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Volumn 27, Issue 2, 2007, Pages 311-323

Retraction Notice to: Sealing of Chromosomal DNA Nicks during Nucleotide Excision Repair Requires XRCC1 and DNA Ligase IIIα in a Cell-Cycle-Specific Manner (Molecular Cell (2007) 27(2) (311–323), (S1097276507004042), (10.1016/j.molcel.2007.06.014));Sealing of Chromosomal DNA Nicks during Nucleotide Excision Repair Requires XRCC1 and DNA Ligase IIIα in a Cell-Cycle-Specific Manner

Author keywords

DNA

Indexed keywords

CYCLINE; DNA BINDING PROTEIN; DNA DIRECTED DNA POLYMERASE DELTA; DNA DIRECTED DNA POLYMERASE EPSILON; KI 67 ANTIGEN; POLYDEOXYRIBONUCLEOTIDE SYNTHASE; POLYDEOXYRIBONUCLEOTIDE SYNTHASE IIIALPHA; PROTEIN P89; PROTEIN XRCC1; UNCLASSIFIED DRUG;

EID: 34447302016     PISSN: 10972765     EISSN: 10974164     Source Type: Journal    
DOI: 10.1016/j.molcel.2021.11.022     Document Type: Erratum
Times cited : (222)

References (52)
  • 1
    • 27544489816 scopus 로고    scopus 로고
    • A role for polymerase eta in the cellular tolerance to cisplatin-induced damage
    • Albertella M.R., Green C.M., Lehmann A.R., and O'Connor M.J. A role for polymerase eta in the cellular tolerance to cisplatin-induced damage. Cancer Res. 21 (2005) 9799-9806
    • (2005) Cancer Res. , vol.21 , pp. 9799-9806
    • Albertella, M.R.1    Green, C.M.2    Lehmann, A.R.3    O'Connor, M.J.4
  • 3
    • 0242605710 scopus 로고    scopus 로고
    • Nucleotide excision repair of DNA with recombinant human proteins: definition of the minimal set of factors, active forms of TFIIH, and modulation by CAK
    • Araujo S.J., Tirode F., Coin F., Pospiech H., Syvaoja J.E., Stucki M., Hubscher U., Egly J.M., and Wood R.D. Nucleotide excision repair of DNA with recombinant human proteins: definition of the minimal set of factors, active forms of TFIIH, and modulation by CAK. Genes Dev. 14 (2000) 349-359
    • (2000) Genes Dev. , vol.14 , pp. 349-359
    • Araujo, S.J.1    Tirode, F.2    Coin, F.3    Pospiech, H.4    Syvaoja, J.E.5    Stucki, M.6    Hubscher, U.7    Egly, J.M.8    Wood, R.D.9
  • 4
    • 0026680743 scopus 로고
    • Mutations in the DNA ligase I gene of an individual with immunodeficiencies and cellular hypersensitivity to DNA-damaging agents
    • Barnes D.E., Tomkinson A.E., Lehmann A.R., Webster A.D., and Lindahl T. Mutations in the DNA ligase I gene of an individual with immunodeficiencies and cellular hypersensitivity to DNA-damaging agents. Cell 69 (1992) 495-503
    • (1992) Cell , vol.69 , pp. 495-503
    • Barnes, D.E.1    Tomkinson, A.E.2    Lehmann, A.R.3    Webster, A.D.4    Lindahl, T.5
  • 6
    • 33646871568 scopus 로고    scopus 로고
    • DNA ligase I is an in vivo substrate of DNA-dependent protein kinase and is activated by phosphorylation in response to DNA double-strand breaks
    • Bhat K.R., Benton B.J., and Ray R. DNA ligase I is an in vivo substrate of DNA-dependent protein kinase and is activated by phosphorylation in response to DNA double-strand breaks. Biochemistry 20 (2006) 6522-6528
    • (2006) Biochemistry , vol.20 , pp. 6522-6528
    • Bhat, K.R.1    Benton, B.J.2    Ray, R.3
  • 7
    • 18244378812 scopus 로고    scopus 로고
    • XRCC1 is required for DNA single-strand break repair in human cells
    • Brem R., and Hall J. XRCC1 is required for DNA single-strand break repair in human cells. Nucleic Acids Res. 33 (2005) 2512-2520
    • (2005) Nucleic Acids Res. , vol.33 , pp. 2512-2520
    • Brem, R.1    Hall, J.2
  • 8
    • 0034698033 scopus 로고    scopus 로고
    • The oxidative DNA lesion 8,5′-(S)-cyclo-2′-deoxyadenosine is repaired by the nucleotide excision repair pathway and blocks gene expression in mammalian cells
    • Brooks P.J., Wise D.S., Berry D.A., Kosmoski J.V., Smerdon M.J., Somers R.L., Mackie H., Spoonde A.Y., Ackerman E.J., Coleman K., et al. The oxidative DNA lesion 8,5′-(S)-cyclo-2′-deoxyadenosine is repaired by the nucleotide excision repair pathway and blocks gene expression in mammalian cells. J. Biol. Chem. 29 (2000) 22355-22362
    • (2000) J. Biol. Chem. , vol.29 , pp. 22355-22362
    • Brooks, P.J.1    Wise, D.S.2    Berry, D.A.3    Kosmoski, J.V.4    Smerdon, M.J.5    Somers, R.L.6    Mackie, H.7    Spoonde, A.Y.8    Ackerman, E.J.9    Coleman, K.10
  • 9
    • 0028940972 scopus 로고
    • DNA polymerases required for repair of UV-induced damage in Saccharomyces cerevisiae
    • Budd M.E., and Campbell J.L. DNA polymerases required for repair of UV-induced damage in Saccharomyces cerevisiae. Mol. Cell. Biol. 4 (1995) 2173-2179
    • (1995) Mol. Cell. Biol. , vol.4 , pp. 2173-2179
    • Budd, M.E.1    Campbell, J.L.2
  • 10
    • 0018829549 scopus 로고
    • Large-scale isolation of UV-sensitive clones of CHO cells
    • Busch D.B., Cleaver J.E., and Glaser D.A. Large-scale isolation of UV-sensitive clones of CHO cells. Somatic Cell Genet. 6 (1980) 407-418
    • (1980) Somatic Cell Genet. , vol.6 , pp. 407-418
    • Busch, D.B.1    Cleaver, J.E.2    Glaser, D.A.3
  • 11
    • 0041378046 scopus 로고    scopus 로고
    • XRCC1 and DNA strand break repair
    • Caldecott K.W. XRCC1 and DNA strand break repair. DNA Repair (Amst.) 2 (2003) 955-969
    • (2003) DNA Repair (Amst.) , vol.2 , pp. 955-969
    • Caldecott, K.W.1
  • 12
    • 0028862933 scopus 로고
    • Characterization of the XRCC1-DNA ligase III complex in vitro and its absence from mutant hamster cells
    • Caldecott K.W., Tucker J.D., Stanker L.H., and Thompson L.H. Characterization of the XRCC1-DNA ligase III complex in vitro and its absence from mutant hamster cells. Nucleic Acids Res. 23 (1995) 4836-4843
    • (1995) Nucleic Acids Res. , vol.23 , pp. 4836-4843
    • Caldecott, K.W.1    Tucker, J.D.2    Stanker, L.H.3    Thompson, L.H.4
  • 14
    • 0025021446 scopus 로고
    • Biochemical and cytogenetical characterization of Chinese hamster ovary X-ray-sensitive mutant cells xrs 5 and xrs 6. VI. The correlation between UV-induced DNA lesions and chromosomal aberrations, and their modulations with inhibitors of DNA repair synthesis
    • Darroudi F., Natarajan A.T., and van der Schans G.P. Biochemical and cytogenetical characterization of Chinese hamster ovary X-ray-sensitive mutant cells xrs 5 and xrs 6. VI. The correlation between UV-induced DNA lesions and chromosomal aberrations, and their modulations with inhibitors of DNA repair synthesis. Mutat. Res. 235 (1990) 129-135
    • (1990) Mutat. Res. , vol.235 , pp. 129-135
    • Darroudi, F.1    Natarajan, A.T.2    van der Schans, G.P.3
  • 15
    • 0142009654 scopus 로고    scopus 로고
    • A requirement for PARP-1 for the assembly or stability of XRCC1 nuclear foci at sites of oxidative DNA damage
    • El-Khamisy S.F., Masutani M., Suzuki H., and Caldecott K.W. A requirement for PARP-1 for the assembly or stability of XRCC1 nuclear foci at sites of oxidative DNA damage. Nucleic Acids Res. 31 (2003) 5526-5533
    • (2003) Nucleic Acids Res. , vol.31 , pp. 5526-5533
    • El-Khamisy, S.F.1    Masutani, M.2    Suzuki, H.3    Caldecott, K.W.4
  • 17
    • 0018394647 scopus 로고
    • Single-strand breaks in DNA during repair of UV-induced damage in normal human and xeroderma pigmentosum cells as determined by alkaline DNA unwinding and hydroxylapatite chromatography: effects of hydroxyurea, 5-fluorodeoxyuridine and 1-beta-D-arabinofuranosylcytosine on the kinetics of repair
    • Erixon K., and Ahnstrom G. Single-strand breaks in DNA during repair of UV-induced damage in normal human and xeroderma pigmentosum cells as determined by alkaline DNA unwinding and hydroxylapatite chromatography: effects of hydroxyurea, 5-fluorodeoxyuridine and 1-beta-D-arabinofuranosylcytosine on the kinetics of repair. Mutat. Res. 2 (1979) 257-271
    • (1979) Mutat. Res. , vol.2 , pp. 257-271
    • Erixon, K.1    Ahnstrom, G.2
  • 20
    • 0141844487 scopus 로고    scopus 로고
    • Cell cycle-dependent phosphorylation of human DNA ligase I at the cyclin-dependent kinase sites
    • Ferrari G., Rossi R., Arosio D., Vindigni A., Biamonti G., and Montecucco A. Cell cycle-dependent phosphorylation of human DNA ligase I at the cyclin-dependent kinase sites. J. Biol. Chem. 278 (2003) 37761-37767
    • (2003) J. Biol. Chem. , vol.278 , pp. 37761-37767
    • Ferrari, G.1    Rossi, R.2    Arosio, D.3    Vindigni, A.4    Biamonti, G.5    Montecucco, A.6
  • 21
    • 33747194740 scopus 로고    scopus 로고
    • Cockayne syndrome A and B proteins differentially regulate recruitment of chromatin remodeling and repair factors to stalled RNA polymerase II in vivo
    • Fousteri M., Vermeulen W., van Zeeland A.A., and Mullenders L.H. Cockayne syndrome A and B proteins differentially regulate recruitment of chromatin remodeling and repair factors to stalled RNA polymerase II in vivo. Mol. Cell 4 (2006) 471-482
    • (2006) Mol. Cell , vol.4 , pp. 471-482
    • Fousteri, M.1    Vermeulen, W.2    van Zeeland, A.A.3    Mullenders, L.H.4
  • 22
    • 0030013201 scopus 로고    scopus 로고
    • Relationships between DNA repair and transcription
    • Friedberg E.C. Relationships between DNA repair and transcription. Annu. Rev. Biochem. 65 (1996) 15-42
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 15-42
    • Friedberg, E.C.1
  • 23
    • 0032544413 scopus 로고    scopus 로고
    • Requirement for an interaction of XRCC4 with DNA ligase IV for wild-type V(D)J recombination and DNA double-strand break repair in vivo
    • Grawunder U., Zimmer D., Kulesza P., and Lieber M.R. Requirement for an interaction of XRCC4 with DNA ligase IV for wild-type V(D)J recombination and DNA double-strand break repair in vivo. J. Biol. Chem. 273 (1998) 24708-24714
    • (1998) J. Biol. Chem. , vol.273 , pp. 24708-24714
    • Grawunder, U.1    Zimmer, D.2    Kulesza, P.3    Lieber, M.R.4
  • 24
    • 32644450616 scopus 로고    scopus 로고
    • Molecular mechanisms of mammalian global genome nucleotide excision repair
    • Gillet L.C., and Scharer O.D. Molecular mechanisms of mammalian global genome nucleotide excision repair. Chem. Rev. 2 (2006) 253-276
    • (2006) Chem. Rev. , vol.2 , pp. 253-276
    • Gillet, L.C.1    Scharer, O.D.2
  • 25
    • 7944235691 scopus 로고    scopus 로고
    • Genetic variation in XRCC1, sun exposure, and risk of skin cancer
    • Han J., Hankinson S.E., Colditz G.A., and Hunter D.J. Genetic variation in XRCC1, sun exposure, and risk of skin cancer. Br. J. Cancer 91 (2004) 1604-1609
    • (2004) Br. J. Cancer , vol.91 , pp. 1604-1609
    • Han, J.1    Hankinson, S.E.2    Colditz, G.A.3    Hunter, D.J.4
  • 26
    • 33745179533 scopus 로고    scopus 로고
    • A novel T-77C polymorphism in DNA repair gene XRCC1 contributes to diminished promoter activity and increased risk of non-small cell lung cancer
    • Hao B., Miao X., Li Y., Zhang X., Sun T., Liang G., Zhao Y., Zhou Y., Wang H., Chen X., et al. A novel T-77C polymorphism in DNA repair gene XRCC1 contributes to diminished promoter activity and increased risk of non-small cell lung cancer. Oncogene 25 (2006) 3613-3620
    • (2006) Oncogene , vol.25 , pp. 3613-3620
    • Hao, B.1    Miao, X.2    Li, Y.3    Zhang, X.4    Sun, T.5    Liang, G.6    Zhao, Y.7    Zhou, Y.8    Wang, H.9    Chen, X.10
  • 28
    • 0036231641 scopus 로고    scopus 로고
    • ATP-dependent DNA ligases
    • REVIEWS 3005
    • Martin I.V., and MacNeill S.A. ATP-dependent DNA ligases. Genome Biol. 3 (2002) REVIEWS 3005
    • (2002) Genome Biol. , vol.3
    • Martin, I.V.1    MacNeill, S.A.2
  • 30
    • 0034610276 scopus 로고    scopus 로고
    • Mutation of a BRCT domain selectively disrupts DNA single-strand break repair in noncycling Chinese hamster ovary cells
    • Moore D.J., Taylor R.M., Clements P., and Caldecott K.W. Mutation of a BRCT domain selectively disrupts DNA single-strand break repair in noncycling Chinese hamster ovary cells. Proc. Natl. Acad. Sci. USA 97 (2000) 13649-13654
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 13649-13654
    • Moore, D.J.1    Taylor, R.M.2    Clements, P.3    Caldecott, K.W.4
  • 31
    • 0022341621 scopus 로고
    • Analysis of the structure and spatial distribution of ultraviolet-induced DNA repair patches in human cells made in the presence of inhibitors of replicative synthesis
    • Mullenders L.H., van Kesteren-van Leeuwen A.C., van Zeeland A.A., and Natarajan A.T. Analysis of the structure and spatial distribution of ultraviolet-induced DNA repair patches in human cells made in the presence of inhibitors of replicative synthesis. Biochim. Biophys. Acta 826 (1985) 38-48
    • (1985) Biochim. Biophys. Acta , vol.826 , pp. 38-48
    • Mullenders, L.H.1    van Kesteren-van Leeuwen, A.C.2    van Zeeland, A.A.3    Natarajan, A.T.4
  • 32
    • 0030941295 scopus 로고    scopus 로고
    • XRCC1 protein interacts with one of two distinct forms of DNA ligase III
    • Nash R.A., Caldecott K.W., Barnes D.E., and Lindahl T. XRCC1 protein interacts with one of two distinct forms of DNA ligase III. Biochemistry 36 (1997) 5207-5211
    • (1997) Biochemistry , vol.36 , pp. 5207-5211
    • Nash, R.A.1    Caldecott, K.W.2    Barnes, D.E.3    Lindahl, T.4
  • 33
    • 0028826450 scopus 로고
    • Comet assay analysis of repair of DNA strand breaks in normal and deficient human cells exposed to radiations and chemicals. Evidence for a repair pathway specificity of DNA ligation
    • Nocentini S. Comet assay analysis of repair of DNA strand breaks in normal and deficient human cells exposed to radiations and chemicals. Evidence for a repair pathway specificity of DNA ligation. Radiat. Res. 144 (1995) 170-180
    • (1995) Radiat. Res. , vol.144 , pp. 170-180
    • Nocentini, S.1
  • 34
    • 0033064056 scopus 로고    scopus 로고
    • Rejoining kinetics of DNA single- and double-strand breaks in normal and DNA ligase-deficient cells after exposure to ultraviolet C and gamma radiation: an evaluation of ligating activities involved in different DNA repair processes
    • Nocentini S. Rejoining kinetics of DNA single- and double-strand breaks in normal and DNA ligase-deficient cells after exposure to ultraviolet C and gamma radiation: an evaluation of ligating activities involved in different DNA repair processes. Radiat. Res. 151 (1999) 423-432
    • (1999) Radiat. Res. , vol.151 , pp. 423-432
    • Nocentini, S.1
  • 35
    • 33744789415 scopus 로고    scopus 로고
    • The Y-family DNA polymerase kappa (pol kappa) functions in mammalian nucleotide-excision repair
    • Ogi T., and Lehmann A.R. The Y-family DNA polymerase kappa (pol kappa) functions in mammalian nucleotide-excision repair. Nat. Cell Biol. 6 (2006) 640-642
    • (2006) Nat. Cell Biol. , vol.6 , pp. 640-642
    • Ogi, T.1    Lehmann, A.R.2
  • 36
    • 0034693220 scopus 로고    scopus 로고
    • Cellular responses and repair of single-strand breaks introduced by UV damage endonuclease in mammalian cells
    • Okano S., Kanno S., Nakajima S., and Yasui A. Cellular responses and repair of single-strand breaks introduced by UV damage endonuclease in mammalian cells. J. Biol. Chem. 275 (2000) 32635-32641
    • (2000) J. Biol. Chem. , vol.275 , pp. 32635-32641
    • Okano, S.1    Kanno, S.2    Nakajima, S.3    Yasui, A.4
  • 37
    • 0038583869 scopus 로고    scopus 로고
    • Spatial and temporal cellular responses to single-strand breaks in human cells
    • Okano S., Lan L., Caldecott K.W., Mori T., and Yasui A. Spatial and temporal cellular responses to single-strand breaks in human cells. Mol. Cell. Biol. 11 (2003) 3974-3981
    • (2003) Mol. Cell. Biol. , vol.11 , pp. 3974-3981
    • Okano, S.1    Lan, L.2    Caldecott, K.W.3    Mori, T.4    Yasui, A.5
  • 38
    • 33646589977 scopus 로고    scopus 로고
    • Early embryonic lethality due to targeted inactivation of DNA ligase III
    • Puebla-Osorio N., Lacey D.B., Alt F.W., and Zhu C. Early embryonic lethality due to targeted inactivation of DNA ligase III. Mol. Cell. Biol. 10 (2006) 3935-3941
    • (2006) Mol. Cell. Biol. , vol.10 , pp. 3935-3941
    • Puebla-Osorio, N.1    Lacey, D.B.2    Alt, F.W.3    Zhu, C.4
  • 39
    • 0028047308 scopus 로고
    • Aberrant DNA repair and DNA replication due to an inherited enzymatic defect in human DNA ligase I
    • Prigent C., Satoh M.S., Daly G., Barnes D.E., and Lindahl T. Aberrant DNA repair and DNA replication due to an inherited enzymatic defect in human DNA ligase I. Mol. Cell. Biol. 14 (1994) 310-317
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 310-317
    • Prigent, C.1    Satoh, M.S.2    Daly, G.3    Barnes, D.E.4    Lindahl, T.5
  • 40
    • 0141753120 scopus 로고    scopus 로고
    • The comings and goings of nucleotide excision repair factors on damaged DNA
    • Riedl T., Hanaoka F., and Egly J.M. The comings and goings of nucleotide excision repair factors on damaged DNA. EMBO J. 19 (2003) 5293-5303
    • (2003) EMBO J. , vol.19 , pp. 5293-5303
    • Riedl, T.1    Hanaoka, F.2    Egly, J.M.3
  • 41
    • 0033569961 scopus 로고    scopus 로고
    • The replication factory targeting sequence/PCNA-binding site is required in G(1) to control the phosphorylation status of DNA ligase I
    • Rossi R., Villa A., Negri C., Scovassi I., Ciarrocchi G., Biamonti G., and Montecucco A. The replication factory targeting sequence/PCNA-binding site is required in G(1) to control the phosphorylation status of DNA ligase I. EMBO J. 18 (1999) 5745-5754
    • (1999) EMBO J. , vol.18 , pp. 5745-5754
    • Rossi, R.1    Villa, A.2    Negri, C.3    Scovassi, I.4    Ciarrocchi, G.5    Biamonti, G.6    Montecucco, A.7
  • 42
    • 0027318778 scopus 로고
    • DNA excision-repair defect of xeroderma pigmentosum prevents removal of a class of oxygen free radical-induced base lesions
    • Satoh M.S., Jones C.J., Wood R.D., and Lindahl T. DNA excision-repair defect of xeroderma pigmentosum prevents removal of a class of oxygen free radical-induced base lesions. Proc. Natl. Acad. Sci. USA 13 (1993) 6335-6339
    • (1993) Proc. Natl. Acad. Sci. USA , vol.13 , pp. 6335-6339
    • Satoh, M.S.1    Jones, C.J.2    Wood, R.D.3    Lindahl, T.4
  • 43
  • 44
    • 0028965151 scopus 로고
    • Nucleotide excision repair DNA synthesis by DNA polymerase epsilon in the presence of PCNA, RFC, and RPA
    • Shivji M.K., Podust V.N., Hubscher U., and Wood R.D. Nucleotide excision repair DNA synthesis by DNA polymerase epsilon in the presence of PCNA, RFC, and RPA. Biochemistry 15 (1995) 5011-5017
    • (1995) Biochemistry , vol.15 , pp. 5011-5017
    • Shivji, M.K.1    Podust, V.N.2    Hubscher, U.3    Wood, R.D.4
  • 45
    • 0021341569 scopus 로고
    • Nature of DNA repair synthesis resistant to inhibitors of polymerase alpha in human cells
    • Smith C.A., and Okumoto D.S. Nature of DNA repair synthesis resistant to inhibitors of polymerase alpha in human cells. Biochemistry 23 (1984) 1383-1391
    • (1984) Biochemistry , vol.23 , pp. 1383-1391
    • Smith, C.A.1    Okumoto, D.S.2
  • 46
    • 0032537747 scopus 로고    scopus 로고
    • Role of BRCT domain in the interaction of DNA Ligase III-alpha with the DNA repair protein XRCC1
    • Taylor R.M., Wickstead B., Cronin S., and Caldecott K.W. Role of BRCT domain in the interaction of DNA Ligase III-alpha with the DNA repair protein XRCC1. Curr. Biol. 15 (1998) 877-880
    • (1998) Curr. Biol. , vol.15 , pp. 877-880
    • Taylor, R.M.1    Wickstead, B.2    Cronin, S.3    Caldecott, K.W.4
  • 47
    • 0020681852 scopus 로고
    • Multiple hypersensitivity to mutagens in a cell strain (46BR) derived from a patient with immuno-deficiencies
    • Teo I.A., Arlett C.F., Harcourt S.A., Priestley A., and Broughton B.C. Multiple hypersensitivity to mutagens in a cell strain (46BR) derived from a patient with immuno-deficiencies. Mutat. Res. 107 (1983) 371-386
    • (1983) Mutat. Res. , vol.107 , pp. 371-386
    • Teo, I.A.1    Arlett, C.F.2    Harcourt, S.A.3    Priestley, A.4    Broughton, B.C.5
  • 48
    • 0031260117 scopus 로고    scopus 로고
    • Mammalian DNA ligases
    • Tomkinson A.E., and Levin D.S. Mammalian DNA ligases. Bioessays 10 (1997) 893-901
    • (1997) Bioessays , vol.10 , pp. 893-901
    • Tomkinson, A.E.1    Levin, D.S.2
  • 49
    • 0028985014 scopus 로고
    • Transcription-coupled repair removes both cyclobutane pyrimidine dimers and 6-4-photoproducts with equal efficiency and in a sequential way from transcribed DNA in xeroderma-pigmentosum group-C fibroblasts
    • Van Hoffen A., Venema J., Meschini R., Van Zeeland A.A., and Mullenders L.H.F. Transcription-coupled repair removes both cyclobutane pyrimidine dimers and 6-4-photoproducts with equal efficiency and in a sequential way from transcribed DNA in xeroderma-pigmentosum group-C fibroblasts. EMBO J. 14 (1995) 360-367
    • (1995) EMBO J. , vol.14 , pp. 360-367
    • Van Hoffen, A.1    Venema, J.2    Meschini, R.3    Van Zeeland, A.A.4    Mullenders, L.H.F.5
  • 50
    • 33645228027 scopus 로고    scopus 로고
    • A new monoclonal antibody against DNA ligase I is a suitable marker of cell proliferation in cultured cell and tissue section samples
    • Vitolo B., Lidonnici M.R., Montecucco C., and Montecucco A. A new monoclonal antibody against DNA ligase I is a suitable marker of cell proliferation in cultured cell and tissue section samples. Eur. J. Histochem. 49 (2005) 349-354
    • (2005) Eur. J. Histochem. , vol.49 , pp. 349-354
    • Vitolo, B.1    Lidonnici, M.R.2    Montecucco, C.3    Montecucco, A.4
  • 52
    • 0026651211 scopus 로고
    • A Chinese hamster ovary cell mutant (EM-C11) with sensitivity to simple alkylating agents and a very high level of sister chomatid exchanges
    • Zdzienicka M.Z., van der Schans G.P., Natarajan A.T., Thompson L.H., Neuteboom I., and Simons J.W. A Chinese hamster ovary cell mutant (EM-C11) with sensitivity to simple alkylating agents and a very high level of sister chomatid exchanges. Mutagenesis 7 (1992) 265-269
    • (1992) Mutagenesis , vol.7 , pp. 265-269
    • Zdzienicka, M.Z.1    van der Schans, G.P.2    Natarajan, A.T.3    Thompson, L.H.4    Neuteboom, I.5    Simons, J.W.6


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