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Volumn 159, Issue PART 6, 2013, Pages 1179-1189

Levels of control exerted by the Isc iron-sulfur cluster system on biosynthesis of the formate hydrogenlyase complex

Author keywords

[No Author keywords available]

Indexed keywords

CARRIER PROTEIN; FORMATE DEHYDROGENASE; FORMIC ACID; HYDROGEN; IRON SULFUR PROTEIN; PROTEIN ERPA; PROTEIN ISCA; UNCLASSIFIED DRUG;

EID: 84878839839     PISSN: 13500872     EISSN: 14652080     Source Type: Journal    
DOI: 10.1099/mic.0.066142-0     Document Type: Article
Times cited : (14)

References (51)
  • 1
    • 0025043949 scopus 로고
    • Escherichia coli formate-hydrogen lyase. Purification and properties of the seleniumdependent formate dehydrogenase component
    • Axley, M. J., Grahame, D. A. & Stadtman, T. C. (1990). Escherichia coli formate-hydrogen lyase. Purification and properties of the seleniumdependent formate dehydrogenase component. J Biol Chem 265, 18213-18218.
    • (1990) J Biol Chem , vol.265 , pp. 18213-18218
    • Axley, M.J.1    Grahame, D.A.2    Stadtman, T.C.3
  • 4
    • 0022254333 scopus 로고
    • Nickel-containing hydrogenase isoenzymes from anaerobically grown Escherichia coli K-12
    • Ballantine, S. P. & Boxer, D. H. (1985). Nickel-containing hydrogenase isoenzymes from anaerobically grown Escherichia coli K-12. J Bacteriol 163, 454-459.
    • (1985) J Bacteriol , vol.163 , pp. 454-459
    • Ballantine, S.P.1    Boxer, D.H.2
  • 5
    • 0017389525 scopus 로고
    • The identification of mutants of Escherichia coli deficient in formate dehydrogenase and nitrate reductase activities using dye indicator plates
    • Begg, Y. A., Whyte, J. N. & Haddock, B. A. (1977). The identification of mutants of Escherichia coli deficient in formate dehydrogenase and nitrate reductase activities using dye indicator plates. FEMS Microbiol Lett 2, 47-50.
    • (1977) FEMS Microbiol Lett , vol.2 , pp. 47-50
    • Begg, Y.A.1    Whyte, J.N.2    Haddock, B.A.3
  • 6
    • 84875553057 scopus 로고    scopus 로고
    • Coordination of FocA and pyruvate formatelyase synthesis in Escherichia coli demonstrates preferential translocation of formate over other mixed-acid fermentation products
    • Beyer, L., Doberenz, C., Falke, D., Hunger, D., Suppmann, B. & Sawers, R. G. (2013). Coordination of FocA and pyruvate formatelyase synthesis in Escherichia coli demonstrates preferential translocation of formate over other mixed-acid fermentation products. J Bacteriol 195, 1428-1435.
    • (2013) J Bacteriol , vol.195 , pp. 1428-1435
    • Beyer, L.1    Doberenz, C.2    Falke, D.3    Hunger, D.4    Suppmann, B.5    Sawers, R.G.6
  • 7
    • 0023176253 scopus 로고
    • Factors affecting transcriptional regulation of the formate-hydrogen-lyase pathway of Escherichia coli
    • Birkmann, A., Zinoni, F., Sawers, G. & Bö ck, A. (1987). Factors affecting transcriptional regulation of the formate-hydrogen-lyase pathway of Escherichia coli. Arch Microbiol 148, 44-51.
    • (1987) Arch Microbiol , vol.148 , pp. 44-51
    • Birkmann, A.1    Zinoni, F.2    Sawers, G.3    Böck, A.4
  • 8
    • 7044222771 scopus 로고    scopus 로고
    • The complex between hydrogenase-maturation proteins HypC and HypD is an intermediate in the supply of cyanide to the active site iron of [NiFe]-hydrogenases
    • Blokesch, M., Albracht, S. P. J., Matzanke, B. F., Drapal, N. M., Jacobi, A. & Böck, A. (2004). The complex between hydrogenase-maturation proteins HypC and HypD is an intermediate in the supply of cyanide to the active site iron of [NiFe]-hydrogenases. J Mol Biol 344, 155-167.
    • (2004) J Mol Biol , vol.344 , pp. 155-167
    • Blokesch, M.1    Albracht, S.P.J.2    Matzanke, B.F.3    Drapal, N.M.4    Jacobi, A.5    Böck, A.6
  • 10
    • 0025157053 scopus 로고
    • Nucleotide sequence and expression of an operon in Escherichia coli coding for formate hydrogenlyase components
    • Böhm, R., Sauter, M. & Böck, A. (1990). Nucleotide sequence and expression of an operon in Escherichia coli coding for formate hydrogenlyase components. Mol Microbiol 4, 231-243.
    • (1990) Mol Microbiol , vol.4 , pp. 231-243
    • Böhm, R.1    Sauter, M.2    Böck, A.3
  • 11
    • 0031043109 scopus 로고    scopus 로고
    • Crystal structure of formate dehydrogenase H: Catalysis involving Mo, molybdopterin, selenocysteine, and an Fe4S4 cluster
    • Boyington, J. C., Gladyshev, V. N., Khangulov, S. V., Stadtman, T. C. & Sun, P. D. (1997). Crystal structure of formate dehydrogenase H: catalysis involving Mo, molybdopterin, selenocysteine, and an Fe4S4 cluster. Science 275, 1305-1308.
    • (1997) Science , vol.275 , pp. 1305-1308
    • Boyington, J.C.1    Gladyshev, V.N.2    Khangulov, S.V.3    Stadtman, T.C.4    Sun, P.D.5
  • 12
    • 0017129243 scopus 로고
    • Transposition and fusion of the lac genes to selected promoters in Escherichia coli using bacteriophage lambda and Mu
    • Casadaban, M. J. (1976). Transposition and fusion of the lac genes to selected promoters in Escherichia coli using bacteriophage lambda and Mu. J Mol Biol 104, 541-555.
    • (1976) J Mol Biol , vol.104 , pp. 541-555
    • Casadaban, M.J.1
  • 13
    • 0029065955 scopus 로고
    • Gene disruption in Escherichia coli: TcR and KmR cassettes with the option of Flpcatalyzed excision of the antibiotic-resistance determinant
    • Cherepanov, P. P. & Wackernagel, W. (1995). Gene disruption in Escherichia coli: TcR and KmR cassettes with the option of Flpcatalyzed excision of the antibiotic-resistance determinant. Gene 158, 9-14.
    • (1995) Gene , vol.158 , pp. 9-14
    • Cherepanov, P.P.1    Wackernagel, W.2
  • 15
    • 74349124142 scopus 로고    scopus 로고
    • Unexpected oligomeric structure of the FocA formate channel of Escherichia coli: A paradigm for the formate-nitrite transporter family of integral membrane proteins
    • Falke, D., Schulz, K., Doberenz, C., Beyer, L., Lilie, H., Thiemer, B. & Sawers, R. G. (2010). Unexpected oligomeric structure of the FocA formate channel of Escherichia coli: a paradigm for the formate-nitrite transporter family of integral membrane proteins. FEMS Microbiol Lett 303, 69-75.
    • (2010) FEMS Microbiol Lett , vol.303 , pp. 69-75
    • Falke, D.1    Schulz, K.2    Doberenz, C.3    Beyer, L.4    Lilie, H.5    Thiemer, B.6    Sawers, R.G.7
  • 16
    • 34248681266 scopus 로고    scopus 로고
    • Maturation of [NiFe]-hydrogenases in Escherichia coli
    • Forzi, L. & Sawers, R. G. (2007). Maturation of [NiFe]-hydrogenases in Escherichia coli. Biometals 20, 565-578.
    • (2007) Biometals , vol.20 , pp. 565-578
    • Forzi, L.1    Sawers, R.G.2
  • 17
    • 0031973793 scopus 로고    scopus 로고
    • Novel keto acid formate-lyase and propionate kinase enzymes are components of an anaerobic pathway in Escherichia coli that degrades L-threonine to propionate
    • Hesslinger, C., Fairhurst, S. A. & Sawers, G. (1998). Novel keto acid formate-lyase and propionate kinase enzymes are components of an anaerobic pathway in Escherichia coli that degrades L-threonine to propionate. Mol Microbiol 27, 477-492.
    • (1998) Mol Microbiol , vol.27 , pp. 477-492
    • Hesslinger, C.1    Fairhurst, S.A.2    Sawers, G.3
  • 18
    • 0024369217 scopus 로고
    • Reductive cleavage of sarcosine and betaine by Eubacterium acidaminophilum via enzyme systems different from glycine reductase
    • Hormann, K. & Andreesen, J. (1989). Reductive cleavage of sarcosine and betaine by Eubacterium acidaminophilum via enzyme systems different from glycine reductase. Arch Microbiol 153, 50-59.
    • (1989) Arch Microbiol , vol.153 , pp. 50-59
    • Hormann, K.1    Andreesen, J.2
  • 19
    • 20744446399 scopus 로고    scopus 로고
    • Structure, function, and formation of biological iron-sulfur clusters
    • Johnson, D. C., Dean, D. R., Smith, A. D. & Johnson, M. K. (2005). Structure, function, and formation of biological iron-sulfur clusters. Annu Rev Biochem 74, 247-281.
    • (2005) Annu Rev Biochem , vol.74 , pp. 247-281
    • Johnson, D.C.1    Dean, D.R.2    Smith, A.D.3    Johnson, M.K.4
  • 21
    • 0025063286 scopus 로고
    • A radical-chemical route to acetyl- CoA: The anaerobically induced pyruvate formate-lyase system of Escherichia coli
    • Knappe, J. & Sawers, G. (1990). A radical-chemical route to acetyl- CoA: the anaerobically induced pyruvate formate-lyase system of Escherichia coli. FEMS Microbiol Rev 6, 383-398.
    • (1990) FEMS Microbiol Rev , vol.6 , pp. 383-398
    • Knappe, J.1    Sawers, G.2
  • 22
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 25
    • 17644429864 scopus 로고    scopus 로고
    • Dissection of the maturation reactions of the [NiFe] hydrogenase 3 from Escherichia coli taking place after nickel incorporation
    • Magalon, A. & Bö ck, A. (2000). Dissection of the maturation reactions of the [NiFe] hydrogenase 3 from Escherichia coli taking place after nickel incorporation. FEBS Lett 473, 254-258.
    • (2000) FEBS Lett , vol.473 , pp. 254-258
    • Magalon, A.1    Böck, A.2
  • 26
    • 56249090364 scopus 로고    scopus 로고
    • The impact of O2 on the Fe-S cluster biogenesis requirements of Escherichia coli FNR
    • Mettert, E. L., Outten, F. W., Wanta, B. & Kiley, P. J. (2008). The impact of O2 on the Fe-S cluster biogenesis requirements of Escherichia coli FNR. J Mol Biol 384, 798-811.
    • (2008) J Mol Biol , vol.384 , pp. 798-811
    • Mettert, E.L.1    Outten, F.W.2    Wanta, B.3    Kiley, P.J.4
  • 27
    • 0003785155 scopus 로고
    • Cold Spring Harbor: Cold Spring Harbor Laboratory Press
    • Miller, J. (1972). Experiments in Molecular Genetics. Cold Spring Harbor: Cold Spring Harbor Laboratory Press.
    • (1972) Experiments In Molecular Genetics
    • Miller, J.1
  • 28
    • 0032868231 scopus 로고    scopus 로고
    • Hyperproduction of recombinant ferredoxins in Escherichia coli by coexpression of the ORF1-ORF2-iscS-iscU-iscA-hscB-hscA-fdx-ORF3 gene cluster
    • Nakamura, M., Saeki, K. & Takahashi, Y. (1999). Hyperproduction of recombinant ferredoxins in Escherichia coli by coexpression of the ORF1-ORF2-iscS-iscU-iscA-hscB-hscA-fdx-ORF3 gene cluster. J Biochem 126, 10-18.
    • (1999) J Biochem , vol.126 , pp. 10-18
    • Nakamura, M.1    Saeki, K.2    Takahashi, Y.3
  • 29
    • 0037147254 scopus 로고    scopus 로고
    • HypF, a carbamoyl phosphate-converting enzyme involved in [NiFe] hydrogenase maturation
    • Paschos, A., Bauer, A., Zimmermann, A., Zehelein, E. & Böck, A. (2002). HypF, a carbamoyl phosphate-converting enzyme involved in [NiFe] hydrogenase maturation. J Biol Chem 277, 49945-49951.
    • (2002) J Biol Chem , vol.277 , pp. 49945-49951
    • Paschos, A.1    Bauer, A.2    Zimmermann, A.3    Zehelein, E.4    Böck, A.5
  • 30
    • 78049426276 scopus 로고    scopus 로고
    • The role of the ferric-uptake regulator Fur and iron homeostasis in controlling levels of the [NiFe]- hydrogenases in Escherichia coli
    • Pinske, C. & Sawers, R. G. (2010). The role of the ferric-uptake regulator Fur and iron homeostasis in controlling levels of the [NiFe]- hydrogenases in Escherichia coli. Int J Hydrogen Energy 35, 8938-8944.
    • (2010) Int J Hydrogen Energy , vol.35 , pp. 8938-8944
    • Pinske, C.1    Sawers, R.G.2
  • 31
    • 84857408142 scopus 로고    scopus 로고
    • Delivery of iron-sulfur clusters to the hydrogen-oxidizing [NiFe]-hydrogenases in Escherichia coli requires the A-type carrier proteins ErpA and IscA
    • Pinske, C. & Sawers, R. G. (2012a). Delivery of iron-sulfur clusters to the hydrogen-oxidizing [NiFe]-hydrogenases in Escherichia coli requires the A-type carrier proteins ErpA and IscA. PLoS ONE 7, e31755.
    • (2012) PLoS ONE , vol.7
    • Pinske, C.1    Sawers, R.G.2
  • 32
    • 84855895055 scopus 로고    scopus 로고
    • A-type carrier protein ErpA is essential for formation of an active formate-nitrate respiratory pathway in Escherichia coli K-12
    • Pinske, C. & Sawers, R. G. (2012b). A-type carrier protein ErpA is essential for formation of an active formate-nitrate respiratory pathway in Escherichia coli K-12. J Bacteriol 194, 346-353.
    • (2012) J Bacteriol , vol.194 , pp. 346-353
    • Pinske, C.1    Sawers, R.G.2
  • 33
    • 79961064482 scopus 로고    scopus 로고
    • Metabolic deficiencies revealed in the biotechnologically important model bacterium Escherichia coli BL21(DE3)
    • Pinske, C., Bönn, M., Krüger, S., Lindenstrauss, U. & Sawers, R. G. (2011). Metabolic deficiencies revealed in the biotechnologically important model bacterium Escherichia coli BL21(DE3). PLoS ONE 6, e22830.
    • (2011) PLoS ONE , vol.6
    • Pinske, C.1    Bönn, M.2    Krüger, S.3    Lindenstrauss, U.4    Sawers, R.G.5
  • 34
    • 84863494328 scopus 로고    scopus 로고
    • Zymographic differentiation of [NiFe]-hydrogenases 1, 2 and 3 of Escherichia coli K-12
    • Pinske, C., Jaroschinsky, M., Sargent, F. & Sawers, G. (2012). Zymographic differentiation of [NiFe]-hydrogenases 1, 2 and 3 of Escherichia coli K-12. BMC Microbiol 12, 134.
    • (2012) BMC Microbiol , vol.12 , pp. 134
    • Pinske, C.1    Jaroschinsky, M.2    Sargent, F.3    Sawers, G.4
  • 35
    • 77952813340 scopus 로고    scopus 로고
    • Building Fe-S proteins: Bacterial strategies
    • Py, B. & Barras, F. (2010). Building Fe-S proteins: bacterial strategies. Nat Rev Microbiol 8, 436-446.
    • (2010) Nat Rev Microbiol , vol.8 , pp. 436-446
    • Py, B.1    Barras, F.2
  • 37
    • 0025930768 scopus 로고
    • Mechanism of regulation of the formate-hydrogenlyase pathway by oxygen, nitrate, and pH: Definition of the formate regulon
    • Rossmann, R., Sawers, G. & Bö ck, A. (1991). Mechanism of regulation of the formate-hydrogenlyase pathway by oxygen, nitrate, and pH: definition of the formate regulon. Mol Microbiol 5, 2807-2814.
    • (1991) Mol Microbiol , vol.5 , pp. 2807-2814
    • Rossmann, R.1    Sawers, G.2    Böck, A.3
  • 38
    • 0025373543 scopus 로고
    • Transcriptional analysis of the gene encoding pyruvate formate-lyase-activating enzyme of Escherichia coli
    • Sauter, M. & Sawers, R. G. (1990). Transcriptional analysis of the gene encoding pyruvate formate-lyase-activating enzyme of Escherichia coli. Mol Microbiol 4, 355-363.
    • (1990) Mol Microbiol , vol.4 , pp. 355-363
    • Sauter, M.1    Sawers, R.G.2
  • 39
    • 0026725149 scopus 로고
    • Mutational analysis of the operon (hyc) determining hydrogenase 3 formation in Escherichia coli
    • Sauter, M., Bö hm, R. & Böck, A. (1992). Mutational analysis of the operon (hyc) determining hydrogenase 3 formation in Escherichia coli. Mol Microbiol 6, 1523-1532.
    • (1992) Mol Microbiol , vol.6 , pp. 1523-1532
    • Sauter, M.1    Böhm, R.2    Böck, A.3
  • 40
    • 0024109941 scopus 로고
    • Anaerobic regulation of pyruvate formate-lyase from Escherichia coli K-12
    • Sawers, G. & Böck, A. (1988). Anaerobic regulation of pyruvate formate-lyase from Escherichia coli K-12. J Bacteriol 170, 5330-5336.
    • (1988) J Bacteriol , vol.170 , pp. 5330-5336
    • Sawers, G.1    Böck, A.2
  • 41
    • 0026623120 scopus 로고
    • Anaerobic induction of pyruvate formate-lyase gene expression is mediated by the ArcA and FNR proteins
    • Sawers, G. & Suppmann, B. (1992). Anaerobic induction of pyruvate formate-lyase gene expression is mediated by the ArcA and FNR proteins. J Bacteriol 174, 3474-3478.
    • (1992) J Bacteriol , vol.174 , pp. 3474-3478
    • Sawers, G.1    Suppmann, B.2
  • 42
    • 0022376555 scopus 로고
    • Differential expression of hydrogenase isoenzymes in Escherichia coli K-12: Evidence for a third isoenzyme
    • Sawers, R. G., Ballantine, S. P. & Boxer, D. H. (1985). Differential expression of hydrogenase isoenzymes in Escherichia coli K-12: evidence for a third isoenzyme. J Bacteriol 164, 1324-1331.
    • (1985) J Bacteriol , vol.164 , pp. 1324-1331
    • Sawers, R.G.1    Ballantine, S.P.2    Boxer, D.H.3
  • 43
    • 70149124825 scopus 로고    scopus 로고
    • Anaerobic formate and hydrogen metabolism
    • Edited by R. Curtiss III and others. American Society for Microbiology, Washington, DC September 2004, posting date. Chapter 3.5.4
    • Sawers, R. G., Blokesch, M. & Böck, A. (2004). Anaerobic formate and hydrogen metabolism. September 2004, posting date. Chapter 3.5.4. In EcoSal-Escherichia coli and Salmonella: Cellular and Molecular Biology. Edited by R. Curtiss III and others. American Society for Microbiology, Washington, DC. http://www.ecosal.org.
    • (2004) EcoSal-Escherichia Coli and Salmonella: Cellular and Molecular Biology
    • Sawers, R.G.1    Blokesch, M.2    Böck, A.3
  • 44
    • 0023255472 scopus 로고
    • Improved single and multicopy lac-based cloning vectors for protein and operon fusions
    • Simons, R. W., Houman, F. & Kleckner, N. (1987). Improved single and multicopy lac-based cloning vectors for protein and operon fusions. Gene 53, 85-96.
    • (1987) Gene , vol.53 , pp. 85-96
    • Simons, R.W.1    Houman, F.2    Kleckner, N.3
  • 45
    • 79960870552 scopus 로고    scopus 로고
    • The respiratory molybdo-selenoprotein formate dehydrogenases of Escherichia coli have hydrogen: Benzyl viologen oxidoreductase activity
    • Soboh, B., Pinske, C., Kuhns, M., Waclawek, M., Ihling, C., Trchounian, K., Trchounian, A., Sinz, A. & Sawers, G. (2011). The respiratory molybdo-selenoprotein formate dehydrogenases of Escherichia coli have hydrogen: benzyl viologen oxidoreductase activity. BMC Microbiol 11, 173.
    • (2011) BMC Microbiol , vol.11 , pp. 173
    • Soboh, B.1    Pinske, C.2    Kuhns, M.3    Waclawek, M.4    Ihling, C.5    Trchounian, K.6    Trchounian, A.7    Sinz, A.8    Sawers, G.9
  • 46
    • 0028237747 scopus 로고
    • Isolation and characterization of hypophosphite-resistant mutants of Escherichia coli: Identification of the FocA protein, encoded by the pfl operon, as a putative formate transporter
    • Suppmann, B. & Sawers, G. (1994). Isolation and characterization of hypophosphite-resistant mutants of Escherichia coli: identification of the FocA protein, encoded by the pfl operon, as a putative formate transporter. Mol Microbiol 11, 965-982.
    • (1994) Mol Microbiol , vol.11 , pp. 965-982
    • Suppmann, B.1    Sawers, G.2
  • 47
    • 0037047411 scopus 로고    scopus 로고
    • A third bacterial system for the assembly of iron-sulfur clusters with homologs in archaea and plastids
    • Takahashi, Y. & Tokumoto, U. (2002). A third bacterial system for the assembly of iron-sulfur clusters with homologs in archaea and plastids. J Biol Chem 277, 28380-28383.
    • (2002) J Biol Chem , vol.277 , pp. 28380-28383
    • Takahashi, Y.1    Tokumoto, U.2
  • 48
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin, H., Staehelin, T. & Gordon, J. (1979). Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc Natl Acad Sci U S A 76, 4350-4354.
    • (1979) Proc Natl Acad Sci U S A , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 49
    • 67149111967 scopus 로고    scopus 로고
    • Iron-sulfur (Fe/S) protein biogenesis: Phylogenomic and genetic studies of A-type carriers
    • Vinella, D., Brochier-Armanet, C., Loiseau, L., Talla, E. & Barras, F. (2009). Iron-sulfur (Fe/S) protein biogenesis: phylogenomic and genetic studies of A-type carriers. PLoS Genet 5, e1000497.
    • (2009) PLoS Genet , vol.5
    • Vinella, D.1    Brochier-Armanet, C.2    Loiseau, L.3    Talla, E.4    Barras, F.5
  • 50
    • 34250874525 scopus 로고    scopus 로고
    • Crystal structures of [NiFe] hydrogenase maturation proteins HypC, HypD, and HypE: Insights into cyanation reaction by thiol redox signaling
    • Watanabe, S., Matsumi, R., Arai, T., Atomi, H., Imanaka, T. & Miki, K. (2007). Crystal structures of [NiFe] hydrogenase maturation proteins HypC, HypD, and HypE: insights into cyanation reaction by thiol redox signaling. Mol Cell 27, 29-40.
    • (2007) Mol Cell , vol.27 , pp. 29-40
    • Watanabe, S.1    Matsumi, R.2    Arai, T.3    Atomi, H.4    Imanaka, T.5    Miki, K.6
  • 51
    • 0001256080 scopus 로고
    • Nucleotide sequence and expression of the selenocysteine-containing polypeptide of formate dehydrogenase (formate-hydrogen-lyaselinked) from Escherichia coli
    • Zinoni, F., Birkmann, A., Stadtman, T. C. & Bö ck, A. (1986). Nucleotide sequence and expression of the selenocysteine-containing polypeptide of formate dehydrogenase (formate-hydrogen-lyaselinked) from Escherichia coli. Proc Natl Acad Sci U S A 83, 4650-4654.
    • (1986) Proc Natl Acad Sci U S A , vol.83 , pp. 4650-4654
    • Zinoni, F.1    Birkmann, A.2    Stadtman, T.C.3    Böck, A.4


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