DNA Polymerases: Structural Diversity and Common Mechanisms

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

A general two-metal-ion mechanism for catalytic RNA

Steitz, T. A., & Steitz, J. A. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.14.6498 · Cited by 1,171

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

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

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

Production of Bst polymerase for diagnosis of different infections using loop-mediated isothermal amplification

Pika, M. I., Mikheeva, O. O., Соловьева, Е. Д., Владимировна, В. А., Bulanenko, V. P., Александрович, Ч. Е., Petrov, V. V., Krasovitov, K. V., Cherkashina, A. S., & Акимкин, В. Г. (2023) · Journal of microbiology epidemiology immunobiology · doi:10.36233/0372-9311-364 · Cited by 7

The origin of genetic and metabolic systems: Evolutionary structuralinsights

Deng, S. (2023) · Heliyon · doi:10.1016/j.heliyon.2023.e14466 · Cited by 7

Thermally controlled intein splicing of engineered DNA polymerases provides a robust and generalizable solution for accurate and sensitive molecular diagnostics

Wang, Y., Shi, Y., Hellinga, H. W., & Beese, L. S. (2023) · Nucleic Acids Research · doi:10.1093/nar/gkad368 · Cited by 7

Exploring the molecular aspect and updating evolutionary approaches to the DNA polymerase enzymes for biotechnological needs: A comprehensive review

Laatri, S., Khayari, S. E., & Qriouet, Z. (2024) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2024.133924 · Cited by 9

Comparative Analyses of Dynamic Transcriptome Profile of Heart Highlight the Key Response Genes for Heat Stress in Zhikong Scallop Chlamys farreri

Wang, X., Yang, Z., Peng, C., Yu, H., Cui, C., Xing, Q., Hu, J., Bao, Z., & Huang, X. (2024) · Antioxidants · doi:10.3390/antiox13101217 · Cited by 7

Molecular modelling studies of new potential human DNA polymerase α inhibitors

Zdrazil, B., Schwanke, A., Schmitz, B., Schäfer‐Korting, M., & Höltje, H. (2010) · Journal of Enzyme Inhibition and Medicinal Chemistry · doi:10.3109/14756366.2010.503609 · Cited by 7

Kinetic analysis of reverse transcriptase activity of bacterial family A DNA polymerases

Yasukawa, K., Konishi, A., Shinomura, M., Nagaoka, E., & Fujiwara, S. (2012) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2012.09.116 · 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

Platinum Polyoxoniobates Form Adducts with DNA

Yudkina, A. V., Sokolov⧫, M. N., Abramov⧫, P. A., Грин, И. Р., & Zharkov, D. O. (2019) · Russian Journal of Bioorganic Chemistry · doi:10.1134/s1068162019060414 · Cited by 7

Molecular Characterization of a DNA Polymerase from Thermus thermophilus MAT72 Phage vB_Tt72: A Novel Type-A Family Enzyme with Strong Proofreading Activity

Dorawa, S., Werbowy, O., Płotka, M., Kaczorowska, A., Makowska, J., Kozlowski, L. P., Friðjónsson, Ó. H., Hreggviðsson, G. Ó., Aevarsson, A., & Kaczorowski, T. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23147945 · Cited by 7

Kinetic Pathway of Pyrophosphorolysis by a Retrotransposon Reverse Transcriptase

Pandey, M., Patel, S. S., & Gabriel, A. (2008) · PLoS ONE · doi:10.1371/journal.pone.0001389 · Cited by 8

Complex Formation between a Putative 66-Residue Thumb Domain of Bacterial Reverse Transcriptase RT-Ec86 and the Primer Recognition RNA

Inouye, M., Ke, H., Yashio, A., Yamanaka, K., Nariya, H., Shimamoto, T., & Inouye, S. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m408462200 · Cited by 7

The Role of Interface Domain Interactions on Thermal Stability of DNA polymerase I ITB-1

Nurbaiti, S., Hertadi, R., Martoprawiro, M. A., & Akhmaloka, A. (2009) · The Open Structural Biology Journal · doi:10.2174/1874199100903010016 · Cited by 6

Direct DNA Lesion Reversal and Excision Repair in Escherichia coli

Couvé, S., Ishchenko, A. A., Fedorova, O. S., Ramanculov, E. M., Laval, J., & Saparbaev, M. K. (2013) · EcoSal Plus · doi:10.1128/ecosalplus.7.2.4 · Cited by 7

High sensitive one-step RT-PCR using MMLV reverse transcriptase, DNA polymerase with reverse transcriptase activity, and DNA/RNA helicase

Okano, H., Baba, M., Yamasaki, T., Hidese, R., Fujiwara, S., Yanagihara, I., Ujiiye, T., Hayashi, T., Kojima, K., Takita, T., et al. (2017) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2017.04.030 · Cited by 6

Structural and Functional Aspects of Foamy Virus Protease-Reverse Transcriptase

Wöhrl, B. M. (2019) · Viruses · doi:10.3390/v11070598 · 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

Characterization of a gene encoding tRNA nucleotidyltransferase from Candida glabrata

Hanic‐Joyce, P. J., & Joyce, P. B. M. (2002) · Yeast · doi:10.1002/yea.926 · Cited by 7

Genetic and biochemical diversity in the HCV NS5B RNA polymerase in the context of interferon α plus ribavirin therapy

Cao, F., Donlin, M. J., Turner, K., Cheng, X., & Tavis, J. E. (2010) · Journal of Viral Hepatitis · doi:10.1111/j.1365-2893.2010.01316.x · Cited by 7

Relationship Between Conformational Changes in Pol λ’s Active Site Upon Binding Incorrect Nucleotides and Mismatch Incorporation Rates

Foley, M. C., & Tamar Schlick, A. (2009) · The Journal of Physical Chemistry B · doi:10.1021/jp903172x · Cited by 7

Understanding the molecular mechanism of drug resistance of anti-HIV nucleosides by molecular modeling

Chong, Y. (2004) · Frontiers in bioscience · doi:10.2741/1220 · Cited by 7

Mechanisms by which Human Cells Bypass Damaged Bases during DNA Replication after Ultraviolet Irradiation

Cleaver, J. E. (2002) · The Scientific World JOURNAL · doi:10.1100/tsw.2002.348 · Cited by 7

Cloning, Homological Analysis, and Expression of DNA Pol I from Geobacillus thermoleovorans

Akhmaloka, A., Pramono, H., Ambarsari, L., Susanti, E., Nurbaiti, S., & Madayanti, F. (2008) · Cited by 7

Chemotherapeutic intervention by inhibiting DNA polymerases

Dasari, A., Choi, J.-S., & Berdis, A. J. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-803582-5.00007-3 · 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

Role of the LEXE Motif of Protein-primed DNA Polymerases in the Interaction with the Incoming Nucleotide

Santos, E., Lázaro, J. M., Pérez-Arnaiz, P., Salas, M., & de Vega, M. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.530980 · Cited by 6

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

Neutron Spin Echo for the Exploration of Large Scale Macromolecular Dynamics

Richter, D. (2006) · Journal of the Physical Society of Japan · doi:10.1143/jpsj.75.111004 · Cited by 6

The emergence of molecular machines as a prerequisite of the ancient RNA world evolution

Spirin, A. S. (2013) · Paleontological Journal · doi:10.1134/s0031030113090190 · Cited by 6

Analysis of DNA Polymerases Reveals Specific Genes Expansion in Leishmania and Trypanosoma spp.

Poveda, A., Méndez, M., & Armijos‐Jaramillo, V. (2020) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2020.570493 · Cited by 5

CoV-er all the bases: Structural perspectives of SARS-CoV-2 RNA synthesis

Malone, B. F., Campbell, E. A., & Darst, S. A. (2021) · The Enzymes · doi:10.1016/bs.enz.2021.06.004 · Cited by 7

Folding and Catalysis Near Life’s Origin: Support for Fe2+ as a Dominant Divalent Cation

Okafor, C. D., Bowman, J. C., Hud, N. V., Glass, J. B., & Williams, L. D. (2018) · Nucleic acids and molecular biology · doi:10.1007/978-3-319-93584-3_8 · Cited by 6

The Cenancestor and Its Contemporary Biological Relics: The Case of Nucleic Acid Polymerases

Delaye, L., Vázquez, H., & Lazcano, A. (2001) · Springer eBooks · doi:10.1007/978-94-010-1017-7_39 · Cited by 6

Prebiotic Chemistry — Biochemistry — Emergence of Life (4.4-2 Ga)

Pascal, R., Boiteau, L., Forterre, P., Gargaud, M., Lazcano, A., López‐García, P., Moreira, D., Maurel, M., Peretó, J. G., Prieur, D., et al. (2007) · Springer eBooks · doi:10.1007/978-0-387-45083-4_5 · Cited by 7

Enzymatic Functionalization of RNA Oligonucleotides by Terminal Uridylyl Transferase Using Fluorescent and Clickable Nucleotide Analogs

Dutta, S., & Srivatsan, S. G. (2024) · Chemistry - An Asian Journal · doi:10.1002/asia.202400475 · Cited by 5

Emergent and Convergent Features in the Laboratory Evolution of Polymerase Ribozymes

Horning, D. P. (2025) · Biochemistry · doi:10.1021/acs.biochem.5c00160 · Cited by 5

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

Polymerase Switching in Response to DNA Damage

Ollivierre, J. N., Silva, M. C., Sefcikova, J., & Beuning, P. J. (2010) · Biological and medical physics series · doi:10.1007/978-0-387-92808-1_11 · Cited by 5

The Cmr complex: an RNA-guided endoribonuclease

Bailey, S. (2013) · Biochemical Society Transactions · doi:10.1042/bst20130216 · Cited by 5

Nucleic Acid Polymerase Fidelity and Viral Population Fitness

Smidansky, E. D., Arnold, J. J., & Cameron, C. E. (2008) · Elsevier eBooks · doi:10.1016/b978-0-12-374153-0.00006-0 · Cited by 5

Human Mitochondrial DNA Polymerase Metal Dependent UV Lesion Bypassing Ability

Park, J., Baruch‐Torres, N., Iwai, S., Herrmann, G. K., Brieba, L. G., & Yin, Y. W. (2022) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2022.808036 · Cited by 6

Translocation pause of remdesivir-containing primer/template RNA duplex within SARS-CoV-2’s RNA polymerase complexes

Shi, Y., Wang, J., & Batista, V. S. (2022) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2022.999291 · Cited by 5

Atomic Structure of the Herpes Simplex Virus 1 DNA Polymerase

Liu, S., & Homa, F. L. (2009) · Springer eBooks · doi:10.1007/b135974_17 · Cited by 5

Characterization of the RNA binding energetics of the Candida albicans poly(A) polymerase

Bougie, I., & Bisaillon, M. (2007) · Yeast · doi:10.1002/yea.1482 · Cited by 5

Metal ion coordination in the E. coli Nudix hydrolase dihydroneopterin triphosphate pyrophosphatase: New clues into catalytic mechanism

Hill, S. E., Nguyen, E. H., Ukachukwu, C. U., Freeman, D. M., Quirk, S., & Lieberman, R. L. (2017) · PLoS ONE · doi:10.1371/journal.pone.0180241 · Cited by 5

Nucleophilic substitution at di- and triphosphates: leaving group ability of phosphate versus diphosphate

van Beek, B., van Bochove, M. A., Hamlin, T. A., & Bickelhaupt, F. M. (2019) · Electronic Structure · doi:10.1088/2516-1075/ab0af3 · Cited by 5

Binding-Induced Conformational Changes Involved in Sliding Clamp PCNA and DNA Polymerase DPO4

Chu, W., Suo, Z., & Wang, J. (2020) · iScience · doi:10.1016/j.isci.2020.101117 · Cited by 5

DNA replication: In vitro single-molecule manipulation data analysis and models

Jarillo, J., Ibarra, B., & Cao, F. J. (2021) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2021.06.032 · Cited by 5

DNA Replication, Repair, and Mutagenesis

Bhagavan, N. V., & Ha, C. (2011) · Elsevier eBooks · doi:10.1016/b978-0-12-095461-2.00022-9 · 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

DNA Polymerases That Perform Template-Independent DNA Synthesis

Berdis, A. J. (2013) · Nucleic acids and molecular biology · doi:10.1007/978-3-642-39796-7_5 · Cited by 5

MinActionPath2: path generation between different conformations of large macromolecular assemblies by action minimization

Koehl, P., Navaza, R., Tekpinar, M., & Delarue, M. H. (2024) · Nucleic Acids Research · doi:10.1093/nar/gkae421 · Cited by 4

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

Human telomerase protein: Understanding how the catalytic activity is suppressed under single substitutions of some conserved residues. A computational study

Herrera, F. E., & Sferco, S. J. (2018) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.25573 · Cited by 4

Comparative Analysis of Family A DNA-Polymerases as a Searching Tool for Enzymes with New Properties

Bulygin, A. A., Кузнецова, А. А., Fedorova, O. S., & Kuznetsov, N. A. (2023) · Molecular Biology · doi:10.1134/s0026893323020048 · Cited by 4

Structure and function of extreme TLS DNA polymerase TTEDbh from Thermoanaerobacter tengcongensis

Tian, L., Gao, H., Yang, S., Liu, Y., Li, M., Xu, W., & Yan, X. (2023) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2023.126770 · Cited by 4

The proofreading mechanism of the human leading-strand DNA polymerase ε holoenzyme

Wang, F., He, Q., O’Donnell, M. E., & Li, H. (2025) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2507232122 · Cited by 4

ϕ29 DNA Polymerase Active Site: Role of Residue Val250 as Metal–dNTP Complex Ligand and in Protein-Primed Initiation

Pérez-Arnaiz, P., Lázaro, J. M., Salas, M., & de Vega, M. (2009) · Journal of Molecular Biology · doi:10.1016/j.jmb.2009.10.061 · Cited by 4

Optimization of PCR amplification for sensitive capture of Methanopyrus isoleucyl-tRNA synthetase gene in environmental samples

Yu, Z. (2010) · Annals of Microbiology · doi:10.1007/s13213-010-0097-1 · 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

Structure of New Binary and Ternary DNA Polymerase Complexes From Bacteriophage RB69

Park, J., Youn, H., An, J. Y., Lee, Y., Eom, S. H., & Wang, J. (2021) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2021.704813 · Cited by 4

Crystal structure of DNA polymerase I from Thermus phage G20c

Ahlqvist, J., Linares‐Pastén, J. A., Jasilionis, A., Welin, M., Håkansson, M., Svensson, L. A., Wang, L., Watzlawick, H., Aevarsson, A., Friðjónsson, Ó. H., et al. (2022) · Acta Crystallographica Section D Structural Biology · doi:10.1107/s2059798322009895 · Cited by 4

A Comparative Analysis of Translesion DNA Synthesis Catalyzed by a High-Fidelity DNA Polymerase

Dasari, A. K. R., Deodhar, T. J., & Berdis, A. J. (2017) · Journal of Molecular Biology · doi:10.1016/j.jmb.2017.06.003 · Cited by 4

An Unexplored Diversity of Reverse Transcriptases in Bacteria

Zimmerly, S., & Wu, L. (2015) · ASM Press eBooks · doi:10.1128/9781555819217.ch54 · Cited by 5

Proton affinity of dipeptides containing alanine and diaminobutyric acid

Batoon, P. H. M., & Ren, J. (2014) · International Journal of Mass Spectrometry · doi:10.1016/j.ijms.2014.07.025 · 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

Novel HIV-1 non-nucleoside reverse transcriptase inhibitors: A combinatorial approach

Треворович, В.-Э. В., & Kochetkov, S. N. (2017) · Biochemistry (Moscow) · doi:10.1134/s0006297917130107 · Cited by 4

Single-molecule FRET reveals proofreading complexes in the large fragment of Bacillus stearothermophilus DNA polymerase I

Christian, T. D., & Konigsberg, W. H. (2018) · AIMS Biophysics · doi:10.3934/biophy.2018.2.144 · Cited by 4

Val143 of human ribonuclease H2 is not critical for, but plays a role in determining catalytic activity and substrate specificity

Baba, M., Kojima, K., Nishimura, T., Sugiura, T., Takita, T., Uehara, R., Crouch, R. J., & Yasukawa, K. (2020) · PLoS ONE · doi:10.1371/journal.pone.0228774 · Cited by 4

Microbial Evolution and Emerging Diseases

Domingo, E. (2005) · Neurological disease and therapy · doi:10.1201/b14153-2 · Cited by 4

Structural Biology of Telomerase and Associated FactorsPreprint

Sekne, Z., Ludzia, P., Balch, S., & Nguyen, T. H. D. (2025) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a041697 · Cited by 5

The A, B, C, D’s of replicative DNA polymerase fidelity: utilizing high-throughput single-molecule sequencing to understand the molecular basis for DNA polymerase accuracy

Betancurt-Anzola, L., O’Connell, K. C., Potapov, V., Ong, J. L., Tanner, N. A., Sauguet, L., & Zatopek, K. M. (2025) · Nucleic Acids Research · doi:10.1093/nar/gkaf1143 · Cited by 3

The Coronavirus Replication–Transcription Complex

Madhugiri, R., Slanina, H., Saleem-Batcha, R., & Ziebuhr, J. (2026) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-052621-091439 · Cited by 3

Bst DNA Polymerase: Structure, Properties and Engineering Strategies in LAMP

Tikhonova, E. E., Popinako, A., & Sazonov, A. E. (2026) · International Journal of Molecular Sciences · doi:10.3390/ijms27104261 · Cited by 3

Structural features of DNA polymerases β and λ in complex with benzo[a]pyrene-adducted DNA cause a difference in lesion tolerance

Rechkunova, N. I., Zhdanova, P. V., Lebedeva, N. A., Maltseva, E. A., Koval, V. V., & Lavrik, O. I. (2022) · DNA repair · doi:10.1016/j.dnarep.2022.103353 · Cited by 3

Polymerase Synthesis of Base-Modified DNA

Daďová, J., Cahová, H., & Hocek, M. (2016) · Nucleic acids and molecular biology · doi:10.1007/978-3-319-27111-8_6 · Cited by 3

Modulation of RNA primer formation by Mn(II)-substituted T7 DNA primase

Ilic, S., Akabayov, S. R., Froimovici, R., Meiry, R., Vilenchik, D., Hernandez, A. J., Arthanari, H., & Akabayov, B. (2017) · Scientific Reports · doi:10.1038/s41598-017-05534-3 · Cited by 3

An Evolutionary/Biochemical Connection between Promoter- and Primer-Dependent Polymerases Revealed by Systematic Evolution of Ligands by Exponential Enrichment

Fenstermacher, K., Achuthan, V., Schneider, T. D., & DeStefano, J. J. (2018) · Journal of Bacteriology · doi:10.1128/jb.00579-17 · Cited by 3

Structural Articulation of Biochemical Reactions Using Restrained Geometries and Topology Switching

Manjari, S. R., & Banavali, N. K. (2018) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.7b00699 · Cited by 3

Role of Cations in RNA Folding and Function

Bowman, J. C., Petrov, A. S., & Williams, L. D. (2018) · CRC Press eBooks · doi:10.1201/b22230-30 · Cited by 3

Understanding the Effect of Multiple Domain Deletion in DNA Polymerase I from Geobacillus Sp. Strain SK72

Hadrawi, W. H., Norazman, A., Shariff, F. M., Ali, M. S. M., & Rahman, R. N. Z. R. A. (2020) · Catalysts · doi:10.3390/catal10080936 · Cited by 3

Heterozygous POLG variant Ser1181Asn co-segregating in a family with autosomal dominant axonal neuropathy, proximal muscle fatigability, ptosis, and ragged red fibers

Dohrn, M. F., Heller, C., Zengeler, D., Obermaier, C. D., Biskup, S., Weis, J., Nikolin, S., Claeys, K. G., Schöne, U., Beijer, D., et al. (2022) · Neurological Research and Practice · doi:10.1186/s42466-022-00169-w · Cited by 4

Cost-Efficient Sequence-Based Nonextensible Oligonucleotide in Real-Time PCR and High-Throughput Sequencing

Zhang, K., Song, P., Dai, P., Zhang, J. X., Wu, L. R., Cheng, L. Y., Pinto, A., Kwong, L. N., Cabrera, K., Wen, R., et al. (2022) · ACS Sensors · doi:10.1021/acssensors.2c00183 · Cited by 3

Prokaryotic Reverse Transcriptases

Lampson, B. C. (2007) · Springer eBooks · doi:10.1007/1-4020-5377-0_23 · Cited by 3

A molecular dynamics investigation of Taq DNA polymerase and its complex with a DNA substrate using a solid-state nanopore biosensor

Hu, G., Xi, G., Yan, H., Gao, Z., Wu, Z., Lu, Z., & Tu, J. (2022) · Physical Chemistry Chemical Physics · doi:10.1039/d2cp03993a · Cited by 3

DNA and RNA polymerases

Picarazzi, F., & Mori, M. (2023) · Elsevier eBooks · doi:10.1016/b978-0-12-823974-2.00011-5 · Cited by 4

Identification of a New Drug Binding Site in the RNA-Dependent-RNA-Polymerase (RdRp) Domain

Gana, A. S., & Baraniuk, J. N. (2023) · BioMedInformatics · doi:10.3390/biomedinformatics3040055 · Cited by 3

DNAzyme-powered nucleic acid release from solid supports

Cao, T., Wang, Y., Tao, Y., Zhang, L., Zhou, Y., Zhang, X., Heyman, J. A., & Weitz, D. A. (2019) · Chemical Communications · doi:10.1039/c9cc07790a · Cited by 3

Understanding the RNA-Specificity of HCV RdRp: Implications for Anti-HCV Drug Discovery

Kim, J. (2006) · Bulletin of the Korean Chemical Society · doi:10.5012/bkcs.2006.27.1.059 · Cited by 3

Single molecule sensing with carbon nanotube devices

Choi, Y., Sims, P. C., Olsen, T. J., Iftikhar, M., Corso, B. L., Gul, O. T., Weiss, G. A., & Collins, P. G. (2013) · Proceedings of SPIE, the International Society for Optical Engineering/Proceedings of SPIE · doi:10.1117/12.2025661 · Cited by 3

Domain motions of Klenow-like DNA polymerase I ITB-1 in the absence of substrate

Nurbaiti, S., Nagao, H., Saito, H., Hertadi, R., & Martoprawiro, M. A. (2010) · Cited by 3

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Kaufmann, G., & Nethanel, T. (2004) · Progress in nucleic acid research and molecular biology · doi:10.1016/s0079-6603(04)77005-1 · Cited by 3

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Goldman, A. D., Horst, J. A., Hung, L., & Samudrala, R. (2012) · Wiley-VCH eBooks · doi:10.1002/3527600906.mcb.200400157.pub2 · Cited by 3

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Kowalczyk, A. (2014) · doi:10.1002/9781118832738.ch1 · Cited by 3

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Johnson, K. A. (2008) · Wiley Encyclopedia of Chemical Biology · doi:10.1002/9780470048672.wecb609 · Cited by 3

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Sechi, M., Carcelli, M., Rogolino, D., & Neamati, N. (2011) · doi:10.1002/9781118015377.ch20 · Cited by 5

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Saccaggi, D. L. (2007) · UpSpace Institutional Repository (University of Pretoria) · Cited by 3

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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

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