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Volumn 37, Issue 19, 2009, Pages 6439-6453

Biochemical properties and base excision repair complex formation of apurinic/apyrimidinic endonuclease from Pyrococcus furiosus

Author keywords

[No Author keywords available]

Indexed keywords

CYCLINE; DNA (APURINIC OR APYRIMIDINIC SITE) LYASE; EXONUCLEASE; URACIL DNA GLYCOSIDASE;

EID: 70449687206     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkp720     Document Type: Article
Times cited : (30)

References (54)
  • 1
    • 0034734377 scopus 로고    scopus 로고
    • Abasic site recognition by two apurinic/apyrimidinic endonuclease families in DNA base excision repair: The 3 ends justify the means
    • Mol,C.D., Hosfield,D.J. and Tainer,J.A. (2000) Abasic site recognition by two apurinic/apyrimidinic endonuclease families in DNA base excision repair: The 3 ends justify the means. Mutat. Res., 460, 211-229.
    • (2000) Mutat. Res , vol.460 , pp. 211-229
    • Mol, C.D.1    Hosfield, D.J.2    Tainer, J.A.3
  • 2
    • 0348140585 scopus 로고    scopus 로고
    • Abasic sites in DNA: Repair and biological consequences in Saccharomyces cerevisiae
    • Boiteux,S. and Guillet,M. (2004) Abasic sites in DNA: Repair and biological consequences in Saccharomyces cerevisiae. DNA Repair, 3, 1-12.
    • (2004) DNA Repair , vol.3 , pp. 1-12
    • Boiteux, S.1    Guillet, M.2
  • 3
    • 34250900982 scopus 로고    scopus 로고
    • Base-excision repair of oxidative DNA damage
    • David,S.S., O'Shea,V.L. and Kundu,S. (2007) Base-excision repair of oxidative DNA damage. Nature, 447, 941-950.
    • (2007) Nature , vol.447 , pp. 941-950
    • David, S.S.1    O'Shea, V.L.2    Kundu, S.3
  • 4
    • 0015504248 scopus 로고
    • Rate of depurination of native deoxyribonucleic acid
    • Lindahl,T. and Nyberg,B. (1972) Rate of depurination of native deoxyribonucleic acid. Biochemistry, 11, 3610-3618.
    • (1972) Biochemistry , vol.11 , pp. 3610-3618
    • Lindahl, T.1    Nyberg, B.2
  • 5
    • 38049112778 scopus 로고    scopus 로고
    • Early steps in the DNA base excision/single-strand interruption repair pathway in mammalian cells
    • Hegde,M.L., Hazra,T.K. and Mitra,S. (2008) Early steps in the DNA base excision/single-strand interruption repair pathway in mammalian cells. Cell Res., 18, 27-47.
    • (2008) Cell Res , vol.18 , pp. 27-47
    • Hegde, M.L.1    Hazra, T.K.2    Mitra, S.3
  • 6
    • 50649108365 scopus 로고    scopus 로고
    • Base excision repair and its role in maintaining genome stability
    • Baute,J. and Depicker,A. (2008) Base excision repair and its role in maintaining genome stability. Crit. Rev. Biochem. Mol. Biol., 43, 239-276.
    • (2008) Crit. Rev. Biochem. Mol. Biol , vol.43 , pp. 239-276
    • Baute, J.1    Depicker, A.2
  • 8
    • 0017161630 scopus 로고
    • Methyl methane sulfonate-sensitive mutant of Escherichia coli deficient in an endonuclease specific for apurinic sites in deoxyribonucleic acid
    • Ljungquist,S., Lindahl,T. and Howard-Flanders,P. (1976) Methyl methane sulfonate-sensitive mutant of Escherichia coli deficient in an endonuclease specific for apurinic sites in deoxyribonucleic acid. J. Bacteriol., 126, 646-653.
    • (1976) J. Bacteriol , vol.126 , pp. 646-653
    • Ljungquist, S.1    Lindahl, T.2    Howard-Flanders, P.3
  • 9
    • 0017701231 scopus 로고
    • A new endonuclease from Escherichia coli acting at apurinic sites in DNA
    • Ljungquist,S. (1976) A new endonuclease from Escherichia coli acting at apurinic sites in DNA. J. Biol. Chem., 252, 2808-2814.
    • (1976) J. Biol. Chem , vol.252 , pp. 2808-2814
    • Ljungquist, S.1
  • 10
    • 0025324303 scopus 로고
    • Yeast structural gene (APN1) for the major apurinic endonuclease: Homology to Escherichia coli endonuclease IV
    • Popoff,S.C., Spira,A.I., Johnson,A.W. and Demple,B. (1990) Yeast structural gene (APN1) for the major apurinic endonuclease: Homology to Escherichia coli endonuclease IV. Proc. Natl Acad. Sci. USA, 87, 4193-4197.
    • (1990) Proc. Natl Acad. Sci. USA , vol.87 , pp. 4193-4197
    • Popoff, S.C.1    Spira, A.I.2    Johnson, A.W.3    Demple, B.4
  • 11
    • 0032190633 scopus 로고    scopus 로고
    • Identification of APN2, the Saccharomyces cerevisiae homolog of the major human AP endonuclease HAP1, and its role in the repair of abasic sites
    • Johnson,R.E., Torres-Ramos,C.A., Izumi,T., Mitra,S., Prakash,S. and Prakash,L. (1998) Identification of APN2, the Saccharomyces cerevisiae homolog of the major human AP endonuclease HAP1, and its role in the repair of abasic sites. Gene Dev., 12, 3137-3143.
    • (1998) Gene Dev , vol.12 , pp. 3137-3143
    • Johnson, R.E.1    Torres-Ramos, C.A.2    Izumi, T.3    Mitra, S.4    Prakash, S.5    Prakash, L.6
  • 12
    • 0026323008 scopus 로고
    • Cloning and expression of APE, the cDNA encoding the major human apurinic endonuclease: Definition of a family of DNA repair enzymes
    • Demple,B., Herman,T. and Chen,D.S. (1991) Cloning and expression of APE, the cDNA encoding the major human apurinic endonuclease: Definition of a family of DNA repair enzymes. Proc. Natl Acad. Sci. USA, 88, 11450-11454.
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 11450-11454
    • Demple, B.1    Herman, T.2    Chen, D.S.3
  • 13
    • 0034531986 scopus 로고    scopus 로고
    • Second human protein with homology to the Escherichia coli abasic endonuclease exonuclease III
    • Hadi,M.Z. and Wilson,D.M. III (2000) Second human protein with homology to the Escherichia coli abasic endonuclease exonuclease III. Environ. Mol. Mutagen., 36, 312-324.
    • (2000) Environ. Mol. Mutagen , vol.36 , pp. 312-324
    • Hadi, M.Z.1    Wilson III, D.M.2
  • 15
    • 0037474210 scopus 로고    scopus 로고
    • Characterization of an endonuclease IV 3-5 exonuclease activity
    • Kerins,S.M., Collins,R. and McCarthy,T.V. (2003) Characterization of an endonuclease IV 3-5 exonuclease activity. J. Biol. Chem., 278, 3048-3054.
    • (2003) J. Biol. Chem , vol.278 , pp. 3048-3054
    • Kerins, S.M.1    Collins, R.2    McCarthy, T.V.3
  • 16
    • 33745219158 scopus 로고    scopus 로고
    • A versatile endonuclease IV from Thermus thermophilus has uracil-excising and 3-5 exonuclease activity
    • Back,J.H., Chung,J.H., Park,J.H. and Han,Y.S. (2006) A versatile endonuclease IV from Thermus thermophilus has uracil-excising and 3-5 exonuclease activity. Biochem. Biophys. Res. Commun., 346, 889-895.
    • (2006) Biochem. Biophys. Res. Commun , vol.346 , pp. 889-895
    • Back, J.H.1    Chung, J.H.2    Park, J.H.3    Han, Y.S.4
  • 17
    • 33744502385 scopus 로고    scopus 로고
    • Human Ape2 protein has a 3-5 exonuclease activity that acts preferentially on mismatched base pairs
    • Burkovics,P., Szukacsov,V., Unk,I. and Haracska,L. (2006) Human Ape2 protein has a 3-5 exonuclease activity that acts preferentially on mismatched base pairs. Nucleic Acids Res., 34, 2508-2515.
    • (2006) Nucleic Acids Res , vol.34 , pp. 2508-2515
    • Burkovics, P.1    Szukacsov, V.2    Unk, I.3    Haracska, L.4
  • 18
    • 0141815703 scopus 로고    scopus 로고
    • Modulation of the 3->5-exonuclease activity of human apurinic endonuclease (Ape1) by its 5-incised abasic DNA product
    • Wong,D., DeMott,M.S. and Demple,B. (2003) Modulation of the 3->5-exonuclease activity of human apurinic endonuclease (Ape1) by its 5-incised abasic DNA product. J. Biol. Chem., 278, 36242-36249.
    • (2003) J. Biol. Chem , vol.278 , pp. 36242-36249
    • Wong, D.1    DeMott, M.S.2    Demple, B.3
  • 19
    • 0036707526 scopus 로고    scopus 로고
    • Stimulation of 3->5 exonuclease and 3-phosphodiesterase activities of yeast apn2 by proliferating cell nuclear antigen
    • Unk,I., Haracska,L., Gomes,X.V., Burgers,P.M., Prakash,L. and Prakash,S. (2002) Stimulation of 3->5 exonuclease and 3-phosphodiesterase activities of yeast apn2 by proliferating cell nuclear antigen. Mol. Cell Biol., 22, 6480-6486.
    • (2002) Mol. Cell Biol , vol.22 , pp. 6480-6486
    • Unk, I.1    Haracska, L.2    Gomes, X.V.3    Burgers, P.M.4    Prakash, L.5    Prakash, S.6
  • 20
    • 57349184695 scopus 로고    scopus 로고
    • Proliferating cell nuclear antigen: A proteomics view
    • Naryzhny,S.N. (2008) Proliferating cell nuclear antigen: A proteomics view. Cell Mol. Life Sci., 65, 3789-3808.
    • (2008) Cell Mol. Life Sci , vol.65 , pp. 3789-3808
    • Naryzhny, S.N.1
  • 21
    • 34249066085 scopus 로고    scopus 로고
    • PCNA, the maestro of the replication fork
    • Moldovan,G.L., Pfander,B. and Jentsch,S. (2007) PCNA, the maestro of the replication fork. Cell, 129, 665-679.
    • (2007) Cell , vol.129 , pp. 665-679
    • Moldovan, G.L.1    Pfander, B.2    Jentsch, S.3
  • 22
    • 67949109632 scopus 로고    scopus 로고
    • Role of PCNA-dependent stimulation of 3-phosphodiesterase and 3-5 exonuclease activities of human Ape2 in repair of oxidative DNA damage
    • Burkovics,P., Hajdu,I., Szukacsov,V., Unk,I. and Haracska,L. (2009) Role of PCNA-dependent stimulation of 3-phosphodiesterase and 3-5 exonuclease activities of human Ape2 in repair of oxidative DNA damage. Nucleic Acids Res., 37, 4247-4255.
    • (2009) Nucleic Acids Res , vol.37 , pp. 4247-4255
    • Burkovics, P.1    Hajdu, I.2    Szukacsov, V.3    Unk, I.4    Haracska, L.5
  • 23
    • 0036734527 scopus 로고    scopus 로고
    • Physical interaction between proliferating cell nuclear antigen and replication factor C from Pyrococcus furiosus
    • Matsumiya,S., Ishino,S., Ishino,Y. and Morikawa,K. (2002) Physical interaction between proliferating cell nuclear antigen and replication factor C from Pyrococcus furiosus. Genes Cells, 7, 911-922.
    • (2002) Genes Cells , vol.7 , pp. 911-922
    • Matsumiya, S.1    Ishino, S.2    Ishino, Y.3    Morikawa, K.4
  • 24
    • 33645851036 scopus 로고    scopus 로고
    • The archaeal Hjm helicase has recQ-like functions, and may be involved in repair of stalled replication fork
    • Fujikane,R., Shinagawa,H. and Ishino,Y. (2006) The archaeal Hjm helicase has recQ-like functions, and may be involved in repair of stalled replication fork. Genes Cells, 11, 99-110.
    • (2006) Genes Cells , vol.11 , pp. 99-110
    • Fujikane, R.1    Shinagawa, H.2    Ishino, Y.3
  • 25
    • 33748767654 scopus 로고    scopus 로고
    • Identification of a novel binding motif in Pyrococcus furiosus DNA ligase for the functional interaction with proliferating cell nuclear antigen
    • Kiyonari,S., Takayama,K., Nishida,H. and Ishino,Y. (2006) Identification of a novel binding motif in Pyrococcus furiosus DNA ligase for the functional interaction with proliferating cell nuclear antigen. J. Biol. Chem., 281, 28023-28032.
    • (2006) J. Biol. Chem , vol.281 , pp. 28023-28032
    • Kiyonari, S.1    Takayama, K.2    Nishida, H.3    Ishino, Y.4
  • 26
    • 53049086145 scopus 로고    scopus 로고
    • Physical and functional interactions between uracil-DNA glycosylase and proliferating cell nuclear antigen from the euryarchaeon Pyrococcus furiosus
    • Kiyonari,S., Uchimura,M., Shirai,T. and Ishino,Y. (2008) Physical and functional interactions between uracil-DNA glycosylase and proliferating cell nuclear antigen from the euryarchaeon Pyrococcus furiosus. J. Biol. Chem., 283, 24185-24193.
    • (2008) J. Biol. Chem , vol.283 , pp. 24185-24193
    • Kiyonari, S.1    Uchimura, M.2    Shirai, T.3    Ishino, Y.4
  • 27
    • 34547615757 scopus 로고    scopus 로고
    • DNA polymerases BI and D from the hyperthermophilic archaeon Pyrococcus furiosus both bind to proliferating cell nuclear antigen with their C-terminal PIP-box motifs
    • Tori,K., Kimizu,M., Ishino,S. and Ishino,Y. (2007) DNA polymerases BI and D from the hyperthermophilic archaeon Pyrococcus furiosus both bind to proliferating cell nuclear antigen with their C-terminal PIP-box motifs. J. Bacteriol., 189, 5652-5657.
    • (2007) J. Bacteriol , vol.189 , pp. 5652-5657
    • Tori, K.1    Kimizu, M.2    Ishino, S.3    Ishino, Y.4
  • 28
    • 0016257644 scopus 로고
    • Heat-induced deamination of cytosine residues in deoxyribonucleic acid
    • Lindahl,T. and Nyberg,B. (1974) Heat-induced deamination of cytosine residues in deoxyribonucleic acid. Biochemistry, 13, 3405-3410.
    • (1974) Biochemistry , vol.13 , pp. 3405-3410
    • Lindahl, T.1    Nyberg, B.2
  • 29
    • 0034576553 scopus 로고    scopus 로고
    • The alpha/beta fold uracil DNA glycosylases: A common origin with diverse fates
    • Aravind,L. and Koonin,E.V. (2000) The alpha/beta fold uracil DNA glycosylases: A common origin with diverse fates. Genome, Biol., 1, 0007.1-0007.8.
    • (2000) Genome, Biol , vol.1
    • Aravind, L.1    Koonin, E.V.2
  • 30
    • 0034734383 scopus 로고    scopus 로고
    • Structure and function in the uracil-DNA glycosylase superfamily
    • Pearl,L.H. (2000) Structure and function in the uracil-DNA glycosylase superfamily. Mutat. Res., 460, 165-181.
    • (2000) Mutat. Res , vol.460 , pp. 165-181
    • Pearl, L.H.1
  • 31
    • 33749000862 scopus 로고    scopus 로고
    • Characterization of the AP endonucleases from Thermoplasma volcanium and Lactobacillus plantarum: Contributions of two important tryptophan residues to AP site recognition
    • Kaneda,K., Ohishi,K., Sekiguchi,J. and Shida,T. (2006) Characterization of the AP endonucleases from Thermoplasma volcanium and Lactobacillus plantarum: Contributions of two important tryptophan residues to AP site recognition. Biosci. Biotechnol. Biochem., 70, 2213-2221.
    • (2006) Biosci. Biotechnol. Biochem , vol.70 , pp. 2213-2221
    • Kaneda, K.1    Ohishi, K.2    Sekiguchi, J.3    Shida, T.4
  • 32
    • 13844320315 scopus 로고    scopus 로고
    • A recombinant exonuclease III homologue of the thermophilic archaeon Methanothermobacter thermautotrophicus
    • Pfeifer,S. and Greiner-Stöffele,T. (2005) A recombinant exonuclease III homologue of the thermophilic archaeon Methanothermobacter thermautotrophicus. DNA Repair, 4, 433-444.
    • (2005) DNA Repair , vol.4 , pp. 433-444
    • Pfeifer, S.1    Greiner-Stöffele, T.2
  • 33
    • 0038408981 scopus 로고    scopus 로고
    • The xthA gene product of Archaeoglobus fulgidus is an unspecific DNase
    • Miertzschke,M. and Greiner-Stöffele,T. (2003) The xthA gene product of Archaeoglobus fulgidus is an unspecific DNase. Eur. J. Biochem., 270, 1838-1849.
    • (2003) Eur. J. Biochem , vol.270 , pp. 1838-1849
    • Miertzschke, M.1    Greiner-Stöffele, T.2
  • 34
    • 0041589201 scopus 로고    scopus 로고
    • Enzymology of base excision repair in the hyperthermophilic archaeon Pyrobaculum aerophilum
    • Sartori,A.A. and Jiricny,J. (2003) Enzymology of base excision repair in the hyperthermophilic archaeon Pyrobaculum aerophilum. J. Biol. Chem. 278, 24563-24576.
    • (2003) J. Biol. Chem , vol.278 , pp. 24563-24576
    • Sartori, A.A.1    Jiricny, J.2
  • 35
    • 0242418186 scopus 로고    scopus 로고
    • Endonuclease IV enhances base excision repair of endonuclease III from Methanobacterium thermoautotrophicum
    • Back,J.H., Chung,J.H., Park,Y.I., Kim,K.S. and Han,Y.S. (2003) Endonuclease IV enhances base excision repair of endonuclease III from Methanobacterium thermoautotrophicum. DNA Repair, 2, 455-470.
    • (2003) DNA Repair , vol.2 , pp. 455-470
    • Back, J.H.1    Chung, J.H.2    Park, Y.I.3    Kim, K.S.4    Han, Y.S.5
  • 36
    • 33750362182 scopus 로고    scopus 로고
    • Overexpression of the genes from thermophiles in Escherichia coli by high-temperature cultivation
    • Koma,D., Sawai,T., Harayama,S. and Kino,K. (2006) Overexpression of the genes from thermophiles in Escherichia coli by high-temperature cultivation. Appl. Microbiol. Biotechnol., 73, 172-180.
    • (2006) Appl. Microbiol. Biotechnol , vol.73 , pp. 172-180
    • Koma, D.1    Sawai, T.2    Harayama, S.3    Kino, K.4
  • 37
    • 0037377527 scopus 로고    scopus 로고
    • Intermolecular ion pairs maintain the toroidal structure of Pyrococcus furiosus PCNA
    • Matsumiya,S., Ishino,S., Ishino,Y. and Morikawa,K. (2003) Intermolecular ion pairs maintain the toroidal structure of Pyrococcus furiosus PCNA. Protein Sci., 12, 823-831.
    • (2003) Protein Sci , vol.12 , pp. 823-831
    • Matsumiya, S.1    Ishino, S.2    Ishino, Y.3    Morikawa, K.4
  • 38
    • 33747605277 scopus 로고    scopus 로고
    • Chemical synthesis of oligonucleotides containing damaged bases for biological studies
    • Iwai,S. (2006) Chemical synthesis of oligonucleotides containing damaged bases for biological studies. Nucleosides Nucleotides Nucleic Acids 25, 561-582.
    • (2006) Nucleosides Nucleotides Nucleic Acids , vol.25 , pp. 561-582
    • Iwai, S.1
  • 39
    • 0033529716 scopus 로고    scopus 로고
    • Structure of the DNA repair enzyme endonuclease IV and its DNA complex: Double-nucleotide flipping at abasic sites and three-metal-ion catalysis
    • Hosfield,D.J., Guan,Y., Haas,B.J., Cunningham,R.P. and Tainer,J.A. (1999) Structure of the DNA repair enzyme endonuclease IV and its DNA complex: Double-nucleotide flipping at abasic sites and three-metal-ion catalysis. Cell, 98, 397-408.
    • (1999) Cell , vol.98 , pp. 397-408
    • Hosfield, D.J.1    Guan, Y.2    Haas, B.J.3    Cunningham, R.P.4    Tainer, J.A.5
  • 40
    • 33846799362 scopus 로고    scopus 로고
    • Unraveling the three-metal-ion catalytic mechanism of the DNA repair enzyme endonuclease IV
    • Ivanov,I., Tainer,J.A. and McCammon,J.A. (2007) Unraveling the three-metal-ion catalytic mechanism of the DNA repair enzyme endonuclease IV. Proc. Natl Acad. Sci. USA, 104, 1465-1470.
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 1465-1470
    • Ivanov, I.1    Tainer, J.A.2    McCammon, J.A.3
  • 42
    • 1842735418 scopus 로고    scopus 로고
    • Human AP endonuclease (APE1) demonstrates endonucleolytic activity against AP sites in single-stranded DNA
    • Marenstein,D.R., Wilson,D.M. III and Teebor,G.W. (2004) Human AP endonuclease (APE1) demonstrates endonucleolytic activity against AP sites in single-stranded DNA. DNA Repair, 3, 527-533.
    • (2004) DNA Repair , vol.3 , pp. 527-533
    • Marenstein, D.R.1    Wilson III, D.M.2    Teebor, G.W.3
  • 43
    • 27844477712 scopus 로고    scopus 로고
    • Chlamydia pneumoniae AP endonuclease IV could cleave AP sites of double- and single-stranded DNA
    • Liu,X. and Liu,J. (2005) Chlamydia pneumoniae AP endonuclease IV could cleave AP sites of double- and single-stranded DNA. Biochim. Biophys. Acta, 1753, 217-225.
    • (2005) Biochim. Biophys. Acta , vol.1753 , pp. 217-225
    • Liu, X.1    Liu, J.2
  • 44
    • 0035940441 scopus 로고    scopus 로고
    • Interaction of human AP endonuclease 1 with flap endonuclease 1 and proliferating cell nuclear antigen involved in long-patch base excision repair
    • Dianova,I.I., Bohr,V.A. and Dianov,G.L. (2001) Interaction of human AP endonuclease 1 with flap endonuclease 1 and proliferating cell nuclear antigen involved in long-patch base excision repair. Biochemistry, 40, 12639-12644.
    • (2001) Biochemistry , vol.40 , pp. 12639-12644
    • Dianova, I.I.1    Bohr, V.A.2    Dianov, G.L.3
  • 45
    • 0035369734 scopus 로고    scopus 로고
    • Human APE2 protein is mostly localized in the nuclei and to some extent in the mitochondria, while nuclear APE2 is partly associated with proliferating cell nuclear antigen
    • Tsuchimoto,D., Sakai,Y., Sakumi,K., Nishioka,K., Sasaki,M., Fujiwara,T. and Nakabeppu,Y. (2001) Human APE2 protein is mostly localized in the nuclei and to some extent in the mitochondria, while nuclear APE2 is partly associated with proliferating cell nuclear antigen. Nucleic Acids Res., 29, 2349-2360.
    • (2001) Nucleic Acids Res , vol.29 , pp. 2349-2360
    • Tsuchimoto, D.1    Sakai, Y.2    Sakumi, K.3    Nishioka, K.4    Sasaki, M.5    Fujiwara, T.6    Nakabeppu, Y.7
  • 47
    • 33751012715 scopus 로고    scopus 로고
    • Georg,J., Schomacher,L., Chong,J.P., Majerni' k,A.I., Raabe,M., Urlaub,H., Müller,S., Ciirdaeva,E., Kramer,W. and Fritz,H.J. (2006) The Methanothermobacter thermautotrophicus ExoIII homologue Mth212 is a DNA uridine endonuclease. Nucleic Acids Res., 34, 5325-5336.
    • Georg,J., Schomacher,L., Chong,J.P., Majerni' k,A.I., Raabe,M., Urlaub,H., Müller,S., Ciirdaeva,E., Kramer,W. and Fritz,H.J. (2006) The Methanothermobacter thermautotrophicus ExoIII homologue Mth212 is a DNA uridine endonuclease. Nucleic Acids Res., 34, 5325-5336.
  • 48
    • 34548363938 scopus 로고    scopus 로고
    • A single amino acid substitution in the DNA-binding domain of Aeropyrum pernix DNA ligase impairs its interaction with proliferating cell nuclear antigen
    • Kiyonari,S., Kamigochi,T. and Ishino,Y. (2007) A single amino acid substitution in the DNA-binding domain of Aeropyrum pernix DNA ligase impairs its interaction with proliferating cell nuclear antigen. Extremophiles, 11, 675-684.
    • (2007) Extremophiles , vol.11 , pp. 675-684
    • Kiyonari, S.1    Kamigochi, T.2    Ishino, Y.3
  • 49
    • 34247128593 scopus 로고    scopus 로고
    • Human base excision repair complex is physically associated to DNA replication and cell cycle regulatory proteins
    • Parlanti,E., Locatelli,G., Maga,G. and Dogliotti,E. (2007) Human base excision repair complex is physically associated to DNA replication and cell cycle regulatory proteins. Nucleic Acids Res., 35, 1569-1577.
    • (2007) Nucleic Acids Res , vol.35 , pp. 1569-1577
    • Parlanti, E.1    Locatelli, G.2    Maga, G.3    Dogliotti, E.4
  • 52
    • 33747617313 scopus 로고    scopus 로고
    • Comprehensive search for DNA polymerase in the hyperthermophilic archaeon, Pyrococcus furiosus
    • Ishino,S. and Ishino,Y. (2006) Comprehensive search for DNA polymerase in the hyperthermophilic archaeon, Pyrococcus furiosus. Nucleosides Nucleotides Nucleic Acids, 25, 681-691.
    • (2006) Nucleosides Nucleotides Nucleic Acids , vol.25 , pp. 681-691
    • Ishino, S.1    Ishino, Y.2
  • 53
    • 0034981262 scopus 로고    scopus 로고
    • DNA polymerases from euryarchaeota
    • Ishino,Y. and Ishino,S. (2001) DNA polymerases from euryarchaeota. Methods Enzymol., 334, 249-260.
    • (2001) Methods Enzymol , vol.334 , pp. 249-260
    • Ishino, Y.1    Ishino, S.2
  • 54
    • 33645063724 scopus 로고    scopus 로고
    • +-dependent DNA ligases share an essential function in the halophilic archaeon Haloferax volcanii
    • +-dependent DNA ligases share an essential function in the halophilic archaeon Haloferax volcanii. Mol. Microbiol., 59, 743-752.
    • (2006) Mol. Microbiol , vol.59 , pp. 743-752
    • Zhao, A.1    Gray, F.C.2    MacNeill, S.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.