128733 scopus 로고
    • CadC, the transcriptional regulatory protein of the cadmium resistance system of Staphylococcus aureus plasmid pI258
    • Endo G. Silver S. 1995 CadC, the transcriptional regulatory protein of the cadmium resistance system of Staphylococcus aureus plasmid pI258 J Bacteriol 177 4437 4441
    • (1995) J Bacteriol , vol.177 , pp. 4437-4441
    • Endo, G.1    Silver, S.2
  • 17
    • 0038246333 scopus 로고    scopus 로고
    • Bacillus subtilis CPx-type ATPases: Characterisation of Cd, Zn, Co and Cu efflux systems
    • Gaballa A. Helmann JD. 2003 Bacillus subtilis CPx-type ATPases: characterisation of Cd, Zn, Co and Cu efflux systems Biometals 16 497 505
    • (2003) Biometals , vol.16 , pp. 497-505
    • Gaballa, A.1    Helmann, J.D.2
  • 18
    • 0036889461 scopus 로고    scopus 로고
    • Functional analysis of the Bacillus subtilis Zur regulon
    • Gaballa A. Wang T. Ye RW. Helmann JD. 2002 Functional analysis of the Bacillus subtilis Zur regulon J Bacteriol 184 6508 6514
    • (2002) J Bacteriol , vol.184 , pp. 6508-6514
    • Gaballa, A.1    Wang, T.2    Ye, R.W.3    Helmann, J.D.4
  • 19
    • 0346252345 scopus 로고    scopus 로고
    • Two MerR homologues that affect copper induction of the Bacillus subtilis copZA operon
    • Gaballa A. Cao M. Helmann JD. 2003 Two MerR homologues that affect copper induction of the Bacillus subtilis copZA operon Microbiology 149 3413 3421
    • (2003) Microbiology , vol.149 , pp. 3413-3421
    • Gaballa, A.1    Cao, M.2    Helmann, J.D.3
  • 21
    • 0038349048 scopus 로고    scopus 로고
    • Origins of metal ion selectivity in the DtxR/MntR family of metalloregulators
    • Guedon E. Helmann JD. 2003 Origins of metal ion selectivity in the DtxR/MntR family of metalloregulators Mol Microbiol 48 495 506
    • (2003) Mol Microbiol , vol.48 , pp. 495-506
    • Guedon, E.1    Helmann, J.D.2
  • 22
    • 0042952817 scopus 로고    scopus 로고
    • The global transcriptional response of Bacillus subtilis to manganese involves the MntR, Fur, TnrA and sigmaB regulons
    • Guedon E. Moore CM. Que Q. Wang T. Ye RW. Helmann JD. 2003 The global transcriptional response of Bacillus subtilis to manganese involves the MntR, Fur, TnrA and sigmaB regulons Mol Microbiol 49 1477 1491
    • (2003) Mol Microbiol , vol.49 , pp. 1477-1491
    • Guedon, E.1    Moore, C.M.2    Que, Q.3    Wang, T.4    Ye, R.W.5    Helmann, J.D.6
  • 24
    • 0035091245 scopus 로고    scopus 로고
    • Development of a new integration site within the Bacillus subtilis chromosome and construction of compatible expression cassettes
    • Härtl B. Werhl W. Wiegert T. Homuth G. Schumann W. 2001 Development of a new integration site within the Bacillus subtilis chromosome and construction of compatible expression cassettes J Bacteriol 183 2696 2699
    • (2001) J Bacteriol , vol.183 , pp. 2696-2699
    • Härtl, B.1    Werhl, W.2    Wiegert, T.3    Homuth, G.4    Schumann, W.5
  • 25
    • 0027434568 scopus 로고
    • Isolation of a prokaryotic metallothionein locus and analysis of transcriptional control by trace metal ions
    • Huckle JW. Morby AP. Turner JS. Robinson NJ. 1993 Isolation of a prokaryotic metallothionein locus and analysis of transcriptional control by trace metal ions Mol Microbiol 7 177 187
    • (1993) Mol Microbiol , vol.7 , pp. 177-187
    • Huckle, J.W.1    Morby, A.P.2    Turner, J.S.3    Robinson, N.J.4
  • 28
    • 0033037505 scopus 로고    scopus 로고
    • Chromosome-determined zinc-responsible operon czr in Staphylococcus aureus strain 912
    • Kuroda M. Hayashi H. Ohta T. 1999 Chromosome-determined zinc-responsible operon czr in Staphylococcus aureus strain 912 Microbiol Immunol 43 115 125
    • (1999) Microbiol Immunol , vol.43 , pp. 115-125
    • Kuroda, M.1    Hayashi, H.2    Ohta, T.3
  • 29
    • 2342444646 scopus 로고    scopus 로고
    • A novel cyanobacterial SmtB/ArsR family repressor regulates the expression of a CPx-ATPase and a metallothionein in response to both Cu(I)/Ag(I) and Zn(II)/Cd(II)
    • Liu T. Nakashima S. Hirose K. Shibasaka M. Katsuhara M. Ezaki B. et al. 2004 A novel cyanobacterial SmtB/ArsR family repressor regulates the expression of a CPx-ATPase and a metallothionein in response to both Cu(I)/Ag(I) and Zn(II)/Cd(II) J Biol Chem 17 17810 17818
    • (2004) J Biol Chem , vol.17 , pp. 17810-17818
    • Liu, T.1    Nakashima, S.2    Hirose, K.3    Shibasaka, M.4    Katsuhara, M.5    Ezaki, B.6
  • 30
    • 15744374882 scopus 로고    scopus 로고
    • Metal ion homeostasis in Bacillus subtilis
    • Moore CM. Helmann JD. 2005 Metal ion homeostasis in Bacillus subtilis Curr Opin Microbiol 8 188 195
    • (2005) Curr Opin Microbiol , vol.8 , pp. 188-195
    • Moore, C.M.1    Helmann, J.D.2
  • 31
    • 15744390704 scopus 로고    scopus 로고
    • Genetic and physiological responses of Bacillus subtilis to metal ion stress
    • Moore CM. Gaballa A. Hui M. Ye RW. Helmann JD. 2005 Genetic and physiological responses of Bacillus subtilis to metal ion stress Mol Microbiol 57 27 40
    • (2005) Mol Microbiol , vol.57 , pp. 27-40
    • Moore, C.M.1    Gaballa, A.2    Hui, M.3    Ye, R.W.4    Helmann, J.D.5
  • 32
    • 0027247583 scopus 로고
    • SmtB is a metal-regulated repressor of the cyanobacterial metallothionein gene smtA: Identification of a Zn-inhibited DNA-protein complex
    • Morby AP. Turner JS. Huckle JW. Robinson NJ. 1993 SmtB is a metal-regulated repressor of the cyanobacterial metallothionein gene smtA: identification of a Zn-inhibited DNA-protein complex Nucleic Acids Res 21 921 925
    • (1993) Nucleic Acids Res , vol.21 , pp. 921-925
    • Morby, A.P.1    Turner, J.S.2    Huckle, J.W.3    Robinson, N.J.4
  • 33
    • 0037565061 scopus 로고    scopus 로고
    • Efflux-mediated heavy metal resistance in prokaryotes
    • Nies DH. 2003 Efflux-mediated heavy metal resistance in prokaryotes FEMS Microbiol Rev 27 313 339
    • (2003) FEMS Microbiol Rev , vol.27 , pp. 313-339
    • Nies, D.H.1
  • 34
    • 0037993832 scopus 로고    scopus 로고
    • Transition metal speciation in the cell: Insights from the chemistry of metal ion receptors
    • O'Halloran TV. Finney LA. 2003 Transition metal speciation in the cell: insights from the chemistry of metal ion receptors Science 300 931 936
    • (2003) Science , vol.300 , pp. 931-936
    • O'Halloran, T.V.1    Finney, L.A.2
  • 35
    • 0028938093 scopus 로고
    • Two trans-acting metalloregulatory proteins controlling expression of the copper-ATPases of Enterococcus hirae
    • Odermatt A. Solioz M. 1995 Two trans-acting metalloregulatory proteins controlling expression of the copper-ATPases of Enterococcus hirae J Biol Chem 270 4349 4354
    • (1995) J Biol Chem , vol.270 , pp. 4349-4354
    • Odermatt, A.1    Solioz, M.2
  • 36
    • 0035968001 scopus 로고    scopus 로고
    • Femtomolar sensitivity of metalloregulatory proteins controlling zinc homeostasis
    • Outten CE. O'Halloran TV. 2001 Femtomolar sensitivity of metalloregulatory proteins controlling zinc homeostasis Science 292 2488 2492
    • (2001) Science , vol.292 , pp. 2488-2492
    • Outten, C.E.1    O'Halloran, T.V.2
  • 38
    • 0036260722 scopus 로고    scopus 로고
    • Regulatory interactions between the Pho and sigma B-dependent general stress regulons of Bacillus subtilis
    • Pragai Z. Harwood CR. 2002 Regulatory interactions between the Pho and sigma B-dependent general stress regulons of Bacillus subtilis Microbiology 148 1593 1602
    • (2002) Microbiology , vol.148 , pp. 1593-1602
    • Pragai, Z.1    Harwood, C.R.2
  • 40
    • 0031896498 scopus 로고    scopus 로고
    • The ars operon in the skin element of Bacillus subtilis confers resistance to arsenate and arsenite
    • Sato T. Kobayashi Y. 1998 The ars operon in the skin element of Bacillus subtilis confers resistance to arsenate and arsenite J Bacteriol 180 1655 1661
    • (1998) J Bacteriol , vol.180 , pp. 1655-1661
    • Sato, T.1    Kobayashi, Y.2
  • 41
    • 0028027443 scopus 로고
    • Identification of a putative metal-binding site in a new family of metalloregulatory proteins
    • Shi W. Wu J. Rosen BP. 1994 Identification of a putative metal-binding site in a new family of metalloregulatory proteins J Biol Chem 269 19826 19829
    • (1994) J Biol Chem , vol.269 , pp. 19826-19829
    • Shi, W.1    Wu, J.2    Rosen, B.P.3
  • 42
    • 0029873177 scopus 로고    scopus 로고
    • The role of arsenic-thiol interactions in metalloregulation of the ars operon
    • Shi W. Dong J. Scott RA. Ksenzenko MY. Rosen BP. 1996 The role of arsenic-thiol interactions in metalloregulation of the ars operon J Biol Chem 271 9291 9297
    • (1996) J Biol Chem , vol.271 , pp. 9291-9297
    • Shi, W.1    Dong, J.2    Scott, R.A.3    Ksenzenko, M.Y.4    Rosen, B.P.5
  • 43
    • 0033009421 scopus 로고    scopus 로고
    • ZntR is an autoregulatory protein and negatively regulates the chromosomal zinc resistance operon znt of Staphylococcus aureus
    • Singh VK. Xiong A. Usgaard TR. Chakrabarti S. Deora R. Misra TK. Jayawal RK. 1999 ZntR is an autoregulatory protein and negatively regulates the chromosomal zinc resistance operon znt of Staphylococcus aureus Mol Microbiol 33 200 207
    • (1999) Mol Microbiol , vol.33 , pp. 200-207
    • Singh, V.K.1    Xiong, A.2    Usgaard, T.R.3    Chakrabarti, S.4    Deora, R.5    Misra, T.K.6    Jayawal, R.K.7
  • 44
    • 0035805549 scopus 로고    scopus 로고
    • Role of cysteinyl residues in sensing Pb(II), Cd(II), and Zn(II) by the plasmid pI258 CadC repressor
    • Sun Y. Wong MD. Rosen BP. 2001 Role of cysteinyl residues in sensing Pb(II), Cd(II), and Zn(II) by the plasmid pI258 CadC repressor J Biol Chem 276 14955 14960
    • (2001) J Biol Chem , vol.276 , pp. 14955-14960
    • Sun, Y.1    Wong, M.D.2    Rosen, B.P.3
  • 45
    • 0032168014 scopus 로고    scopus 로고
    • An SmtB-like repressor from Synechocystis PCC 6803 regulates a zinc exporter
    • Thelwell C. Robinson NJ. Turner-Cavet JS. 1998 An SmtB-like repressor from Synechocystis PCC 6803 regulates a zinc exporter Proc Natl Acad Sci USA 95 10728 10733
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 10728-10733
    • Thelwell, C.1    Robinson, N.J.2    Turner-Cavet, J.S.3
  • 46
    • 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 JD. Higgins DG. Gibson TJ. 1994 clustal w : improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice Nucleic Acids Res 22 4673 4680
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 47
    • 0037085443 scopus 로고    scopus 로고
    • A copper metallochaperone for photosynthesis and respiration reveals metal-specific targets, interaction with an importer, and alternative sites for copper acquisition
    • Tottey S. Rondet SAM. Borrelly GPM. Robinson PJ. Rich PR. Robinson NJ. 2002 A copper metallochaperone for photosynthesis and respiration reveals metal-specific targets, interaction with an importer, and alternative sites for copper acquisition J Biol Chem 277 5490 5497
    • (2002) J Biol Chem , vol.277 , pp. 5490-5497
    • Tottey, S.1    Rondet, S.A.M.2    Borrelly, G.P.M.3    Robinson, P.J.4    Rich, P.R.5    Robinson, N.J.6
  • 48
    • 27644580799 scopus 로고    scopus 로고
    • Understanding how cells allocate metals using metal sensors and metallochaperones
    • Tottey S. Harvie DR. Robinson NJ. 2005 Understanding how cells allocate metals using metal sensors and metallochaperones Acc Chem Res 38 775 783
    • (2005) Acc Chem Res , vol.38 , pp. 775-783
    • Tottey, S.1    Harvie, D.R.2    Robinson, N.J.3
  • 49
    • 0029662326 scopus 로고    scopus 로고
    • Zinc-sensing by the cyanobacterial metallothionein repressor SmtB: Different motifs mediate metal-induced protein-DNA dissociation
    • Turner JS. Glands PD. Samson ACR. Robinson NJ. 1996 Zinc-sensing by the cyanobacterial metallothionein repressor SmtB: different motifs mediate metal-induced protein-DNA dissociation Nucleic Acids Res 24 3714 3721
    • (1996) Nucleic Acids Res , vol.24 , pp. 3714-3721
    • Turner, J.S.1    Glands, P.D.2    Samson, A.C.R.3    Robinson, N.J.4
  • 50
    • 0031737309 scopus 로고    scopus 로고
    • A vector for systematic gene inactivation in Bacillus subtilis
    • Vagner V. Dervyn E. Ehrlich SD. 1998 A vector for systematic gene inactivation in Bacillus subtilis Microbiology 144 3097 3104
    • (1998) Microbiology , vol.144 , pp. 3097-3104
    • Vagner, V.1    Dervyn, E.2    Ehrlich, S.D.3
  • 51
    • 0034718523 scopus 로고    scopus 로고
    • The zinc metalloregulatory protein Synechococcus PCC 7942 SmtB binds a single zinc ion per monomer with high affinity in a tetrahedral coordination geometry
    • VanZile ML. Cosper NJ. Scott RA. Giedroc DP. 2000 The zinc metalloregulatory protein Synechococcus PCC 7942 SmtB binds a single zinc ion per monomer with high affinity in a tetrahedral coordination geometry Biochemistry 39 11818 11829
    • (2000) Biochemistry , vol.39 , pp. 11818-11829
    • Vanzile, M.L.1    Cosper, N.J.2    Scott, R.A.3    Giedroc, D.P.4
  • 52
    • 0037031312 scopus 로고    scopus 로고
    • Structural characterization of distinct α3N and α5 metal sites in the cyanobacterial zinc sensor SmtB
    • VanZile ML. Chen X. Giedroc DP. 2002a Structural characterization of distinct α3N and α5 metal sites in the cyanobacterial zinc sensor SmtB Biochemistry 41 9765 9775
    • (2002) Biochemistry , vol.41 , pp. 9765-9775
    • Vanzile, M.L.1    Chen, X.2    Giedroc, D.P.3
  • 53
    • 0037031290 scopus 로고    scopus 로고
    • Allosteric negative regulation of smt O/P binding of the zinc-sensor, SmtB, by metal ions: A coupled equilibrium analysis
    • VanZile ML. Chen X. Giedroc DP. 2002b Allosteric negative regulation of smt O/P binding of the zinc-sensor, SmtB, by metal ions: a coupled equilibrium analysis Biochemistry 41 9776 9786
    • (2002) Biochemistry , vol.41 , pp. 9776-9786
    • Vanzile, M.L.1    Chen, X.2    Giedroc, D.P.3
  • 55
    • 0025815528 scopus 로고
    • The ArsR protein is a trans-acting regulatory protein
    • Wu J. Rosen BP. 1991 The ArsR protein is a trans-acting regulatory protein Mol Microbiol 5 1331 1336
    • (1991) Mol Microbiol , vol.5 , pp. 1331-1336
    • Wu, J.1    Rosen, B.P.2
  • 56
    • 0031859042 scopus 로고    scopus 로고
    • Molecular characterization of a chromosomal determinant conferring resistance to zinc and cobalt ions in Staphylococcus aureus
    • Xiong A. Jayaswal RK. 1998 Molecular characterization of a chromosomal determinant conferring resistance to zinc and cobalt ions in Staphylococcus aureus J Bacteriol 180 4024 4029
    • (1998) J Bacteriol , vol.180 , pp. 4024-4029
    • Xiong, A.1    Jayaswal, R.K.2
  • 57
    • 20444466105 scopus 로고    scopus 로고
    • Crystal structure of the Staphylococcus aureus pI258 CadC Cd(II)/Pb(II)/Zn(II)-responsive repressor
    • Ye J. Kandegedara A. Martin P. Rosen BP. 2005 Crystal structure of the Staphylococcus aureus pI258 CadC Cd(II)/Pb(II)/Zn(II)-responsive repressor J Bacteriol 187 4214 4221
    • (2005) J Bacteriol , vol.187 , pp. 4214-4221
    • Ye, J.1    Kandegedara, A.2    Martin, P.3    Rosen, B.P.4
  • 58
    • 0025788344 scopus 로고
    • Regulation of the CadA cadmium resistance determinant of Staphylococcus aureus plasmid PI258
    • Yoon KP. Misra TK. Silver S. 1991 Regulation of the CadA cadmium resistance determinant of Staphylococcus aureus plasmid PI258 J Bacteriol 173 7643 7649
    • (1991) J Bacteriol , vol.173 , pp. 7643-7649
    • Yoon, K.P.1    Misra, T.K.2    Silver, S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.