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Volumn 39, Issue 17, 2011, Pages 7586-7597

Determinants of redox sensitivity in RsrA, a zinc-containing anti-sigma factor for regulating thiol oxidative stress response

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; BACTERIAL PROTEIN; CYSTEINE; SIGMA FACTOR; THIOL; UNCLASSIFIED DRUG; ZINC CONTAINING ANTI SIGMA FACTOR RSRA;

EID: 80053219302     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkr477     Document Type: Article
Times cited : (18)

References (49)
  • 1
    • 42049122814 scopus 로고    scopus 로고
    • Regulation of bacterial RNA polymerase sigma factor activity: A structural perspective
    • Campbell, E.A., Westblade, L.F. and Darst, S.A. (2008) Regulation of bacterial RNA polymerase sigma factor activity: a structural perspective. Curr. Opin. Microbiol., 11, 121-127.
    • (2008) Curr. Opin. Microbiol. , vol.11 , pp. 121-127
    • Campbell, E.A.1    Westblade, L.F.2    Darst, S.A.3
  • 2
    • 80052804067 scopus 로고    scopus 로고
    • Regulation by alternative sigma factors
    • Storz, G. and Hengge, R. (eds) 2nd edn. ASM press, Washington
    • Helmann, J.D. (2010) Regulation by alternative sigma factors. In Storz, G. and Hengge, R. (eds), Bacterial Stress Responses, 2nd edn. ASM press, Washington, pp. 31-41.
    • (2010) Bacterial Stress Responses , pp. 31-41
    • Helmann, J.D.1
  • 3
    • 34548252292 scopus 로고    scopus 로고
    • A conserved structural module regulates transcriptional responses to diverse stress signals in bacteria
    • DOI 10.1016/j.molcel.2007.07.009, PII S1097276507004807
    • Campbell, E.A., Greenwell, R., Anthony, J.R., Wang, S., Lim, L., Das, K., Sofia, H.J., Donohue, T.J. and Darst, S.A. (2007) A conserved structural module regulates transcriptional responses to diverse stress signals in bacteria. Mol. Cell, 27, 793-805. (Pubitemid 47333225)
    • (2007) Molecular Cell , vol.27 , Issue.5 , pp. 793-805
    • Campbell, E.A.1    Greenwell, R.2    Anthony, J.R.3    Wang, S.4    Lim, L.5    Das, K.6    Sofia, H.J.7    Donohue, T.J.8    Darst, S.A.9
  • 4
    • 0035985580 scopus 로고    scopus 로고
    • The extracytoplasmic function (ECF) sigma factors
    • Helmann, J.D. (2002) The extracytoplasmic function (ECF) sigma factors. Adv. Microb. Physiol., 46, 47-110.
    • (2002) Adv. Microb. Physiol. , vol.46 , pp. 47-110
    • Helmann, J.D.1
  • 5
    • 0242692671 scopus 로고    scopus 로고
    • Multiple sigma subunits and the partitioning of bacterial transcription space
    • DOI 10.1146/annurev.micro.57.030502.090913
    • Gruber, T.M. and Gross, C.A. (2003) Multiple sigma subunits and the partitioning of bacterial transcription space. Annu. Rev. Microbiol., 57, 441-466. (Pubitemid 37392951)
    • (2003) Annual Review of Microbiology , vol.57 , pp. 441-466
    • Gruber, T.M.1    Gross, C.A.2
  • 6
    • 0037261948 scopus 로고    scopus 로고
    • The sigma70 family of sigma factors
    • Paget, M.S. and Helmann, J.D. (2003) The sigma70 family of sigma factors. Genome Biol., 4, 203.
    • (2003) Genome Biol. , vol.4 , pp. 203
    • Paget, M.S.1    Helmann, J.D.2
  • 7
    • 45249100907 scopus 로고    scopus 로고
    • The extracytoplasmic stress factor, sigmaE, is required to maintain cell envelope integrity in Escherichia coli
    • Hayden, J.D. and Ades, S.E. (2008) The extracytoplasmic stress factor, sigmaE, is required to maintain cell envelope integrity in Escherichia coli. PLoS One, 3, e1573.
    • (2008) PLoS One , vol.3
    • Hayden, J.D.1    Ades, S.E.2
  • 8
    • 84877983608 scopus 로고    scopus 로고
    • Envelope stress
    • Storz, G. and Hengge, R. (eds) 2nd edn. ASM press, Washington
    • Ades, S.E., Hayden, J.D. and Laubacher, M.E. (2010) Envelope stress. In Storz, G. and Hengge, R. (eds), Bacterial Stress Responses, 2nd edn. ASM press, Washington, pp. 115-131.
    • (2010) Bacterial Stress Responses , pp. 115-131
    • Ades, S.E.1    Hayden, J.D.2    Laubacher, M.E.3
  • 10
    • 0035116721 scopus 로고    scopus 로고
    • Mutational analysis of RsrA, a zinc-binding anti-sigma factor with a thiol-disulphide redox switch
    • DOI 10.1046/j.1365-2958.2001.02298.x
    • Paget, M.S., Bae, J.B., Hahn, M.Y., Li, W., Kleanthous, C., Roe, J.H. and Buttner, M.J. (2001) Mutational analysis of RsrA, a zinc-binding anti-sigma factor with a thiol-disulphide redox switch. Mol. Microbiol., 39, 1036-1047. (Pubitemid 32176346)
    • (2001) Molecular Microbiology , vol.39 , Issue.4 , pp. 1036-1047
    • Paget, M.S.B.1    Bae, J.-B.2    Hahn, M.-Y.3    Li, W.4    Kleanthous, C.5    Roe, J.-H.6    Buttner, M.J.7
  • 12
    • 0242521392 scopus 로고    scopus 로고
    • RshA, an anti-sigma factor that regulates the activity of the mycobacterial stress response sigma factor SigH
    • DOI 10.1046/j.1365-2958.2003.03739.x
    • Song, T., Dove, S.L., Lee, K.H. and Husson, R.N. (2003) RshA, an anti-sigma factor that regulates the activity of the mycobacterial stress response sigma factor SigH. Mol. Microbiol., 50, 949-959. (Pubitemid 37372255)
    • (2003) Molecular Microbiology , vol.50 , Issue.3 , pp. 949-959
    • Song, T.1    Dove, S.L.2    Lee, K.H.3    Husson, R.N.4
  • 13
    • 0036046191 scopus 로고    scopus 로고
    • M regulons
    • DOI 10.1046/j.1365-2958.2002.03050.x
    • Cao, M., Wang, T., Ye, R. and Helmann, J.D. (2002) Antibiotics that inhibit cell wall biosynthesis induce expression of the Bacillus subtilis sigma(W) and sigma(M) regulons. Mol. Microbiol., 45, 1267-1276. (Pubitemid 35015351)
    • (2002) Molecular Microbiology , vol.45 , Issue.5 , pp. 1267-1276
    • Cao, M.1    Wang, T.2    Ye, R.3    Helmann, J.D.4
  • 14
    • 3142683280 scopus 로고    scopus 로고
    • W anti-sigma factor RsiW is degraded by intramembrane proteolysis through YluC
    • DOI 10.1111/j.1365-2958.2004.04031.x
    • Schobel, S., Zellmeier, S., Schumann, W. and Wiegert, T. (2004) The Bacillus subtilis sigmaW anti-sigma factor RsiW is degraded by intramembrane proteolysis through YluC. Mol. Microbiol., 52, 1091-1105. (Pubitemid 38916176)
    • (2004) Molecular Microbiology , vol.52 , Issue.4 , pp. 1091-1105
    • Schobel, S.1    Zellmeier, S.2    Schumann, W.3    Wiegert, T.4
  • 15
    • 0034816770 scopus 로고    scopus 로고
    • RNA polymerase sigma factor that blocks morphological differentiation by Streptomyces coelicolor
    • DOI 10.1128/JB.183.20.5991-5996.2001
    • Gehring, A.M., Yoo, N.J. and Losick, R. (2001) RNA polymerase sigma factor that blocks morphological differentiation by Streptomyces coelicolor. J. Bacteriol., 183, 5991-5996. (Pubitemid 32917418)
    • (2001) Journal of Bacteriology , vol.183 , Issue.20 , pp. 5991-5996
    • Gehring, A.M.1    Yoo, N.J.2    Losick, R.3
  • 17
    • 26444518218 scopus 로고    scopus 로고
    • The Mycobacterium tuberculosis extracytoplasmic-function sigma factor SigL regulates polyketide synthases and secreted or membrane proteins and is required for virulence
    • DOI 10.1128/JB.187.20.7062-7071.2005
    • Hahn, M.Y., Raman, S., Anaya, M. and Husson, R.N. (2005) The Mycobacterium tuberculosis extracytoplasmic-function sigma factor SigL regulates polyketide synthases and secreted or membrane proteins and is required for virulence. J. Bacteriol., 187, 7062-7071. (Pubitemid 41428883)
    • (2005) Journal of Bacteriology , vol.187 , Issue.20 , pp. 7062-7071
    • Hahn, M.-Y.1    Raman, S.2    Anaya, M.3    Husson, R.N.4
  • 18
    • 77952987449 scopus 로고    scopus 로고
    • Identification of a novel anti-sigmaE factor in Neisseria meningitidis
    • Hopman, C.T., Speijer, D., van der Ende, A. and Pannekoek, Y. (2010) Identification of a novel anti-sigmaE factor in Neisseria meningitidis. BMC Microbiol., 10, 164.
    • (2010) BMC Microbiol. , vol.10 , pp. 164
    • Hopman, C.T.1    Speijer, D.2    Van Der Ende, A.3    Pannekoek, Y.4
  • 19
    • 0346996698 scopus 로고    scopus 로고
    • Redox-dependent changes in RsrA an anti-sigma factor in Streptomyces coelicolor: Zinc release and disulfide bond formation
    • Bae, J.B., Park, J.H., Hahn, M.Y., Kim, M.S. and Roe, J.H. (2004) Redox-dependent changes in RsrA, an anti-sigma factor in Streptomyces coelicolor: zinc release and disulfide bond formation. J. Mol. Biol., 335, 425-435.
    • (2004) J. Mol. Biol. , vol.335 , pp. 425-435
    • Bae, J.B.1    Park, J.H.2    Hahn, M.Y.3    Kim, M.S.4    Roe, J.H.5
  • 20
    • 0141645618 scopus 로고    scopus 로고
    • The role of zinc in the disulphide stress-regulated anti-sigma factor RsrA from Streptomyces coelicolor
    • DOI 10.1016/j.jmb.2003.08.038
    • Li, W., Bottrill, A.R., Bibb, M.J., Buttner, M.J., Paget, M.S. and Kleanthous, C. (2003) The Role of zinc in the disulphide stress-regulated anti-sigma factor RsrA from Streptomyces coelicolor. J. Mol. Biol., 333, 461-472. (Pubitemid 37188585)
    • (2003) Journal of Molecular Biology , vol.333 , Issue.2 , pp. 461-472
    • Li, W.1    Bottrill, A.R.2    Bibb, M.J.3    Buttner, M.J.4    Paget, M.S.B.5    Kleanthous, C.6
  • 21
    • 33745837091 scopus 로고    scopus 로고
    • Assignment of the zinc ligands in RsrA, a redox-sensing ZAS protein from Streptomyces coelicolor
    • DOI 10.1021/bi060711v
    • Zdanowski, K., Doughty, P., Jakimowicz, P., O'Hara, L., Buttner, M.J., Paget, M.S. and Kleanthous, C. (2006) Assignment of the zinc ligands in RsrA, a redox-sensing ZAS protein from Streptomyces coelicolor. Biochemistry, 45, 8294-8300. (Pubitemid 44036535)
    • (2006) Biochemistry , vol.45 , Issue.27 , pp. 8294-8300
    • Zdanowski, K.1    Doughty, P.2    Jakimowicz, P.3    O'Hara, L.4    Buttner, M.J.5    Paget, M.S.B.6    Kleanthous, C.7
  • 22
    • 77953220053 scopus 로고    scopus 로고
    • The sigmaR regulon of Streptomyces coelicolor A32 reveals a key role in protein quality control during disulphide stress
    • Kallifidas, D., Thomas, D., Doughty, P. and Paget, M.S. (2010) The sigmaR regulon of Streptomyces coelicolor A32 reveals a key role in protein quality control during disulphide stress. Microbiology, 156, 1661-1672.
    • (2010) Microbiology , vol.156 , pp. 1661-1672
    • Kallifidas, D.1    Thomas, D.2    Doughty, P.3    Paget, M.S.4
  • 23
    • 0035171384 scopus 로고    scopus 로고
    • R regulon
    • DOI 10.1046/j.1365-2958.2001.02675.x
    • Paget, M.S., Molle, V., Cohen, G., Aharonowitz, Y. and Buttner, M.J. (2001) Defining the disulphide stress response in Streptomyces coelicolor A3(2): identification of the sigmaR regulon. Mol. Microbiol., 42, 1007-1020. (Pubitemid 33078383)
    • (2001) Molecular Microbiology , vol.42 , Issue.4 , pp. 1007-1020
    • Paget, M.S.B.1    Molle, V.2    Cohen, G.3    Aharonowitz, Y.4    Buttner, M.J.5
  • 24
    • 42549139480 scopus 로고    scopus 로고
    • Mycothiol regulates and is regulated by a thiol-specific antisigma factor RsrA and sigma(R) in Streptomyces coelicolor
    • Park, J.H. and Roe, J.H. (2008) Mycothiol regulates and is regulated by a thiol-specific antisigma factor RsrA and sigma(R) in Streptomyces coelicolor. Mol. Microbiol., 68, 861-870.
    • (2008) Mol. Microbiol. , vol.68 , pp. 861-870
    • Park, J.H.1    Roe, J.H.2
  • 26
    • 34347397183 scopus 로고    scopus 로고
    • The extracytoplasmic function-type sigma factor SigM of Corynebacterium glutamicum ATCC 13032 is involved in transcription of disulfide stress-related genes
    • DOI 10.1128/JB.00382-07
    • Nakunst, D., Larisch, C., Huser, A.T., Tauch, A., Puhler, A. and Kalinowski, J. (2007) The extracytoplasmic function-type sigma factor SigM of Corynebacterium glutamicum ATCC 13032 is involved in transcription of disulfide stress-related genes. J. Bacteriol., 189, 4696-4707. (Pubitemid 47025581)
    • (2007) Journal of Bacteriology , vol.189 , Issue.13 , pp. 4696-4707
    • Nakunst, D.1    Larisch, C.2    Huser, A.T.3    Tauch, A.4    Puhler, A.5    Kalinowski, J.6
  • 27
    • 77950517981 scopus 로고    scopus 로고
    • Structural and biochemical bases for the redox sensitivity of Mycobacterium tuberculosis RslA
    • Thakur, K.G., Praveena, T. and Gopal, B. (2010) Structural and biochemical bases for the redox sensitivity of Mycobacterium tuberculosis RslA. J. Mol. Biol., 397, 1199-1208.
    • (2010) J. Mol. Biol. , vol.397 , pp. 1199-1208
    • Thakur, K.G.1    Praveena, T.2    Gopal, B.3
  • 28
    • 33644502850 scopus 로고    scopus 로고
    • Transcriptional analysis of the ylaABCD operon of Bacillus subtilis encoding a sigma factor of extracytoplasmic function family
    • Matsumoto, T., Nakanishi, K., Asai, K. and Sadaie, Y. (2005) Transcriptional analysis of the ylaABCD operon of Bacillus subtilis encoding a sigma factor of extracytoplasmic function family. Genes Genet. Syst., 80, 385-393.
    • (2005) Genes Genet. Syst. , vol.80 , pp. 385-393
    • Matsumoto, T.1    Nakanishi, K.2    Asai, K.3    Sadaie, Y.4
  • 29
    • 33745796418 scopus 로고    scopus 로고
    • YlaC is an extracytoplasmic function (ECF) sigma factor contributing to hydrogen peroxide resistance in Bacillus subtilis
    • Ryu, H.B., Shin, I., Yim, H.S. and Kang, S.O. (2006) YlaC is an extracytoplasmic function (ECF) sigma factor contributing to hydrogen peroxide resistance in Bacillus subtilis. J. Microbiol., 44, 206-216. (Pubitemid 44874797)
    • (2006) Journal of Microbiology , vol.44 , Issue.2 , pp. 206-216
    • Ryu, H.-B.1    Shin, I.2    Yim, H.-S.3    Kang, S.-O.4
  • 31
    • 34547781750 scopus 로고    scopus 로고
    • MEGA4: Molecular Evolutionary Genetics Analysis (MEGA) software version 4.0
    • DOI 10.1093/molbev/msm092
    • Tamura, K., Dudley, J., Nei, M. and Kumar, S. (2007) MEGA4: Molecular Evolutionary Genetics Analysis (MEGA) software version 4.0. Mol. Biol. Evol., 24, 1596-1599. (Pubitemid 47236692)
    • (2007) Molecular Biology and Evolution , vol.24 , Issue.8 , pp. 1596-1599
    • Tamura, K.1    Dudley, J.2    Nei, M.3    Kumar, S.4
  • 32
    • 0347383758 scopus 로고    scopus 로고
    • Modeller: Generation and refinement of homology-based protein structure models
    • DOI 10.1016/S0076-6879(03)74020-8
    • Fiser, A. and Sali, A. (2003) Modeller: generation and refinement of homology-based protein structure models. Methods Enzymol., 374, 461-491. (Pubitemid 37531821)
    • (2003) Methods in Enzymology , vol.374 , pp. 461-491
    • Fiser, A.1    Sali, A.2
  • 34
    • 0033625531 scopus 로고    scopus 로고
    • T(E)Xshade: Shading and labeling of multiple sequence alignments using L(A)T(E)X2ε
    • Beitz, E. (2000) TEXshade: shading and labeling of multiple sequence alignments using LATEX2 epsilon. Bioinformatics, 16, 135-139. (Pubitemid 30248590)
    • (2000) Bioinformatics , vol.16 , Issue.2 , pp. 135-139
    • Beitz, E.1
  • 36
    • 70350135937 scopus 로고    scopus 로고
    • Positive and negative feedback regulatory loops of thiol-oxidative stress response mediated by an unstable isoform of sigmaR in actinomycetes
    • Kim, M.S., Hahn, M.Y., Cho, Y., Cho, S.N. and Roe, J.H. (2009) Positive and negative feedback regulatory loops of thiol-oxidative stress response mediated by an unstable isoform of sigmaR in actinomycetes. Mol. Microbiol., 73, 815-825.
    • (2009) Mol. Microbiol. , vol.73 , pp. 815-825
    • Kim, M.S.1    Hahn, M.Y.2    Cho, Y.3    Cho, S.N.4    Roe, J.H.5
  • 37
    • 0030977752 scopus 로고    scopus 로고
    • Overlapping PCR for bidirectional PCR amplification of specific alleles: A rapid one-tube method for simultaneously differentiating homozygotes and heterozygotes
    • Liu, Q., Thorland, E.C., Heit, J.A. and Sommer, S.S. (1997) Overlapping PCR for bidirectional PCR amplification of specific alleles: a rapid one-tube method for simultaneously differentiating homozygotes and heterozygotes. Genome Res., 7, 389-398. (Pubitemid 27183007)
    • (1997) Genome Research , vol.7 , Issue.4 , pp. 389-398
    • Liu, Q.1    Thorland, E.C.2    Heit, J.A.3    Sommer, S.S.4
  • 38
    • 0037376655 scopus 로고    scopus 로고
    • Sniffers, buzzers, toggles and blinkers: Dynamics of regulatory and signaling pathways in the cell
    • DOI 10.1016/S0955-0674(03)00017-6
    • Tyson, J.J., Chen, K.C. and Novak, B. (2003) Sniffers, buzzers, toggles and blinkers: dynamics of regulatory and signaling pathways in the cell. Curr. Opin. Cell. Biol., 15, 221-231. (Pubitemid 36332198)
    • (2003) Current Opinion in Cell Biology , vol.15 , Issue.2 , pp. 221-231
    • Tyson, J.J.1    Chen, K.C.2    Novak, B.3
  • 39
    • 0034663597 scopus 로고    scopus 로고
    • Application of multiple sequence alignment profiles to improve protein secondary structure prediction
    • DOI 10.1002/1097-0134(20000815 )40:3<502::AID-PROT170>3.0.CO;2-Q
    • Cuff, J.A. and Barton, G.J. (2000) Application of multiple sequence alignment profiles to improve protein secondary structure prediction. Proteins, 40, 502-511. (Pubitemid 30624459)
    • (2000) Proteins: Structure, Function and Genetics , vol.40 , Issue.3 , pp. 502-511
    • Cuff, J.A.1    Barton, G.J.2
  • 40
    • 33745865202 scopus 로고    scopus 로고
    • Zinc center as redox switch - New function for an old motif
    • DOI 10.1089/ars.2006.8.835
    • Ilbert, M., Graf, P.C. and Jakob, U. (2006) Zinc center as redox switch-new function for an old motif. Antioxid. Redox. Signal, 8, 835-846. (Pubitemid 44036501)
    • (2006) Antioxidants and Redox Signaling , vol.8 , Issue.5-6 , pp. 835-846
    • Ilbert, M.1    Graf, P.C.F.2    Jakob, U.3
  • 41
    • 71549143840 scopus 로고    scopus 로고
    • Disulfides as redox switches: From molecular mechanisms to functional significance
    • Wouters, M.A., Fan, S.W. and Haworth, N.L. (2010) Disulfides as redox switches: from molecular mechanisms to functional significance. Antioxid. Redox. Signal, 12, 53-91.
    • (2010) Antioxid. Redox. Signal , vol.12 , pp. 53-91
    • Wouters, M.A.1    Fan, S.W.2    Haworth, N.L.3
  • 42
    • 33750901634 scopus 로고    scopus 로고
    • Zinc coordination environments in proteins as redox sensors and signal transducers
    • DOI 10.1089/ars.2006.8.1419
    • Maret, W. (2006) Zinc coordination environments in proteins as redox sensors and signal transducers. Antioxid. Redox. Signal, 8, 1419-1441. (Pubitemid 44726320)
    • (2006) Antioxidants and Redox Signaling , vol.8 , Issue.9-10 , pp. 1419-1441
    • Maret, W.1
  • 43
    • 0035857417 scopus 로고    scopus 로고
    • Reactivity of zinc finger cores: Analysis of protein packing and electrostatic screening
    • DOI 10.1021/ja0011616
    • Maynard, A.T. and Covell, D.G. (2001) Reactivity of zinc finger cores: analysis of protein packing and electrostatic screening. J. Am. Chem. Soc., 123, 1047-1058. (Pubitemid 32148172)
    • (2001) Journal of the American Chemical Society , vol.123 , Issue.6 , pp. 1047-1058
    • Maynard, A.T.1    Covell, D.G.2
  • 44
    • 0037471640 scopus 로고    scopus 로고
    • Control of thiolate nucleophilicity and specificity in zinc metalloproteins by hydrogen bonding: Lessons from model compound studies
    • DOI 10.1021/ja029418i
    • Smith, J.N., Shirin, Z. and Carrano, C.J. (2003) Control of thiolate nucleophilicity and specificity in zinc metalloproteins by hydrogen bonding: lessons from model compound studies. J. Am. Chem. Soc., 125, 868-869. (Pubitemid 36152628)
    • (2003) Journal of the American Chemical Society , vol.125 , Issue.4 , pp. 868-869
    • Smith, J.N.1    Shirin, Z.2    Carrano, C.J.3
  • 45
    • 77954608795 scopus 로고    scopus 로고
    • Protein-protein interaction as a powering source of oxidoreductive reactivity
    • Lin, T.Y. (2010) Protein-protein interaction as a powering source of oxidoreductive reactivity. Mol. Biosyst., 6, 1454-1462.
    • (2010) Mol. Biosyst. , vol.6 , pp. 1454-1462
    • Lin, T.Y.1
  • 46
    • 0942301389 scopus 로고    scopus 로고
    • A positive charge at position 33 of thioredoxin primarily affects its interaction with other proteins but not redox potential
    • Lin, T.Y. and Chen, T.S. (2004) A positive charge at position 33 of thioredoxin primarily affects its interaction with other proteins but not redox potential. Biochemistry, 43, 945-952.
    • (2004) Biochemistry , vol.43 , pp. 945-952
    • Lin, T.Y.1    Chen, T.S.2
  • 48
    • 0030934272 scopus 로고    scopus 로고
    • The CXXC motif: A rheostat in the active site
    • DOI 10.1021/bi9628580
    • Chivers, P.T., Prehoda, K.E. and Raines, R.T. (1997) The CXXC motif: a rheostat in the active site. Biochemistry, 36, 4061-4066. (Pubitemid 27171576)
    • (1997) Biochemistry , vol.36 , Issue.14 , pp. 4061-4066
    • Chivers, P.T.1    Prehoda, K.E.2    Raines, R.T.3


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