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Volumn 251, Issue 3, 1998, Pages 924-934

Biochemical characterization of Anabaena sp. strain PCC 7120 non- specific nuclease NucA and its inhibitor NuiA

Author keywords

Nuclease; Nuclease inhibitor; Protein protein interaction; Steady state kinetics

Indexed keywords

NUCLEASE;

EID: 0032006766     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1998.2510924.x     Document Type: Article
Times cited : (47)

References (55)
  • 1
    • 0026746322 scopus 로고
    • Identification, genetic analysis and characterization of a sugar-non-specific nuclease from the cyanobacterium Anabaena sp. strain PCC 7120
    • Muro-Pastor, A. M., Flores, E., Herrero, A. & Wolk, C. P. (1992) Identification, genetic analysis and characterization of a sugar-non-specific nuclease from the cyanobacterium Anabaena sp. strain PCC 7120, Mol. Microbiol. 6, 3021-3030.
    • (1992) Mol. Microbiol. , vol.6 , pp. 3021-3030
    • Muro-Pastor, A.M.1    Flores, E.2    Herrero, A.3    Wolk, C.P.4
  • 2
    • 0031560778 scopus 로고    scopus 로고
    • The nuiA gene from Anabaena sp.encoding an inhibitor of the NucA sugar-non-specific nuclease
    • Muro-Pastor, A. M., Herrero, A. & Flores, E. (1997) The nuiA gene from Anabaena sp.encoding an inhibitor of the NucA sugar-non-specific nuclease, J. Mol. Biol. 268, 589-598.
    • (1997) J. Mol. Biol. , vol.268 , pp. 589-598
    • Muro-Pastor, A.M.1    Herrero, A.2    Flores, E.3
  • 4
    • 0029084590 scopus 로고
    • Sequence preferences in cleavage of dsDNA and ssDNA by the extracellular Serratia marcescens endonuclease
    • Meiss, G., Friedhoff, P., Hahn, M., Gimadutdinow, O. & Pingoud, A. (1995) Sequence preferences in cleavage of dsDNA and ssDNA by the extracellular Serratia marcescens endonuclease, Biochemistry 34, 11979-11988.
    • (1995) Biochemistry , vol.34 , pp. 11979-11988
    • Meiss, G.1    Friedhoff, P.2    Hahn, M.3    Gimadutdinow, O.4    Pingoud, A.5
  • 5
    • 0014670660 scopus 로고
    • An extracellular nuclease from Serratia marcescens - I. Purification and some properties of the enzyme
    • Nestle, M. & Roberts, W. K. (1969) An extracellular nuclease from Serratia marcescens - I. Purification and some properties of the enzyme, J. Biol. Chem. 244, 5213-5218.
    • (1969) J. Biol. Chem. , vol.244 , pp. 5213-5218
    • Nestle, M.1    Roberts, W.K.2
  • 6
    • 0014670710 scopus 로고
    • An extracellular nuclease from Serratia marcescens - II. Specificity of the enzyme
    • Nestle, M. & Roberts, W. K. (1969) An extracellular nuclease from Serratia marcescens - II. Specificity of the enzyme, J. Biol. Chem. 244, 5219-5225.
    • (1969) J. Biol. Chem. , vol.244 , pp. 5219-5225
    • Nestle, M.1    Roberts, W.K.2
  • 7
    • 0023470603 scopus 로고
    • The extracellular nuclease gene of Serratia marcescens and its secretion from Escherichia coli
    • Ball, T. K., Saurugger, P. N. & Benedik, M. J. (1987) The extracellular nuclease gene of Serratia marcescens and its secretion from Escherichia coli. Gene (Amst.) 57, 183-192.
    • (1987) Gene (Amst.) , vol.57 , pp. 183-192
    • Ball, T.K.1    Saurugger, P.N.2    Benedik, M.J.3
  • 8
    • 0025315488 scopus 로고
    • Genetic and structural characterization of EndA: A membrane-bound nuclease required tor transformation of Streptococcus pneumoniae
    • Puyet, A., Greenberg, B. & Lacks, S. A. (1990) Genetic and structural characterization of EndA: A membrane-bound nuclease required tor transformation of Streptococcus pneumoniae, J. Mol. Biol. 213, 727-738.
    • (1990) J. Mol. Biol. , vol.213 , pp. 727-738
    • Puyet, A.1    Greenberg, B.2    Lacks, S.A.3
  • 9
    • 0024296644 scopus 로고
    • Sequence and expression of NUC1, the gene encoding the mitochondrial nuclease in Saccharomyces cerevisiae
    • Vincent, R. D., Hofmann, T. J. & Zassenhaus, H. P. (1988) Sequence and expression of NUC1, the gene encoding the mitochondrial nuclease in Saccharomyces cerevisiae, Nucleic Acids Res. 16, 3297-3312.
    • (1988) Nucleic Acids Res. , vol.16 , pp. 3297-3312
    • Vincent, R.D.1    Hofmann, T.J.2    Zassenhaus, H.P.3
  • 10
    • 0024278708 scopus 로고
    • Purification and properties of the major nuclease from mitochondria of Saccharomyces cerevisiae
    • Dake, E., Hofmann, T. J., McIntire, S., Hudson, A. & Zassenhaus, H. P. (1988) Purification and properties of the major nuclease from mitochondria of Saccharomyces cerevisiae, J. Biol. Chem. 263, 7691-7702.
    • (1988) J. Biol. Chem. , vol.263 , pp. 7691-7702
    • Dake, E.1    Hofmann, T.J.2    McIntire, S.3    Hudson, A.4    Zassenhaus, H.P.5
  • 11
    • 0027234753 scopus 로고
    • Deoxyribonuclease of Syncephalastrum racemosum: Enzymatic properties and molecular structure
    • Chen, L. Y., Ho, H. C.,Tsai, Y. C. & Liao, T. H. (1993) Deoxyribonuclease of Syncephalastrum racemosum: enzymatic properties and molecular structure. Arch. Biochem. Biophys, 303, 51-56.
    • (1993) Arch. Biochem. Biophys , vol.303 , pp. 51-56
    • Chen, L.Y.1    Ho, H.C.2    Tsai, Y.C.3    Liao, T.H.4
  • 12
    • 0027284549 scopus 로고
    • Primers for mitochondrial DNA replication generated by endonuclease G
    • Ruiz-Carrillo, A. & Cote, J. (1993) Primers for mitochondrial DNA replication generated by endonuclease G, Science 261, 765-769.
    • (1993) Science , vol.261 , pp. 765-769
    • Ruiz-Carrillo, A.1    Cote, J.2
  • 13
    • 0029857896 scopus 로고    scopus 로고
    • Identification and characterization of a mitochondrial endonuclease from yeast, Schizosaccharomyces pombe
    • Ikeda, S., Maeda, N., Ohshima, T. & Takata, N. (1996) Identification and characterization of a mitochondrial endonuclease from yeast, Schizosaccharomyces pombe, Biochem. Mol. Biol. Int. 40, 1017-1024.
    • (1996) Biochem. Mol. Biol. Int. , vol.40 , pp. 1017-1024
    • Ikeda, S.1    Maeda, N.2    Ohshima, T.3    Takata, N.4
  • 14
    • 0028956422 scopus 로고
    • Chromosomal localization of mitochondrial transcription factor A (TCF6), single-stranded DNA-binding protein (SSBP), and endonuclease G (ENDOG), three human housekeeping genes involved in mitochondrial biogenesis
    • Tiranti, V., Rossi, E., Ruiz-Carrillo, A., Rossi, G., Rocchi, M., DiDonato, S., Zuffardi, O. & Zeviani, M. (1995) Chromosomal localization of mitochondrial transcription factor A (TCF6), single-stranded DNA-binding protein (SSBP), and endonuclease G (ENDOG), three human housekeeping genes involved in mitochondrial biogenesis, Genomics 25, 559-564.
    • (1995) Genomics , vol.25 , pp. 559-564
    • Tiranti, V.1    Rossi, E.2    Ruiz-Carrillo, A.3    Rossi, G.4    Rocchi, M.5    DiDonato, S.6    Zuffardi, O.7    Zeviani, M.8
  • 15
    • 0028120676 scopus 로고
    • Transfer of a genetic marker from a megaplasmid of Anabaena sp. strain PCC 7120 to a megaplasmid of a different Anabaena strain
    • Muro-Pastor, A. M., Kuritz, T., Flores, E., Herrero, A. & Wolk, C. P. (1994) Transfer of a genetic marker from a megaplasmid of Anabaena sp. strain PCC 7120 to a megaplasmid of a different Anabaena strain, J. Bacteriol. 176, 1093-1098.
    • (1994) J. Bacteriol. , vol.176 , pp. 1093-1098
    • Muro-Pastor, A.M.1    Kuritz, T.2    Flores, E.3    Herrero, A.4    Wolk, C.P.5
  • 17
    • 0001713635 scopus 로고
    • Isolation and properties of an exocellular nuclease of Serratia marcescens
    • Eaves, G. N. & Jeffries, C. D. (1963) Isolation and properties of an exocellular nuclease of Serratia marcescens, J. Bacteriol. 85, 273-278.
    • (1963) J. Bacteriol. , vol.85 , pp. 273-278
    • Eaves, G.N.1    Jeffries, C.D.2
  • 18
    • 0020761009 scopus 로고
    • Isolation and characterization of nucleases from a clinical isolate of Serratia marcescens kums 3958
    • Yonemura, K., Matsumoto, K. & Maeda, H. (1983) Isolation and characterization of nucleases from a clinical isolate of Serratia marcescens kums 3958, J. Biochem. (Tokyo) 93, 1287-1295.
    • (1983) J. Biochem. (Tokyo) , vol.93 , pp. 1287-1295
    • Yonemura, K.1    Matsumoto, K.2    Maeda, H.3
  • 19
    • 0028114075 scopus 로고
    • Identification of catalytically relevant amino acids of the extracellular Serratia marcescens endonuclease by alignment-guided mutagenesis
    • Friedhoff, P., Gimadutdinow, O. & Pingoud, A. (1994) Identification of catalytically relevant amino acids of the extracellular Serratia marcescens endonuclease by alignment-guided mutagenesis, Nucleic Acids Res. 22, 3280-3287.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 3280-3287
    • Friedhoff, P.1    Gimadutdinow, O.2    Pingoud, A.3
  • 20
    • 0030571045 scopus 로고    scopus 로고
    • A quantitative microtiter plate nuclease assay based on ethidium/DNA fluorescence
    • Friedhoff, P., Matzen, S. E., Meiss, G. & Pingoud, A. (1996) A quantitative microtiter plate nuclease assay based on ethidium/DNA fluorescence. Anal. Biochem. 240, 283-288.
    • (1996) Anal. Biochem. , vol.240 , pp. 283-288
    • Friedhoff, P.1    Matzen, S.E.2    Meiss, G.3    Pingoud, A.4
  • 21
    • 0027977143 scopus 로고
    • 2.1 Å structure of Serratia endonuclease suggests a mechanism for binding to double-stranded DNA
    • Miller, M. D., Tanner, J., Alpaugh, M., Benedik, M. J. & Krause, K. L. (1994) 2.1 Å structure of Serratia endonuclease suggests a mechanism for binding to double-stranded DNA. Nature Struct. Biol. 1, 461-468.
    • (1994) Nature Struct. Biol. , vol.1 , pp. 461-468
    • Miller, M.D.1    Tanner, J.2    Alpaugh, M.3    Benedik, M.J.4    Krause, K.L.5
  • 22
    • 0030068478 scopus 로고    scopus 로고
    • Identification of the Serratia endonuclease dimer: Structural basis and implications for catalysis
    • Miller, M. D. & Krause, K. L. (1996) Identification of the Serratia endonuclease dimer: Structural basis and implications for catalysis, Protein Sci. 5, 24-33.
    • (1996) Protein Sci. , vol.5 , pp. 24-33
    • Miller, M.D.1    Krause, K.L.2
  • 24
    • 0030592844 scopus 로고    scopus 로고
    • Analysis of the reaction mechanism of the non-specific endonuclease of Serratia marcescens using an artificial substrate
    • Kolmes, B., Franke, I., Friedhoff, P. & Pingoud, A. (1996) Analysis of the reaction mechanism of the non-specific endonuclease of Serratia marcescens using an artificial substrate, FEBS Lett. 397, 343-346.
    • (1996) FEBS Lett. , vol.397 , pp. 343-346
    • Kolmes, B.1    Franke, I.2    Friedhoff, P.3    Pingoud, A.4
  • 25
    • 0028373557 scopus 로고
    • A procedure for renaturation and purification of the extracellular Serratia marcescens nuclease from genetically engineered Escherichia coli
    • Friedhoff, P., Gimadutdinow, O., Rüter, T., Wende, W., Urbanke, C., Thole, H. & Pingoud, A. (1994) A procedure for renaturation and purification of the extracellular Serratia marcescens nuclease from genetically engineered Escherichia coli, Protein Exp. Purif. 5, 37-43.
    • (1994) Protein Exp. Purif. , vol.5 , pp. 37-43
    • Friedhoff, P.1    Gimadutdinow, O.2    Rüter, T.3    Wende, W.4    Urbanke, C.5    Thole, H.6    Pingoud, A.7
  • 26
    • 0025311083 scopus 로고
    • Use of a conditionally lethal gene in Anabaena sp. PCC7120 to select for double recombinants and to entrap insertion sequences
    • Cai, Y. & Wolk, C. P. (1990) Use of a conditionally lethal gene in Anabaena sp. PCC7120 to select for double recombinants and to entrap insertion sequences. J. Bacteriol. 172, 3138-3145.
    • (1990) J. Bacteriol. , vol.172 , pp. 3138-3145
    • Cai, Y.1    Wolk, C.P.2
  • 29
    • 0029962371 scopus 로고    scopus 로고
    • Mutational analysis of mammalian poly(A) polymerase identifies a region for primer binding and a catalytic domain, homologuous to the family X polymerases, and to other nucleotidyltransferases
    • Martin, G. & Keller, W. (1996) Mutational analysis of mammalian poly(A) polymerase identifies a region for primer binding and a catalytic domain, homologuous to the family X polymerases, and to other nucleotidyltransferases, EMBO J. 15, 2593-2603.
    • (1996) EMBO J. , vol.15 , pp. 2593-2603
    • Martin, G.1    Keller, W.2
  • 30
    • 0025606431 scopus 로고
    • Molecular cloning and expression of a hexameric Drosophila heat shock factor subject to negative regulation
    • Clos, J., Westwood, J. T., Becker, P. B., Wilson, S., Lambert, K. & Wu, C. (1990) Molecular cloning and expression of a hexameric Drosophila heat shock factor subject to negative regulation, Cell 63, 1085-1097.
    • (1990) Cell , vol.63 , pp. 1085-1097
    • Clos, J.1    Westwood, J.T.2    Becker, P.B.3    Wilson, S.4    Lambert, K.5    Wu, C.6
  • 31
    • 0026556568 scopus 로고
    • The role of the N terminus in Tet repressor for tet operator binding determined by a mutational analysis
    • Berens, C., Altschmied, L. & Hillen, W. (1992) The role of the N terminus in Tet repressor for tet operator binding determined by a mutational analysis, J. Biol. Chem. 267, 1945-1952.
    • (1992) J. Biol. Chem. , vol.267 , pp. 1945-1952
    • Berens, C.1    Altschmied, L.2    Hillen, W.3
  • 32
    • 0028555357 scopus 로고
    • Use of the tetracycline promoter for the tightly regulated production of a murine antibody fragment in Escherichia coli
    • Skerra, A. (1994) Use of the tetracycline promoter for the tightly regulated production of a murine antibody fragment in Escherichia coli, Gene (Amst.) 151, 131-135.
    • (1994) Gene (Amst.) , vol.151 , pp. 131-135
    • Skerra, A.1
  • 33
    • 0020338572 scopus 로고
    • Enhanced expression of cro-beta-galactosidase fusion proteins under the control of the PR promoter of bacteriophage lambda
    • Zabeuu, M. & Stanley, K. K. (1982) Enhanced expression of cro-beta-galactosidase fusion proteins under the control of the PR promoter of bacteriophage lambda, EMBO J. 1, 1217-1222.
    • (1982) EMBO J. , vol.1 , pp. 1217-1222
    • Zabeuu, M.1    Stanley, K.K.2
  • 34
    • 0028871804 scopus 로고
    • How to measure and predict the molar absorption coefficient of a protein
    • Pace, C. N., Vajdos, F., Fee, L., Grimsley, G. & Gray, T. (1995) How to measure and predict the molar absorption coefficient of a protein, Protein Sci. 4, 2411-2425.
    • (1995) Protein Sci. , vol.4 , pp. 2411-2425
    • Pace, C.N.1    Vajdos, F.2    Fee, L.3    Grimsley, G.4    Gray, T.5
  • 35
    • 76549250377 scopus 로고
    • Crystalline deoxyribonuclease I. Isolation and general properties. Spectrophotometric method for the measurement of desoxyribonuclease activity
    • Kunitz, M. (1950) Crystalline deoxyribonuclease I. Isolation and general properties. Spectrophotometric method for the measurement of desoxyribonuclease activity, J. Gen. Physiol. 33, 349-362.
    • (1950) J. Gen. Physiol. , vol.33 , pp. 349-362
    • Kunitz, M.1
  • 38
    • 0343678026 scopus 로고
    • Determination of the secondary structure of proteins from their circular dichroism spectra. I. Protein reference spectra for alpha-, beta- and irregular structures
    • Bolotina, I. A., Chekhov, V. O., Lugauskas, V., Finkel'shtein, A. V. & Ptitsyn, O. B. (1980) Determination of the secondary structure of proteins from their circular dichroism spectra. I. Protein reference spectra for alpha-, beta- and irregular structures, Mol. Biol. Mosk. 14, 891-902.
    • (1980) Mol. Biol. Mosk. , vol.14 , pp. 891-902
    • Bolotina, I.A.1    Chekhov, V.O.2    Lugauskas, V.3    Finkel'shtein, A.V.4    Ptitsyn, O.B.5
  • 39
    • 0029120603 scopus 로고
    • The roles of arginine 41 and tyrosine 76 in the coupling of DNA recognition to phosphodiester bond cleavage by DNaseI: A study using site directed mutagenesis
    • Doherty, A. J., Worrall, A. F. & Connolly, B. A. (1995) The roles of arginine 41 and tyrosine 76 in the coupling of DNA recognition to phosphodiester bond cleavage by DNaseI: a study using site directed mutagenesis. J. Mol. Biol 251, 366-377.
    • (1995) J. Mol. Biol , vol.251 , pp. 366-377
    • Doherty, A.J.1    Worrall, A.F.2    Connolly, B.A.3
  • 40
    • 0026675734 scopus 로고
    • Disulfide bonds are required for Serratia marcescens nuclease activity
    • Ball, T. K., Sih, Y. & Benedik, M. J. (1992) Disulfide bonds are required for Serratia marcescens nuclease activity, Nucleic Acids Res. 20, 4971-4974.
    • (1992) Nucleic Acids Res. , vol.20 , pp. 4971-4974
    • Ball, T.K.1    Sih, Y.2    Benedik, M.J.3
  • 41
    • 0022180173 scopus 로고
    • High-level production of the EcoR1 endonuclease under control of the pL promoter of bacteriophage lambda
    • Botterman, J. & Zabeau, M. (1985) High-level production of the EcoR1 endonuclease under control of the pL promoter of bacteriophage lambda, Gene (Amst.) 37, 229-239.
    • (1985) Gene (Amst.) , vol.37 , pp. 229-239
    • Botterman, J.1    Zabeau, M.2
  • 42
    • 0024293097 scopus 로고
    • Barnase and barstar: Expression of its cloned inhibitor permits expression of a cloned ribonuclease
    • Hartley, R. W. (1988) Barnase and barstar: expression of its cloned inhibitor permits expression of a cloned ribonuclease, J. Mol. Biol. 202, 913-915.
    • (1988) J. Mol. Biol. , vol.202 , pp. 913-915
    • Hartley, R.W.1
  • 43
    • 0024276066 scopus 로고
    • Expression of the chemically synthesized gene for ribonuclease T1 in Escherichia coli using a secretion cloning vector
    • Quaas, R., McKeown, Y., Stanssens, P., Frank, R., Blöcker, H. & Hahn, U. (1988) Expression of the chemically synthesized gene for ribonuclease T1 in Escherichia coli using a secretion cloning vector, Eur. J. Biochem. 173, 617-622.
    • (1988) Eur. J. Biochem. , vol.173 , pp. 617-622
    • Quaas, R.1    McKeown, Y.2    Stanssens, P.3    Frank, R.4    Blöcker, H.5    Hahn, U.6
  • 46
    • 0031004544 scopus 로고    scopus 로고
    • The application of circular dichroism to studies of protein folding and unfolding
    • Kelly, S. M. & Price, N. C. (1997) The application of circular dichroism to studies of protein folding and unfolding, Biochim. Biophys, Acta 1338, 161-185.
    • (1997) Biochim. Biophys, Acta , vol.1338 , pp. 161-185
    • Kelly, S.M.1    Price, N.C.2
  • 47
    • 0023662556 scopus 로고
    • 1H NMR spectroscopy of conformational changes accompanying substitution for glutamic acid-43
    • 1H NMR spectroscopy of conformational changes accompanying substitution for glutamic acid-43, Biochemistry 26, 6278-6286.
    • (1987) Biochemistry , vol.26 , pp. 6278-6286
    • Hibler, D.W.1    Stolowich, N.J.2    Reynolds, M.A.3    Gerlt, J.A.4
  • 49
    • 0021140818 scopus 로고
    • DNA structural variations in the E. coli tyrT promoter
    • Drew, H. R. & Travers, A. A. (1984) DNA structural variations in the E. coli tyrT promoter, Cell 37, 491-502.
    • (1984) Cell , vol.37 , pp. 491-502
    • Drew, H.R.1    Travers, A.A.2
  • 50
    • 0028220190 scopus 로고
    • Characterization of preferred deoxyribonuclease 1 cleavage sites
    • Herrera, J. E. & Chairs, J. B. (1994) Characterization of preferred deoxyribonuclease 1 cleavage sites, J. Mol. Biol 236, 405-411.
    • (1994) J. Mol. Biol , vol.236 , pp. 405-411
    • Herrera, J.E.1    Chairs, J.B.2
  • 51
    • 0029039118 scopus 로고
    • Sequence-dependent bending propensity of DNA as revealed by DNasel: Parameters for trinucleotides
    • Brukner, I., Sanchez, R., Suck, D. & Pongor, S. (1995) Sequence-dependent bending propensity of DNA as revealed by DNasel: parameters for trinucleotides, EMBO J. 14, 1812-1818.
    • (1995) EMBO J. , vol.14 , pp. 1812-1818
    • Brukner, I.1    Sanchez, R.2    Suck, D.3    Pongor, S.4
  • 52
    • 0030902167 scopus 로고    scopus 로고
    • Effects of non-conservative changes to tyrosine 76, A key DNA binding residue of DNasel, on phosphodiester bond cleavage and DNA hydrolysis selectivity
    • Warren, M. A., Steven, J. E. & Connolly, B. A. (1997) Effects of non-conservative changes to tyrosine 76, a key DNA binding residue of DNasel, on phosphodiester bond cleavage and DNA hydrolysis selectivity, Protein Eng. 10, 279-283.
    • (1997) Protein Eng. , vol.10 , pp. 279-283
    • Warren, M.A.1    Steven, J.E.2    Connolly, B.A.3
  • 53
    • 0027177102 scopus 로고
    • Interaction of barnase with its polypeptide inhibitor barstar studied by protein engineering
    • Schreiber, G. & Fersht, A. R. (1993) Interaction of barnase with its polypeptide inhibitor barstar studied by protein engineering, Biochemistry 32, 5145-5150.
    • (1993) Biochemistry , vol.32 , pp. 5145-5150
    • Schreiber, G.1    Fersht, A.R.2
  • 54
    • 0014528703 scopus 로고
    • The action of staphylococcal nuclease on synthetic substrates
    • Cuatrecasas, P., Wilchek, M. & Anfinson, C. B. (1969) The action of staphylococcal nuclease on synthetic substrates, Biochemistry 8, 2277-2284.
    • (1969) Biochemistry , vol.8 , pp. 2277-2284
    • Cuatrecasas, P.1    Wilchek, M.2    Anfinson, C.B.3
  • 55
    • 0027179892 scopus 로고
    • Mechanism of the reaction catalyzed by Staphylococcal nuclease: Identification of the rate-determining step
    • Hale, S. P., Poole, L. B. & Gerlt, J. A. (1993) Mechanism of the reaction catalyzed by Staphylococcal nuclease: Identification of the rate-determining step, Biochemistry 32, 7479-7487.
    • (1993) Biochemistry , vol.32 , pp. 7479-7487
    • Hale, S.P.1    Poole, L.B.2    Gerlt, J.A.3


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