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Volumn 55, Issue 7, 2016, Pages 1168-1177

Effects of Acyclovir, Foscarnet, and Ribonucleotides on Herpes Simplex Virus-1 DNA Polymerase: Mechanistic Insights and a Novel Mechanism for Preventing Stable Incorporation of Ribonucleotides into DNA

Author keywords

[No Author keywords available]

Indexed keywords

BINS; CARBON; DRUG PRODUCTS; MACHINERY; POLYMERIZATION; VIRUSES;

EID: 84959320645     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/acs.biochem.6b00065     Document Type: Article
Times cited : (21)

References (52)
  • 1
    • 0019869763 scopus 로고
    • Acyclovir-resistant mutants of herpes simplex virus type 1 express altered DNA polymerase or reduced acyclovir phosphorylating activities
    • Furman, P. A., Coen, D. M., St Clair, M. H., and Schaffer, P. A. (1981) Acyclovir-resistant mutants of herpes simplex virus type 1 express altered DNA polymerase or reduced acyclovir phosphorylating activities J. Virol 40, 936-941
    • (1981) J. Virol , vol.40 , pp. 936-941
    • Furman, P.A.1    Coen, D.M.2    St Clair, M.H.3    Schaffer, P.A.4
  • 2
    • 0019906766 scopus 로고
    • Genetic mechanisms of resistance to acyclovir in herpes simplex virus
    • Crumpacker, C. S., Schnipper, L. E., Chartrand, P., and Knopf, K. W. (1982) Genetic mechanisms of resistance to acyclovir in herpes simplex virus Am. J. Med. 73, 361-368 10.1016/0002-9343(82)90123-1
    • (1982) Am. J. Med. , vol.73 , pp. 361-368
    • Crumpacker, C.S.1    Schnipper, L.E.2    Chartrand, P.3    Knopf, K.W.4
  • 3
    • 0018821740 scopus 로고
    • Resistance of herpes simplex virus to acycloguanosine - Genetic and physical analysis
    • Crumpacker, C. S., Chartrand, P., Subak-Sharpe, J. H., and Wilkie, N. M. (1980) Resistance of herpes simplex virus to acycloguanosine - genetic and physical analysis Virology 105, 171-184 10.1016/0042-6822(80)90165-8
    • (1980) Virology , vol.105 , pp. 171-184
    • Crumpacker, C.S.1    Chartrand, P.2    Subak-Sharpe, J.H.3    Wilkie, N.M.4
  • 4
    • 0019904116 scopus 로고
    • Biochemical and genetic analysis of acyclovir-resistant mutants of herpes simplex virus type 1
    • Coen, D. M., Schaffer, P. A., Furman, P. A., Keller, P. M., and St. Clair, M. H. (1982) Biochemical and genetic analysis of acyclovir-resistant mutants of herpes simplex virus type 1 Am. J. Med. 73, 351-360 10.1016/0002-9343(82)90122-X
    • (1982) Am. J. Med. , vol.73 , pp. 351-360
    • Coen, D.M.1    Schaffer, P.A.2    Furman, P.A.3    Keller, P.M.4    St. Clair, M.H.5
  • 5
    • 13044290052 scopus 로고    scopus 로고
    • The enzymological basis for resistance of herpesvirus DNA polymerase mutants to acyclovir: relationship to the structure of alpha-like DNA polymerases
    • Huang, L., Ishii, K. K., Zuccola, H., Gehring, A. M., Hwang, C. B., Hogle, J., and Coen, D. M. (1999) The enzymological basis for resistance of herpesvirus DNA polymerase mutants to acyclovir: relationship to the structure of alpha-like DNA polymerases Proc. Natl. Acad. Sci. U. S. A. 96, 447-452 10.1073/pnas.96.2.447
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 447-452
    • Huang, L.1    Ishii, K.K.2    Zuccola, H.3    Gehring, A.M.4    Hwang, C.B.5    Hogle, J.6    Coen, D.M.7
  • 6
    • 0020073036 scopus 로고
    • Mutations in the herpes simplex virus DNA polymerase gene can confer resistance to 9-beta-D-arabinofuranosyladenine
    • Coen, D. M., Furman, P. A., Gelep, P. T., and Schaffer, P. A. (1982) Mutations in the herpes simplex virus DNA polymerase gene can confer resistance to 9-beta-D-arabinofuranosyladenine J. Virol 41, 909-918
    • (1982) J. Virol , vol.41 , pp. 909-918
    • Coen, D.M.1    Furman, P.A.2    Gelep, P.T.3    Schaffer, P.A.4
  • 8
    • 0031008223 scopus 로고    scopus 로고
    • Herpes simplex virus DNA replication
    • Boehmer, P. E. and Lehman, I. R. (1997) Herpes simplex virus DNA replication Annu. Rev. Biochem. 66, 347-384 10.1146/annurev.biochem.66.1.347
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 347-384
    • Boehmer, P.E.1    Lehman, I.R.2
  • 9
    • 33744769406 scopus 로고    scopus 로고
    • The two helicases of herpes simplex virus type 1 (HSV-1)
    • Chattopadhyay, S., Chen, Y., and Weller, S. K. (2006) The two helicases of herpes simplex virus type 1 (HSV-1) Front. Biosci., Landmark Ed. 11, 2213-2223 10.2741/1964
    • (2006) Front. Biosci., Landmark Ed. , vol.11 , pp. 2213-2223
    • Chattopadhyay, S.1    Chen, Y.2    Weller, S.K.3
  • 10
    • 0033215473 scopus 로고    scopus 로고
    • Replication of herpes simplex virus DNA
    • Lehman, I. R. and Boehmer, P. E. (1999) Replication of herpes simplex virus DNA J. Biol. Chem. 274, 28059-28062 10.1074/jbc.274.40.28059
    • (1999) J. Biol. Chem. , vol.274 , pp. 28059-28062
    • Lehman, I.R.1    Boehmer, P.E.2
  • 11
    • 0029803094 scopus 로고    scopus 로고
    • Herpes simplex virus type 1 DNA polymerase. Mutational analysis of the 3′-5′-exonuclease domain
    • Kuhn, F. J. and Knopf, C. W. (1996) Herpes simplex virus type 1 DNA polymerase. Mutational analysis of the 3′-5′-exonuclease domain J. Biol. Chem. 271, 29245-29254 10.1074/jbc.271.46.29245
    • (1996) J. Biol. Chem. , vol.271 , pp. 29245-29254
    • Kuhn, F.J.1    Knopf, C.W.2
  • 12
    • 0030819366 scopus 로고    scopus 로고
    • Effects of mutations in the Exo III motif of the herpes simplex virus DNA polymerase gene on enzyme activities, viral replication, and replication fidelity
    • Hwang, Y. T., Liu, B. Y., Coen, D. M., and Hwang, C. B. (1997) Effects of mutations in the Exo III motif of the herpes simplex virus DNA polymerase gene on enzyme activities, viral replication, and replication fidelity J. Virol 71, 7791-7798
    • (1997) J. Virol , vol.71 , pp. 7791-7798
    • Hwang, Y.T.1    Liu, B.Y.2    Coen, D.M.3    Hwang, C.B.4
  • 13
    • 0037244124 scopus 로고    scopus 로고
    • Herpes simplex virus resistance to acyclovir and penciclovir after two decades of antiviral therapy
    • Bacon, T. H., Levin, M. J., Leary, J. J., Sarisky, R. T., and Sutton, D. (2003) Herpes simplex virus resistance to acyclovir and penciclovir after two decades of antiviral therapy Clin Microbiol Rev. 16, 114-128 10.1128/CMR.16.1.114-128.2003
    • (2003) Clin Microbiol Rev. , vol.16 , pp. 114-128
    • Bacon, T.H.1    Levin, M.J.2    Leary, J.J.3    Sarisky, R.T.4    Sutton, D.5
  • 14
    • 0034966673 scopus 로고    scopus 로고
    • Antiviral drugs: current state of the art
    • De Clercq, E. (2001) Antiviral drugs: current state of the art J. Clin. Virol. 22, 73-89 10.1016/S1386-6532(01)00167-6
    • (2001) J. Clin. Virol. , vol.22 , pp. 73-89
    • De Clercq, E.1
  • 15
    • 0019925472 scopus 로고
    • Acyclovir inhibition of viral DNA chain elongation in herpes simplex virus-infected cells
    • McGuirt, P. V. and Furman, P. A. (1982) Acyclovir inhibition of viral DNA chain elongation in herpes simplex virus-infected cells Am. J. Med. 73, 67-71 10.1016/0002-9343(82)90066-3
    • (1982) Am. J. Med. , vol.73 , pp. 67-71
    • McGuirt, P.V.1    Furman, P.A.2
  • 16
    • 0019257150 scopus 로고
    • Inhibition of cellular alpha and virally induced deoxyribonucleic acid polymerases by the triphosphate of acyclovir
    • St Clair, M. H., Furman, P. A., Lubbers, C. M., and Elion, G. B. (1980) Inhibition of cellular alpha and virally induced deoxyribonucleic acid polymerases by the triphosphate of acyclovir Antimicrob. Agents Chemother. 18, 741-745 10.1128/AAC.18.5.741
    • (1980) Antimicrob. Agents Chemother. , vol.18 , pp. 741-745
    • St Clair, M.H.1    Furman, P.A.2    Lubbers, C.M.3    Elion, G.B.4
  • 18
    • 84884565658 scopus 로고    scopus 로고
    • The DNA helicase-primase complex as a target for herpes viral infection
    • Weller, S. K. and Kuchta, R. D. (2013) The DNA helicase-primase complex as a target for herpes viral infection Expert Opin. Ther. Targets 17, 1119-1132 10.1517/14728222.2013.827663
    • (2013) Expert Opin. Ther. Targets , vol.17 , pp. 1119-1132
    • Weller, S.K.1    Kuchta, R.D.2
  • 19
    • 0021191524 scopus 로고
    • Acyclovir triphosphate is a suicide inactivator of the herpes simplex virus DNA polymerase
    • Furman, P. A., St, Clair, M. H., and Spector, T. (1984) Acyclovir triphosphate is a suicide inactivator of the herpes simplex virus DNA polymerase J. Biol. Chem. 259, 9575-9579
    • (1984) J. Biol. Chem. , vol.259 , pp. 9575-9579
    • Furman, P.A.1    St2    Clair, M.H.3    Spector, T.4
  • 20
    • 0019888670 scopus 로고
    • Inhibition of purified human and herpes simplex virus-induced DNA polymerases by 9-(2-hydroxyethoxymethyl)guanine triphosphate. Effects on primer-template function
    • Derse, D., Cheng, Y. C., Furman, P. A., St Clair, M. H., and Elion, G. B. (1981) Inhibition of purified human and herpes simplex virus-induced DNA polymerases by 9-(2-hydroxyethoxymethyl)guanine triphosphate. Effects on primer-template function J. Biol. Chem. 256, 11447-11451
    • (1981) J. Biol. Chem. , vol.256 , pp. 11447-11451
    • Derse, D.1    Cheng, Y.C.2    Furman, P.A.3    St Clair, M.H.4    Elion, G.B.5
  • 21
    • 0018251481 scopus 로고
    • Thymidine kinase from herpes simplex virus phosphorylates the new antiviral compound, 9-(2-hydroxyethoxymethyl)guanine
    • Fyfe, J. A., Keller, P. M., Furman, P. A., Miller, R. L., and Elion, G. B. (1978) Thymidine kinase from herpes simplex virus phosphorylates the new antiviral compound, 9-(2-hydroxyethoxymethyl)guanine J. Biol. Chem. 253, 8721-8727
    • (1978) J. Biol. Chem. , vol.253 , pp. 8721-8727
    • Fyfe, J.A.1    Keller, P.M.2    Furman, P.A.3    Miller, R.L.4    Elion, G.B.5
  • 22
    • 0019321437 scopus 로고
    • Phosphorylation of acyclovir (acycloguanosine) monophosphate by GMP kinase
    • Miller, W. H. and Miller, R. L. (1980) Phosphorylation of acyclovir (acycloguanosine) monophosphate by GMP kinase J. Biol. Chem. 255, 7204-7207
    • (1980) J. Biol. Chem. , vol.255 , pp. 7204-7207
    • Miller, W.H.1    Miller, R.L.2
  • 23
    • 0020408238 scopus 로고
    • Phosphorylation of acyclovir diphosphate by cellular enzymes
    • Miller, W. H. and Miller, R. L. (1982) Phosphorylation of acyclovir diphosphate by cellular enzymes Biochem. Pharmacol. 31, 3879-3884 10.1016/0006-2952(82)90305-7
    • (1982) Biochem. Pharmacol. , vol.31 , pp. 3879-3884
    • Miller, W.H.1    Miller, R.L.2
  • 24
    • 0024584523 scopus 로고
    • Herpes simplex virus type 1 DNA polymerase. Mechanism of inhibition by acyclovir triphosphate
    • Reardon, J. E. and Spector, T. (1989) Herpes simplex virus type 1 DNA polymerase. Mechanism of inhibition by acyclovir triphosphate J. Biol. Chem. 264, 7405-7411
    • (1989) J. Biol. Chem. , vol.264 , pp. 7405-7411
    • Reardon, J.E.1    Spector, T.2
  • 25
    • 84918590290 scopus 로고    scopus 로고
    • Mechanism of ganciclovir-induced chain termination revealed by resistant viral polymerase mutants with reduced exonuclease activity
    • Chen, H., Beardsley, G. P., and Coen, D. M. (2014) Mechanism of ganciclovir-induced chain termination revealed by resistant viral polymerase mutants with reduced exonuclease activity Proc. Natl. Acad. Sci. U. S. A. 111, 17462-17467 10.1073/pnas.1405981111
    • (2014) Proc. Natl. Acad. Sci. U. S. A. , vol.111 , pp. 17462-17467
    • Chen, H.1    Beardsley, G.P.2    Coen, D.M.3
  • 26
    • 0026553933 scopus 로고
    • Mechanism of action of foscarnet against viral polymerases
    • Crumpacker, C. S. (1992) Mechanism of action of foscarnet against viral polymerases Am. J. Med. 92, S3-S7 10.1016/0002-9343(92)90329-A
    • (1992) Am. J. Med. , vol.92 , pp. S3-S7
    • Crumpacker, C.S.1
  • 27
    • 0017105494 scopus 로고
    • Mechanism of phosphonoacetate inhibition of herpesvirus-induced DNA polymerase
    • Leinbach, S. S., Reno, J. M., Lee, L. F., Isbell, A. F., and Boezi, J. A. (1976) Mechanism of phosphonoacetate inhibition of herpesvirus-induced DNA polymerase Biochemistry 15, 426-430 10.1021/bi00647a029
    • (1976) Biochemistry , vol.15 , pp. 426-430
    • Leinbach, S.S.1    Reno, J.M.2    Lee, L.F.3    Isbell, A.F.4    Boezi, J.A.5
  • 29
    • 34548337282 scopus 로고    scopus 로고
    • Enzymatic therapeutic index of acyclovir. Viral versus human polymerase gamma specificity
    • Hanes, J. W., Zhu, Y., Parris, D. S., and Johnson, K. A. (2007) Enzymatic therapeutic index of acyclovir. Viral versus human polymerase gamma specificity J. Biol. Chem. 282, 25159-25167 10.1074/jbc.M703972200
    • (2007) J. Biol. Chem. , vol.282 , pp. 25159-25167
    • Hanes, J.W.1    Zhu, Y.2    Parris, D.S.3    Johnson, K.A.4
  • 30
    • 84922330345 scopus 로고    scopus 로고
    • Polymerase and exonuclease activities in herpes simplex virus type 1 DNA polymerase are not highly coordinated
    • Vashishtha, A. K. and Kuchta, R. D. (2015) Polymerase and exonuclease activities in herpes simplex virus type 1 DNA polymerase are not highly coordinated Biochemistry 54, 240-249 10.1021/bi500840v
    • (2015) Biochemistry , vol.54 , pp. 240-249
    • Vashishtha, A.K.1    Kuchta, R.D.2
  • 31
    • 0037058824 scopus 로고    scopus 로고
    • Key role of template sequence for primer synthesis by the herpes simplex virus 1 helicase-primase
    • Ramirez-Aguilar, K. A., Low-Nam, N. A., and Kuchta, R. D. (2002) Key role of template sequence for primer synthesis by the herpes simplex virus 1 helicase-primase Biochemistry 41, 14569-14579 10.1021/bi026680v
    • (2002) Biochemistry , vol.41 , pp. 14569-14579
    • Ramirez-Aguilar, K.A.1    Low-Nam, N.A.2    Kuchta, R.D.3
  • 33
    • 0018770603 scopus 로고
    • Properties of herpes simplex virus DNA polymerase and characterization of its associated exonuclease activity
    • Knopf, K. W. (1979) Properties of herpes simplex virus DNA polymerase and characterization of its associated exonuclease activity Eur. J. Biochem. 98, 231-244 10.1111/j.1432-1033.1979.tb13181.x
    • (1979) Eur. J. Biochem. , vol.98 , pp. 231-244
    • Knopf, K.W.1
  • 34
    • 0019837866 scopus 로고
    • Herpes simplex virus type I DNA polymerase. Kinetic properties of the associated 3′-5′ exonuclease activity and its role in araAMP incorporation
    • Derse, D. and Cheng, Y. C. (1981) Herpes simplex virus type I DNA polymerase. Kinetic properties of the associated 3′-5′ exonuclease activity and its role in araAMP incorporation J. Biol. Chem. 256, 8525-8530
    • (1981) J. Biol. Chem. , vol.256 , pp. 8525-8530
    • Derse, D.1    Cheng, Y.C.2
  • 35
    • 0019165310 scopus 로고
    • Properties of herpes simplex virus type 1 and type 2 DNA polymerase
    • Ostrander, M. and Cheng, Y. C. (1980) Properties of herpes simplex virus type 1 and type 2 DNA polymerase Biochim. Biophys. Acta, Nucleic Acids Protein Synth. 609, 232-245 10.1016/0005-2787(80)90234-8
    • (1980) Biochim. Biophys. Acta, Nucleic Acids Protein Synth. , vol.609 , pp. 232-245
    • Ostrander, M.1    Cheng, Y.C.2
  • 36
    • 59449102872 scopus 로고    scopus 로고
    • Initiation of new DNA strands by the herpes simplex virus-1 primase-helicase complex and either herpes DNA polymerase or human DNA polymerase alpha
    • Cavanaugh, N. A. and Kuchta, R. D. (2008) Initiation of new DNA strands by the herpes simplex virus-1 primase-helicase complex and either herpes DNA polymerase or human DNA polymerase alpha J. Biol. Chem. 284, 1523-1532 10.1074/jbc.M805476200
    • (2008) J. Biol. Chem. , vol.284 , pp. 1523-1532
    • Cavanaugh, N.A.1    Kuchta, R.D.2
  • 39
    • 35549011905 scopus 로고    scopus 로고
    • Fluorescence of 2-aminopurine reveals rapid conformational changes in the RB69 DNA polymerase-primer/template complexes upon binding and incorporation of matched deoxynucleoside triphosphates
    • Zhang, H., Cao, W., Zakharova, E., Konigsberg, W., and De La Cruz, E. M. (2007) Fluorescence of 2-aminopurine reveals rapid conformational changes in the RB69 DNA polymerase-primer/template complexes upon binding and incorporation of matched deoxynucleoside triphosphates Nucleic Acids Res. 35, 6052-6062 10.1093/nar/gkm587
    • (2007) Nucleic Acids Res. , vol.35 , pp. 6052-6062
    • Zhang, H.1    Cao, W.2    Zakharova, E.3    Konigsberg, W.4    De La Cruz, E.M.5
  • 40
    • 0031587827 scopus 로고    scopus 로고
    • Crystal structure of a pol alpha 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 alpha family replication DNA polymerase from bacteriophage RB69 Cell 89, 1087-1099 10.1016/S0092-8674(00)80296-2
    • (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
  • 41
    • 79952077426 scopus 로고    scopus 로고
    • Insights into base selectivity from the 1.8 A resolution structure of an RB69 DNA polymerase ternary complex
    • Wang, M., Xia, S., Blaha, G., Steitz, T. A., Konigsberg, W. H., and Wang, J. (2011) Insights into base selectivity from the 1.8 A resolution structure of an RB69 DNA polymerase ternary complex Biochemistry 50, 581-590 10.1021/bi101192f
    • (2011) Biochemistry , vol.50 , pp. 581-590
    • Wang, M.1    Xia, S.2    Blaha, G.3    Steitz, T.A.4    Konigsberg, W.H.5    Wang, J.6
  • 42
    • 34547175132 scopus 로고    scopus 로고
    • Structures of phi29 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 phi29 DNA polymerase complexed with substrate: the mechanism of translocation in B-family polymerases EMBO J. 26, 3494-3505 10.1038/sj.emboj.7601780
    • (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
  • 43
    • 0035369086 scopus 로고    scopus 로고
    • Structure of the replicating complex of a pol alpha family DNA polymerase
    • Franklin, M. C., Wang, J., and Steitz, T. A. (2001) Structure of the replicating complex of a pol alpha family DNA polymerase Cell 105, 657-667 10.1016/S0092-8674(01)00367-1
    • (2001) Cell , vol.105 , pp. 657-667
    • Franklin, M.C.1    Wang, J.2    Steitz, T.A.3
  • 44
    • 84861584310 scopus 로고    scopus 로고
    • Contribution of partial charge interactions and base stacking to the efficiency of primer extension at and beyond abasic sites in DNA
    • Xia, S., Vashishtha, A., Bulkley, D., Eom, S. H., Wang, J., and Konigsberg, W. H. (2012) Contribution of partial charge interactions and base stacking to the efficiency of primer extension at and beyond abasic sites in DNA Biochemistry 51, 4922-4931 10.1021/bi300296q
    • (2012) Biochemistry , vol.51 , pp. 4922-4931
    • Xia, S.1    Vashishtha, A.2    Bulkley, D.3    Eom, S.H.4    Wang, J.5    Konigsberg, W.H.6
  • 45
    • 79960134404 scopus 로고    scopus 로고
    • Phosphonoformic acid inhibits viral replication by trapping the closed form of the DNA polymerase
    • Zahn, K. E., Tchesnokov, E. P., Gotte, M., and Doublie, S. (2011) Phosphonoformic acid inhibits viral replication by trapping the closed form of the DNA polymerase J. Biol. Chem. 286, 25246-25255 10.1074/jbc.M111.248864
    • (2011) J. Biol. Chem. , vol.286 , pp. 25246-25255
    • Zahn, K.E.1    Tchesnokov, E.P.2    Gotte, M.3    Doublie, S.4
  • 46
    • 0028342556 scopus 로고
    • Interaction of herpes simplex virus type 1 DNA polymerase and the UL42 accessory protein with a model primer template
    • Gottlieb, J. and Challberg, M. D. (1994) Interaction of herpes simplex virus type 1 DNA polymerase and the UL42 accessory protein with a model primer template J. Virol 68, 4937-4945
    • (1994) J. Virol , vol.68 , pp. 4937-4945
    • Gottlieb, J.1    Challberg, M.D.2
  • 47
    • 0032508624 scopus 로고    scopus 로고
    • Impaired mismatch extension by a herpes simplex DNA polymerase mutant with an editing nuclease defect
    • Baker, R. O. and Hall, J. D. (1998) Impaired mismatch extension by a herpes simplex DNA polymerase mutant with an editing nuclease defect J. Biol. Chem. 273, 24075-24082 10.1074/jbc.273.37.24075
    • (1998) J. Biol. Chem. , vol.273 , pp. 24075-24082
    • Baker, R.O.1    Hall, J.D.2
  • 48
  • 49
    • 84872485372 scopus 로고    scopus 로고
    • Ribonucleotide incorporation, proofreading and bypass by human DNA polymerase delta
    • Clausen, A. R., Zhang, S., Burgers, P. M., Lee, M. Y., and Kunkel, T. A. (2013) Ribonucleotide incorporation, proofreading and bypass by human DNA polymerase delta DNA Repair 12, 121-127 10.1016/j.dnarep.2012.11.006
    • (2013) DNA Repair , vol.12 , pp. 121-127
    • Clausen, A.R.1    Zhang, S.2    Burgers, P.M.3    Lee, M.Y.4    Kunkel, T.A.5
  • 50
    • 84864309091 scopus 로고    scopus 로고
    • Proofreading of ribonucleotides inserted into DNA by yeast DNA polymerase varepsilon
    • Williams, J. S., Clausen, A. R., Nick McElhinny, S. A., Watts, B. E., Johansson, E., and Kunkel, T. A. (2012) Proofreading of ribonucleotides inserted into DNA by yeast DNA polymerase varepsilon DNA Repair 11, 649-656 10.1016/j.dnarep.2012.05.004
    • (2012) DNA Repair , vol.11 , pp. 649-656
    • Williams, J.S.1    Clausen, A.R.2    Nick McElhinny, S.A.3    Watts, B.E.4    Johansson, E.5    Kunkel, T.A.6
  • 51
    • 84920076425 scopus 로고    scopus 로고
    • Kinetic mechanisms governing stable ribonucleotide incorporation in individual DNA polymerase complexes
    • Dahl, J. M., Wang, H., Lazaro, J. M., Salas, M., and Lieberman, K. R. (2014) Kinetic mechanisms governing stable ribonucleotide incorporation in individual DNA polymerase complexes Biochemistry 53, 8061-8076 10.1021/bi501216a
    • (2014) Biochemistry , vol.53 , pp. 8061-8076
    • Dahl, J.M.1    Wang, H.2    Lazaro, J.M.3    Salas, M.4    Lieberman, K.R.5


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