The DOI matches its Crossref record; 67 of the 68 references it cites were found in a registry or an index.
polι, a remarkably error-prone human DNA polymerase
Open accessAbstract
The Saccharomyces cerevisiae RAD30 gene encodes DNA polymerase η. Humans possess two Rad30 homologs. One ( RAD30A/POLH ) has previously been characterized and shown to be defective in humans with the Xeroderma pigmentosum variant phenotype. Here, we report experiments demonstrating that the second human homolog ( RAD30B ), also encodes a novel DNA polymerase that we designate polι. polι, is a distributive enzyme that is highly error-prone when replicating undamaged DNA. At template G or C, the average error frequency was ∼1 × 10 −2 . Our studies revealed, however, a striking asymmetry in misincorporation frequency at template A and T. For example, template A was replicated with the greatest accuracy, with misincorporation of G, A, or C occurring with a frequency of ∼1 × 10 −4 to 2 × 10 −4 . In dramatic contrast, most errors occurred at template T, where the misincorporation of G was, in fact, favored ∼3:1 over the correct nucleotide, A, and misincorporation of T occurred at a frequency of ∼6.7 × 10 −1 . These findings demonstrate that polι is one of the most error-prone eukaryotic polymerases reported to date and exhibits an unusual misincorporation spectrum in vitro.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
The cited source doesn’t support the claim as written.
In the citing paper
“The most striking violation of Watson-Crick base pairing rules is exhibited by Pol , which inserts dGTP opposite template T even more efficiently than it inserts A opposite T (12-14), i.e. its error rate for this mispair approaches 1 (Fig. 1).”
From DNA Replication Fidelity (2004) · cites this paper as [12]
Checked by a reasoning model — may be wrong.
Experimental — accuracy not yet measured
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
The Genome Sequence of Drosophila melanogaster
Adams, M. D., Celniker, S., Holt, R. A., Evans, C. A., Gocayne, J. D., Amanatides, P. G., Scherer, S. E., Li, P. W., Hoskins, R. A., Galle, R. F., et al. (2000) · Science · doi:10.1126/science.287.5461.2185 · Cited by 5,902
The XPV (xeroderma pigmentosum variant) gene encodes human DNA polymerase η
Masutani, C., Kusumoto, R., Yamada, A., Dohmae, N., Yokoi, M., Yuasa, M., Araki, M., Iwai, S., Takio, K., & Hanaoka, F. (1999) · Nature · doi:10.1038/21447 · Cited by 1,292
Efficient Bypass of a Thymine-Thymine Dimer by Yeast DNA Polymerase, Polη
Johnson, R. E., Prakash, S., & Prakash, L. (1999) · Science · doi:10.1126/science.283.5404.1001 · Cited by 736
hRAD30 Mutations in the Variant Form of Xeroderma Pigmentosum
Johnson, R. E., Kondratick, C. M., Prakash, S., & Prakash, L. (1999) · Science · doi:10.1126/science.285.5425.263 · Cited by 732
Thymine-Thymine Dimer Bypass by Yeast DNA Polymerase ζ
Nelson, J. R., Lawrence, C. W., & Hinkle, D. C. (1996) · Science · doi:10.1126/science.272.5268.1646 · Cited by 660
Kato, T., & Shinoura, Y. (1977) · Molecular and General Genetics MGG · doi:10.1007/bf00283484 · Cited by 569
UmuD′ 2 C is an error-prone DNA polymerase, Escherichia coli pol V
Tang, M., Shen, X., Frank, E. G., O’Donnell, M. E., Woodgate, R., & Goodman, M. F. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.16.8919 · Cited by 537
Self-citationThe dinB Gene Encodes a Novel E. coli DNA Polymerase, DNA Pol IV, Involved in Mutagenesis
Wagner, J. E., Grúz, P., Kim, S.-R., Yamada, M., Matsui, K., Fuchs, R. P., & Nohmi, T. (1999) · Molecular Cell · doi:10.1016/s1097-2765(00)80376-7 · Cited by 474
Roles of E. coli DNA polymerases IV and V in lesion-targeted and untargeted SOS mutagenesis
Tang, M., Pham, P., Shen, X., Taylor, J.-S., O'Donnell, M., Woodgate, R., & Goodman, M. F. (2000) · Nature · doi:10.1038/35010020 · Cited by 443
Self-citationMasutani, C., Araki, M., Yamada, A., Kusumoto, R., Nogimori, T., Maekawa, T., Iwai, S., & Hanaoka, F. (1999) · The EMBO Journal · doi:10.1093/emboj/18.12.3491 · Cited by 434
Cited by
Sorted by citations
Items 201–300 of 316
Replication across Regioisomeric Ethylated Thymidine Lesions by Purified DNA Polymerases
Andersen, N., Wang, P., & Wang, Y. (2013) · Chemical Research in Toxicology · doi:10.1021/tx4002995 · Cited by 20
Mechanistic Studies with DNA Polymerases Reveal Complex Outcomes following Bypass of DNA Damage
Eoff, R. L., Choi, J., & Guengerich, F. P. (2010) · Journal of Nucleic Acids · doi:10.4061/2010/830473 · Cited by 20
“Indeed, the misregulation of their activity is believed to participate in mutagenic events and antagonistic pleiotropy associated with tumorigenesis and aging because they do not possess exonuclease “proofreading” ability and they are generally more likely to make mistakes on undamaged template DNA (Figure 2) [17–24].”
BackgroundPolymerase Bypass of N6-Deoxyadenosine Adducts Derived from Epoxide Metabolites of 1,3-Butadiene
Kotapati, S., Wickramaratne, S., Esades, A., Boldry, E. J., Dorr, D. Q., Pence, M. G., Guengerich, F. P., & Tretyakova, N. Y. (2015) · Chemical Research in Toxicology · doi:10.1021/acs.chemrestox.5b00166 · Cited by 21
Translesion DNA Synthesis and Carcinogenesis
Shilkin, E. S., Boldinova, E. O., Stolyarenko, A. D., Гончарова, Р. И., Chuprov‐Netochin, R. N., Khairullin, R. F., Smal, M. P., & Makarova, А. V. (2020) · Biochemistry (Moscow) · doi:10.1134/s0006297920040033 · Cited by 23
“An unusual property of Pol ι is prevalent incorpora tion of dGMP opposite thymine, uracil, and its deriva tives [12, 34, 35].”
BackgroundEukaryotic Y-Family Polymerases: A Biochemical and Structural Perspective
Pryor, J. M., Dieckman, L. M., Boehm, E. M., & Washington, M. T. (2013) · Nucleic acids and molecular biology · doi:10.1007/978-3-642-39796-7_4 · Cited by 20
Sun, H., Zou, S., Zhang, S., Liu, B., Meng, X., Li, X., Yu, J., Wu, J., & Zhou, J. (2015) · Europe PMC (PubMed Central) · Cited by 19
Maddukuri, L., Ketkar, A. D., Eddy, S., Zafar, M. K., & Eoff, R. L. (2014) · Nucleic Acids Research · doi:10.1093/nar/gku913 · Cited by 20
“is known to preferentially insert dGMP opposite template dT (72).”
BackgroundSakai, W. (2003) · DNA repair · doi:10.1016/s1568-7864(02)00223-9 · Cited by 19
Discrimination against the Cytosine Analog tC by Escherichia coli DNA Polymerase IV DinB
Walsh, J. M., Bouamaïed, I., Brown, T. P., Wilhelmsson, L. M., & Beuning, P. J. (2011) · Journal of Molecular Biology · doi:10.1016/j.jmb.2011.03.069 · Cited by 18
Donny-Clark, K., Shapiro, R., & Broyde, S. B. (2008) · Biochemistry · doi:10.1021/bi801283d · Cited by 18
Kotapati, S., Maddukuri, L., Wickramaratne, S., Seneviratne, U. I., Goggin, M. M., Pence, M. G., Villalta, P. W., Guengerich, F. P., Marnett, L. J., & Tretyakova, N. Y. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.396788 · Cited by 19
Bypass of Mutagenic O6-Carboxymethylguanine DNA Adducts by Human Y- and B-Family Polymerases
Räz, M. H., Dexter, H. R., Millington, C. L., van Loon, B., Williams, D. M., & Sturla, S. J. (2016) · Chemical Research in Toxicology · doi:10.1021/acs.chemrestox.6b00168 · Cited by 18
A new class of errant DNA polymerases provides candidates for somatic hypermutation
Tippin, B. L., & Goodman, M. F. (2001) · Philosophical Transactions of the Royal Society B Biological Sciences · doi:10.1098/rstb.2000.0747 · Cited by 18
Donny-Clark, K., & Broyde, S. B. (2009) · Nucleic Acids Research · doi:10.1093/nar/gkp745 · Cited by 17
Asymmetry of DNA replication and translesion synthesis of UV-induced thymine dimers
Cordeiro‐Stone, M., & Nikolaishvili‐Feinberg, N. (2002) · Mutation research. Fundamental and molecular mechanisms of mutagenesis · doi:10.1016/s0027-5107(02)00255-5 · Cited by 17
Eukaryotic error-prone DNA polymerases: The presumed roles in replication, repair, and mutagenesis
Krutyakov, V. M. (2006) · Molecular Biology · doi:10.1134/s0026893306010018 · Cited by 18
Transcription, β–like DNA polymerases and hypermutation
Reynaud, C., Frey, S., Aoufouchi, S., Faili, A., Bertocci, B., Dahan, A., Flatter, E., Delbos, F., Storck, S., Zober, C., et al. (2001) · Philosophical Transactions of the Royal Society B Biological Sciences · doi:10.1098/rstb.2000.0753 · Cited by 18
Insights into the cellular role of enigmatic DNA polymerase ι
Vidal, A. E., & Woodgate, R. (2009) · DNA repair · doi:10.1016/j.dnarep.2008.12.007 · Cited by 17
Self-citationSuzuki, M., Kino, K., Kawada, T., Morikawa, M., Kobayashi, T., & Miyazawa, H. (2015) · Chemical Research in Toxicology · doi:10.1021/acs.chemrestox.5b00114 · Cited by 17
Translesion DNA replication proteins as molecular targets for cancer prevention
Watson, N. B., Mukhopadhyay, S., & McGregor, W. G. (2005) · Cancer Letters · doi:10.1016/j.canlet.2005.10.013 · Cited by 16
DNA polymerases in immunity: profiting from errors
Storb, U. (2001) · Nature Immunology · doi:10.1038/88673 · Cited by 16
Yoon, J.-H., Hodge, R. P., Hackfeld, L. C., Park, J., Choudhury, J. R., Prakash, S., & Prakash, L. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra117.000962 · Cited by 15
Makarova, А. V., Ignatov, A., Miropolskaya, N., & Kulbachinskiy, A. V. (2014) · DNA repair · doi:10.1016/j.dnarep.2014.07.006 · Cited by 15
Inomata, Y., Abe, T., Tsuda, M., Takeda, S., & Hirota, K. (2021) · PLoS ONE · doi:10.1371/journal.pone.0252587 · Cited by 14
Chi, L. M., & Lam, S. L. (2008) · Biochemistry · doi:10.1021/bi8001456 · Cited by 15
Chi, L. M., & Lam, S. L. (2006) · FEBS Letters · doi:10.1016/j.febslet.2006.11.001 · Cited by 15
Posttranslational Regulation of Human DNA Polymerase ι
McIntyre, J., McLenigan, M. P., Frank, E. G., Dai, X., Yang, W., Wang, Y., & Woodgate, R. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.675769 · Cited by 15
Self-citationBálint, É., & Unk, I. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms25010363 · Cited by 14
Kumar, S., Lamarche, B. J., & Tsai, M. (2007) · Biochemistry · doi:10.1021/bi061501l · Cited by 14
“0× 10-4 (66) bypass of alkylated bases ( 67) bypass of thyminecis-syndimers (20, 68) bypass of pyrimidine (6-4) pyrimidone photoproduct ( 68) ASFV Pol X 3.”
BackgroundYoshioka, K., Matsuno, Y., Hyodo, M., & Fujimori, H. (2019) · Cancers · doi:10.3390/cancers11111643 · Cited by 14
Isolation and Characterization of High Affinity Aptamers Against DNA Polymerase Iota
Лахин, А. В., Kazakov, A. A., Makarova, А. V., Pavlov, Y. I., Efremova, A. S., Shram, S. I., Tarantul, V. Z., & Gening, L. V. (2012) · Nucleic Acid Therapeutics · doi:10.1089/nat.2011.0324 · Cited by 14
“The enzyme has unusual biochemical properties and is extremely error-prone (Kunkel et al., 2003; Tissier et al., 2000).”
Exclusion of Madh2, Madh4 , and Madh7 as candidates for the modifier of Min 2 ( Mom2 ) locus
Silverman, K. A., Koratkar, R., Siracusa, L. D., & Buchberg, A. M. (2003) · Mammalian Genome · doi:10.1007/s00335-002-2214-3 · Cited by 14
“We have also excluded ElaC ortholog 1 (ELAC1), a tumor suppressor gene involved in lung carcinogenesis (Yanaihara et al. 2001), as well as Polymerase iota (RAD30B; Poliota), a highly errorprone, low-fidelity DNA polymerase (Tissier et al. 2000).”
BackgroundBostian, A. C. L., & Eoff, R. L. (2016) · Chemical Research in Toxicology · doi:10.1021/acs.chemrestox.6b00255 · Cited by 14
Ultraviolet Radiation Carcinogenesis
Cleaver, J. E., Ortiz‐Urda, S., Gulhar, R., Arron, S. T., Brookes, L., & Mitchell, D. L. (2017) · Wiley eBooks · doi:10.1002/9781119000822.hfcm026 · Cited by 14
Starostenko, L. V., Rechkunova, N. I., Lebedeva, N. A., Kolbanovskiy, A., Geacintov, N. E., & Lavrik, O. I. (2014) · DNA repair · doi:10.1016/j.dnarep.2014.10.005 · Cited by 13
Identification of mucAB-like homologs on two IncT plasmids, R394 and Rts-1
Koch, W. H., de Henestrosa, A. R. F., & Woodgate, R. (2000) · Mutation research. Fundamental and molecular mechanisms of mutagenesis · doi:10.1016/s0027-5107(00)00134-2 · Cited by 13
Self-citationChen, Z., Xu, X., Harrison, J. K., & Gan, W. A. N. G. (2004) · Biochemical Journal · doi:10.1042/bj20031143 · Cited by 11
Stalling of Eukaryotic Translesion DNA Polymerases at DNA-Protein Cross-Links
Yudkina, A. V., Shilkin, E. S., Makarova, А. V., & Zharkov, D. O. (2022) · Genes · doi:10.3390/genes13020166 · Cited by 12
“hPOLι is a low-processivity DNA polymerase, typically incorporating 1–3 nucleotides per association [46].”
BackgroundHe, C. S., Wu, S., Gao, A., Su, Y., Min, H., Shang, Z., Wu, J., Yang, L., Ding, W., & Zhou, J. (2017) · Cancer Science · doi:10.1111/cas.13399 · Cited by 12
Kazachenko, K., Miropolskaya, N., Gening, L. V., Tarantul, V. Z., & Makarova, А. V. (2017) · DNA repair · doi:10.1016/j.dnarep.2017.01.001 · Cited by 12
DNA polymerase iota-like activity in crude cell extracts of different mouse organs
Gening, L. V., Petrochenkov, A. N., Reshetnyak, A. B., Андреева, Л. Е., & Tarantul, V. Z. (2009) · Biochemistry (Moscow) · doi:10.1134/s0006297909010192 · Cited by 12
Biochemical Evolution of DNA Polymerase η: Properties of Plant, Human, and Yeast Proteins
Hoffman, P. D., Curtis, M. J., Iwai, S., & Hays, J. B. (2008) · Biochemistry · doi:10.1021/bi701781p · Cited by 12
Louat, T., Servant, L., Rols, M., Bieth, A., Teissié, J., Hoffmann, J., & Cazaux, C. (2001) · Molecular Pharmacology · doi:10.1016/s0026-895x(24)12618-1 · Cited by 12
“, 2000), and Pol (Tissier et al., 2000) produce errors at high rates in copying undamaged DNA.”
BackgroundResponse of human DNA polymerase ι promoter to N-methyl-N′-nitro-N-nitrosoguanidine
Zhu, H., Fan, Y., Jiang, H., Shen, J., Qi, H., Mei, R., & Shao, J. (2009) · Environmental Toxicology and Pharmacology · doi:10.1016/j.etap.2009.11.001 · Cited by 12
Scaringe, W. A., Li, K., Gu, D., Hagman, K. D. F., Chen, Z., Hill, K. A., & Sommer, S. S. (2008) · Human Molecular Genetics · doi:10.1093/hmg/ddn190 · Cited by 11
Mysterious and fascinating: DNA polymerase ɩ remains enigmatic 20 years after its discovery
Vaisman, A., & Woodgate, R. (2020) · DNA repair · doi:10.1016/j.dnarep.2020.102914 · Cited by 10
Self-citationReplication, Repair, and Translesion Polymerase Bypass of N6-Oxopropenyl-2′-deoxyadenosine
Maddukuri, L., Shuck, S. C., Eoff, R. L., Zhao, L., Rizzo, C. J., Guengerich, F. P., & Marnett, L. J. (2013) · Biochemistry · doi:10.1021/bi401103k · Cited by 10
“However, all of the Y-family polymerases preferred insertion of dTTP opposite OPdA, and though it lost some accuracy relative to template dA, hPol κ (19-526) actually exhibited the greatest ability to select dTTP over mispairs when catalyzing insertion opposite OPdA, preferring dTTP ~1000-fold more than dCTP.”
BackgroundInfluentialPerrino, F., Harvey, S., Blans, P., Gelhaus, S. L., LaCourse, W., & Fishbein, J. (2005) · Chemical Research in Toxicology · doi:10.1021/tx050114u · Cited by 9
Alkyladenine DNA glycosylase (Aag) in somatic hypermutation and class switch recombination
Longerich, S., Meira, L. B., Shah, D., Samson, L. D., & Storb, U. (2007) · DNA repair · doi:10.1016/j.dnarep.2007.06.012 · Cited by 10
Taggart, D. J., Camerlengo, T., Harrison, J. K., Sherrer, S. M., Kshetry, A. K., Taylor, J., Huang, K., & Suo, Z. (2013) · Nucleic Acids Research · doi:10.1093/nar/gkt141 · Cited by 9
“This template sequence-bias of dNTP incorporation fidelity for hPoli has been predicted by kinetic assays (37).”
BackgroundDNA polymerase ι is acetylated in response to SN2 alkylating agents
McIntyre, J., Sobolewska, A., Fedorowicz, M., McLenigan, M. P., Macias, M., Woodgate, R., & Śledziewska-Gójska, E. (2019) · Scientific Reports · doi:10.1038/s41598-019-41249-3 · Cited by 9
Self-citationKetkar, A. D., Zafar, M. K., Banerjee, S., Márquez, V. E., Egli, M., & Eoff, R. L. (2012) · Journal of the American Chemical Society · doi:10.1021/ja304176q · Cited by 9
Poltoratsky, V. P., Horton, J. K., Prasad, R., Beard, W. A., Woodgate, R., & Wilson, S. H. (2008) · DNA repair · doi:10.1016/j.dnarep.2008.02.013 · Cited by 8
Self-citationDNA Polymerases and Mutagenesis in Human Cancers
Crespan, E., Amoroso, A., & Maga, G. (2009) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-90-481-3471-7_9 · Cited by 8
The pattern of somatic hypermutation of Ig genes is altered when p53 is inactivated
Ratnam, S., Bozek, G., Nicolae, D. L., & Storb, U. (2010) · Molecular Immunology · doi:10.1016/j.molimm.2010.05.291 · Cited by 8
DNA Polymerase Iota-Like Activity in Crude Cell Extracts of Different Mouse Organs
Gening, L. V., Petrochenkov, A. N., Reshetnyak, A. B., Андреева, Л. Е., & Tarantul, V. Z. (2004) · Biochemistry (Moscow) · doi:10.1023/b:biry.0000026201.71587.a2 · Cited by 8
Copy-Number Fluctuation by Unequal Crossing-Over in the Chicken Avidin Gene Family
Ahlroth, M. K., Ahlroth, P., & Kulomaa, M. S. (2001) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2001.5760 · Cited by 8
Martins, D. J., Singh, J. K., Jahjah, T., Vessoni, A. T., Leandro, G. D. S., Silva, M. M., Biard, D. S. F., Quinet, A., & Menck, C. F. M. (2023) · Photochemistry and Photobiology · doi:10.1111/php.13879 · Cited by 7
Лахин, А. В., Efremova, A. S., Makarova, I. V., Гришина, Е. Е., Shram, S. I., Tarantul, V. Z., & Gening, L. V. (2013) · Molecular Genetics Microbiology and Virology · doi:10.3103/s0891416813010035 · Cited by 7
129-Derived Mouse Strains Express an Unstable but Catalytically Active DNA Polymerase Iota Variant
Aoufouchi, S., Smet, A. D., Delbos, F., Gelot, C., Guerrera, I. C., Weill, J., & Reynaud, C. (2015) · Molecular and Cellular Biology · doi:10.1128/mcb.00371-15 · Cited by 7
Makarova, А. V., Gening, L. V., Makarova, I. V., & Tarantul, V. Z. (2008) · Russian Journal of Developmental Biology · doi:10.1134/s1062360408050068 · Cited by 7
Foley, M. C., & Tamar Schlick, A. (2009) · The Journal of Physical Chemistry B · doi:10.1021/jp903172x · Cited by 7
Zavilgelsky, G. B. (2013) · Molecular Biology · doi:10.1134/s0026893313050221 · Cited by 6
Evolution of DNA polymerase ι structure and function in eukaryotes
Makarova, А. V., Tarantul, V. Z., & Gening, L. V. (2008) · Biochemistry (Moscow) · doi:10.1134/s0006297908030176 · Cited by 6
Xie, P. (2011) · Theoretical Biology and Medical Modelling · doi:10.1186/1742-4682-8-22 · Cited by 6
DNA polymerase ι: The long and the short of it!
Frank, E. G., McLenigan, M. P., McDonald, J. P., Huston, D., Mead, S., & Woodgate, R. (2017) · DNA repair · doi:10.1016/j.dnarep.2017.08.006 · Cited by 6
Self-citationTranslesion Synthesis And Errorprone Polymerases
Green, C., & Lehmann, A. R. (2006) · Springer eBooks · doi:10.1007/1-4020-3764-3_7 · Cited by 6
Polymerase Switching in Response to DNA Damage
Ollivierre, J. N., Silva, M. C., Sefcikova, J., & Beuning, P. J. (2010) · Biological and medical physics series · doi:10.1007/978-0-387-92808-1_11 · Cited by 5
DNA polymerase ι of mammals as a participant in translesion synthesis of DNA
Gening, L. V. (2011) · Biochemistry (Moscow) · doi:10.1134/s0006297911010081 · Cited by 5
Manganese-induced infidelity of DNA synthesis as a possible cause of manganism
Лахин, А. В., Tarantul, V. Z., & Gening, L. V. (2014) · Molecular Genetics Microbiology and Virology · doi:10.3103/s0891416814010030 · Cited by 5
Ramadan, K., Maga, G., & Hübscher, U. (2006) · Springer eBooks · doi:10.1007/7050_005 · Cited by 5
Bryn Bridges and mutagenesis: exploring the intellectual space
Walker, G. C. (2001) · Mutation Research/DNA Repair · doi:10.1016/s0921-8777(00)00075-6 · Cited by 5
Somatic hypernnitation in human B cell subsets
Longo, N. S., & Lipsky, P. E. (2001) · Springer Seminars in Immunopathology · doi:10.1007/s281-001-8165-0 · Cited by 5
Frank, E. G., McDonald, J. P., Yang, W., & Woodgate, R. (2016) · DNA repair · doi:10.1016/j.dnarep.2016.12.004 · Cited by 4
Self-citationVaisman, A., McDonald, J. P., Smith, M. R., Aspelund, S. L., Evans, T. C., & Woodgate, R. (2021) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2021.778400 · Cited by 3
Self-citationTranslesion DNA Synthesis and Damage Tolerance Pathways
Masuda, Y., Hanaoka, F., & Masutani, C. (2016) · Springer eBooks · doi:10.1007/978-4-431-55873-6_11 · Cited by 3
DNA Polymerase and dRP-lyase activities of polymorphic variants of human Pol ι
Shilkin, E. S., Gromova, A. S., Smal, M. P., & Makarova, А. V. (2021) · Biochemical Journal · doi:10.1042/bcj20200491 · Cited by 3
DNA polymerases and carcinogenesis
Krutyakov, V. M., & Kravetskaya, T. P. (2010) · Biochemistry (Moscow) · doi:10.1134/s000629791008002x · Cited by 3
Mechanism of Bypass Polymerases in Eukaryotes
Wang, Z. (2005) · doi:10.1201/9780849352683-32 · Cited by 3
Cellular Responses to DNA Damage
Watson, N. B., & McGregor, W. G. (2010) · Elsevier eBooks · doi:10.1016/b978-0-08-046884-6.00221-9 · Cited by 3
Insights into the error bypass of 1-Nitropyrene DNA adduct by DNA polymerase ι: A QM/MM study
Li, Y., Bao, L., Zhang, R., Tang, X., Zhang, Q., & Wang, W. (2017) · Chemical Physics Letters · doi:10.1016/j.cplett.2017.08.017 · Cited by 3
Tiefenbach, T. E. (2011) · MacSphere (McMaster University) · doi:10.71548/16276 · Cited by 3
DNA Damage Tolerance and Mutagenesis in Eukaryotic Cells
(2014) · ASM Press eBooks · doi:10.1128/9781555816704.ch17 · Cited by 3
Ultraviolet Radiation Carcinogenesis
Cleaver, J. E., Ortiz‐Urda, S., & Arron, S. T. (2022) · Wiley eBooks · doi:10.1002/9781119000822.hfcm026.pub2 · Cited by 3
Hreusová, M., Brabec, V., & Nováková, O. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms221910838 · Cited by 2
Molecular mechanisms of DNA lesion and repair during antibody somatic hypermutation
Hao, Q., Li, J., & Yeap, L.-S. (2024) · Science China Life Sciences · doi:10.1007/s11427-024-2615-1 · Cited by 3
“In vitro studies have shown that Pol ι preferentially inserts a G instead of an A opposite T (Tissier et al., 2000; Zhang et al., 2000), potentially resulting in G to A and C to T transition mutations during SHM.”
REV1 inhibition enhances trinucleotide repeat mutagenesis
Siegel, A., Almstead, D., Kothandaraman, N., Reich, J., Lamkin, E. N., Victor, J., Grover, A., Ikeh, K., Koval, H., Crompton, A., et al. (2025) · Open Biology · doi:10.1098/rsob.250234 · Cited by 2
Moro, S. L., & Cocco, M. J. (2015) · Biomolecular NMR Assignments · doi:10.1007/s12104-015-9626-y · Cited by 2
“1999a, b), pol i (McDonald et al. 1999; Tissier et al. 2000), and Rev1 (Lin et al.”
BackgroundSelective Modulation of DNA Polymerase Activity by Fixed‐Conformation Nucleoside Analogues
Eoff, R. L., McGrath, C. E., Maddukuri, L., Salamanca-Pinzon, S. G., Márquez, V. E., Marnett, L. J., Guengerich, F. P., & Egli, M. (2010) · Angewandte Chemie · doi:10.1002/ange.201003168 · Cited by 2
Cellular Responses to DNA Damage
Klapacz, J., & Gollapudi, B. B. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-801238-3.95611-3 · Cited by 2
DNA damage tolerance in mammalian cells
Andersen, P. L. (2009) · University Library - University of Saskatchewan (University of Saskatchewan) · Cited by 2
The role of DNA polymerases, in particular DNA polymerase ε in DNA repair and replication
Pospiech, H. (2002) · Cited by 2
Masutani, C., & Hanaoka, F. (2018) · Springer eBooks · doi:10.1007/978-981-10-6722-8_12 · Cited by 1
Strauss, B. S. (2015) · Elsevier eBooks · doi:10.1016/b978-0-12-800892-8.00001-4 · Cited by 1
IMPLICATIONS FOR THERAPY Personalized Therapy of Cancer
Yamanaka, K., & Lloyd, R. (2013) · CRC Press eBooks · doi:10.1201/b14587-12 · Cited by 1
Enhanced Activity of DNA Polymerase Iota in Mouse Brain Cells Is Associated with Aggressiveness
Gening, L. V., Kamensky, A. A., Levitskaya, N. G., Petrochenkov, A. N., Полетаева, И. И., & Tarantul, V. Z. (2005) · Biochemistry (Moscow) · doi:10.1007/s10541-005-0240-y · Cited by 1
The Biology of Xeroderma Pigmentosum
Cleaver, J. E. (2007) · Humana Press eBooks · doi:10.1007/978-1-59259-994-3_16 · Cited by 1
Cleaver, J. E., Collins, C. C., Ellis, J., & Volik, S. V. (2003) · Genomics · doi:10.1016/s0888-7543(03)00180-0
DNA Damage Tolerance and Translesion Synthesis
Lehmann, A. R. (2009) · Springer eBooks · doi:10.1007/978-90-481-2561-6_10
“opposite a template T [139].”
Metadata
- Authors
- Tissier, A., McDonald, J. P., Frank, E. G., & Woodgate, R.
- Affiliations
- National Institutes of Health (US)
- Venue
- Genes & Development
- Publisher
- Cold Spring Harbor Laboratory
- Published
- 2000-07-01
- Volume
- 14
- Issue
- 13
- Pages
- 1642-1650
- ISSN
- 0890-9369 (ISSN-L)
- 1549-5477
- PMC
- PMC316739
- OpenAlex
- W1908705633
- Cited by
- 315
- References
- 68
- Citations by year
- 2026: 2 · 2025: 2 · 2024: 2 · 2023: 4 · 2022: 2 · 2021: 7 · 2020: 5 · 2019: 7 · 2018: 5 · 2017: 11 · 2016: 9 · 2015: 10 · 2014: 9 · 2013: 11 · 2012: 11
- Type
- posted content
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Genes & Development (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA and Nucleic Acid Chemistry
- Health Sciences › Medicine › Pathology and Forensic Medicine › Genetic factors in colorectal cancer
- Keywords
- DNA polymerase eta, error-prone DNA replication, xeroderma pigmentosum variant, Saccharomyces cerevisiae
- MeSH terms
- Base Sequence, DNA-Directed DNA Polymerase, Humans, Isoenzymes, Mutation, DNA Primers
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review