The DOI matches its Crossref record; 40 of the 40 references it cites were found in a registry or an index.
Preferential Incorporation of G Opposite Template T by the Low-Fidelity Human DNA Polymerase ι
Open accessAbstract
DNA polymerase activity is essential for replication, recombination, repair, and mutagenesis. All DNA polymerases studied so far from any biological source synthesize DNA by the Watson-Crick base-pairing rule, incorporating A, G, C, and T opposite the templates T, C, G, and A, respectively. Non-Watson-Crick base pairs would lead to mutations. In this report, we describe the ninth human DNA polymerase, Pol(iota), encoded by the RAD30B gene. We show that human Pol(iota) violates the Watson-Crick base-pairing rule opposite template T. During base selection, human Pol(iota) preferred T-G base pairing, leading to G incorporation opposite template T. The resulting T-G base pair was less efficiently extended by human Pol(iota) compared to the Watson-Crick base pairs. Consequently, DNA synthesis frequently aborted opposite template T, a property we designated the T stop. This T stop restricted human Pol(iota) to a very short stretch of DNA synthesis. Furthermore, kinetic analyses show that human Pol(iota) copies template C with extraordinarily low fidelity, misincorporating T, A, and C with unprecedented frequencies of 1/9, 1/10, and 1/11, respectively. Human Pol(iota) incorporated one nucleotide opposite a template abasic site more efficiently than opposite a template T, suggesting a role for human Pol(iota) in DNA lesion bypass. The unique features of preferential G incorporation opposite template T and T stop suggest that DNA Pol(iota) may additionally play a specialized function in human biology.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
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?
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 [13]
Citations
Cites
Genetical Implications of the Structure of Deoxyribonucleic Acid
Watson, J. D., & Crick, F. H. C. (1953) · Nature · doi:10.1038/171964b0 · Cited by 2,196
Genetical Implications of the Structure of Deoxyribonucleic Acid
Watson, J. D., & Crick, F. H. C. (2017) · Klassische Texte der Wissenschaft · doi:10.1007/978-3-662-47150-0_5 · Cited by 1,310
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
Kubota, Y., Nash, R. A., Klungland, A., Schär, P., Barnes, D. E., & Lindahl, T. L. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb01056.x · Cited by 776
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
Deoxycytidyl transferase activity of yeast REV1 protein
Nelson, J. R., Lawrence, C. W., & Hinkle, D. C. (1996) · Nature · doi:10.1038/382729a0 · Cited by 583
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
The 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
Flagged first, then by citations
Research works printed but not linked: 3
- Insel R. A., 1998, Curr. Top. Microbiol. Immunol., 229, 33
- Kornberg A., DNA replication
- Washington M. T., 2000, Proc. Natl. Acad. Sci. USA, 97, 3094
Cited by
Sorted by citations
Items 101–200 of 200
Mutagenic and Nonmutagenic Bypass of DNA Lesions byDrosophila DNA Polymerases dpolη and dpolι
Ishikawa, T., Uematsu, N., Mizukoshi, T., Iwai, S., Iwasaki, H., Masutani, C., Hanaoka, F., Ueda, R., Ohmori, H., & Todo, T. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m009822200 · Cited by 37
Dieckman, L. M., Johnson, R. E., Prakash, S., & Washington, M. (2010) · Biochemistry · doi:10.1021/bi100556m · Cited by 37
Sherrer, S. M., Fiala, K. A., Fowler, J. D., Newmister, S. A., Pryor, J. M., & Suo, Z. (2010) · Nucleic Acids Research · doi:10.1093/nar/gkq719 · Cited by 36
The Base Substitution Fidelity of DNA Polymerase β-dependent Single Nucleotide Base Excision Repair
Matsuda, T., Vande Berg, B. J., Bebenek, K., Osheroff, W. P., Wilson, S. H., & Kunkel, T. A. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.c300170200 · Cited by 35
Carlson, K. D., Johnson, R. E., Prakash, L., Prakash, S., & Washington, M. T. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0605785103 · Cited by 35
Structure and function relationships in mammalian DNA polymerases
Hoitsma, N. M., Whitaker, A. M., Schaich, M. A., Smith, M. R., Fairlamb, M. S., & Freudenthal, B. (2019) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-019-03368-y · Cited by 37
Johnson, R. E., Haracska, L., Prakash, L., & Prakash, S. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.00851-06 · Cited by 35
Structure of human DNA polymerase iota and the mechanism of DNA synthesis
Makarova, А. V., & Kulbachinskiy, A. V. (2012) · Biochemistry (Moscow) · doi:10.1134/s0006297912060016 · Cited by 33
The role of DNA polymerase ι in UV mutational spectra
Choi, J., Nia, A. B., Lee, D.-H., Lee, C.-S., & Pfeifer, G. P. (2006) · Mutation research. Fundamental and molecular mechanisms of mutagenesis · doi:10.1016/j.mrfmmm.2006.01.003 · Cited by 33
Lee, G., Nishimori, H., Sasaki, Y., Matsushita, H., Kitagawa, T., & Tokino, T. (2003) · Oncogene · doi:10.1038/sj.onc.1206387 · Cited by 32
Non-bulky Lesions in Human DNA: The Ways of Formation, Repair, and Replication
Ignatov, А. V., Bondarenko, K. A., & Makarova, A. V. (2017) · Acta Naturae · doi:10.32607/20758251-2017-9-3-12-26 · Cited by 31
Hang, B., Chenna, A., Guliaev, A. B., & Singer, B. (2003) · Mutation research. Fundamental and molecular mechanisms of mutagenesis · doi:10.1016/j.mrfmmm.2003.07.006 · Cited by 31
Mechanisms of direct replication restart at stressed replisomes
Conti, B. A., & Smogorzewska, A. (2020) · DNA repair · doi:10.1016/j.dnarep.2020.102947 · Cited by 34
Vaisman, A., Lehmann, A. R., & Woodgate, R. (2004) · Advances in protein chemistry · doi:10.1016/s0065-3233(04)69007-3 · Cited by 30
Taggart, D. J., Fredrickson, S. W., Gadkari, V. V., & Suo, Z. (2014) · Chemical Research in Toxicology · doi:10.1021/tx500088e · Cited by 26
Choi, J., Lim, S., Eoff, R. L., & Guengerich, F. P. (2009) · Journal of Molecular Biology · doi:10.1016/j.jmb.2009.04.023 · Cited by 28
Vaisman, A., Takasawa, K., Iwai, S., & Woodgate, R. (2005) · DNA repair · doi:10.1016/j.dnarep.2005.09.011 · Cited by 28
Inaccurate DNA Synthesis in Cell Extracts of Yeast Producing Active Human DNA Polymerase Iota
Makarova, А. V., Grabow, C. E., Gening, L. V., Tarantul, V. Z., Tahirov, T. H., Bessho, T., & Pavlov, Y. I. (2011) · PLoS ONE · doi:10.1371/journal.pone.0016612 · Cited by 27
Sez4 gene encoding an elongation subunit of DNA polymerase ζ is required for normal embryogenesis
Kajiwara, K., Wang, J. O., Sakurai, T., Yamashita, S., Tanaka, M., Sato, M., Tagawa, M., Sugaya, E., Nakamura, K., Nakao, K., et al. (2001) · Genes to Cells · doi:10.1046/j.1365-2443.2001.00410.x · Cited by 26
Ohm‐Laursen, L., & Barington, T. (2007) · The Journal of Immunology · doi:10.4049/jimmunol.178.7.4322 · Cited by 25
Yadav, S., Mukhopadhyay, S., Anbalagan, M., & Makridakis, N. M. (2015) · Human Mutation · doi:10.1002/humu.22820 · Cited by 23
A strategy for the expression of recombinant proteins traditionally hard to purify
Frank, E. G., McDonald, J. P., Karata, K., Huston, D., & Woodgate, R. (2012) · Analytical Biochemistry · doi:10.1016/j.ab.2012.07.016 · Cited by 24
Replication across Template T/U by Human DNA Polymerase-ι
Jain, R., Nair, D. T., Johnson, R. E., Prakash, L., Prakash, S., & Aggarwal, A. K. (2009) · Structure · doi:10.1016/j.str.2009.04.011 · Cited by 22
Bypass of a Psoralen DNA Interstrand Cross-Link by DNA Polymerases β, ι, and κ in Vitro
Smith, L. A., Makarova, А. V., Samson, L., Thiesen, K. E., Dhar, A., & Bessho, T. (2012) · Biochemistry · doi:10.1021/bi3008565 · Cited by 21
Biochemical reconstitution of UV-induced mutational processes
Sugiyama, T., & Chen, Y. (2019) · Nucleic Acids Research · doi:10.1093/nar/gkz335 · Cited by 21
Eukaryotic 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
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
Boldinova, E. O., Stojkovič, G., Khairullin, R. F., Wanrooij, S., & Makarova, А. V. (2017) · PLoS ONE · doi:10.1371/journal.pone.0184489 · Cited by 18
Donny-Clark, K., & Broyde, S. B. (2009) · Nucleic Acids Research · doi:10.1093/nar/gkp745 · Cited by 17
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
Suzuki, 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
A false note of DNA polymerase iota in the choir of genome caretakers in mammals
Gening, L. V., Makarova, А. V., Малашенко, А. М., & Tarantul, V. Z. (2006) · Biochemistry (Moscow) · doi:10.1134/s0006297906020064 · Cited by 17
Bhattacharya, P., Grigera, F., Rogozin, I. B., McCarty, T. C., Morse, H. C., & Kenter, A. L. (2007) · European Journal of Immunology · doi:10.1002/eji.200737664 · Cited by 16
Visions & Reflections¶Family growth: the eukaryotic DNA polymerase revolution
Bębenek, K., & Kunkel, T. A. (2002) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-002-8405-y · Cited by 16
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
In Silico Studies of the African Swine Fever Virus DNA Polymerase X Support an Induced-Fit Mechanism
Benitez, B. A. S., Arora, K., & Tamar Schlick, A. (2005) · Biophysical Journal · doi:10.1529/biophysj.105.071944 · 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
Bálint, É., & Unk, I. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms25010363 · 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
Determinants of adenine-mutagenesis in diversity-generating retroelements
Handa, S., Reyna, A., Wiryaman, T., & Ghosh, P. (2020) · Nucleic Acids Research · doi:10.1093/nar/gkaa1240 · Cited by 13
Sherrer, S. M., Taggart, D. J., Pack, L. R., Malik, C. K., Basu, A. K., & Suo, Z. (2012) · Mutation research. Fundamental and molecular mechanisms of mutagenesis · doi:10.1016/j.mrfmmm.2012.08.002 · Cited by 13
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
Chu, T., Li, R., Shao, M.-H., Ye, J.-Y., & Han, B. (2016) · Acta Pharmacologica Sinica · doi:10.1038/aps.2016.100 · Cited by 12
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
Langerak, P., Krijger, P. H. L., Heideman, M. R., van den Berk, P. C. M., & Jacobs, H. (2008) · Philosophical Transactions of the Royal Society B Biological Sciences · doi:10.1098/rstb.2008.0223 · Cited by 14
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
Controlled Expression of Recombinant Genes and Preparation of Cell-Free Extracts in Yeast
Wang, Z. (2005) · Humana Press eBooks · doi:10.1385/1-59259-958-3:317 · Cited by 11
Self-citationEffect of human cell malignancy on activity of DNA polymerase ι
Kazakov, A. A., Гришина, Е. Е., Tarantul, V. Z., & Gening, L. V. (2010) · Biochemistry (Moscow) · doi:10.1134/s0006297910070138 · Cited by 10
Perrino, F., Harvey, S., Blans, P., Gelhaus, S. L., LaCourse, W., & Fishbein, J. (2005) · Chemical Research in Toxicology · doi:10.1021/tx050114u · Cited by 9
Han, J. J., Bertin, N., Hao, T., Goldberg, D. S., Berriz, G. F., Zhang, L. V., Dupuy, D., Walhout, A. J. M., Cusick, M. E., Roth, F. P., et al. (2004) · Nature · doi:10.1038/nature02795 · 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
DNA 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
Repair of clustered damage and DNA polymerase iota
Belousova, E. A., & Lavrik, O. I. (2015) · Biochemistry (Moscow) · doi:10.1134/s0006297915080064 · Cited by 8
DNA 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
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
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
Cranford, M. T., Dahmen, S. N., Cortez, D., & Dewar, J. M. (2025) · Nucleic Acids Research · doi:10.1093/nar/gkaf975 · Cited by 6
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
Association between high activity of DNA polymerase iota and the development of human uveal melanoma
Gening, L. V., Гришина, Е. Е., Petrochenkov, A. N., & Tarantul, V. Z. (2006) · Russian Journal of Genetics · doi:10.1134/s1022795406010121 · Cited by 6
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
Ramadan, K., Maga, G., & Hübscher, U. (2006) · Springer eBooks · doi:10.1007/7050_005 · 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
Are There Mutator Polymerases?
García–Díaz, M., Ruiz, J. F., Juárez, R., Terrados, G., & Blanco, L. (2003) · The Scientific World JOURNAL · doi:10.1100/tsw.2003.32 · Cited by 4
Transient expression and activity of human DNA polymerase iota in loach embryos
Makarova, I. V., Kazakov, A. A., Makarova, А. V., Khaidarova, N. V., Kozikova, L. V., Nenasheva, V. V., Gening, L. V., Tarantul, V. Z., & Andreeva, L. E. (2011) · Biotechnology Letters · doi:10.1007/s10529-011-0764-8 · Cited by 4
Shilkin, E. S., Petrova, D. V., Poltorachenko, V. A., Boldinova, E. O., Zharkov, D. O., & Makarova, А. V. (2021) · Molecular Biology · doi:10.1134/s0026893321020138 · Cited by 4
Vaisman, 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
Translesion 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
Mechanism of Bypass Polymerases in Eukaryotes
Wang, Z. (2005) · doi:10.1201/9780849352683-32 · Cited by 3
Self-citationShilkin, E. S., Petrova, D. V., Poltorachenko, V. A., Boldinova, E. O., Zharkov, D. O., & Макарова, А. В. (2021) · Molecular Biology · doi:10.31857/s0026898421020130 · Cited by 3
DNA Damage Tolerance and Mutagenesis in Eukaryotic Cells
(2014) · ASM Press eBooks · doi:10.1128/9781555816704.ch17 · Cited by 3
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
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
Error-Prone and Error-Free Resolution of AID Lesions in SHM
Krijger, P. H. L., Storb, U., & Jacobs, H. (2010) · Modecular medicine and medicinal · doi:10.1142/9781848165939_0006 · Cited by 1
Recognition and Repair of Abasic Sites
Lowry, D. M. W. I. A. D. F. (2005) · doi:10.1201/9780849352683-25 · Cited by 1
“Mirror” Method to Estimate Mutagenic Activity of DNA Lesions
Gening, L. V., Shevchenko, O., Kazachenko, K., & Tarantul, V. Z. (2018) · Methods and Protocols · doi:10.3390/mps1030032 · 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
Kotapati, S. (2013) · University of Minnesota Digital Conservancy (University of Minnesota)
Highly Frequent Frameshift DNA Synthesis by Human
Zhang, Y., Wu, X., Yuan, F., Xie, Z., & Wang, Z. (2001)
Self-citationMolecular and Cellular Levels of Biological Evolution
Radman, M. (2005) · Kluwer Academic Publishers eBooks · doi:10.1007/0-306-48662-8_14
Determinants of Adenine-mutagenesis in Diversity-Generating RetroelementsPreprint
Handa, S., Reyna, A., Wiryaman, T., & Ghosh, P. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.04.29.068544
Formation, Degradation, and Bypass of DNA-Protein Crosslinks
Sedgeman, C. A. (2018)
Determinants of adenine-mutagenesis in diversity-generating retroelements.
Handa, S., Reyna, A., Wiryaman, T., & Ghosh, P. (2021) · eScholarship (California Digital Library)
Structural insights into DNA replication and lesion bypass by Y family DNA polymerases
Kirouac, K. N. (2010) · Scholarship@Western (Western University)
Recognition and Repair of Abasic Sites
Lowry, D. M. W. I. A. D. F., & Wilson, D. M. (2005) · CRC Press eBooks · doi:10.1201/9780849352683.ch19
Mechanism of Bypass Polymerases in Eukaryotes
Wang, Z. (2005) · CRC Press eBooks · doi:10.1201/9780849352683.ch24
Self-citationCaractérisation fonctionnelle de la tolérance aux endommagements de l’ADN des embryons précoces
Furno, E. L. (2019) · theses.fr (ABES) · doi:10.70675/cf32bcd5z3031z4693z8b1bz62fe76673ccc
Regulation of the DNA polymerase zeta in response to genotoxic stress in mammalian cells
Goulas, J. (2025) · theses.fr (ABES) · doi:10.70675/7894ebf5zbdf7z4147z940ezc553e0ed0e18
Metadata
- Authors
- Zhang, Y., Yuan, F., Wu, X., & Wang, Z.
- Affiliations
- University of Kentucky (US)
- Graduate Center for Toxicology, University of Kentucky, Lexington, Kentucky 40536
- Venue
- Molecular and Cellular Biology
- Publisher
- Informa UK Limited
- Published
- 2000-10-15
- Volume
- 20
- Issue
- 19
- Pages
- 7099-7108
- ISSN
- 0270-7306 (ISSN-L)
- 1098-5549
- PMC
- PMC86254
- OpenAlex
- W2120072997
- Cited by
- 200
- References
- 40
- Citations by year
- 2025: 2 · 2024: 1 · 2023: 2 · 2022: 1 · 2021: 5 · 2020: 4 · 2019: 6 · 2018: 3 · 2017: 5 · 2016: 3 · 2015: 6 · 2014: 7 · 2013: 6 · 2012: 11
- FWCI
- 6.38
- Type
- journal article
- Language
- en
- Open access
- green
- europepmc.org
- Locations
- Molecular and Cellular Biology (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Burroughs Wellcome Fund
- University of Kentucky
- Francis Crick Institute
- 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
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Molecular Research
- Keywords
- DNA polymerase iota, Poli, non-Watson-Crick base pairing, base selection, DNA damage bypass, DNA replication, mutagenesis
- MeSH terms
- DNA Polymerase iota, DNA-Directed DNA Polymerase, DNA Replication, Genetic Code, Guanosine Triphosphate, Humans, Kinetics, Substrate Specificity, Templates, Genetic, Thymine Nucleotides, Mutagenesis, Base Pairing
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