An open and closed case for all polymerases

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

Kohlstaedt, L. A., Wang, J., Friedman, J. M., Rice, P. A., & Steitz, T. A. (1992) · Science · doi:10.1126/science.1377403 · Cited by 1,914

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

Huang, H., Chopra, R., Verdine, G. L., & Harrison, S. C. (1998) · Science · doi:10.1126/science.282.5394.1669 · Cited by 1,420

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

Doublié, S., Tabor, S., Long, A. M., Richardson, C. C., & Ellenberger, T. (1998) · Nature · doi:10.1038/34593 · Cited by 1,184

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

Jacobo-Molina, A., Ding, J., Nanni, R. G., Clark, A. D., Lu, X., Tantillo, C., Williams, R. L., Kamer, G., Ferris, A. L., Clark, P., et al. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.13.6320 · Cited by 1,115

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

Beese, L. S., & Steitz, T. A. (1991) · The EMBO Journal · doi:10.1002/j.1460-2075.1991.tb07917.x · Cited by 1,059

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

Ollis, D. L., Brick, P., Hamlin, R. C., Xuong, N., & Steitz, T. A. (1985) · Nature · doi:10.1038/313762a0 · Cited by 848

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

Pelletier, H., Sawaya, M. R., Kumar, A., Wilson, S. H., & Kraut, J. (1994) · Worldwide Protein Data Bank · doi:10.2210/pdb2bpf/pdb · Cited by 694

Crystal structures of open and closed forms of binary and ternary complexes of the large fragment of Thermus aquaticus DNA polymerase I: structural basis for nucleotide incorporation

Li, Y., Korolev, S., & Waksman, G. (1998) · The EMBO Journal · doi:10.1093/emboj/17.24.7514 · Cited by 689

An attempt to unify the structure of polymerases

Delarue, M. H., Poch, O., Tordo, N., Moras, D., & Argos, P. (1990) · Protein Engineering Design and Selection · doi:10.1093/protein/3.6.461 · Cited by 638

Structures of Ternary Complexes of Rat DNA Polymerase β, a DNA Template-Primer, and ddCTP

Pelletier, H., Sawaya, M. R., Kumar, A., Wilson, S. H., & Kraut, J. (1994) · Science · doi:10.1126/science.7516580 · Cited by 598

Structural Studies of a Bacterial tRNAHIS Guanylyltransferase (Thg1)-Like Protein, with Nucleotide in the Activation and Nucleotidyl Transfer Sites

Hyde, S. J., Rao, B. S., Eckenroth, B. E., Jackman, J. E., & Doublié, S. (2013) · PLoS ONE · doi:10.1371/journal.pone.0067465 · Cited by 17

Site-specific labeling of T7 DNA polymerase with a conformationally sensitive fluorophore and its use in detecting single-nucleotide polymorphisms

Tsai, Y., Jin, Z., & Johnson, K. A. (2008) · Analytical Biochemistry · doi:10.1016/j.ab.2008.09.006 · Cited by 17

Human Immunodeficiency Virus Reverse Transcriptase

Wendeler, M., Miller, J. T., & Grice, S. F. J. L. (2009) · Springer eBooks · doi:10.1007/b135974_19 · Cited by 17

I260Q DNA polymerase β highlights precatalytic conformational rearrangements critical for fidelity

Liptak, C., Mahmoud, M. M., Eckenroth, B. E., Moreno, M. V., East, K. W., Alnajjar, K. S., Huang, J. W., Towle-Weicksel, J. B., Doublié, S., Loria, J. P., et al. (2018) · Nucleic Acids Research · doi:10.1093/nar/gky825 · Cited by 17

Structural Maturation of HIV-1 Reverse Transcriptase—A Metamorphic Solution to Genomic Instability

London, R. E. (2016) · Viruses · doi:10.3390/v8100260 · Cited by 15

Conformational Dynamics of a Y-Family DNA Polymerase during Substrate Binding and Catalysis As Revealed by Interdomain Forster Resonance Energy Transfer

Maxwell, B. A., Xu, C., & Suo, Z. (2014) · Biochemistry · doi:10.1021/bi5000146 · Cited by 15

DNA Polymerase Conformational Dynamics and the Role of Fidelity-Conferring Residues: Insights from Computational Simulations

Meli, M., Sustarsic, M., Craggs, T. D., Kapanidis, A. N., & Colombo, G. (2016) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2016.00020 · Cited by 15

BP[dG]-induced distortions to DNA polymerase and DNA duplex: A detailed mechanism of BP adducts blocking replication

Wu, Z., Peng, L., Hu, Y., Xie, T., Yan, H., Wan, H., Liu, W., Liang, L., Xie, Z., Liu, K., et al. (2020) · Food and Chemical Toxicology · doi:10.1016/j.fct.2020.111325 · Cited by 15

Contrasting Effects of W781V and W780V Mutations in Helix N of Herpes Simplex Virus 1 and Human Cytomegalovirus DNA Polymerases on Antiviral Drug Susceptibility

Piret, J., Goyette, N., Eckenroth, B. E., Drouot, E., Götte, M., & Boivin, G. (2015) · Journal of Virology · doi:10.1128/jvi.03360-14 · 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

A Unique Region in Bacteriophage T7 DNA Polymerase Important for Exonucleolytic Hydrolysis of DNA

Kumar, J. K., Chiu, E. T., Tabor, S., & Richardson, C. C. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m406103200 · Cited by 15

Structural Mechanism for the Fidelity Modulation of DNA Polymerase λ

Liu, M., Tsai, H., Liu, X., Ho, M., Wu, W., & Tsai, M. (2016) · Journal of the American Chemical Society · doi:10.1021/jacs.5b13368 · Cited by 15

A 70-kDa chloroplast DNA polymerase from pea (Pisum sativum) that shows high processivity and displays moderate fidelity

Gaikwad, A. S., Hop, D. V., & Mukherjee, S. K. (2002) · Molecular Genetics and Genomics · doi:10.1007/s00438-001-0631-8 · Cited by 15

Structural organization of viral RNA-dependent RNA polymerases

Shatskaya, G. S., & Dmitrieva, T. M. (2013) · Biochemistry (Moscow) · doi:10.1134/s0006297913030036 · Cited by 14

2.0 Å resolution crystal structure of human polκ reveals a new catalytic function of N-clasp in DNA replication

Jha, V., & Ling, H. (2018) · Scientific Reports · doi:10.1038/s41598-018-33371-5 · Cited by 14

How a B family DNA polymerase has been evolved to copy RNA

Choi, W. S., He, P., Pothukuchy, A., Gollihar, J., Ellington, A. D., & Yang, W. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2009415117 · 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

Prechemistry Nucleotide Selection Checkpoints in the Reaction Pathway of DNA Polymerase I and Roles of Glu710 and Tyr766

Bermek, O., Grindley, N. D. F., & Joyce, C. M. (2013) · Biochemistry · doi:10.1021/bi400837k · Cited by 13

Evidence for functional significance of the permuted C motif in Co2+-stimulated RNA-dependent RNA polymerase of infectious bursal disease virus

Letzel, T., Mundt, E., & Gorbalenya, A. E. (2007) · Journal of General Virology · doi:10.1099/vir.0.82890-0 · 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

Role of Histidine 932 of the Human Mitochondrial DNA Polymerase in Nucleotide Discrimination and Inherited Disease

Batabyal, D., McKenzie, J., & Johnson, K. A. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.156182 · Cited by 13

The Effect of Increased Processivity on Overall Fidelity of Human Immunodeficiency Virus Type 1 Reverse Transcriptase

Rezende, L. F., Kew, Y., & Prasad, V. R. (2001) · Journal of Biomedical Science · doi:10.1007/bf02256413 · Cited by 13

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

Challenges at the frontiers of structural biology

Šali, A., & Kuriyan, J. (1999) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(99)01494-2 · Cited by 13

A Transition-State Perspective on Y-Family DNA Polymerase η Fidelity in Comparison with X-Family DNA Polymerases λ and β

Oertell, K., Florián, J., Haratipour, P., Crans, D. C., Kashemirov, B. A., Wilson, S. H., McKenna, C. E., & Goodman, M. F. (2019) · Biochemistry · doi:10.1021/acs.biochem.9b00087 · Cited by 12

The mechano-chemistry of a monomeric reverse transcriptase

Malik, O., Khamis, H., Rudnizky, S., & Kaplan, A. (2017) · Nucleic Acids Research · doi:10.1093/nar/gkx1168 · Cited by 12

Investigation of Intradomain Motions of a Y-Family DNA Polymerase during Substrate Binding and Catalysis

Raper, A. T., & Suo, Z. (2016) · Biochemistry · doi:10.1021/acs.biochem.6b00878 · Cited by 12

Enzymatic Polymerization of Phosphonate Nucleosides

Renders, M., Lievrouw, R., Krečmerová, M., Holý, A., & Herdewijn, P. A. (2008) · ChemBioChem · doi:10.1002/cbic.200800494 · Cited by 12

Norovirus RNA‐dependent RNA polymerase: A computational study of metal‐binding preferences

Shaik, M. M., Bhattacharjee, N., Feliks, M., Ng, K. K.-S., & Field, M. J. (2017) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.25304 · Cited by 11

Coordination and Substitution of DNA Polymerases in Response to Genomic Obstacles

Trakselis, M. A., Cranford, M. T., & Chu, A. M. (2017) · Chemical Research in Toxicology · doi:10.1021/acs.chemrestox.7b00190 · Cited by 11

DNA polymerase activity in water-structured and confined environment of reverse micelles

Anarbaev, R. O., Khodyreva, S. N., Zakharenko, A. L., Rechkunova, N. I., & Lavrik, O. I. (2005) · Journal of Molecular Catalysis B Enzymatic · doi:10.1016/j.molcatb.2005.01.004 · 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

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

Insertion of oxidized nucleotide triggers rapid DNA polymerase opening

Kim, T., Freudenthal, B., Beard, W. A., Wilson, S. H., & Tamar Schlick, A. (2016) · Nucleic Acids Research · doi:10.1093/nar/gkw174 · Cited by 10

Flexibility of telomerase in binding the RNA template and DNA telomeric repeat

Choi, W. S., Weng, P. J., & Yang, W. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2116159118 · 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

Signal Transduction in the Escherichia coli SOS Response

Foti, J. J., Simmons, L. A., Beuning, P., & Walker, G. (2010) · Elsevier eBooks · doi:10.1016/b978-0-12-374145-5.00258-8 · Cited by 7

Substitution of a residue contacting the triphosphate moiety of the incoming nucleotide increases the fidelity of yeast DNA polymerase ζ

Howell, C. A., Kondratick, C. M., & Washington, M. T. (2008) · Nucleic Acids Research · doi:10.1093/nar/gkn023 · Cited by 10

Structure of a backtracked state reveals conformational changes similar to the state following nucleotide incorporation in human norovirus polymerase

Zamyatkin, D. F., Rao, C., Hoffarth, E. R., Jurca, G., Rho, H., Parra, F., Grochulski, P., & Ng, K. K.-S. (2014) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s1399004714021518 · 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

Coordinated DNA polymerization by Polγ and the region of LonP1 regulated proteolysis

Riccio, A. A., Brannon, A. J., Krahn, J. M., Bouvette, J., Williams, J. G., Borgnia, M. J., & Copeland, W. C. (2024) · Nucleic Acids Research · doi:10.1093/nar/gkae539 · Cited by 9

Rescue of Bacteriophage T7 DNA Polymerase of Low Processivity by Suppressor Mutations Affecting Gene 3 Endonuclease

Lee, S., Chowdhury, K., Tabor, S., & Richardson, C. C. (2009) · Journal of Virology · doi:10.1128/jvi.00855-09 · 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

Interference of dengue replication by blocking the access of 3′ SL RNA to the viral RNA-dependent RNA polymerase

Tunghirun, C., Narkthong, V., Chaicumpa, W., & Chimnaronk, S. (2020) · Antiviral Research · doi:10.1016/j.antiviral.2020.104921 · Cited by 9

The Impact of Human DNA Glycosylases on the Activity of DNA Polymerase β toward Various Base Excision Repair Intermediates

Bakman, A. S., Boichenko, S. S., Кузнецова, А. А., Ishchenko, A. A., Saparbaev, M. K., & Kuznetsov, N. A. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24119594 · Cited by 9

A Mutation in the Gene-encoding Bacteriophage T7 DNA Polymerase That Renders the Phage Temperature-sensitive

Kumar, J. K., Kremsdorf, R. A., Tabor, S., & Richardson, C. C. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m106319200 · 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

Molecular Flexibility and Discontinuous Translocation of a Non-templated Polymerase

Johnson, L., Liu, S., & Gershon, P. D. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.01.058 · Cited by 9

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

Novel Escherichia coli active site dnaE alleles with altered base and sugar selectivity

Vaisman, A., Łazowski, K., Reijns, M. A. M., Walsh, E. M., McDonald, J. P., Moreno, K. C., Quiros, D. R., Schmidt, M., Kranz, H. D., Yang, W., et al. (2021) · Molecular Microbiology · doi:10.1111/mmi.14779 · Cited by 9

Catalytic Mechanism of DNA Polymerases

Roettger, M. P., Bakhtina, M., Kumar, S., & Tsai, M. (2010) · Elsevier eBooks · doi:10.1016/b978-008045382-8.00669-9 · Cited by 8

Mutations in the middle domain of yeast poly(A) polymerase affect interactions with RNA but not ATP

Zhelkovsky, A. M., Helmling, S., Bohm, A., & Moore, C. L. (2004) · RNA · doi:10.1261/rna.5238704 · Cited by 8

The Rate-limiting Step of DNA Synthesis by DNA Polymerase Occurs in the Fingers-closed Conformation

Evans, G. W., Craggs, T. D., & Kapanidis, A. N. (2021) · Journal of Molecular Biology · doi:10.1016/j.jmb.2021.167410 · Cited by 7

Enzymes and Enzyme Activity Encoded by Nonenveloped Viruses

Azad, K., Banerjee, M., & Johnson, J. E. (2017) · Annual Review of Virology · doi:10.1146/annurev-virology-101416-041944 · Cited by 7

Bulky Lesion Bypass Requires Dpo4 Binding in Distinct Conformations

Liyanage, P. S., Walker, A. R., Brenlla, A., Cisneros, G. A., Romano, L. J., & Rueda, D. (2017) · Scientific Reports · doi:10.1038/s41598-017-17643-0 · Cited by 7

2-Alkylmalonic Acid: Amphiphilic Chelator and a Potent Inhibitor of Metalloenzyme

Ojha, B., Singh, A. K., Adhikari, M. D., Ramesh, A., & Das, G. C. (2010) · The Journal of Physical Chemistry B · doi:10.1021/jp1013847 · Cited by 7

How to accurately bypass damage

Broyde, S. B., & Patel, D. J. (2010) · Nature · doi:10.1038/4651023a · Cited by 7

Bacterial DNA Polymerase I

Allen, W. J., Li, Y., & Waksman, G. (2010) · Wiley eBooks · doi:10.1002/9780470015902.a0001043.pub2 · Cited by 9

Structural Insight into Polymerase Mechanism via a Chiral Center Generated with a Single Selenium Atom

Qin, T., Hu, B., Zhao, Q., Wang, Y., Wang, S., Luo, D., Lyu, J., Chen, Y., Gan, J., & Huang, Z. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms242115758 · Cited by 6

A nucleotide binding rectification Brownian ratchet model for translocation of Y-family DNA polymerases

Xie, P. (2011) · Theoretical Biology and Medical Modelling · doi:10.1186/1742-4682-8-22 · Cited by 6

Human mitochondrial RNA polymerase structures reveal transcription start site and slippage mechanism

Shen, J., Goovaerts, Q., Ajjugal, Y., De Wijngaert, B., Das, K., & Patel, S. S. (2025) · Molecular Cell · doi:10.1016/j.molcel.2025.07.002 · Cited by 5

Advanced preparation of fragment libraries enabled by oligonucleotide-modified 2′,3′-dideoxynucleotides

Medžiūnė, J., Kapustina, Ž., Žeimytė, S., Jakubovska, J., Sindikevičienė, R., Čikotienė, I., & Lubys, A. (2022) · Communications Chemistry · doi:10.1038/s42004-022-00649-9 · Cited by 5

Inhibition of Viruses

Gupta, S. P. (2018) · Elsevier eBooks · doi:10.1016/b978-0-12-813330-9.00003-x · Cited by 5

Priming DNA Replication from Triple Helix Oligonucleotides: Possible Threestranded DNA in DNA Polymerases

Lestienne, P. P. (2011) · Molecular Biology International · doi:10.4061/2011/562849 · Cited by 4

High-throughput Kinetics using capillary Electrophoresis and Robotics (HiKER) platform used to study T7, T3, and Sp6 RNA polymerase misincorporation

Carter, Z. I., O’Brien, W. B., Lund, S. R., & Gardner, A. F. (2024) · PLoS ONE · doi:10.1371/journal.pone.0312743 · Cited by 4

Modeling translocation dynamics of strand displacement DNA synthesis by DNA polymerase I

Xie, P. (2011) · Journal of Molecular Modeling · doi:10.1007/s00894-011-1222-1 · Cited by 4

Are there three polynucleotide strands in the catalytic centre of DNA polymerases?

Lestienne, P. P. (2009) · Biochimie · doi:10.1016/j.biochi.2009.07.008 · Cited by 4

Incoming nucleotide binds to Klenow ternary complex leading to stable physical sequestration of preceding dNTP on DNA

Ramanathan, S. (2001) · Nucleic Acids Research · doi:10.1093/nar/29.10.2097 · Cited by 4

DNA polymerase β reveals enhanced activity and processivity in reverse micelles

Anarbaev, R. O., Rogozina, A. L., & Lavrik, O. I. (2008) · Biophysical Chemistry · doi:10.1016/j.bpc.2008.12.004 · Cited by 4

A polymerase-site-jumping model for strand transfer during DNA synthesis by reverse transcriptase

Xie, P. (2009) · Virus Research · doi:10.1016/j.virusres.2009.03.022 · Cited by 4

A model for the dynamics of mammalian family X DNA polymerases

Xie, P. (2011) · Journal of Theoretical Biology · doi:10.1016/j.jtbi.2011.02.018 · Cited by 4

Minimalist Model for Force-Dependent DNA Replication

Nong, E., DeVience, S. J., & Herschbach, D. R. (2012) · Biophysical Journal · doi:10.1016/j.bpj.2012.01.020 · Cited by 4

Challenges at the frontiers of structural biology

Šali, A., & Kuriyan, J. (1999) · Trends in Genetics · doi:10.1016/s0168-9525(99)01908-3 · Cited by 4

Structures of Complexes Formed by HIV-1 Reverse Transcriptase at a Termination Site of DNA Synthesis

Lavigne, M., Polomack, L., & BUC, H. C. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m102976200 · Cited by 4

Cryo-EM Structures of the Plasmodium falciparum Apicoplast DNA Polymerase

Lo, C., Ung, A. R., Koley, T., Nelson, S. W., & Gao, Y. (2024) · Journal of Molecular Biology · doi:10.1016/j.jmb.2024.168842 · Cited by 3

Coordination between human DNA polymerase β and apurinic/apyrimidinic endonuclease 1 in the course of DNA repair

Bakman, A. S., Boichenko, S. S., Кузнецова, А. А., Ishchenko, A. A., Saparbaev, M. K., & Kuznetsov, N. A. (2023) · Biochimie · doi:10.1016/j.biochi.2023.10.007 · Cited by 3

Structure and flexibility of the DNA polymerase holoenzyme of vaccinia virus

Burmeister, W. P., Boutin, L., Balestra, A. C., Gröger, H., Ballandras-Colas, A., Hutin, S., Kraft, C., Grimm, C., Böttcher, B., Fischer, U., et al. (2024) · PLOS Pathogens · doi:10.1371/journal.ppat.1011652 · Cited by 3

Collapsed State Mediates the Low Fidelity of the DNA Polymerase β I260 Mutant

Fijen, C., Chavira, C., Alnajjar, K. S., Sawyer, D. L., & Sweasy, J. B. (2024) · Biochemistry · doi:10.1021/acs.biochem.4c00263 · Cited by 2

Nucleoside Analogue Inhibitors of Human Immunodeficiency Virus Reverse Transcriptase

Deval, J., & Götte, M. (2014) · ASM Press eBooks · doi:10.1128/9781555815493.ch4 · Cited by 2

A steric gate prevents mutagenic dATP incorporation opposite 8‐oxo‐deoxyguanosine in mitochondrial DNA polymerases

Baruch‐Torres, N., Trasviña‐Arenas, C. H., Gilea, A. I., Dissanayake, U. C., Molina‐Jiménez, M., García‐Medel, P. L., Díaz‐Quezada, C., Lodi, T., Cisneros, G. A., Baruffini, E., et al. (2025) · FEBS Journal · doi:10.1111/febs.70064 · Cited by 2

Purification of M-MLVH- RT on a 9-Aminoethyladenine-(1,6-diamine-hexane)-triazine Selected from a Combinatorial Library of dNTP-Mimetic Ligands

Melissis, S., Papageorgiou, A. C., Labrou, N. E., & Clonis, Y. D. (2010) · Journal of Chromatographic Science · doi:10.1093/chromsci/48.6.496 · Cited by 2

Design and interpretation of experiments to establish enzyme pathway and define the role of conformational changes in enzyme specificity

Dangerfield, T. L., & Johnson, K. A. (2023) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2023.03.018 · Cited by 2

Dynamics of DNA polymerase I (Klenow fragment) under external force

Xie, P. (2012) · Journal of Molecular Modeling · doi:10.1007/s00894-012-1688-5 · Cited by 2

Replication of DNA Containing Mirror-Image Thymidine in E. coli Cells

Kan, Y., Chen, L., Lin, D., Bu, X., Mo, M., Yan, L., Yang, Z., Yuan, L., Wu, L., & He, Y. (2020) · Chemical Research in Toxicology · doi:10.1021/acs.chemrestox.9b00502 · Cited by 2

Acceleration of DNA Replication of Klenow Fragment by Small Resisting Force

Liu, Y.-R., Wang, P.-Y., Li, W., & Xie, P. (2021) · Chinese Physics Letters · doi:10.1088/0256-307x/38/11/118701 · Cited by 2

Unraveling the mysteries of transcription.

Ellenberger, T. (1999) · Nature Structural Biology · doi:10.1038/9260 · Cited by 2

Telomerase - strategies to exploit an important chemotherapeutic target

Fletcher, T. M. (2001) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728222.5.3.363 · Cited by 2

A mass spectrometry-based approach for identifying novel DNA polymerase substrates from a pool of dNTP analogues

Kincaid, K., & Kuchta, R. D. (2006) · Nucleic Acids Research · doi:10.1093/nar/gkl632 · Cited by 2

Live culture-based qPCR screening of Taq DNA polymerase variants for resistance to PCR inhibitors

Kermekchiev, M. B., Zhang, Z., & Barnes, W. M. (2025) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2025.1624735 · Cited by 1

RNA-Dependent RNA Polymerase Activity as a Basis for the Detection of Positive-Strand RNA Viruses by Vertebrate Host Cells

Nikonov, A. (2014) · DSpace repository (University of Tartu) · Cited by 1

Infidelity Out in the Open

Doublié, S. (2004) · Structure · doi:10.1016/j.str.2004.09.002 · Cited by 1

Structural Basis for DNA Replication and Uracil Repair in Phage A-Family DNA PolymerasesPreprint

Missoury, S., Lucas‐Staat, S., Sieskind, R., & Delarue, M. H. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.03.26.645540 · Cited by 1

New insights into the mechanism of dna replication on unmodified and benzo[a]pyrene modified templates using surface plasmon resonance

Federley, R. (2011) · Human Biology

STRUCTURAL AND CONFORMATIONAL INSIGHTS INTO BULKY ARYLAMINE-INDUCED MUTAGENESIS

Xu, L. (2014) · doi:10.23860/diss-xu-lifang-2014

Precision Optical Measurements of DNA Structure and Synthesis

Ma, Z. (2008) · doi:10.7907/vknw-bs41

Chromosomal DNA Replication on a Protein “Chip”

Jeruzalmi, D. (2004) · Structure · doi:10.1016/j.str.2004.11.003

Substrate recognition by the yeast Rev1 protein and DNA polymerase ζ

Howell, C. A. (2008) · doi:10.17077/etd.fy291k5g

Structure and Function of DNA Repair Proteins: Lesion Recognition

Yang, W. (2007) · WORLD SCIENTIFIC eBooks · doi:10.1142/9789812706782_0008

Structural Features of Bypass Polymerases

Kisker, C. (2005) · doi:10.1201/9780849352683-33

The ligase detection reaction: the evolution of a mutation detection strategy

Farquar, H. D. (2002) · doi:10.31390/gradschool_dissertations.3855

Structure and functional implications of the polymerase active site region in a complex of HIV-1 RT with a double-stranded DNA template-primer and an antibody fab fragment at 2.8 Å resolution

Ding, J., Das, K., Hsiou, Y., Sarafianos, S. G., Clark, A. D., Jacobo‐Molina, A., Tantillo, C., Hughes, S. H., & Arnold, E. (1998) · Journal of Molecular Biology · doi:10.1006/jmbi.1998.2208 · Cited by 323

Rational design of polymerase inhibitors as antiviral drugs

Öberg, B. F. (2006) · Antiviral Research · doi:10.1016/j.antiviral.2006.05.012 · Cited by 55

Structural Insights into Mechanisms of Catalysis and Inhibition in Norwalk Virus Polymerase

Zamyatkin, D. F., Parra, F., Martín-Alonso, J. M., Harki, D. A., Peterson, B. R., Grochulski, P., & Ng, K. K.-S. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m709563200 · Cited by 141

The structure and functions of HIV-1 polymerase and the development of its inhibitors

Liu, X. (2006) · Zhongguo yaowu huaxue zazhi

HIV-1 Reverse Transcriptase: Structure Predictions for the Polymerase Domain

Barber, A. M., Hizi, A., Maizel, J. V., & Hughes, S. H. (1990) · AIDS Research and Human Retroviruses · doi:10.1089/aid.1990.6.1061 · Cited by 73