DNA Polymerases: Structural Diversity and Common Mechanisms

Crystal structure at 3.5 A resolution of HIV-1 reverse transcriptase complexed with an inhibitor

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Structure of a Covalently Trapped Catalytic Complex of HIV-1 Reverse Transcriptase: Implications for Drug Resistance

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Crystal structure of a bacteriophage T7 DNA replication complex at 2.2 Å resolution

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A general two-metal-ion mechanism for catalytic RNA

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Crystal structure of human immunodeficiency virus type 1 reverse transcriptase complexed with double-stranded DNA at 3.0 A resolution shows bent DNA

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Structural basis for the 3′‐5′ exonuclease activity of Escherichia coli DNA polymerase I: a two metal ion mechanism.

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Structure of large fragment of Escherichia coli DNA polymerase I complexed with dTMP

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STRUCTURES OF TERNARY COMPLEXES OF RAT DNA POLYMERASE BETA, A DNA TEMPLATE-PRIMER, AND DDCTP

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An attempt to unify the structure of polymerases

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FUNCTION AND STRUCTURE RELATIONSHIPS IN DNA POLYMERASES

Joyce, C. M., & Steitz, T. A. (1994) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.63.070194.004021 · Cited by 620

The translesion polymerase ζ has roles dependent and independent of the nuclease MUS81 and the helicase RECQ4A in DNA damage repair in Arabidopsis

Kobbe, S., Trapp, O., Knoll, A., Mannuß, A., & Puchta, H. (2015) · PLANT PHYSIOLOGY · doi:10.1104/pp.15.00806 · Cited by 14

Paeoniflorigenone purified from Paeonia daurica roots potently inhibits viral and bacterial DNA polymerases: investigation by experimental validation and docking simulation

Demi̇r, A., Turumtay, H., Emirik, M., Sandallı, C., Kanbolat, Ş., Özgen, U., & Turumtay, E. A. (2019) · Medicinal Chemistry Research · doi:10.1007/s00044-019-02449-8 · Cited by 14

Evidence for a Non-Catalytic Ion-Binding Site in Multiple RNA-Dependent RNA Polymerases

Mönttinen, H. A. M., Ravantti, J., & Poranen, M. M. (2012) · PLoS ONE · doi:10.1371/journal.pone.0040581 · Cited by 14

A deep phylogeny of viral and cellular right-hand polymerases

Černý, J., Bolfíková, B. Č., Zanotto, P. M. D. A., Grubhoffer, L., & Růžek, D. (2015) · Infection Genetics and Evolution · doi:10.1016/j.meegid.2015.09.026 · Cited by 16

Crystal Structure of the Apicoplast DNA Polymerase from Plasmodium falciparum: The First Look at a Plastidic A-Family DNA Polymerase

Milton, M. E., Choe, J., Honzatko, R. B., & Nelson, S. W. (2016) · Journal of Molecular Biology · doi:10.1016/j.jmb.2016.07.016 · Cited by 14

Mapping Functional Substrate–Enzyme Interactions in the pol β Active Site through Chemical Biology: Structural Responses to Acidity Modification of Incoming dNTPs

Batra, V. K., Oertell, K., Beard, W. A., Kashemirov, B. A., McKenna, C. E., Goodman, M. F., & Wilson, S. H. (2018) · Biochemistry · doi:10.1021/acs.biochem.8b00418 · Cited by 14

Nuclear Magnetic Ions of Magnesium, Calcium, and Zinc as a Powerful and Universal Means for Killing Cancer Cells

Kuznetsov, D. A., & Buchachenko, A. L. (2018) · Russian Journal of Physical Chemistry B · doi:10.1134/s1990793118040267 · Cited by 14

Catalytic mechanism of DNA polymerases—Two metal ions or three?

Tsai, M. (2018) · Protein Science · doi:10.1002/pro.3542 · Cited by 14

Optimized expression of large fragment DNA polymerase I from Geobacillus stearothermophilus in Escherichia coli expression system

Agustriana, E., Nuryana, I., Laksmi, F. A., Dewi, K. S., Wijaya, H., Rahmani, N., Yudiargo, D. R., Ismadara, A., Helbert, Hadi, M. I., et al. (2022) · Preparative Biochemistry & Biotechnology · doi:10.1080/10826068.2022.2095573 · Cited by 14

Effect of A and B Metal Ion Site Occupancy on Conformational Changes in an RB69 DNA Polymerase Ternary Complex

Wang, M., Lee, H. R., & Konigsberg, W. H. (2009) · Biochemistry · doi:10.1021/bi801627h · Cited by 14

Following an environmental carcinogen N2-dG adduct through replication: elucidating blockage and bypass in a high-fidelity DNA polymerase

Xu, P., Oum, L., Beese, L. S., Geacintov, N. E., & Broyde, S. B. (2007) · Nucleic Acids Research · doi:10.1093/nar/gkm416 · Cited by 14

A Transposon-Derived DNA Polymerase from Entamoeba histolytica Displays Intrinsic Strand Displacement, Processivity and Lesion Bypass

Pastor-Palacios, G., López-Ramírez, V., Cardona-Félix, C. S., & Brieba, L. G. (2012) · PLoS ONE · doi:10.1371/journal.pone.0049964 · Cited by 14

A Carboxylate Triad Is Essential for the Polymerase Activity ofEscherichia coli DNA Polymerase I (Klenow Fragment)

Gangurde, R., Kaushik, N., Singh, K., & Modak, M. J. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m002307200 · Cited by 14

The (I/Y)XGG Motif of Adenovirus DNA Polymerase Affects Template DNA Binding and the Transition from Initiation to Elongation

Brenkman, A. B., Heideman, M. R., Truniger, V., Salas, M., & van der Vliet, P. C. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m103159200 · Cited by 14

Enzymatic properties of rat DNA polymerase beta mutants obtained by randomized mutagenesis

Skandalis, A. (2001) · Nucleic Acids Research · doi:10.1093/nar/29.11.2418 · Cited by 14

Incorporation of non-nucleoside triphosphate analogues opposite to an abasic site by human DNA polymerases and

Crespan, E. (2005) · Nucleic Acids Research · doi:10.1093/nar/gki723 · Cited by 14

A High-Throughput Screening Method to Reengineer DNA Polymerases for Random Mutagenesis

Kardashliev, T., Ruff, A. J., Zhao, J. B., & Schwaneberg, U. (2013) · Molecular Biotechnology · doi:10.1007/s12033-013-9706-0 · Cited by 13

Influence of the Linkage between Leaving Group and Nucleoside on Substrate Efficiency for Incorporation in DNA Catalyzed by Reverse Transcriptase

Giraut, A., & Herdewijn, P. A. (2010) · ChemBioChem · doi:10.1002/cbic.201000128 · Cited by 13

A possible mechanism for the dynamics of transition between polymerase and exonuclease sites in a high-fidelity DNA polymerase

Xie, P. (2009) · Journal of Theoretical Biology · doi:10.1016/j.jtbi.2009.04.009 · Cited by 13

Impact of Amino Acid Substitutions in Region II and Helix K of Herpes Simplex Virus 1 and Human Cytomegalovirus DNA Polymerases on Resistance to Foscarnet

Zarrouk, K., Zhu, X., Phạm, V. D., Goyette, N., Piret, J., Shi, R., & Boivin, G. (2021) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.00390-21 · Cited by 13

LigD: A Structural Guide to the Multi-Tool of Bacterial Non-Homologous End Joining

Amare, B., Mo, A., Khan, N., Sowa, D. J., Warner, M. M., Tetenych, A., & Andres, S. N. (2021) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2021.787709 · Cited by 13

Mechanism of nucleotide discrimination by the translesion synthesis polymerase Rev1

Weaver, T., Click, T. H., Khoang, T. H., Washington, M. T., Agarwal, P. K., & Freudenthal, B. (2022) · Nature Communications · doi:10.1038/s41467-022-30577-0 · Cited by 13

DNA Polymerase I of Mycobacterium tuberculosis

Arrigo, C. J., Singh, K., & Modak, M. J. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m108536200 · Cited by 13

Amplification yield enhancement of short DNA templates using bulk and surface-attached amine-functionalized single-wall carbon nanotubes

Yüce, M., Uysal, E., & Budak, H. (2015) · Applied Surface Science · doi:10.1016/j.apsusc.2015.04.216 · Cited by 13

Structure of an open conformation of T7 DNA polymerase reveals novel structural features regulating primer-template stabilization at the polymerization active site

Juárez-Quintero, V., Peralta-Castro, A., Benítez‐Cardoza, C. G., Ellenberger, T., & Brieba, L. G. (2021) · Biochemical Journal · doi:10.1042/bcj20200922 · Cited by 13

Synthesis of Oligonucleotides Containing Thiazole and Thiazole N-Oxide Nucleobases

Miller, T. J., Farquar, H. D., Sheybani, A., Tallini, C. E., Saurage, A. S., Fronczek, F. R., & Hammer, R. P. (2002) · Organic Letters · doi:10.1021/ol017003g · Cited by 13

Unifying Themes in DNA Replication: Reconciling Single Molecule Kinetic Studies with Structural Data on DNA Polymerases

Goel, A., Ellenberger, T., Frank-Kamenetskii, M. D., & Herschbach, D. R. (2002) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2002.10506764 · Cited by 13

Phosphodiester Substrates for Incorporation of Nucleotides in DNA Using HIV‐1 Reverse Transcriptase

Giraut, A., Dyubankova, N., Song, X., & Herdewijn, P. A. (2009) · ChemBioChem · doi:10.1002/cbic.200900270 · Cited by 13

Error Frequencies of Picornavirus RNA Polymerases: Evolutionary Implications for Virus Populations

Domingo, E., Baranowski, É., Escarmı́s, C., Sobrino, F., & Holland, J. J. (2014) · ASM Press eBooks · doi:10.1128/9781555817916.ch23 · Cited by 12

Biochemical Analysis of Point Mutations in the 5′-3′ Exonuclease of DNA Polymerase I of Streptococcus pneumoniae

Amblar, M., de Lacoba, M. G., Corrales, M. A., & López, P. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m008678200 · Cited by 13

Synthesis, Reverse Transcription, Replication, and Inter-Transcription of 2′-Modified Nucleic Acids with Evolved Thermophilic Polymerases: Efforts toward Multidimensional Expansion of the Central Dogma

Qin, Y., Ma, X., Tao, R. X., Du, Y., & Chen, T. (2023) · ACS Synthetic Biology · doi:10.1021/acssynbio.3c00213 · Cited by 12

A wide survey of heavy metals-induced in-vitro DNA replication stress characterized by rate-limited replication

Ren, Q., Guo, X., Dong, Y., Zhao, C., Zhang, X., & Xia, X. (2024) · Current Research in Toxicology · doi:10.1016/j.crtox.2024.100152 · Cited by 12

What Is life? Rethinking Biology in Light of Fundamental Parameters

Fantini, J., Matveeva, M., Lefebvre, M., & Chahinian, H. (2024) · Life · doi:10.3390/life14030280 · Cited by 15

DNA Polymerases as targets for gene therapy of hepatocellular carcinoma

Liu, H., Wei, Q., Wang, J., Huang, X., Li, C., Zheng, Q., Cao, J., & Jia, Z. (2015) · BMC Cancer · doi:10.1186/s12885-015-1339-1 · Cited by 12

Regulation of Small Mitochondrial DNA Replicative Advantage by Ribonucleotide Reductase inSaccharomyces cerevisiae

Bradshaw, E., Yoshida, M., & Ling, F. (2017) · G3 Genes Genomes Genetics · doi:10.1534/g3.117.043851 · Cited by 12

When DNA Polymerases Multitask: Functions Beyond Nucleotidyl Transfer

Carvajal-Maldonado, D., Beckham, L. D., Wood, R. D., & Doublié, S. (2022) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2021.815845 · Cited by 11

Nano-RNases: oligo- or dinucleases?

Lee, V. T., Sondermann, H., & Winkler, W. C. (2022) · FEMS Microbiology Reviews · doi:10.1093/femsre/fuac038 · Cited by 12

Molecular characterization of a novel cryptic virus infecting pigeonpea plants

Kumar, S. B., Subbarao, B. L., Kumari, R., & Hallan, V. K. (2017) · PLoS ONE · doi:10.1371/journal.pone.0181829 · Cited by 12

The crystal structure of a natural DNA polymerase complexed with mirror DNA

An, J., Choi, J., Hwang, D., Park, J., Pemble, C. W., IV, Duong, T. H. M., Kim, K., Ahn, H., Chung, H. S., & Ahn, D. (2020) · Chemical Communications · doi:10.1039/c9cc09351f · Cited by 12

Sliding of HIV-1 reverse transcriptase over DNA creates a transient P pocket – targeting P-pocket by fragment screening

Singh, A. K., Martinez, S. E., Gu, W., Nguyen, H. V., Schols, D., Herdewijn, P. A., Jonghe, S. D., & Das, K. (2021) · Nature Communications · doi:10.1038/s41467-021-27409-y · Cited by 12

Metal‐mediated Targeting in the Body

Tang, X., & Liang, X. (2012) · Chemical Biology & Drug Design · doi:10.1111/cbdd.12090 · Cited by 13

Mechanism of U-Insertion RNA Editing in Trypanosome Mitochondria: Characterization of RET2 Functional Domains by Mutational Analysis

Ringpis, G.-E. E., Stagno, J. R., & Aphasizhev, R. (2010) · Journal of Molecular Biology · doi:10.1016/j.jmb.2010.04.035 · Cited by 12

A Nuclear Family A DNA Polymerase from Entamoeba histolytica Bypasses Thymine Glycol

Pastor-Palacios, G., Azuara-Liceaga, E. I., & Brieba, L. G. (2010) · PLoS neglected tropical diseases · doi:10.1371/journal.pntd.0000786 · Cited by 12

Ability of Polymerase η and T7 DNA Polymerase to Bypass Bulge Structures

Cannistraro, V. J., & Taylor, J. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m608478200 · Cited by 12

Simulations of DNA Pol λ R517 Mutants Indicate 517's Crucial Role in Ternary Complex Stability and Suggest DNA Slippage Origin

Foley, M. C., & Tamar Schlick, A. (2008) · Journal of the American Chemical Society · doi:10.1021/ja077982t · Cited by 12

Targeting structural dynamics of the RNA-dependent RNA polymerase for anti-viral strategies

Boehr, D. D., Liu, X., & Yang, X. (2014) · Current Opinion in Virology · doi:10.1016/j.coviro.2014.08.006 · Cited by 12

Bioinformatic prediction of polymerase elements in the rotavirus VP1 protein

Carpio, R. V., MORALES, J. L., Barro, M., Ricardo, A., & Spencer, E. (2006) · Biological Research · doi:10.4067/s0716-97602006000500008 · Cited by 12

Mutant Thermotoga neapolitana DNA polymerase I: altered catalytic properties for non-templated nucleotide addition and incorporation of correct nucleotides

Yang, S.-W. (2002) · Nucleic Acids Research · doi:10.1093/nar/gkf547 · Cited by 12

The Gly-952 Residue of Saccharomyces cerevisiae DNA Polymerase α Is Important in Discriminating Correct Deoxyribonucleotides from Incorrect Ones

Limsirichaikul, S., Ogawa, M., Niimi, A., Iwai, S., Murate, T., Yoshida, S., & Suzuki, M. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m208604200 · Cited by 12

Coordination Chemistry of Nucleotides and Antivirally Active Acyclic Nucleoside Phosphonates, including Mechanistic Considerations

Sigel, A., Sigel, H., & Sigel, R. K. O. (2022) · Molecules · doi:10.3390/molecules27092625 · Cited by 11

DNA polymerases of herpesviruses and their inhibitors

Piret, J., & Boivin, G. (2021) · The Enzymes · doi:10.1016/bs.enz.2021.07.003 · Cited by 11

Molecular Dynamics of a Food Carcinogen−DNA Adduct in a Replicative DNA Polymerase Suggest Hindered Nucleotide Incorporation and Extension

Zhang, L., Shapiro, R., & Broyde, S. B. (2005) · Chemical Research in Toxicology · doi:10.1021/tx050132b · Cited by 11

Unusual relatives of the multisubunit RNA polymerase

Forrest, D. (2018) · Biochemical Society Transactions · doi:10.1042/bst20180505 · Cited by 11

DNA polymerases lose their grip.

Beard, W. A., & Wilson, S. H. (2001) · Nature Structural Biology · doi:10.1038/nsb1101-915 · Cited by 11

The anatomy of infidelity.

Ellenberger, T., & Silvian, L. F. (2001) · Nature Structural Biology · doi:10.1038/nsb1001-827 · Cited by 11

Comparison of Bacterial and Eukaryotic Replisome Components

Yao, N. Y., & O’Donnell, M. E. (2015) · Elsevier eBooks · doi:10.1016/b978-0-12-394447-4.10038-0 · Cited by 12

The role of human replicative DNA polymerases in DNA repair and replication

Rytkönen, A. K. (2006) · Cited by 11

DNA polymerases β and λ and their roles in DNA replication and repair

Belousova, E. A., & Lavrik, O. I. (2010) · Molecular Biology · doi:10.1134/s0026893310060014 · Cited by 10

Time Course Analysis of Enzyme-Catalyzed DNA Polymerization

Rentergent, J., Driscoll, M. D., & Hay, S. (2016) · Biochemistry · doi:10.1021/acs.biochem.6b00442 · Cited by 10

Structural Analysis of Monomeric RNA-Dependent Polymerases Revisited

Jácome, R., Campillo-Balderas, J. A., Becerra, A., & Lazcano, A. (2022) · Journal of Molecular Evolution · doi:10.1007/s00239-022-10059-z · Cited by 10

A rescue act: Translesion DNA synthesis past N 2‐deoxyguanosine adducts

Nair, D. T., Kottur, J., & Sharma, R. (2015) · IUBMB Life · doi:10.1002/iub.1403 · Cited by 10

DNA Pol λˈs Extraordinary Ability To Stabilize Misaligned DNA

Foley, M. C., Padow, V. A., & Tamar Schlick, A. (2010) · Journal of the American Chemical Society · doi:10.1021/ja1049687 · Cited by 10

Hepatitis C virus polymerase–polymerase contact interface: Significance for virus replication and antiviral design

Jiménez, A. J. L., Clemente-Casares, P., Sabariegos, R., Valero, M. L., Bellón-Echeverría, I., Encinar, J. A., Kaushik‐Basu, N., Froeyen, M., & Más, A. (2014) · Antiviral Research · doi:10.1016/j.antiviral.2014.04.009 · Cited by 10

From RNA to DNA: Insights about the transition of informational molecule in the biological systems based on the structural proximity between the polymerases

dos Santos, A. P., José, M. V., & de Farías, S. T. (2021) · Biosystems · doi:10.1016/j.biosystems.2021.104442 · Cited by 10

Replisome Dynamics during Chromosome Duplication

Kurth, I., & O’Donnell, M. E. (2009) · EcoSal Plus · doi:10.1128/ecosalplus.4.4.2 · Cited by 11

Effect of oxidatively damaged DNA on the active site preorganization during nucleotide incorporation in a high fidelity polymerase from Bacillus stearothermophilus

Venkatramani, R., & Radhakrishnan, R. (2007) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.21824 · Cited by 10

Pyrophosphorolysis of CCA Addition: Implication for Fidelity

Igarashi, T., Liu, C., Morinaga, H., Kim, S., & Hou, Y. (2011) · Journal of Molecular Biology · doi:10.1016/j.jmb.2011.09.036 · Cited by 10

Insertions in the β3–β4 loop of reverse transcriptase of human immunodeficiency virus type 1 and their mechanism of action, influence on drug susceptibility and viral replication capacity

Eggink, D., Huigen, M. C. D. G., Boucher, C. A., Götte, M., & Nijhuis, M. (2007) · Antiviral Research · doi:10.1016/j.antiviral.2007.03.001 · Cited by 10

Impact of Chemical Adducts on Translesion Synthesis in Replicative and Bypass DNA Polymerases: From Structure to Function

Eoff, R. L., Egli, M., & Guengerich, F. P. (2010) · Wiley eBooks · doi:10.1002/9783527630110.ch13 · Cited by 9

Virus Evolution

Domingo, E., & Perales, C. (2014) · Wiley eBooks · doi:10.1002/9780470015902.a0000436.pub3 · Cited by 9

Double domain fusion improves the reverse transcriptase activity and inhibitor tolerance of Bst DNA polymerase

Xiang, R., Liu, G., Hou, Y., Xie, L.-X., Wang, Q., & Hu, S. (2024) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2024.133243 · Cited by 10

Computational Investigation of Locked Nucleic Acid (LNA) Nucleotides in the Active Sites of DNA Polymerases by Molecular Docking Simulations

Poongavanam, V., Madala, P. K., Højland, T., & Veedu, R. N. (2014) · PLoS ONE · doi:10.1371/journal.pone.0102126 · Cited by 9

New insights into DNA polymerase mechanisms provided by time-lapse crystallography

Weaver, T., Washington, M. T., & Freudenthal, B. (2022) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2022.102465 · Cited by 9

Substrate Specificity Diversity of Human Terminal Deoxynucleotidyltransferase May Be a Naturally Programmed Feature Facilitating Its Biological Function

Кузнецова, А. А., Senchurova, S. I., Gavrilova, A. A., Tyugashev, T. E., Mikushina, E. S., & Kuznetsov, N. A. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25020879 · Cited by 9

Innovative Agents for Actinic Keratosis and Nanocarriers Enhancing Skin Penetration

Schäfer‐Korting, M., Höltje, M., Körting, H. C., & Höltje, H. ‐. (2010) · Skin Pharmacology and Physiology · doi:10.1159/000257258 · Cited by 9

The control of the discrimination between dNTP and rNTP in DNA and RNA polymerase

Yoon, H., & Warshel, A. (2016) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.25104 · Cited by 9

Structural dynamics and determinants of 2-aminoadenine specificity in DNA polymerase DpoZ of vibriophage ϕVC8

Czernecki, D., Hu, H., Romoli, F., & Delarue, M. H. (2021) · Nucleic Acids Research · doi:10.1093/nar/gkab955 · Cited by 9

Diagnosis of Xeroderma Pigmentosum and Related DNA Repair-Deficient Cutaneous Diseases.

Cleaver, J. E. (2008) · PubMed · Cited by 8

A Novel Replicative Enzyme Encoded by the LinearArthrobacterPlasmid pAL1

Kolkenbrock, S., Naumann, B., Hippler, M., & Fetzner, S. (2010) · Journal of Bacteriology · doi:10.1128/jb.00614-10 · Cited by 9

Targeting human DNA polymerase α for the inhibition of keratinocyte proliferation. Part 1. Homology model, active site architecture and ligand binding

Richartz, A., Höltje, M., Brandt, B., Schäfer‐Korting, M., & Höltje, H. (2008) · Journal of Enzyme Inhibition and Medicinal Chemistry · doi:10.1080/14756360701433414 · Cited by 9

“Gate-keeper” Residues and Active-Site Rearrangements in DNA Polymerase μ Help Discriminate Non-cognate Nucleotides

Li, Y., & Tamar Schlick, A. (2013) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1003074 · Cited by 9

Mouse models of DNA polymerases

Menezes, M. R., & Sweasy, J. B. (2012) · Environmental and Molecular Mutagenesis · doi:10.1002/em.21731 · Cited by 9

Insights into the Roles of Desolvation and π‐Electron Interactions during DNA Polymerization

Motea, E. A., Lee, I., & Berdis, A. J. (2013) · ChemBioChem · doi:10.1002/cbic.201200649 · Cited by 9

A hand-off of DNA between archaeal polymerases allows high-fidelity replication to resume at a discrete intermediate three bases past 8-oxoguanine

Cranford, M. T., Kaszubowski, J. D., & Trakselis, M. A. (2020) · Nucleic Acids Research · doi:10.1093/nar/gkaa803 · Cited by 9

Structural and energetic characterization of nucleic acid‐binding to the fingers domain of Moloney murine leukemia virus reverse transcriptase

Crowther, R. L., Remeta, D. P., Minetti, C. A. S. A., Das, D., Montaño, S. P., & Georgiadis, M. M. (2004) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.20224 · Cited by 9

Altering DNA Polymerase Incorporation Fidelity by Distorting the dNTP Binding Pocket with a Bulky Carcinogen-Damaged Template

Yan, S. F., Wu, M., Geacintov, N. E., & Broyde, S. B. (2004) · Biochemistry · doi:10.1021/bi0499516 · Cited by 9

Evidence for action of ribavirin through the hepatitis C virus RNA polymerase

Cannon, N. A., Donlin, M. J., Mayes, L. M., Lyra, A. C., Bisceglie, A. M. D., & Tavis, J. E. (2009) · Journal of Viral Hepatitis · doi:10.1111/j.1365-2893.2009.01109.x · Cited by 9

Retrons

Yamanaka, K., Shimamoto, T., Inouye, S., & Inoye, M. (2007) · doi:10.1128/9781555817954.ch32 · Cited by 9

DNA Polymerase-Parental DNA Interaction Is Essential for Helicase-Polymerase Coupling during Bacteriophage T7 DNA Replication

Lo, C., & Gao, Y. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23031342 · Cited by 8

A sophisticated mechanism governs Pol ζ activity in response to replication stress

Li, C., Fan, S., Li, P., Bai, Y., Wang, Y., Cui, Y., Li, M., Wang, R., Shao, Y., Wang, Y., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-52112-z · Cited by 8

Structural basis for intrinsic strand displacement activity of mitochondrial DNA polymerase

Nayak, A. R., Sokolova, V. E., Sillamaa, S., Herbine, K., Sedman, J., & Temiakov, D. (2025) · Nature Communications · doi:10.1038/s41467-025-57594-z · Cited by 8

Directed evolution of a TNA polymerase identifies independent paths to fidelity and catalysis

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