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

DNA Polymerase Template Interactions Probed by Degenerate Isosteric Nucleobase Analogs

Paul, N., Nashine, V. C., Hoops, G. C., Zhang, P., Zhou, J., Bergstrom, D. E., & Davisson, V. J. (2003) · Chemistry & Biology · doi:10.1016/j.chembiol.2003.08.008 · Cited by 37

Inhibition of Klenow DNA polymerase and poly(A)-specific ribonuclease by aminoglycosides

Ren, Y., NEZ, J. M., Kirsebom, L. A., & Virtanen, A. (2002) · RNA · doi:10.1017/s1355838202021015 · Cited by 38

Evaluating the contributions of desolvation and base-stacking during translesion DNA synthesis

Zhang, X., Lee, I., & Berdis, A. J. (2004) · Organic & Biomolecular Chemistry · doi:10.1039/b401732c · Cited by 37

Structures of telomerase subunits provide functional insights

Sekaran, V. G., Soares, J., & Jarstfer, M. B. (2009) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2009.07.019 · Cited by 36

DNA Synthesis across an Abasic Lesion by Yeast Rev1 DNA Polymerase

Nair, D. T., Johnson, R. E., Prakash, L., Prakash, S., & Aggarwal, A. K. (2010) · Journal of Molecular Biology · doi:10.1016/j.jmb.2010.12.016 · Cited by 36

Iron mediates catalysis of nucleic acid processing enzymes: support for Fe(II) as a cofactor before the great oxidation event

Okafor, C. D., Lanier, K. A., Petrov, A. S., Athavale, S. S., Bowman, J. C., Hud, N. V., & Williams, L. D. (2017) · Nucleic Acids Research · doi:10.1093/nar/gkx171 · Cited by 36

Extensive free-energy simulations identify water as the base in nucleotide addition by DNA polymerase

Roston, D., Demapan, D., & Cui, Q. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1914613116 · Cited by 37

Determinants of DNA Mismatch Recognition within the Polymerase Domain of the Klenow Fragment

Thompson, E. H. Z., Bailey, M. F., der Schans, E. J. C. V., Joyce, C. M., & Millar, D. P. (2001) · Biochemistry · doi:10.1021/bi0114271 · Cited by 36

Enzyme−Substrate Interactions with an Antibiotic Resistance Enzyme: Aminoglycoside Nucleotidyltransferase(2‘ ‘)-Ia Characterized by Kinetic and Thermodynamic Methods

Wright, E., & SERPERSU, E. H. (2005) · Biochemistry · doi:10.1021/bi050797c · Cited by 37

Calcium Is a Cofactor of Polymerization but Inhibits Pyrophosphorolysis by the Sulfolobus solfataricus DNA Polymerase Dpo4

Irimia, A., Zang, H., Loukachevitch, L. V., Eoff, R. L., Guengerich, F. P., & Egli, M. (2006) · Biochemistry · doi:10.1021/bi052511+ · Cited by 36

Intramolecular and Intermolecular Uridylylation by Poliovirus RNA-Dependent RNA Polymerase

Richards, O. C., Spagnolo, J. F., Lyle, J. M., Vleck, S. E., Kuchta, R. D., & Kirkegaard, K. (2006) · Journal of Virology · doi:10.1128/jvi.02533-05 · Cited by 36

Dependence of DNA Polymerase Replication Rate on External Forces: A Model Based on Molecular Dynamics Simulations

Andricioaei, I., Goel, A., Herschbach, D. R., & Karplus, M. (2004) · Biophysical Journal · doi:10.1529/biophysj.103.039313 · Cited by 36

N4 RNA Polymerase II, a Heterodimeric RNA Polymerase with Homology to the Single-Subunit Family of RNA Polymerases

Willis, S. H., Kazmierczak, K. M., Carter, R. H., & Rothman‐Denes, L. B. (2002) · Journal of Bacteriology · doi:10.1128/jb.184.18.4952-4961.2002 · Cited by 36

Toward Understanding the Mutagenicity of an Environmental Carcinogen: Structural Insights into Nucleotide Incorporation Preferences

Perlow, R. A., & Broyde, S. B. (2002) · Journal of Molecular Biology · doi:10.1016/s0022-2836(02)00751-9 · Cited by 36

Reverse transcriptase in motion: Conformational dynamics of enzyme–substrate interactions

Götte, M., Rausch, J. W., Marchand, B., Sarafianos, S. G., & Grice, S. F. J. L. (2009) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2009.07.020 · Cited by 35

Study of involvement of ImuB and DnaE2 in stationary-phase mutagenesis in Pseudomonas putida

Koorits, L., Tegova, R., Tark‐Dame, M., Tarassova, K., Tover, A., & Kivisaar, M. (2007) · DNA repair · doi:10.1016/j.dnarep.2007.01.010 · Cited by 37

Mode of inhibition of HIV-1 reverse transcriptase by polyacetylenetriol, a novel inhibitor of RNA- and DNA-directed DNA polymerases

Loya, S., Rudi, A., Kashman, Y., & Hizi, A. (2002) · Biochemical Journal · doi:10.1042/0264-6021:3620685 · Cited by 34

Magnetic Control of Enzymatic Phosphorylation

Buchachenko, A. L. (2014) · Journal of Physical Chemistry & Biophysics · doi:10.4172/2161-0398.1000142 · Cited by 35

The Catalytic Mechanism of DNA and RNA Polymerases

Genna, V., Donati, E., & Vivo, M. D. (2018) · ACS Catalysis · doi:10.1021/acscatal.8b03363 · Cited by 36

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

Kinetic Mechanism of the Mg2+-dependent Nucleotidyl Transfer Catalyzed by T4 DNA and RNA Ligases

Cherepanov, A. V., & de Vries, S. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m109616200 · Cited by 35

The Spacious Active Site of a Y-Family DNA Polymerase Facilitates Promiscuous Nucleotide Incorporation Opposite a Bulky Carcinogen-DNA Adduct

Perlow-Poehnelt, R. A., Likhterov, I., Scicchitano, D. A., Geacintov, N. E., & Broyde, S. B. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m404332200 · Cited by 35

DNA polymerase IV - DNA ternary complex 14

Kottur, J., & Nair, D. T. (2017) · Worldwide Protein Data Bank · doi:10.2210/pdb5yv2/pdb · Cited by 35

DNA polymerases provide a canon of strategies for translesion synthesis past oxidatively generated lesions

Zahn, K. E., Wallace, S. S., & Doublié, S. (2011) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2011.03.008 · Cited by 34

Role of Human DNA Polymerase κ in Extension Opposite from a cis–syn Thymine Dimer

Carpio, R. V., Silverstein, T. D., Lone, S., Johnson, R. E., Prakash, L., Prakash, S., & Aggarwal, A. K. (2011) · Journal of Molecular Biology · doi:10.1016/j.jmb.2011.02.042 · Cited by 34

A Small Post-Translocation Energy Bias Aids Nucleotide Selection in T7 RNA Polymerase Transcription

Yu, J. H., & OSTER, G. F. (2012) · Biophysical Journal · doi:10.1016/j.bpj.2011.12.028 · Cited by 34

PCR performance of the highly thermostable proof-reading B-type DNA polymerase from Pyrococcus abyssi

Dietrich, J., Schmitt, P., Zieger, M., Preve, B., Rolland, J., Chaabihi, H., & Gueguen, Y. (2002) · FEMS Microbiology Letters · doi:10.1016/s0378-1097(02)01037-6 · Cited by 34

Multiple deprotonation paths of the nucleophile 3′-OH in the DNA synthesis reaction

Gregory, M., Gao, Y., Cui, Q., & Yang, W. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2103990118 · Cited by 27

Nucleotide selection by the Y-family DNA polymerase Dpo4 involves template translocation and misalignment

Brenlla, A., Markiewicz, R. P., Rueda, D., & Romano, L. J. (2013) · Nucleic Acids Research · doi:10.1093/nar/gkt1149 · Cited by 33

Evolutionary placement of Xanthomonadales based on conserved protein signature sequences

Cutiño-Jiménez, A. M., Martins-Pinheiro, M., de Lima, W. C., Tornet, A. M., Morales, O. G., & Menck, C. F. M. (2009) · Molecular Phylogenetics and Evolution · doi:10.1016/j.ympev.2009.09.026 · Cited by 33

Structural Basis for Error-free Replication of Oxidatively Damaged DNA by Yeast DNA Polymerase η

Silverstein, T. D., Jain, R., Johnson, R. E., Prakash, L., Prakash, S., & Aggarwal, A. K. (2010) · Structure · doi:10.1016/j.str.2010.08.019 · Cited by 35

Replicative DNA polymerases.

Albà, M. M. (2001) · Genome biology · doi:10.1186/gb-2001-2-1-reviews3002 · Cited by 33

Effects of Nucleotides and Nucleotide Analogue Inhibitors of HIV-1 Reverse Transcriptase in a Ratchet Model of Polymerase Translocation

Götte, M. (2006) · Current Pharmaceutical Design · doi:10.2174/138161206776873626 · Cited by 32

Recapitulation of the cellular xeroderma pigmentosum-variant phenotypes using short interfering RNA for DNA polymerase H.

Laposa, R. R., Feeney, L., & Cleaver, J. E. (2003) · PubMed · Cited by 33

Pre‐Steady‐State Kinetic Analysis of Truncated and Full‐Length Saccharomyces cerevisiae DNA Polymerase Eta

Brown, J. A., Zhang, L., Sherrer, S. M., Taylor, J., Burgers, P., & Suo, Z. (2010) · Journal of Nucleic Acids · doi:10.4061/2010/871939 · Cited by 32

2’-5’ Oligoadenylate synthetase shares active site architecture with the archaeal CCA-adding enzyme

Torralba, S., Sojat, J., & Hartmann, R. (2008) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-008-8164-5 · Cited by 32

Novel Phenalenone Derivatives from a Marine-Derived Fungus Exhibit Distinct Inhibition Spectra against Eukaryotic DNA Polymerases

Perpelescu, M., Kobayashi, J., Furuta, M., Ito, Y., Izuta, S., Takemura, M., Suzuki, M., & Yoshida, S. (2002) · Biochemistry · doi:10.1021/bi020115a · Cited by 32

Probing DNA Polymerase Fidelity Mechanisms Using Time-Resolved Fluorescence Anisotropy

Bailey, M. F., Thompson, E. H. Z., & Millar, D. P. (2001) · Methods · doi:10.1006/meth.2001.1216 · Cited by 32

Exploring the Impact of Primer–Template Mismatches on PCR Performance of DNA Polymerases Varying in Proofreading Activity

Huang, K., Zhang, J., Li, J., Qiu, H., Wei, L., Yang, Y., & Wang, C. (2024) · Genes · doi:10.3390/genes15020215 · Cited by 40

Structure–function relationship and biogenesis regulation of the human telomerase holoenzyme

Hukezalie, K. R., & Wong, J. M. Y. (2013) · FEBS Journal · doi:10.1111/febs.12272 · Cited by 32

Assembly of a G-Quadruplex Repair Complex by the FANCJ DNA Helicase and the REV1 Polymerase

Lowran, K., Campbell, L., Popp, P., & Wu, C. G. (2019) · Genes · doi:10.3390/genes11010005 · Cited by 30

Tieing together loose ends: telomere instability in cancer and aging

Borges, G. D. O., Criqui, M., & Harrington, L. A. (2022) · Molecular Oncology · doi:10.1002/1878-0261.13299 · Cited by 34

Molecular Dynamics Free-Energy Simulations of the Binding Contribution to the Fidelity of T7 DNA Polymerase

Florián, J., Warshel, A., & Goodman, M. F. (2002) · The Journal of Physical Chemistry B · doi:10.1021/jp020791m · Cited by 31

The Activity of Selected RB69 DNA Polymerase Mutants Can Be Restored by Manganese Ions: The Existence of Alternative Metal Ion Ligands Used during the Polymerization Cycle

Zakharova, E., Wang, J., & Konigsberg, W. H. (2004) · Biochemistry · doi:10.1021/bi049615p · Cited by 31

Genotyping of simple sequence repeat factors implicated in shadow band generation revisited

Olejniczak, M., & Krzyżosiak, W. J. (2006) · Electrophoresis · doi:10.1002/elps.200600136 · Cited by 31

The handbook of plant mutation screening: mining of natural and induced alleles.

Meksem, K., & Kahl, G. (2010) · Cited by 31

A relaxed active site after exon ligation by the group I intron

Lipchock, S. V., & Strobel, S. A. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0712016105 · Cited by 31

Deep-sea vent phage DNA polymerase specifically initiates DNA synthesis in the absence of primers

Zhu, B., Wang, L., Mitsunobu, H., Lu, X., Hernandez, A. J., Yoshida‐Takashima, Y., Nunoura, T., Tabor, S., & Richardson, C. C. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1700280114 · Cited by 30

DNA polymerase beta and other gap-filling enzymes in mammalian base excision repair

Beard, W. A., & Wilson, S. H. (2019) · The Enzymes · doi:10.1016/bs.enz.2019.08.002 · Cited by 30

Bacterial and Eukaryotic Replisome Machines.

Yao, N. Y., & O’Donnell, M. E. (2016) · PubMed · Cited by 29

Sequence-specific stalling of DNA polymerase γ and the effects of mutations causing progressive ophthalmoplegia†

Atanassova, N., Fusté, J. M., Wanrooij, S., Macao, B., Goffart, S., Bäckström, S., Farge, G., Khvorostov, I., Larsson, N., Spelbrink, J. N., et al. (2011) · Human Molecular Genetics · doi:10.1093/hmg/ddq565 · Cited by 28

The Family X DNA Polymerase from Deinococcus radiodurans Adopts a Non-standard Extended Conformation

Leulliot, N., Cladière, L., Lecointe, F., Christiane, D. D., Hübscher, U., & TILBEURGH, H. V. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m809342200 · Cited by 30

Key Role of Template Sequence for Primer Synthesis by the Herpes Simplex Virus 1 Helicase−Primase

Ramirez‐Aguilar, K. A., Low-Nam, N. A., & Kuchta, R. D. (2002) · Biochemistry · doi:10.1021/bi026680v · Cited by 30

dNTP versus NTP discrimination by phenylalanine 451 in duck hepatitis B virus P protein indicates a common structure of the dNTP-binding pocket with other reverse transcriptases

Beck, J. (2002) · Nucleic Acids Research · doi:10.1093/nar/30.7.1679 · Cited by 30

Dynamic stereoisomerization in inherently chiral bimetallic [2]catenanes

Prakasam, T., Lusi, M., Nauha, E., Olsen, J., Sy, M., Platas‐Iglesias, C., Charbonnière, L. J., & Trabolsi, A. (2014) · Chemical Communications · doi:10.1039/c4cc07392d · Cited by 29

Enhancement of Polymerase Activity of the Large Fragment in DNA Polymerase I fromGeobacillus stearothermophilusby Site-Directed Mutagenesis at the Active Site

Ma, Y., Zhang, B., Wang, M., Ou, Y., Wang, J., & Li, S. (2016) · BioMed Research International · doi:10.1155/2016/2906484 · Cited by 29

International Journal of Current Microbiology and Applied Sciences

Publishers, P. E. (2020) · ADVANCED SCIENCES INDEX · Cited by 29

The proofreading exonuclease subunit ε of Escherichia coli DNA polymerase III is tethered to the polymerase subunit α via a flexible linker

Ozawa, K., Jergic, S., Park, A. Y., Dixon, N. E., & Otting, G. (2008) · Nucleic Acids Research · doi:10.1093/nar/gkn489 · Cited by 28

Carcinogenic adducts induce distinct DNA polymerase binding orientations

Vrtis, K. B., Markiewicz, R. P., Romano, L. J., & Rueda, D. (2013) · Nucleic Acids Research · doi:10.1093/nar/gkt554 · Cited by 28

Biochemical characterization of enterovirus 71 3D RNA polymerase

Jiang, H., Weng, L., Zhang, N., Arita, M., Li, R., Chen, L., & Toyoda, T. (2011) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2011.01.001 · Cited by 28

Contribution of the Reverse Rate of the Conformational Step to Polymerase β Fidelity

Bakhtina, M., Roettger, M. P., & Tsai, M. (2009) · Biochemistry · doi:10.1021/bi802119f · Cited by 28

Identification of Critical Residues for G−1 Addition and Substrate Recognition by tRNAHis Guanylyltransferase

Jackman, J. E., & Phizicky, E. M. (2008) · Biochemistry · doi:10.1021/bi702517q · Cited by 28

Excision of Incorporated Nucleotide Analogue Chain-terminators can Diminish their Inhibitory Effects on Viral RNA-dependent RNA Polymerases

D’Abramo, C. M., Cellai, L., & Götte, M. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.01.030 · Cited by 27

Enzymatic synthesis of random sequences of RNA and RNA analogues by DNA polymerase theta mutants for the generation of aptamer libraries

Randrianjatovo-Gbalou, I., Rosario, S., Sismeiro, O., Varet, H., Legendre, R., Coppée, J., Huteau, V., Pochet, S., & Delarue, M. H. (2018) · Nucleic Acids Research · doi:10.1093/nar/gky413 · Cited by 28

The invariant glutamate of human PrimPol DxE motif is critical for its Mn2+-dependent distinctive activities

Calvo, P. A., Sastre-Moreno, G., Perpiñá-Viciano, C., Guerra, S., Martínez-Jiménez, M. I., & Blanco, L. (2019) · DNA repair · doi:10.1016/j.dnarep.2019.03.006 · Cited by 27

Alpha-carboxy nucleoside phosphonates as universal nucleoside triphosphate mimics

Balzarini, J. M., Das, K., Bernatchez, J. A., Martinez, S. E., Ngure, M., Keane, S., Ford, A., Maguire, N. M., Mullins, N., John, J., et al. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1420233112 · Cited by 27

Polymerase‐Functionalized Hierarchical Mesoporous Titania Thin Films: Towards a Nanoreactor Platform for DNA Amplification

Bellino, M. G., Tropper, I., Durán, H., Regazzoni, A. E., & Soler‐Illia, G. J. A. A. (2010) · Small · doi:10.1002/smll.201000066 · Cited by 27

Recombinant viral RdRps can initiate RNA synthesis from circular templates

Ranjith-Kumar, C. T., & Kao, C. C. (2005) · RNA · doi:10.1261/rna.2163106 · Cited by 29

Fidelity of Nucleotide Incorporation by the RNA-Dependent RNA Polymerase from Poliovirus

Cameron, C. E., Moustafa, I. M., & Arnold, J. J. (2016) · The Enzymes · doi:10.1016/bs.enz.2016.02.002 · Cited by 27

Nuclear spin selectivity in enzymatic catalysis: A caution for applied biophysics

Buchachenko, A. L., Bukhvostov, A. A., Ermakov, K. V., & Kuznetsov, D. A. (2019) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2019.04.005 · Cited by 27

Extending the Understanding of Mutagenicity: Structural Insights into Primer-extension Past a Benzo[a]pyrene Diol Epoxide-DNA adduct

Perlow, R. A., & Broyde, S. B. (2003) · Journal of Molecular Biology · doi:10.1016/s0022-2836(03)00187-6 · Cited by 27

Computational drug design strategies applied to the modelling of human immunodeficiency virus-1 reverse transcriptase inhibitors

Santos, L. H., Ferreira, R. S., & Caffarena, E. R. (2015) · Memórias do Instituto Oswaldo Cruz · doi:10.1590/0074-02760150239 · Cited by 26

Molecular insight on the binding of NNRTI to K103N mutated HIV-1 RT: molecular dynamics simulations and dynamic pharmacophore analysis

Nizami, B., Sydow, D., Wolber, G., & Honarparvar, B. (2016) · Molecular BioSystems · doi:10.1039/c6mb00428h · Cited by 26

Two-Metal-Ion Catalysis: Inhibition of DNA Polymerase Activity by a Third Divalent Metal Ion

Wang, J., & Konigsberg, W. H. (2022) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2022.824794 · Cited by 26

Mechanisms of Hepatitis B Virus Resistance Development

Warner, N., & LOCARNINI, S. A. (2014) · Intervirology · doi:10.1159/000360940 · Cited by 26

Rapid incorporation kinetics and improved fidelity of a novel class of 3′-OH unblocked reversible terminators

Gardner, A. F., Wang, J., Wu, W., Karouby, J., Li, H., Stupi, B. P., Jack, W. E., Hersh, M. N., & Metzker, M. L. (2012) · Nucleic Acids Research · doi:10.1093/nar/gks330 · Cited by 26

Inhibition of HIV-1 reverse transcription: basic principles of drug action and resistance

Götte, M. (2004) · Expert Review of Anti-infective Therapy · doi:10.1586/14789072.2.5.707 · Cited by 26

Herpesvirus DNA Polymerase Mutants—How Important Is Faithful Genome Replication?

Trimpert, J., & Osterrieder, N. (2019) · Current Clinical Microbiology Reports · doi:10.1007/s40588-019-00135-2 · Cited by 25

A Tyr Residue in the Reverse Transcriptase Domain Can Mimic the Protein-Priming Tyr Residue in the Terminal Protein Domain of a Hepadnavirus P Protein

Beck, J., & Nassal, M. (2011) · Journal of Virology · doi:10.1128/jvi.00482-11 · Cited by 25

Pre-steady-state Kinetic Analysis of a Family D DNA Polymerase from Thermococcus sp. 9°N Reveals Mechanisms for Archaeal Genomic Replication and Maintenance

Schermerhorn, K. M., & Gardner, A. F. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.662841 · Cited by 26

Architecture of the Saccharomyces cerevisiae Replisome

Bai, L., Yuan, Z., Sun, J., Georgescu, R. E., O’Donnell, M. E., & Li, H. (2017) · Advances in experimental medicine and biology · doi:10.1007/978-981-10-6955-0_10 · Cited by 25

The DNA Replication Machine: Structure and Dynamic Function

Yao, N. Y., & O’Donnell, M. E. (2020) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-3-030-58971-4_5 · Cited by 27

Structural insights into the assembly and mechanism of mpox virus DNA polymerase complex F8-A22-E4-H5

Wang, X., Ma, L., Li, N., & Gao, N. (2023) · Molecular Cell · doi:10.1016/j.molcel.2023.10.038 · Cited by 24

Mutagenicity and Genotoxicity of (5′S)-8,5′-Cyclo-2′-deoxyadenosine in Escherichia coli and Replication of (5′S)-8,5′-Cyclopurine-2′-deoxynucleosides in Vitro by DNA Polymerase IV, Exo-Free Klenow Fragment, and Dpo4

Pednekar, V., Weerasooriya, S., Jasti, V. P., & Basu, A. K. (2014) · Chemical Research in Toxicology · doi:10.1021/tx4002786 · Cited by 25

How a Low-Fidelity DNA Polymerase Chooses Non-Watson–Crick from Watson–Crick Incorporation

Wu, W., Su, M., Wu, J., Kumar, S., Lim, L.-H., Wang, C., Nelissen, F. H. T., Chen, M.-C. C., Doreleijers, J. F., Wijmenga, S. S., et al. (2014) · Journal of the American Chemical Society · doi:10.1021/ja4102375 · Cited by 25

Presence of 18-Å Long Hydrogen Bond Track in the Active Site of Escherichia coli DNA Polymerase I (Klenow Fragment)

Singh, K., & Modak, M. J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m211496200 · Cited by 25

Mechanism of Hepatitis C Virus RNA Polymerase Inhibition with Dihydroxypyrimidines

Powdrill, M. H., Deval, J., Narjes, F., Francesco, R. D., & Götte, M. (2009) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.01216-09 · Cited by 25

Energetics, Conformation, and Recognition of DNA Duplexes Modified by Monodentate RuII Complexes Containing Terphenyl Arenes

Nováková, O., Malina, J., Suchánková, T., Kašpárková, J., Bugarcic, T., Sadler, P. J., & Brabec, V. (2010) · Chemistry - A European Journal · doi:10.1002/chem.200903078 · Cited by 25

Mechanism of Taq DNA Polymerase Inhibition by Fullerene Derivatives: Insight from Computer Simulations

Nedumpully-Govindan, P., Monticelli, L., & Salonen, E. (2012) · The Journal of Physical Chemistry B · doi:10.1021/jp3046577 · Cited by 25

The msDNAs of bacteria

Lampson, B. C., Inouye, M., & Inouye, S. (2001) · Progress in nucleic acid research and molecular biology · doi:10.1016/s0079-6603(01)67025-9 · Cited by 25

A DNA Polymerase β Mutator Mutant with Reduced Nucleotide Discrimination and Increased Protein Stability,

Shah, A. M., Conn, D. A., Li, S., Capaldi, A. P., Jäger, J., & Sweasy, J. B. (2001) · Biochemistry · doi:10.1021/bi010755y · Cited by 25

Base Selectivity Is Impaired by Mutants that Perturb Hydrogen Bonding Networks in the RB69 DNA Polymerase Active Site

Yang, G., Wang, J., & Konigsberg, W. H. (2005) · Biochemistry · doi:10.1021/bi047921x · Cited by 25

Multiple Roles of Metal Ions in Large Ribozymes

Donghi, D., & Schnabl, J. (2011) · Royal Society of Chemistry eBooks · doi:10.1039/9781849732512-00197 · Cited by 26

Molecular basis of genetic variation of viruses

Domingo, E. (2019) · Elsevier eBooks · doi:10.1016/b978-0-12-816331-3.00002-7 · Cited by 26

Structural and functional insights into the enzymatic plasticity of the SARS-CoV-2 NiRAN domain

Small, G. I., Fedorova, O., Olinares, P. D. B., Chandanani, J., Banerjee, A., Choi, Y. J., Molina, H., Chait, B. T., Darst, S. A., & Campbell, E. A. (2023) · Molecular Cell · doi:10.1016/j.molcel.2023.10.001 · Cited by 24

Crystal Structure of Human Poly(A) Polymerase Gamma Reveals a Conserved Catalytic Core for Canonical Poly(A) Polymerases

Yang, Q., Nausch, L., Martin, G., Keller, W., & Doublié, S. (2013) · Journal of Molecular Biology · doi:10.1016/j.jmb.2013.09.025 · Cited by 24

Kinetic Analysis of 3′–5′ Nucleotide Addition Catalyzed by Eukaryotic tRNAHis Guanylyltransferase

Smith, B. A., & Jackman, J. E. (2011) · Biochemistry · doi:10.1021/bi201397f · Cited by 25

The crystal structure of the CRISPR-associated protein Csn2 from Streptococcus agalactiae

Ellinger, P., Arslan, Z., Wurm, R., Tschapek, B., MacKenzie, C. R., Pfeffer, K., Panjikar, S., Wagner, R., Schmitt, L., Gohlke, H., et al. (2012) · Journal of Structural Biology · doi:10.1016/j.jsb.2012.04.006 · Cited by 24

Examination of the Long-range Effects of Aminofluorene-induced Conformational Heterogeneity and Its Relevance to the Mechanism of Translesional DNA Synthesis

Meneni, S., Liang, F., & Cho, B. P. (2006) · Journal of Molecular Biology · doi:10.1016/j.jmb.2006.12.023 · Cited by 24

Structural Studies of Klenow Fragment: An Enzyme with Two Active SitesPreprint

Steitz, T. A., Beese, L. S., Freemont, P. S., Friedman, J. M., & Sanderson, M. R. (1987) · Cold Spring Harbor Symposia on Quantitative Biology · doi:10.1101/sqb.1987.052.01.053 · Cited by 41

DNA Polymerase Structure and Mechanisms of Action

Hingorani, M., & O'Donne, M. (2000) · Current Organic Chemistry · doi:10.2174/1385272003375996 · Cited by 14

DNA Replication Fidelity

Kunkel, T. A. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.r400006200 · Cited by 754

DNA-polimeraza: mehanizami kojima se ostvaruje visoka vjernost replikacije

Poljak, K. (2009)

Getting a grip on how DNA polymerases function.

Patel, P. H., & Loeb, L. A. (2001) · Nature Structural Biology · doi:10.1038/90344 · Cited by 89