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Volumn 36, Issue 5, 2008, Pages 1731-1740

Substitution of a residue contacting the triphosphate moiety of the incoming nucleotide increases the fidelity of yeast DNA polymerase ζ

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; ARGININE; DNA POLYMERASE; DNA POLYMERASE ZETA; FUNGAL DNA; LYSINE; MUTANT PROTEIN; NUCLEOTIDE; UNCLASSIFIED DRUG;

EID: 41149181377     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkn023     Document Type: Article
Times cited : (6)

References (52)
  • 1
    • 0033548231 scopus 로고    scopus 로고
    • Efficient bypass of a thymine-thymine dimer by yeast DNA polymerase
    • Johnson,R.E., Prakash,S. and Prakash,L. (1999) Efficient bypass of a thymine-thymine dimer by yeast DNA polymerase, Pohη. Science, 283, 1001-1004.
    • (1999) Pohη. Science , vol.283 , pp. 1001-1004
    • Johnson, R.E.1    Prakash, S.2    Prakash, L.3
  • 2
    • 0034425754 scopus 로고    scopus 로고
    • Efficient and accurate replication in the presence of 7,8-dihydro-8-oxoguanine by DNA polymerase η
    • Haracska,L., Yu,S.L., Johnson,R.E., Prakash,L. and Prakash,S. (2000) Efficient and accurate replication in the presence of 7,8-dihydro-8-oxoguanine by DNA polymerase η. Nat. Genet., 25 458-461.
    • (2000) Nat. Genet , vol.25 , pp. 458-461
    • Haracska, L.1    Yu, S.L.2    Johnson, R.E.3    Prakash, L.4    Prakash, S.5
  • 3
    • 0030735538 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae RAD30 gene, a homologue of Escherichia coli dinB and umuC, is DNA damage inducible and functions in a novel error-free postreplication repair mechanism
    • McDonald,J.P., Levine,A.S. and Woodgate,R. (1997) The Saccharomyces cerevisiae RAD30 gene, a homologue of Escherichia coli dinB and umuC, is DNA damage inducible and functions in a novel error-free postreplication repair mechanism. Genetics, 147, 1557-1568.
    • (1997) Genetics , vol.147 , pp. 1557-1568
    • McDonald, J.P.1    Levine, A.S.2    Woodgate, R.3
  • 4
    • 0031921639 scopus 로고    scopus 로고
    • Deletion of the Saccharomyces cerevisiae gene RAD30 encoding an Escherichia coli DinB homolog confers UV radiation sensitivity and altered mutability
    • Roush,A.A., Suarez,M., Friedberg,E.C., Radman,M. and Siede,W. (1998) Deletion of the Saccharomyces cerevisiae gene RAD30 encoding an Escherichia coli DinB homolog confers UV radiation sensitivity and altered mutability. Mol. Gen. Genet., 257, 686-692.
    • (1998) Mol. Gen. Genet , vol.257 , pp. 686-692
    • Roush, A.A.1    Suarez, M.2    Friedberg, E.C.3    Radman, M.4    Siede, W.5
  • 5
    • 0033522984 scopus 로고    scopus 로고
    • Requirement of DNA polymerase activity of yeast Rad30 protein for its biological function
    • Johnson,R.E., Prakash,S. and Prakash,L. (1999) Requirement of DNA polymerase activity of yeast Rad30 protein for its biological function. J. Biol. Chem., 274, 15975-15977.
    • (1999) J. Biol. Chem , vol.274 , pp. 15975-15977
    • Johnson, R.E.1    Prakash, S.2    Prakash, L.3
  • 6
    • 0033538470 scopus 로고    scopus 로고
    • hRAD30 mutations in the variant form of xeroderma pigmentosum
    • Johnson,R.E., Kondratick,C.M., Prakash,S. and Prakash,L. (1999) hRAD30 mutations in the variant form of xeroderma pigmentosum. Science, 285, 263-265.
    • (1999) Science , vol.285 , pp. 263-265
    • Johnson, R.E.1    Kondratick, C.M.2    Prakash, S.3    Prakash, L.4
  • 8
    • 0024461293 scopus 로고
    • REV3, a Saccharomyces cerevisiae gene whose function is required for induced mutagenesis, is predicted to encode a nonessential DNA polymerase
    • Morrison,A., Christensen,R.B., Alley,J., Beck,A.K., Bernstine,E.G., Lemontt,J.F. and Lawrence,C.W. (1989) REV3, a Saccharomyces cerevisiae gene whose function is required for induced mutagenesis, is predicted to encode a nonessential DNA polymerase. J. Bacteriol. 171, 5659-5667.
    • (1989) J. Bacteriol , vol.171 , pp. 5659-5667
    • Morrison, A.1    Christensen, R.B.2    Alley, J.3    Beck, A.K.4    Bernstine, E.G.5    Lemontt, J.F.6    Lawrence, C.W.7
  • 9
    • 0029952294 scopus 로고    scopus 로고
    • Thyminethymine dimer bypass by yeast DNA polymerase ζ
    • Nelson,J.R., Lawrence,C.W. and Hinkle,D.C. (1996) Thyminethymine dimer bypass by yeast DNA polymerase ζ. Science, 272, 1646-1649.
    • (1996) Science , vol.272 , pp. 1646-1649
    • Nelson, J.R.1    Lawrence, C.W.2    Hinkle, D.C.3
  • 11
    • 0037150492 scopus 로고    scopus 로고
    • lular roles of DNA polymerase ζ and Rev1 protein
    • Lawrence,C.W. (2002) lular roles of DNA polymerase ζ and Rev1 protein. DNA Repair, 1, 425-435.
    • (2002) DNA Repair , vol.1 , pp. 425-435
    • Lawrence, C.W.1
  • 12
    • 0037226587 scopus 로고    scopus 로고
    • Yeast DNA polymerase ζ is essential for error-free replication past thymine glycol
    • Johnson,R.E., Yu,S.L., Prakash,S. and Prakash,L. (2003) Yeast DNA polymerase ζ is essential for error-free replication past thymine glycol. Genes Dev., 17, 77-87.
    • (2003) Genes Dev , vol.17 , pp. 77-87
    • Johnson, R.E.1    Yu, S.L.2    Prakash, S.3    Prakash, L.4
  • 13
    • 0001908121 scopus 로고
    • Mutants of yeast defective in mutation induced by ultraviolet light
    • Lemontt,J.F. (1971) Mutants of yeast defective in mutation induced by ultraviolet light. Genetics, 68, 21-33.
    • (1971) Genetics , vol.68 , pp. 21-33
    • Lemontt, J.F.1
  • 14
    • 0018731397 scopus 로고
    • Ultraviolet-induced reversion of cyc1 alleles in radiation-sensitive strains of yeast. III. The rev3 mutant strains
    • Lawrence,C.W. and Christensen,R.B. (1979) Ultraviolet-induced reversion of cyc1 alleles in radiation-sensitive strains of yeast. III. The rev3 mutant strains. Genetics, 92, 397-408.
    • (1979) Genetics , vol.92 , pp. 397-408
    • Lawrence, C.W.1    Christensen, R.B.2
  • 15
    • 0021204089 scopus 로고
    • UV-induced reversion of his4 frameshift mutations in rad6, rev1, and rev3 mutants of yeast
    • Lawrence,C.W., O'Brien,T. and Bond,J. (1984) UV-induced reversion of his4 frameshift mutations in rad6, rev1, and rev3 mutants of yeast. Mol. Gen. Genet., 195, 487-490.
    • (1984) Mol. Gen. Genet , vol.195 , pp. 487-490
    • Lawrence, C.W.1    O'Brien, T.2    Bond, J.3
  • 16
    • 0032499748 scopus 로고    scopus 로고
    • A human homolog of the Saccharomyces cereviside REV3 gene, which encoded the catalytic subunit of DNA ppplymerase ζ
    • Gibbs,P.E. M., McGregor,W.G., Maher,V.M.,. Nisson,P. and Lawrence,C.W. (1998) A human homolog of the Saccharomyces cereviside REV3 gene, which encoded the catalytic subunit of DNA ppplymerase ζ. Proc. Natl Acad. Sci. USA, 95, 6876-6880.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 6876-6880
    • Gibbs, P.E.M.1    McGregor, W.G.2    Maher, V.M.3    Nisson, P.4    Lawrence, C.W.5
  • 17
    • 0034738983 scopus 로고    scopus 로고
    • Eukaryotic polymerase ι and ζ act sequentially to bypass DN4 lesions
    • Johnson,R.E., Washington,M.T., Haracska,L., Prakash,S. and Prakash,L. (2000) Eukaryotic polymerase ι and ζ act sequentially to bypass DN4 lesions. Nature, 406, 1015-1019.
    • (2000) Nature , vol.406 , pp. 1015-1019
    • Johnson, R.E.1    Washington, M.T.2    Haracska, L.3    Prakash, S.4    Prakash, L.5
  • 18
    • 0024552845 scopus 로고
    • Differential extension of 3' mispairs is a major contribution to the high fidelity of calf thymus DNA polymerase-α
    • Perrino,F.W. and Loeb,L.A. (1989) Differential extension of 3' mispairs is a major contribution to the high fidelity of calf thymus DNA polymerase-α. J. Biol. Chem., 264, 2898-2905.
    • (1989) J. Biol. Chem , vol.264 , pp. 2898-2905
    • Perrino, F.W.1    Loeb, L.A.2
  • 19
    • 0033601194 scopus 로고    scopus 로고
    • Fidelity and processivitity of Saccharomyces cerevisiae DNA polymerase η
    • Washington,M.T., Johnson,A.E., Prakash,S. and Prakash,L. (1999) Fidelity and processivitity of Saccharomyces cerevisiae DNA polymerase η. J. Biol. Chem., 274, 36835-36838.
    • (1999) J. Biol. Chem , vol.274 , pp. 36835-36838
    • Washington, M.T.1    Johnson, A.E.2    Prakash, S.3    Prakash, L.4
  • 21
  • 22
    • 0035910469 scopus 로고    scopus 로고
    • Mismatch extension ability of yeast and human DNA polymerase η
    • Washington,M.T., Johnson,R.E., Prakash,S. and Prakash,L. (2001), Mismatch extension ability of yeast and human DNA polymerase η. J. Biol. Chem., 276, 2263-2266.
    • (2001) J. Biol. Chem , vol.276 , pp. 2263-2266
    • Washington, M.T.1    Johnson, R.E.2    Prakash, S.3    Prakash, L.4
  • 23
    • 0036682979 scopus 로고    scopus 로고
    • Translesion DNA synthesis in eukaryotes: A one- or two-polymerase affair
    • Prakash,S. and Prakash,L. (2002) Translesion DNA synthesis in eukaryotes: A one- or two-polymerase affair. Genes Dev., 16, 1872-1883.
    • (2002) Genes Dev , vol.16 , pp. 1872-1883
    • Prakash, S.1    Prakash, L.2
  • 24
    • 21244506437 scopus 로고    scopus 로고
    • Eukaryotic translesion synthesis DNA polymerases: Specificity of structure and function
    • Prakah,S., Johnson,R.E. and Prakash,L. (2005) Eukaryotic translesion synthesis DNA polymerases: Specificity of structure and function. Annu. Rev. Biochem., 74, 317-353.
    • (2005) Annu. Rev. Biochem , vol.74 , pp. 317-353
    • Prakah, S.1    Johnson, R.E.2    Prakash, L.3
  • 26
    • 0031587827 scopus 로고    scopus 로고
    • Crystal structure of a pol α family replication DNA polymerase from bacteriophage RB69
    • Wang,J., Sattar,A.K., Wang,C.C., Karam,J.D., Konigsberg,W.H. and Steitz,T.A. (1997) Crystal structure of a pol α family replication DNA polymerase from bacteriophage RB69. Cell, 89, 1087-1099.
    • (1997) Cell , vol.89 , pp. 1087-1099
    • Wang, J.1    Sattar, A.K.2    Wang, C.C.3    Karam, J.D.4    Konigsberg, W.H.5    Steitz, T.A.6
  • 27
    • 0035369086 scopus 로고    scopus 로고
    • Structure of the replicating complex of a pol α family DNA polymerase
    • Franklin,M.C., Wang,J. and Steitz,T.A. (2001) Structure of the replicating complex of a pol α family DNA polymerase. Cell, 105, 657-667.
    • (2001) Cell , vol.105 , pp. 657-667
    • Franklin, M.C.1    Wang, J.2    Steitz, T.A.3
  • 28
    • 34547175132 scopus 로고    scopus 로고
    • Structures of φ29 DNA polymerase complexed with substrate: The mechanism of translocation in B-family polymerases
    • Berman,A.J., Kamtekar,S., Goodman,J.L., Lazaro,J.M., de Vega,M., Blanco,L., Salas,M. and Steitz,T.A. (2007) Structures of φ29 DNA polymerase complexed with substrate: The mechanism of translocation in B-family polymerases. EMBO J., 26, 3494-3505.
    • (2007) EMBO J , vol.26 , pp. 3494-3505
    • Berman, A.J.1    Kamtekar, S.2    Goodman, J.L.3    Lazaro, J.M.4    de Vega, M.5    Blanco, L.6    Salas, M.7    Steitz, T.A.8
  • 29
  • 31
    • 2342419732 scopus 로고    scopus 로고
    • DNA replication fidelity
    • Kunkel,T.A. (2004) DNA replication fidelity. J. Biol. Chem., 279, 16895-16898.
    • (2004) J. Biol. Chem , vol.279 , pp. 16895-16898
    • Kunkel, T.A.1
  • 32
    • 4644258145 scopus 로고    scopus 로고
    • Structural insights into DNA polymerase beta deterrents for misincorporation support an induced-fit mechanism for fidelity
    • Krahn,J.M., Beard,W.A. and Wilson,S.H. (2004) Structural insights into DNA polymerase beta deterrents for misincorporation support an induced-fit mechanism for fidelity. Structure, 12, 1823-1832.
    • (2004) Structure , vol.12 , pp. 1823-1832
    • Krahn, J.M.1    Beard, W.A.2    Wilson, S.H.3
  • 33
    • 1642588255 scopus 로고    scopus 로고
    • Structures of mismatch replication errors observed in a DNA polymerase
    • Johnson,S.J. and Beese,L.S. (2004) Structures of mismatch replication errors observed in a DNA polymerase. Cell, 116, 803-816.
    • (2004) Cell , vol.116 , pp. 803-816
    • Johnson, S.J.1    Beese, L.S.2
  • 34
    • 0024266139 scopus 로고
    • New yeast-Escherichia coli shuttle vectors constructed with in vitro mutagenized yeast genes lacking six-base pair restriction sites
    • Gietz,R.D. and Sugino,A. (1988) New yeast-Escherichia coli shuttle vectors constructed with in vitro mutagenized yeast genes lacking six-base pair restriction sites. Gene, 74, 527-534.
    • (1988) Gene , vol.74 , pp. 527-534
    • Gietz, R.D.1    Sugino, A.2
  • 35
    • 0035966270 scopus 로고    scopus 로고
    • Yeast DNA polymerase η utilizes an induced-fit mechanism of nucleotide incorporation
    • Washington,M.T., Prakash,L. and Prakash,S. (2001) Yeast DNA polymerase η utilizes an induced-fit mechanism of nucleotide incorporation. Cell, 107, 917-927.
    • (2001) Cell , vol.107 , pp. 917-927
    • Washington, M.T.1    Prakash, L.2    Prakash, S.3
  • 37
    • 0028834955 scopus 로고
    • Gel fidelity assay measuring nucleotide misinsertion, exonucleolytic proofreading, and lesion bypass efficiencies
    • Creighton,S., Bloom,L.B. and Goodman,M.F. (1995) Gel fidelity assay measuring nucleotide misinsertion, exonucleolytic proofreading, and lesion bypass efficiencies. Method Enzymol., 262, 232-256.
    • (1995) Method Enzymol , vol.262 , pp. 232-256
    • Creighton, S.1    Bloom, L.B.2    Goodman, M.F.3
  • 38
    • 0029112798 scopus 로고
    • Mutational studies of human DNA polymerase α. Lysine 950 in the third most conserved region of α-like DNA polymerases is involved in binding the deoxynucleoside triphosphate
    • Dong,Q. and Wang,T.S. (1995) Mutational studies of human DNA polymerase α. Lysine 950 in the third most conserved region of α-like DNA polymerases is involved in binding the deoxynucleoside triphosphate. J. Biol. Chem., 270, 21563-21570.
    • (1995) J. Biol. Chem , vol.270 , pp. 21563-21570
    • Dong, Q.1    Wang, T.S.2
  • 39
    • 0030611410 scopus 로고    scopus 로고
    • φ29 DNA polymerase residue Lys383, invariant at motif B of DNA-dependent polymerases, is involved in dNTP binding
    • Saturno,J., Lazaro,J.M., Esteban,F.J., Blanco,L. and Salas,M. (1997) φ29 DNA polymerase residue Lys383, invariant at motif B of DNA-dependent polymerases, is involved in dNTP binding. J. Mol. Biol. 269, 313-325.
    • (1997) J. Mol. Biol , vol.269 , pp. 313-325
    • Saturno, J.1    Lazaro, J.M.2    Esteban, F.J.3    Blanco, L.4    Salas, M.5
  • 40
    • 0033594982 scopus 로고    scopus 로고
    • Steady-state kinetic characterization of RB69 DNA polymerase mutants that affect dNTP incorporation
    • Yang,G., Lin,T., Karam,J. and Konigsberg,W.H. (1999) Steady-state kinetic characterization of RB69 DNA polymerase mutants that affect dNTP incorporation. Biochemistry, 38, 8094-8101.
    • (1999) Biochemistry , vol.38 , pp. 8094-8101
    • Yang, G.1    Lin, T.2    Karam, J.3    Konigsberg, W.H.4
  • 41
    • 0036529501 scopus 로고    scopus 로고
    • A positively charged residue of φ29 DNA polymerase, highly conserved in DNA polymerases from families A and B, is involved in binding the incoming nucleotide
    • Truniger,V., Lazaro,J.M., Esteban,F.J., Blanco,L. and Salas,M. (2002) A positively charged residue of φ29 DNA polymerase, highly conserved in DNA polymerases from families A and B, is involved in binding the incoming nucleotide. Nucleic Acids Res., 30, 1483-1492.
    • (2002) Nucleic Acids Res , vol.30 , pp. 1483-1492
    • Truniger, V.1    Lazaro, J.M.2    Esteban, F.J.3    Blanco, L.4    Salas, M.5
  • 42
    • 0028915013 scopus 로고
    • Learning about DNA polymerase function by studying antimutator DNA polymerases
    • Reha-Krantz,L.J. (1995) Learning about DNA polymerase function by studying antimutator DNA polymerases. Trends Biochem. Sci., 20 136-140.
    • (1995) Trends Biochem. Sci , vol.20 , pp. 136-140
    • Reha-Krantz, L.J.1
  • 43
    • 0032552971 scopus 로고    scopus 로고
    • Kinetic characterization of a bacteriophage T4 antimutator DNA polymerase
    • Wu,P., Nossal,N. and Benkovic,S.J. (1998) Kinetic characterization of a bacteriophage T4 antimutator DNA polymerase. Biochemistry, 37 14785-14755.
    • (1998) Biochemistry , vol.37 , pp. 14785-14755
    • Wu, P.1    Nossal, N.2    Benkovic, S.J.3
  • 44
    • 0037150445 scopus 로고    scopus 로고
    • Substitutions of Phe-61 located in the vicinity or template 5'overhang influence polymerase fidelity and nucleoside analog sensitivity of HIV-1 reverse transcriptase
    • Fisher,T.S. and Prasad,V.R. (2002) Substitutions of Phe-61 located in the vicinity or template 5'overhang influence polymerase fidelity and nucleoside analog sensitivity of HIV-1 reverse transcriptase. J. Biol. Chem., 277, 22345-22352.
    • (2002) J. Biol. Chem , vol.277 , pp. 22345-22352
    • Fisher, T.S.1    Prasad, V.R.2
  • 45
    • 0032731354 scopus 로고    scopus 로고
    • Uniquely altered DNA replication fidelity conferred by an amino acid change in the nucleotide binding pocket of human immunodeficiency virus type 1 reverse transcriptase
    • Lewis,D.A., Bebenek,K., Beard,W.A., Wilson,S.H. and Kunkel,T.A. (1999) Uniquely altered DNA replication fidelity conferred by an amino acid change in the nucleotide binding pocket of human immunodeficiency virus type 1 reverse transcriptase. J. Biol. Chem., 274, 32924-32930.
    • (1999) J. Biol. Chem , vol.274 , pp. 32924-32930
    • Lewis, D.A.1    Bebenek, K.2    Beard, W.A.3    Wilson, S.H.4    Kunkel, T.A.5
  • 46
    • 0034609584 scopus 로고    scopus 로고
    • Molecular architecture of the-mutagenic active site of human immunodeficiency virus type 1 reverse transcriptase: Roles of the β8-αE loop in fidelity, processivity, and substrate interactions
    • Weiss,K.K., Isaacs,S.J., Tran,N.H., Adman,E.T. and Kim,B. (2000) Molecular architecture of the-mutagenic active site of human immunodeficiency virus type 1 reverse transcriptase: Roles of the β8-αE loop in fidelity, processivity, and substrate interactions. Biochemistry, 39, 10684-10694.
    • (2000) Biochemistry , vol.39 , pp. 10684-10694
    • Weiss, K.K.1    Isaacs, S.J.2    Tran, N.H.3    Adman, E.T.4    Kim, B.5
  • 47
    • 0037151020 scopus 로고    scopus 로고
    • Mechanistic role of residue Gln-151 in error prone DNA synthesis y human immunodeficiency virus type 1 (HIV-1) reverse transcriptase (RT). Pre-steady state kinetic study of the Q151N HIV-1 RT mutant with increased fidelity
    • Weiss,K.K., Bambara,R.A. and Kim,B. (2002) Mechanistic role of residue Gln-151 in error prone DNA synthesis y human immunodeficiency virus type 1 (HIV-1) reverse transcriptase (RT). Pre-steady state kinetic study of the Q151N HIV-1 RT mutant with increased fidelity. J. Biol. Chem., 277, 22662-22669.
    • (2002) J. Biol. Chem , vol.277 , pp. 22662-22669
    • Weiss, K.K.1    Bambara, R.A.2    Kim, B.3
  • 48
    • 0032574695 scopus 로고    scopus 로고
    • Fidelity of mutant HIV-1 reverse transcriptase: Interactions with the single-stranded template influences the accuracy of DNA synthesis
    • Kim,B., Hathaway,T.R. and Loeb,L.A. (1998) Fidelity of mutant HIV-1 reverse transcriptase: Interactions with the single-stranded template influences the accuracy of DNA synthesis. Biochemistry, 37, 5831-5839.
    • (1998) Biochemistry , vol.37 , pp. 5831-5839
    • Kim, B.1    Hathaway, T.R.2    Loeb, L.A.3
  • 49
    • 0033600921 scopus 로고    scopus 로고
    • New human immunodeficiency virus type 1 reverse transcriptase (HIV-1 RT) mutants with increased fidelity of DNA synthesis
    • Kim,B., Ayran,J.C. Sagar,S.G., Adman,E.T., Fuller,S.M., Tran,N.H. and Horrigan,J. (1999) New human immunodeficiency virus type 1 reverse transcriptase (HIV-1 RT) mutants with increased fidelity of DNA synthesis. J. Biol. Chem., 274, 27666-27673.
    • (1999) J. Biol. Chem , vol.274 , pp. 27666-27673
    • Kim, B.1    Ayran, J.C.2    Sagar, S.G.3    Adman, E.T.4    Fuller, S.M.5    Tran, N.H.6    Horrigan, J.7
  • 50
    • 0030000114 scopus 로고
    • Increased polymerase fidelity of E89G, a nucleoside analog-resistant variant of human immunodeficiency virus type 1 reverse transcriptase
    • Drosopoulos,W.C. and Prasad,V.R. (1995) Increased polymerase fidelity of E89G, a nucleoside analog-resistant variant of human immunodeficiency virus type 1 reverse transcriptase. J. Virology, 70, 4834-4838.
    • (1995) J. Virology , vol.70 , pp. 4834-4838
    • Drosopoulos, W.C.1    Prasad, V.R.2
  • 51
    • 34249660610 scopus 로고    scopus 로고
    • Highly tolerant amino acid substitutions increase the fidelity of Escherichia coli DNA polymerase I
    • Lohn,E., Choe,J. and Loeb,L.A. (2007) Highly tolerant amino acid substitutions increase the fidelity of Escherichia coli DNA polymerase I. J. Biol. Chem., 282, 12201-12209.
    • (2007) J. Biol. Chem , vol.282 , pp. 12201-12209
    • Lohn, E.1    Choe, J.2    Loeb, L.A.3
  • 52
    • 0038143221 scopus 로고    scopus 로고
    • Amino acid substitutions at conserved tyrosine 52 alter fidelity and bypass efficiency of human DNA polymerase η
    • Glick,E., Chau,J.S., Vigna,K.L., McCulloch,S.D., Admam,E.T., Kunkel,T.A. and Loeb,L.A. (2003) Amino acid substitutions at conserved tyrosine 52 alter fidelity and bypass efficiency of human DNA polymerase η. J. Biol. Chem., 278, 19341-19346.
    • (2003) J. Biol. Chem , vol.278 , pp. 19341-19346
    • Glick, E.1    Chau, J.S.2    Vigna, K.L.3    McCulloch, S.D.4    Admam, E.T.5    Kunkel, T.A.6    Loeb, L.A.7


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