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Volumn 9, Issue 1, 2000, Pages 53-63

The use of nucleotide analogs to evaluate the mechanism of the heterotropic response of Escherichia coli aspartate transcarbamoylase

Author keywords

Allosteric enzyme; Electrostatic interactions; Regulation

Indexed keywords

ASPARTATE CARBAMOYLTRANSFERASE; NUCLEOTIDE DERIVATIVE;

EID: 0033974204     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.9.1.53     Document Type: Article
Times cited : (5)

References (49)
  • 1
    • 0022432722 scopus 로고
    • Conformations of bound nucleoside triphosphate effectors in aspartate transcarbamolyase. Evidence for the London-Schmidt model by transferred nuclear overhauser effects
    • Banerjee A, Levy HR, Levy GC, Chan WW-C. 1985. Conformations of bound nucleoside triphosphate effectors in aspartate transcarbamolyase. Evidence for the London-Schmidt Model by transferred nuclear Overhauser effects. Biochemistry 24:1593-1598.
    • (1985) Biochemistry , vol.24 , pp. 1593-1598
    • Banerjee, A.1    Levy, H.R.2    Levy, G.C.3    Chan, W.-C.4
  • 2
    • 0014250308 scopus 로고
    • Allosteric interactions in aspartate transcarbamoylase: Binding of specific ligands to the native enzyme and isolated subunits
    • Changeux J-P, Gerhart JC, Schachman HK. 1968. Allosteric interactions in aspartate transcarbamoylase: Binding of specific ligands to the native enzyme and isolated subunits. Biochemistry 7:531-538.
    • (1968) Biochemistry , vol.7 , pp. 531-538
    • Changeux, J.-P.1    Gerhart, J.C.2    Schachman, H.K.3
  • 3
    • 0024593467 scopus 로고
    • Discrimination between nucleotide effector responses of aspartate transcarbamoylase due to a singe site substitution in the allosteric binding site
    • Corder TS, Wild JR. 1989. Discrimination between nucleotide effector responses of aspartate transcarbamoylase due to a singe site substitution in the allosteric binding site. J Biol Chem 264:7425-7430.
    • (1989) J Biol Chem , vol.264 , pp. 7425-7430
    • Corder, T.S.1    Wild, J.R.2
  • 4
    • 78651153791 scopus 로고
    • Disc electrophoresis - II. Method and application to human serum proteins
    • Davis BJ. 1964. Disc electrophoresis - II. Method and application to human serum proteins. Ann NY Acad Sci 121:680-685.
    • (1964) Ann NY Acad Sci , vol.121 , pp. 680-685
    • Davis, B.J.1
  • 5
    • 0032537602 scopus 로고    scopus 로고
    • The influence of the regulatory chain amino acids Glu-62 and Ile-12 on the heterotropic properties of Escherichia coli aspartate transcarbamoylase
    • Dutta M, Kantrowitz ER. 1998. The influence of the regulatory chain amino acids Glu-62 and Ile-12 on the heterotropic properties of Escherichia coli aspartate transcarbamoylase. Biochemistry 57:8653-8658.
    • (1998) Biochemistry , vol.57 , pp. 8653-8658
    • Dutta, M.1    Kantrowitz, E.R.2
  • 6
    • 0027609916 scopus 로고
    • SETOR: Hardware-lighted three-dimensional solid representations of macromolecules
    • Evans SV. 1993. SETOR: Hardware-lighted three-dimensional solid representations of macromolecules. J Mol Graphics 11:134-138.
    • (1993) J Mol Graphics , vol.11 , pp. 134-138
    • Evans, S.V.1
  • 7
    • 0014216815 scopus 로고
    • The purification of aspartate transcarbamylase of Escherichia coli and separation of its protein subunits
    • Gerhart JC, Holoubek H. 1967. The purification of aspartate transcarbamylase of Escherichia coli and separation of its protein subunits. J Biol Chem 242:2886-2892.
    • (1967) J Biol Chem , vol.242 , pp. 2886-2892
    • Gerhart, J.C.1    Holoubek, H.2
  • 8
    • 0001425337 scopus 로고
    • Enzymology of control by feedback inhibition
    • Gerhart JC, Pardee AB. 1962. Enzymology of control by feedback inhibition. J Biol Chem 237:891-896.
    • (1962) J Biol Chem , vol.237 , pp. 891-896
    • Gerhart, J.C.1    Pardee, A.B.2
  • 9
    • 0000572386 scopus 로고
    • The effect of the feedback inhibitor CTP, on subunit interactions in aspartate transcarbamylase
    • Gerhart JC, Pardee AB. 1963. The effect of the feedback inhibitor CTP, on subunit interactions in aspartate transcarbamylase. Cold Spring Harbor Symp Quant Biol 28:491-496.
    • (1963) Cold Spring Harbor Symp Quant Biol , vol.28 , pp. 491-496
    • Gerhart, J.C.1    Pardee, A.B.2
  • 10
    • 0025081851 scopus 로고
    • Crystal structures of aspartate carbamoyltransferase ligated with phosphonoacetamide, malonate and CTP or ATP at 2.8 Å resolution and neutral pH
    • Gouaux JE, Stevens RC, Lipscomb WN. 1990. Crystal structures of aspartate carbamoyltransferase ligated with phosphonoacetamide, malonate and CTP or ATP at 2.8 Å resolution and neutral pH. Biochemistry 29:7702-7715.
    • (1990) Biochemistry , vol.29 , pp. 7702-7715
    • Gouaux, J.E.1    Stevens, R.C.2    Lipscomb, W.N.3
  • 11
    • 0015822120 scopus 로고
    • Interaction of aspartate transcarbamylase with regulatory nucleotides
    • Gray CW, Chamberlin M, Gray D. 1973. Interaction of aspartate transcarbamylase with regulatory nucleotides. J Biol Chem 248:6071-6079.
    • (1973) J Biol Chem , vol.248 , pp. 6071-6079
    • Gray, C.W.1    Chamberlin, M.2    Gray, D.3
  • 12
    • 0020347099 scopus 로고
    • Interactions of metal-nucleotide complexes with aspartate carbamoyltransferase in the crystalline state
    • Honzatko RB, Lipscomb WN. 1982a. Interactions of metal-nucleotide complexes with aspartate carbamoyltransferase in the crystalline state. Proc Natl Acad Sci USA 79:7171-7174.
    • (1982) Proc Natl Acad Sci USA , vol.79 , pp. 7171-7174
    • Honzatko, R.B.1    Lipscomb, W.N.2
  • 13
    • 0020367718 scopus 로고
    • Interactions of phosphate ligands with Escherichia coli aspartate cambamoyltransferase in the crystalline state
    • Honzatko RB, Lipscomb WN. 1982b. Interactions of phosphate ligands with Escherichia coli aspartate cambamoyltransferase in the crystalline state. J Mol Biol 160:265-286.
    • (1982) J Mol Biol , vol.160 , pp. 265-286
    • Honzatko, R.B.1    Lipscomb, W.N.2
  • 14
    • 0025058563 scopus 로고
    • Escherichia coli aspartate transcarbamoylase: The molecular basis for a concerted allosteric transition
    • Kantrowitz ER, Lipscomb WN. 1990. Escherichia coli aspartate transcarbamoylase: The molecular basis for a concerted allosteric transition. Trends Biochem Sci (Pers Ed) 15:53-59.
    • (1990) Trends Biochem Sci (Pers Ed) , vol.15 , pp. 53-59
    • Kantrowitz, E.R.1    Lipscomb, W.N.2
  • 15
    • 0027399487 scopus 로고
    • Crystal structure of CTP-ligated T state aspartate transcarbamoylase at 2.5 Å resolution: Implications for aspartate transcarbamoylase mutants and the mechanism of negative cooperativity
    • Kosman RP, Gouaux JE, Lipscomb WN. 1993. Crystal structure of CTP-ligated T state aspartate transcarbamoylase at 2.5 Å resolution: Implications for aspartate transcarbamoylase mutants and the mechanism of negative cooperativity. Proteins Struct Funct Genet 75:147-176.
    • (1993) Proteins Struct Funct Genet , vol.75 , pp. 147-176
    • Kosman, R.P.1    Gouaux, J.E.2    Lipscomb, W.N.3
  • 16
    • 0023160005 scopus 로고
    • 2.5 Å structure of aspartate carbamoyltransferase complexed with the bisubstrate analog N-(phosphonacetyl)-L-aspartate
    • Krause KL, Voltz KW, Lipscomb WN. 1987. 2.5 Å structure of aspartate carbamoyltransferase complexed with the bisubstrate analog N-(phosphonacetyl)-L-aspartate. J Mol Biol 193:527-553.
    • (1987) J Mol Biol , vol.193 , pp. 527-553
    • Krause, K.L.1    Voltz, K.W.2    Lipscomb, W.N.3
  • 17
    • 0022429817 scopus 로고
    • Structure-function relationship in allosteric aspartate carbamoyltransferase from Escherichia coli: II. Involvement of the C-terminal region of the regulatory chain in homotropic and heterotropic interactions
    • Ladjimi MM, Ghellis C, Feller A, Cunin R, Glansdorff N, Pierard A, Hervé G. 1985. Structure-function relationship in allosteric aspartate carbamoyltransferase from Escherichia coli: II. Involvement of the C-terminal region of the regulatory chain in homotropic and heterotropic interactions. J Mol Biol 186:715-724.
    • (1985) J Mol Biol , vol.186 , pp. 715-724
    • Ladjimi, M.M.1    Ghellis, C.2    Feller, A.3    Cunin, R.4    Glansdorff, N.5    Pierard, A.6    Hervé, G.7
  • 18
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK. 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
  • 19
    • 0028144138 scopus 로고
    • Aspartate transcarbamoylase from Escherichia coli: Activity and regulation
    • Lipscomb WN. 1994. Aspartate transcarbamoylase from Escherichia coli: Activity and regulation. Adv Enzymol 68:67-151.
    • (1994) Adv Enzymol , vol.68 , pp. 67-151
    • Lipscomb, W.N.1
  • 20
    • 0015384106 scopus 로고
    • A model for nucleotide regulation of aspartate transcarbamylase
    • London RE, Schmidt PG. 1972. A model for nucleotide regulation of aspartate transcarbamylase. Biochemistry 11:3136-3142.
    • (1972) Biochemistry , vol.11 , pp. 3136-3142
    • London, R.E.1    Schmidt, P.G.2
  • 21
    • 0024589767 scopus 로고
    • Rapid and efficient synthesis of nucleoside 5′-O-(1-thiotriphosphates), 5-triphosphates and 2′,3′-cyclophosphorothioates using 2-chloro-4H-1,3,2-benzodioxaphosphorin-4-one
    • Ludwig J, Eckstein F. 1989. Rapid and efficient synthesis of nucleoside 5′-O-(1-thiotriphosphates), 5-triphosphates and 2′,3′-cyclophosphorothioates using 2-chloro-4H-1,3,2-benzodioxaphosphorin-4-one. J Org Chem 54:631-635.
    • (1989) J Org Chem , vol.54 , pp. 631-635
    • Ludwig, J.1    Eckstein, F.2
  • 23
    • 0015937197 scopus 로고
    • Equilibrium binding study of the interaction of aspartate transcarbamoylase with cytidine 5′-triphosphate and adenosine 5′-triphosphate
    • Matsumoto S, Hammes GG. 1973. Equilibrium binding study of the interaction of aspartate transcarbamoylase with cytidine 5′-triphosphate and adenosine 5′-triphosphate. Biochemistry 12:1388-1394.
    • (1973) Biochemistry , vol.12 , pp. 1388-1394
    • Matsumoto, S.1    Hammes, G.G.2
  • 24
    • 0000089842 scopus 로고
    • Three-dimensional structures of aspartate carbamoyltransferase from Escherichia coli and of its complex with cytidine triphosphate
    • Monaco HL, Crawford JL, Lipscomb WN. 1978. Three-dimensional structures of aspartate carbamoyltransferase from Escherichia coli and of its complex with cytidine triphosphate. Proc Natl Acad Sci USA 75:5276-5280.
    • (1978) Proc Natl Acad Sci USA , vol.75 , pp. 5276-5280
    • Monaco, H.L.1    Crawford, J.L.2    Lipscomb, W.N.3
  • 25
    • 78651189765 scopus 로고
    • On the nature of allosteric transitions: A plausible model
    • Monod J, Wyman J, Changeux JP. 1965. On the nature of allosteric transitions: A plausible model. J Mol Biol 12:88-118.
    • (1965) J Mol Biol , vol.12 , pp. 88-118
    • Monod, J.1    Wyman, J.2    Changeux, J.P.3
  • 26
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls A, Sharp KA, Honig B. 1991. Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins 11:281-296.
    • (1991) Proteins , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 27
    • 0022382162 scopus 로고
    • Superproduction and rapid purification of E. coli aspartate transcarbamoylase and its catalytic subunit under extreme derepression of the pyrimidine pathway
    • Nowlan SF, Kantrowitz, ER. 1985. Superproduction and rapid purification of E. coli aspartate transcarbamoylase and its catalytic subunit under extreme derepression of the pyrimidine pathway. J Biol Chem 260:14712-14716.
    • (1985) J Biol Chem , vol.260 , pp. 14712-14716
    • Nowlan, S.F.1    Kantrowitz, E.R.2
  • 28
    • 78651163419 scopus 로고
    • Disc electrophoresis - I. Background and theory
    • Ornstein L. 1964. Disc electrophoresis - I. Background and theory. Ann NY Acad Sci 121:321-349.
    • (1964) Ann NY Acad Sci , vol.121 , pp. 321-349
    • Ornstein, L.1
  • 29
    • 0019799867 scopus 로고
    • An improved colorimetric assay for aspartate and ornithine transcarbamylases
    • Pastra-Landis SC, Foote J, Kantrowitz ER. 1981. An improved colorimetric assay for aspartate and ornithine transcarbamylases. Anal Biochem 118: 358-363.
    • (1981) Anal Biochem , vol.118 , pp. 358-363
    • Pastra-Landis, S.C.1    Foote, J.2    Kantrowitz, E.R.3
  • 30
    • 0342416705 scopus 로고
    • Regeneration of active enzyme by formation of hybrids from inactive derivatives: Implications for active sites shared between polypeptide chains of aspartate transcarbamoylase
    • Robey EA, Schachman HK. 1985. Regeneration of active enzyme by formation of hybrids from inactive derivatives: Implications for active sites shared between polypeptide chains of aspartate transcarbamoylase. Proc Natl Acad Sci USA 82:361-365.
    • (1985) Proc Natl Acad Sci USA , vol.82 , pp. 361-365
    • Robey, E.A.1    Schachman, H.K.2
  • 31
    • 0032488598 scopus 로고    scopus 로고
    • The N-terminal region of the regulatory chain of E. coli aspartate transcarbamoylase is important for both nucleotide binding and the heterotropic mechanism
    • Sakash JB, Kantrowitz, ER. 1998. The N-terminal region of the regulatory chain of E. coli aspartate transcarbamoylase is important for both nucleotide binding and the heterotropic mechanism. Biochemistry 37:281-288.
    • (1998) Biochemistry , vol.37 , pp. 281-288
    • Sakash, J.B.1    Kantrowitz, E.R.2
  • 32
    • 0023042212 scopus 로고
    • Involvement of tryptophan 209 in the allosteric interactions of Escherichia coli aspartate transcarbamylase using single amino acid substitution mutants
    • Smith KA, Nowlan SF, Middleton SA, O'Donovan C, Kantrowitz ER. 1986. Involvement of tryptophan 209 in the allosteric interactions of Escherichia coli aspartate transcarbamylase using single amino acid substitution mutants. J Mol Biol 189:227-238.
    • (1986) J Mol Biol , vol.189 , pp. 227-238
    • Smith, K.A.1    Nowlan, S.F.2    Middleton, S.A.3    O'Donovan, C.4    Kantrowitz, E.R.5
  • 33
    • 0024501782 scopus 로고
    • Three residues involved in binding and catalysis in the carbamyl phosphate binding site of Escherichia coli aspartate transcarbamylase
    • Stebbins JW, Xu W, Kantrowitz ER. 1989. Three residues involved in binding and catalysis in the carbamyl phosphate binding site of Escherichia coli aspartate transcarbamylase. Biochemistry 28:2592-2600.
    • (1989) Biochemistry , vol.28 , pp. 2592-2600
    • Stebbins, J.W.1    Xu, W.2    Kantrowitz, E.R.3
  • 34
    • 0025852356 scopus 로고
    • Escherichia coli aspartate carbamoyltransferase: The probing of crystal structure analysis via site-specific mutagenesis
    • Stevens RC, Chook YM, Cho CY, Lipscomb WN, Kantrowitz ER. 1991. Escherichia coli aspartate carbamoyltransferase: The probing of crystal structure analysis via site-specific mutagenesis. Protein Eng 4:391-408.
    • (1991) Protein Eng , vol.4 , pp. 391-408
    • Stevens, R.C.1    Chook, Y.M.2    Cho, C.Y.3    Lipscomb, W.N.4    Kantrowitz, E.R.5
  • 35
    • 0025002987 scopus 로고
    • Structural consequences of effector binding to the T state of aspartate carbamoyltransferase: Crystal structures of the unligated and ATP- and CTP-complexed enzymes at 2.6 Å resolution
    • Stevens RC, Gouaux JE, Lipscomb WN. 1990. Structural consequences of effector binding to the T state of aspartate carbamoyltransferase: Crystal structures of the unligated and ATP- and CTP-complexed enzymes at 2.6 Å resolution. Biochemistry 29:7691-7701.
    • (1990) Biochemistry , vol.29 , pp. 7691-7701
    • Stevens, R.C.1    Gouaux, J.E.2    Lipscomb, W.N.3
  • 36
    • 0025106487 scopus 로고
    • Allosteric control of quaternary states of E. coli aspartate transcarbamoylase
    • Stevens RC, Lipscomb WN. 1990. Allosteric control of quaternary states of E. coli aspartate transcarbamoylase. Biochem Biophys Res Commun 171: 1312-1318.
    • (1990) Biochem Biophys Res Commun , vol.171 , pp. 1312-1318
    • Stevens, R.C.1    Lipscomb, W.N.2
  • 37
    • 0017649170 scopus 로고
    • Asymmetry of binding and physical assignments of CTP and ATP sites in aspartate transcarbamoylase
    • Suter P, Rosenbusch JP. 1977. Asymmetry of binding and physical assignments of CTP and ATP sites in aspartate transcarbamoylase. J Biol Chem 252: 8136-8141.
    • (1977) J Biol Chem , vol.252 , pp. 8136-8141
    • Suter, P.1    Rosenbusch, J.P.2
  • 38
    • 0018233269 scopus 로고
    • The stimulation of E. coli aspartate transcarbamoylase activity by adenosine triphosphate
    • Thiry L, Hervé G. 1978. The stimulation of E. coli aspartate transcarbamoylase activity by adenosine triphosphate. J Mol Biol 125:515-539.
    • (1978) J Mol Biol , vol.125 , pp. 515-539
    • Thiry, L.1    Hervé, G.2
  • 39
    • 0016188295 scopus 로고
    • Interaction of aspartate transcarbamoylase with 5-bromocytidine 5′-tri-, di-, and monophosphates
    • Tondre C, Hammes GG. 1974. Interaction of aspartate transcarbamoylase with 5-bromocytidine 5′-tri-, di-, and monophosphates. Biochemistry 13:3131-3136.
    • (1974) Biochemistry , vol.13 , pp. 3131-3136
    • Tondre, C.1    Hammes, G.G.2
  • 40
    • 0028922586 scopus 로고
    • LIGPLOT: A program to generate schematic diagrams of protein-ligand interactions
    • Wallace AC, Laskowski RA, Thornton JM. 1995. LIGPLOT: A program to generate schematic diagrams of protein-ligand interactions. Protein Eng 8:127-134.
    • (1995) Protein Eng , vol.8 , pp. 127-134
    • Wallace, A.C.1    Laskowski, R.A.2    Thornton, J.M.3
  • 41
    • 0015527834 scopus 로고
    • CIV. Total synthesis of the structural gene for an alanine transfer ribonucleic acid from yeast. Chemical synthesis of an icosadeoxynucleotide corresponding to the nucleotide sequence 21 to 40
    • Weber H, Khorana HG. 1972. CIV. Total synthesis of the structural gene for an alanine transfer ribonucleic acid from yeast. Chemical synthesis of an icosadeoxynucleotide corresponding to the nucleotide sequence 21 to 40. J Mol Biol 72:219-249.
    • (1972) J Mol Biol , vol.72 , pp. 219-249
    • Weber, H.1    Khorana, H.G.2
  • 42
    • 0008697435 scopus 로고
    • Shared active sites in oligomeric enzymes: Model studies with defective mutants of aspartate transcarbamoylase produced by site-directed mutagenesis
    • Wente SR, Schachman HK. 1987. Shared active sites in oligomeric enzymes: Model studies with defective mutants of aspartate transcarbamoylase produced by site-directed mutagenesis. Proc Natl Acad Sci USA 84:31-35.
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 31-35
    • Wente, S.R.1    Schachman, H.K.2
  • 43
    • 0005552966 scopus 로고
    • In the presence of CTP, UTP becomes an allosteric inhibitor of aspartate transcarbamylase
    • Wild JR, Loughrey-Chen SJ, Corder TS. 1989. In the presence of CTP, UTP becomes an allosteric inhibitor of aspartate transcarbamylase. Proc Natl Acad Sci USA 86:46-50.
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 46-50
    • Wild, J.R.1    Loughrey-Chen, S.J.2    Corder, T.S.3
  • 44
    • 0032493680 scopus 로고    scopus 로고
    • A single mutation in the regulatory chain of Escherichia coli aspartate transcarbamoylase is an extreme T-state structure
    • Williams MK, Stec B, Kantrowitz ER. 1998. A single mutation in the regulatory chain of Escherichia coli aspartate transcarbamoylase is an extreme T-state structure. J Mol Biol 281:121-134.
    • (1998) J Mol Biol , vol.281 , pp. 121-134
    • Williams, M.K.1    Stec, B.2    Kantrowitz, E.R.3
  • 45
    • 0014943828 scopus 로고
    • Binding of cytidine triphosphate to aspartate transcarbamylase
    • Winlund CC, Chamberlin MJ. 1970. Binding of cytidine triphosphate to aspartate transcarbamylase. Biochem Biophys Res Commun 40:43-49.
    • (1970) Biochem Biophys Res Commun , vol.40 , pp. 43-49
    • Winlund, C.C.1    Chamberlin, M.J.2
  • 46
    • 0024962397 scopus 로고
    • Lysine-60 in the regulatory chain of Escherichia coli aspartate transcarhamylase is important for the discrimination between CTP and ATP
    • Zhang Y, Kantrowitz ER. 1989. Lysine-60 in the regulatory chain of Escherichia coli aspartate transcarhamylase is important for the discrimination between CTP and ATP. Biochemistry 28:7313-7318.
    • (1989) Biochemistry , vol.28 , pp. 7313-7318
    • Zhang, Y.1    Kantrowitz, E.R.2
  • 47
    • 0025837016 scopus 로고
    • The synergistic inhibition of Escherichia coli aspartate carbamoyltransferase by UTP in the presence of CTP is due to the binding of UTP to the low affinity CTP sites
    • Zhang Y, Kantrowitz ER. 1991. The synergistic inhibition of Escherichia coli aspartate carbamoyltransferase by UTP in the presence of CTP is due to the binding of UTP to the low affinity CTP sites. J Biol Chem 266:22154-22158.
    • (1991) J Biol Chem , vol.266 , pp. 22154-22158
    • Zhang, Y.1    Kantrowitz, E.R.2
  • 48
    • 0026546944 scopus 로고
    • Probing the regulatory site of Escherichia coli aspartate transcarbamoylase by site-specific mutagenesis
    • Zhang Y, Kantrowitz ER. 1992. Probing the regulatory site of Escherichia coli aspartate transcarbamoylase by site-specific mutagenesis. Biochemistry 31:792-798.
    • (1992) Biochemistry , vol.31 , pp. 792-798
    • Zhang, Y.1    Kantrowitz, E.R.2
  • 49
    • 84988138413 scopus 로고
    • Chemical methods of oligonucleotide synthesis
    • Zhdanov RI, Zhenodarova SM. 1975. Chemical methods of oligonucleotide synthesis. Synthesis 4:222-245.
    • (1975) Synthesis , vol.4 , pp. 222-245
    • Zhdanov, R.I.1    Zhenodarova, S.M.2


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