The DOI matches its Crossref record; 30 of the 30 references it cites were found in a registry or an index.
DNA Polymerases: Structural Diversity and Common Mechanisms
Open accessAbstract
Possibly the earliest enzymatic activity to appear in evolution was that of the polynucleotide polymerases, the ability to replicate the genome accurately being a prerequisite for evolution itself. Thus, one might anticipate that the mechanism by which all polymerases work would be both simple and universal. Further, these enzymatic scribes must faithfully copy the sequences of the genome into daughter nucleic acid or the information contained within would be lost; thus some mechanism of assuring fidelity is required.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“Crystal structures (Refs.15-22 and references therein) reveal that polymerase binding to DNA strongly reshapes the primertemplate, e.g. the backbone at the templating base can be bent by 90°.”
From DNA Replication Fidelity (2004) · cites this paper as [17]
In the citing paper
“Polymerases in families A, B, X, and RT have nascent base pair binding pockets that tightly accommodate a correct Watson-Crick base pair (Fig. 2A and additional images in Refs.15-19 and references therein).”
From DNA Replication Fidelity (2004) · cites this paper as [17]
Citations
Cites
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
Self-citationHuang, 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
Self-citationJacobo-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
Beese, L. S., & Steitz, T. A. (1991) · The EMBO Journal · doi:10.1002/j.1460-2075.1991.tb07917.x · Cited by 1,059
Self-citationStructure 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
Self-citationSTRUCTURES 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
Self-citation
Cited by
Sorted by citations
Items 101–200 of 855
Pre-Steady-State Kinetic Studies of the Fidelity of Sulfolobus solfataricus P2 DNA Polymerase IV
Fiala, K. A., & Suo, Z. (2004) · Biochemistry · doi:10.1021/bi0357457 · Cited by 115
Frank, E. G., & Woodgate, R. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m702159200 · Cited by 115
Becerra, A., Delaye, L., Islas, S., & Lazcano, A. (2007) · Annual Review of Ecology, Evolution, and Systematics · doi:10.1146/annurev.ecolsys.38.091206.095825 · Cited by 115
Mechanism of DNA Polymerization Catalyzed by Sulfolobus solfataricus P2 DNA Polymerase IV
Fiala, K. A., & Suo, Z. (2004) · Biochemistry · doi:10.1021/bi035746z · Cited by 114
Poliovirus RNA-dependent RNA Polymerase (3Dpol)
Gohara, D. W., Crotty, S., Arnold, J. J., Yoder, J. D., Andino, R., & Cameron, C. E. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m002671200 · Cited by 113
Berdis, A. J. (2009) · Chemical Reviews · doi:10.1021/cr800530b · Cited by 113
Use of 2-Aminopurine and Tryptophan Fluorescence as Probes in Kinetic Analyses of DNA Polymerase β
Dunlap, C. A., & Tsai, M. (2002) · Biochemistry · doi:10.1021/bi025837g · Cited by 112
Structural Insight into Translesion Synthesis by DNA Pol II
Wang, F., & Yang, W. (2009) · Cell · doi:10.1016/j.cell.2009.11.043 · Cited by 112
Boulé, J.-B., Rougeon, F., & Papanicolaou, C. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m105272200 · Cited by 111
Zalatan, J. G., Fenn, T. D., & Herschlag, D. (2008) · Journal of Molecular Biology · doi:10.1016/j.jmb.2008.09.059 · Cited by 111
Structure of a bifunctional DNA primase-polymerase
Lipps, G., Weinzierl, A. O., von Scheven, G., Buchen, C., & Cramer, P. (2004) · Nature Structural & Molecular Biology · doi:10.1038/nsmb723 · Cited by 109
Coupled protein domain motion in Taq polymerase revealed by neutron spin-echo spectroscopy
Bu, Z., Biehl, R., Monkenbusch, M., Richter, D., & Callaway, D. J. E. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0503388102 · Cited by 107
Transmission of SARS-CoV-2 in free-ranging white-tailed deer in the United States
Feng, A., Bevins, S. N., Chandler, J. C., Deliberto, T. J., Ghai, R. R., Lantz, K., Lenoch, J. B., Retchless, A. C., Shriner, S. A., Tang, C. Y., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-39782-x · Cited by 112
Terminal Deoxynucleotidyl Transferase in the Synthesis and Modification of Nucleic Acids
Sarac, I., & Hollenstein, M. (2018) · ChemBioChem · doi:10.1002/cbic.201800658 · Cited by 105
Nováková, O. (2003) · Nucleic Acids Research · doi:10.1093/nar/gkg863 · Cited by 105
Delaney, W. E., LOCARNINI, S. A., & Shaw, T. (2001) · Antiviral chemistry & chemotherapy · doi:10.1177/095632020101200101 · Cited by 103
A novel type of replicative enzyme harbouring ATPase, primase and DNA polymerase activity
Lipps, G., Röther, S., Hart, C., & Krauss, G. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg246 · Cited by 102
Jácome, R., Becerra, A., de León, S. P., & Lazcano, A. (2015) · PLoS ONE · doi:10.1371/journal.pone.0139001 · Cited by 103
Inhibiting the HIV Integration Process: Past, Present, and the Future
Santo, R. D. (2013) · Journal of Medicinal Chemistry · doi:10.1021/jm400674a · Cited by 101
Jonsson, C. B., & Schmaljohn, C. S. (2001) · Current topics in microbiology and immunology · doi:10.1007/978-3-642-56753-7_2 · Cited by 99
The Crystal Structure of the RNA-Dependent RNA Polymerase from Human Rhinovirus
Love, R. A., Maegley, K. A., Yu, X., Ferre, R. A., Lingardo, L., Diehl, W. C., Parge, H. E., Dragovich, P. S., & Fuhrman, S. A. (2004) · Structure · doi:10.1016/j.str.2004.05.024 · Cited by 99
Interactions of Carcinogen-Bound DNA with Individual DNA Polymerases
Guengerich, F. P. (2006) · Chemical Reviews · doi:10.1021/cr0404693 · Cited by 99
Molecular mechanisms of HIV-1 resistance to nucleoside reverse transcriptase inhibitors (NRTIs)
Sluis-Cremer, N., Arion, D., & Parniak*, M. A. (2000) · Cellular and Molecular Life Sciences · doi:10.1007/pl00000626 · Cited by 117
Yang, X., Smidansky, E. D., Maksimchuk, K. R., Lum, D., Welch, J. L., Arnold, J. J., Cameron, C. E., & Boehr, D. D. (2012) · Structure · doi:10.1016/j.str.2012.06.012 · Cited by 102
de Jong, R. N., van der Vliet, P. C., & Brenkman, A. B. (2003) · Current topics in microbiology and immunology · doi:10.1007/978-3-662-05597-7_7 · Cited by 97
Sechi, M., Bacchi, A., Carcelli, M., Compari, C., Duce, E., Fisicaro, E., Rogolino, D., Gates, P. J., Derudas, M., Al‐Mawsawi, L. Q., et al. (2006) · Journal of Medicinal Chemistry · doi:10.1021/jm060193m · Cited by 95
DNA Polymerase θ: A Unique Multifunctional End-Joining Machine
Black, S., Kashkina, E., Kent, T., & Pomerantz, R. T. (2016) · Genes · doi:10.3390/genes7090067 · Cited by 101
Retrons, msDNA, and the bacterial genome
Lampson, B. C., Inouye, M., & Inouye, S. (2005) · Cytogenetic and Genome Research · doi:10.1159/000084982 · Cited by 94
RNA polymerase II structure: from core to functional complexes
Cramer, P. (2004) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2004.01.003 · Cited by 106
Structure-based Combinatorial Protein Engineering (SCOPE)
O’Maille, P. E., Bakhtina, M., & Tsai, M. (2002) · Journal of Molecular Biology · doi:10.1016/s0022-2836(02)00675-7 · Cited by 100
Structures, mechanism, regulation and evolution of class III nucleotidyl cyclases
Sinha, S. C., & Sprang, S. R. (2006) · Springer eBooks · doi:10.1007/112_0603 · Cited by 93
DNA damage reduces Taq DNA polymerase fidelity and PCR amplification efficiency
Sikorsky, J. A., Primerano, D. A., Fenger, T. W., & Denvir, J. (2007) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2007.01.169 · Cited by 92
Why magnetic and electromagnetic effects in biology are irreproducible and contradictory?
Buchachenko, A. L. (2015) · Bioelectromagnetics · doi:10.1002/bem.21947 · Cited by 91
Structure and Function of a Mycobacterial NHEJ DNA Repair Polymerase
Pitcher, R. S., Brissett, N. C., Picher, Á. J., Andrade, P. B., Juárez, R., Thompson, D., Fox, G. C., Blanco, L., & Doherty, A. J. (2006) · Journal of Molecular Biology · doi:10.1016/j.jmb.2006.10.046 · Cited by 90
Yang, L., Beard, W. A., Wilson, S. H., Broyde, S. B., & Tamar Schlick, A. (2002) · Journal of Molecular Biology · doi:10.1006/jmbi.2002.5450 · Cited by 90
A widespread class of reverse transcriptase-related cellular genes
Gladyshev, E. A., & Arkhipova, I. R. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1100266108 · Cited by 91
Structure–function studies of DNA polymerase lambda
García–Díaz, M., Bębenek, K., Gao, G., Pedersen, L. C., London, R. E., & Kunkel, T. A. (2005) · DNA repair · doi:10.1016/j.dnarep.2005.09.001 · Cited by 89
Duck Hepatitis B Virus: An Invaluable Model System for HBV Infection
Schultz, U., Grgacic, E. V. L., & Nassal, M. (2004) · Advances in virus research · doi:10.1016/s0065-3527(04)63001-6 · Cited by 88
DNA polymerases drive DNA sequencing-by-synthesis technologies: both past and present
Chen, C.-Y. (2014) · Frontiers in Microbiology · doi:10.3389/fmicb.2014.00305 · Cited by 88
Das, K., Sarafianos, S. G., Clark, A. D., Boyer, P. L., Hughes, S. H., & Arnold, E. (2006) · Journal of Molecular Biology · doi:10.1016/j.jmb.2006.08.097 · Cited by 88
Gardner, A. F. (2002) · Nucleic Acids Research · doi:10.1093/nar/30.2.605 · Cited by 89
Direct Detection and Sequencing of Damaged DNA Bases
Clark, T. A., Spittle, K. E., Turner, S. W., & Korlach, J. (2011) · Genome Integrity · doi:10.1186/2041-9414-2-10 · Cited by 88
Patra, A., Nagy, L. D., Zhang, Q., Su, Y. R., Müller, L., Guengerich, F. P., & Egli, M. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.551820 · Cited by 88
Wing, R. A., Bailey, S., & Steitz, T. A. (2008) · Journal of Molecular Biology · doi:10.1016/j.jmb.2008.07.058 · Cited by 87
Self-citationVariations on a theme: Eukaryotic Y-family DNA polymerases
Washington, M. T., Carlson, K. D., Freudenthal, B., & Pryor, J. M. (2009) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2009.07.004 · Cited by 90
Dima, R. I., & Thirumalai, D. (2006) · Protein Science · doi:10.1110/ps.051767306 · Cited by 87
Li, Y., & Waksman, G. (2001) · Protein Science · doi:10.1110/ps.250101 · Cited by 86
Engineering polymerases for applications in synthetic biology
Nikoomanzar, A., Chim, N., Yik, E. J., & Chaput, J. C. (2020) · Quarterly Reviews of Biophysics · doi:10.1017/s0033583520000050 · Cited by 87
Irimia, A., Eoff, R. L., Guengerich, F. P., & Egli, M. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.003905 · Cited by 85
Palm Mutants in DNA Polymerases α and η Alter DNA Replication Fidelity and Translesion Activity
Niimi, A., Limsirichaikul, S., Yoshida, S., Iwai, S., Masutani, C., Hanaoka, F., Kool, E. T., Nishiyama, Y., & Suzuki, M. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.7.2734-2746.2004 · Cited by 84
Raper, A. T., Reed, A. J., & Suo, Z. (2018) · Chemical Reviews · doi:10.1021/acs.chemrev.7b00685 · Cited by 83
Poole, A. M., & Logan, D. T. (2005) · Molecular Biology and Evolution · doi:10.1093/molbev/msi132 · Cited by 83
Jiang, H.-B., Holtz, L. R., Bauer, I. K., Franz, C. J., Zhao, G.-Y., Bodhidatta, L., Shrestha, S., Kang, G., & Wang, D. (2012) · Virology · doi:10.1016/j.virol.2012.09.040 · Cited by 83
Structural basis for substrate selection by the SARS-CoV-2 replicase
Malone, B. F., Perry, J. K., Olinares, P. D. B., Lee, H. W., Chen, J., Appleby, T. C., Feng, J. Y., Bilello, J. P., Ng, H., Sotiris, J., et al. (2023) · Nature · doi:10.1038/s41586-022-05664-3 · Cited by 86
Structure of a High Fidelity DNA Polymerase Bound to a Benzo[a]pyrene Adduct That Blocks Replication
Hsu, G. W., Huang, X., Luneva, N. P., Geacintov, N. E., & Beese, L. S. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m411276200 · Cited by 82
Visualizing polynucleotide polymerase machines at work
Steitz, T. (2006) · EMBO Journal · doi:10.1038/sj.emboj.7601211 · Cited by 83
Self-citationStructure and mechanism of human PrimPol, a DNA polymerase with primase activity
Rechkoblit, O., Gupta, Y. K., Malik, R., Rajashankar, K. R., Johnson, R. E., Prakash, L., Prakash, S., & Aggarwal, A. K. (2016) · Science Advances · doi:10.1126/sciadv.1601317 · Cited by 82
Herpesvirus DNA polymerases: Structures, functions and inhibitors
Zarrouk, K., Piret, J., & Boivin, G. (2017) · Virus Research · doi:10.1016/j.virusres.2017.01.019 · Cited by 81
Bauer, J., Xing, G., Yagi, H., Sayer, J. M., Jerina, D. M., & Ling, H. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0700717104 · Cited by 81
Bakhtina, M., Lee, S., Wang, Y., Dunlap, C. A., Lamarche, B. J., & Tsai, M. (2005) · Biochemistry · doi:10.1021/bi047664w · Cited by 80
Boudsocq, F. (2002) · DNA Repair · doi:10.1016/s1568-7864(02)00019-8 · Cited by 79
Viral and cellular interactions during adenovirus DNA replication
Charman, M., Herrmann, C., & Weitzman, M. D. (2019) · FEBS Letters · doi:10.1002/1873-3468.13695 · Cited by 82
Folding, Assembly, and Persistence: The Essential Nature and Origins of Biopolymers
Runnels, C. M., Lanier, K. A., Williams, J. K., Bowman, J. C., Petrov, A. S., Hud, N. V., & Williams, L. D. (2018) · Journal of Molecular Evolution · doi:10.1007/s00239-018-9876-2 · Cited by 79
Blanca, G., Shevelev, I., Ramadan, K., Villani, G., Spadari, S., Hübscher, U., & Maga, G. (2003) · Biochemistry · doi:10.1021/bi034198m · Cited by 78
Elongation-Competent Pauses Govern the Fidelity of a Viral RNA-Dependent RNA Polymerase
Dulin, D., Vilfan, I. D., Berghuis, B. A., Hage, S., Bamford, D. H., Poranen, M. M., Depken, M., & Dekker, N. H. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.01.031 · Cited by 76
Pyrophosphate hydrolysis is an intrinsic and critical step of the DNA synthesis reaction
Kottur, J., & Nair, D. T. (2018) · Nucleic Acids Research · doi:10.1093/nar/gky402 · Cited by 78
Structure of the Human Rev1–DNA–dNTP Ternary Complex
Swan, M. K., Johnson, R. E., Prakash, L., Prakash, S., & Aggarwal, A. K. (2009) · Journal of Molecular Biology · doi:10.1016/j.jmb.2009.05.026 · Cited by 76
How DNA polymerases catalyse replication and repair with contrasting fidelity
Wu, W.-J., Yang, W., & Tsai, M.-D. (2017) · Nature Reviews Chemistry · doi:10.1038/s41570-017-0068 · Cited by 76
The DNA-polymerase-X family: controllers of DNA quality?
Ramadan, K., Shevelev, I., & Hübscher, U. (2004) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1530 · Cited by 75
A Light‐Activated DNA Polymerase
Chou, C., Young, D. D., & Deiters, A. (2009) · Angewandte Chemie International Edition · doi:10.1002/anie.200901115 · Cited by 76
Fan, L., Kim, S., Farr, C. L., Schaefer, K. T., Randolph, K. M., Tainer, J. A., & Kaguni, L. S. (2006) · Journal of Molecular Biology · doi:10.1016/j.jmb.2006.02.073 · Cited by 75
Structural insight into recruitment of translesion DNA polymerase Dpo4 to sliding clamp PCNA
Xing, G., Kirouac, K. N., Shin, Y. J., Bell, S. D., & Ling, H. (2008) · Molecular Microbiology · doi:10.1111/j.1365-2958.2008.06553.x · Cited by 73
The DNA Polymerase _-Primase Complex: Multiple Functions and Interactions
Muzi-Falconi, M., Giannattasio, M., Foiani, M., & Plevani, P. (2003) · The Scientific World JOURNAL · doi:10.1100/tsw.2003.05 · Cited by 73
Mechanism of strand displacement synthesis by DNA replicative polymerases
Mañosas, M., Spiering, M. M., Ding, F., Bensimon, D., Allemand, J., Benkovic, S. J., & Croquette, V. (2012) · Nucleic Acids Research · doi:10.1093/nar/gks253 · Cited by 72
Observing Translesion Synthesis of an Aromatic Amine DNA Adduct by a High-fidelity DNA Polymerase
Hsu, G. W., Kiefer, J. R., Burnouf, D., Bécherel, O. J., Fuchs, R. P., & Beese, L. S. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m409224200 · Cited by 72
Temperature Dependence and Thermodynamics of Klenow Polymerase Binding to Primed-Template DNA
Datta, K., Wowor, A. J., Richard, A. J., & LiCata, V. J. (2005) · Biophysical Journal · doi:10.1529/biophysj.105.071837 · Cited by 72
Alley, S. C., Ishmael, F. T., Jones, A. D., & Benkovic, S. J. (2000) · Journal of the American Chemical Society · doi:10.1021/ja000591t · Cited by 72
Inhibition of Reverse Transcription In Vivo by Elevated Manganese Ion Concentration
Bolton, E. C., Mildvan, A. S., & Boeke, J. D. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00495-1 · Cited by 72
Inhibiting DNA Polymerases as a Therapeutic Intervention against Cancer
Berdis, A. J. (2017) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2017.00078 · Cited by 67
Mason, M. M., Schuller, A. P., & Skordalakes, E. (2010) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2010.11.005 · Cited by 71
Showalter, A. K., Lamarche, B. J., Bakhtina, M., Su, M., Tang, K., & Tsai, M. (2006) · Chemical Reviews · doi:10.1021/cr040487k · Cited by 71
Accuracy of lesion bypass by yeast and human DNA polymerase η
Washington, M. T., Johnson, R. E., Prakash, L., & Prakash, S. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.121007298 · Cited by 71
Gouge, J., Rosario, S., Félix, R., Béguin, P., & Delarue, M. H. (2013) · Journal of Molecular Biology · doi:10.1016/j.jmb.2013.07.009 · Cited by 70
Solution structure of a viral DNA polymerase X and evidence for a mutagenic function.
Showalter, A. K., Byeon, I. L., Su, M., & Tsai, M. (2001) · Nature Structural Biology · doi:10.1038/nsb1101-942 · Cited by 70
Idriss, H. T., Al‐Assar, O., & Wilson, S. H. (2002) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/s1357-2725(01)00131-5 · Cited by 69
Golosov, A. A., Warren, J. J., Beese, L. S., & Karplus, M. (2010) · Structure · doi:10.1016/j.str.2009.10.014 · Cited by 71
Radhakrishnan, R., Arora, K., Wang, Y., Beard, W. A., Wilson, S. H., & Tamar Schlick, A. (2006) · Biochemistry · doi:10.1021/bi061353z · Cited by 69
DNA Polymerase β Catalysis: Are Different Mechanisms Possible?
Alberts, I. L., Wang, Y., & Tamar Schlick, A. (2007) · Journal of the American Chemical Society · doi:10.1021/ja071533b · Cited by 69
Li, Y., Dutta, S., Doublié, S., Bdour, H. M., Taylor, J., & Ellenberger, T. (2004) · Nature Structural & Molecular Biology · doi:10.1038/nsmb792 · Cited by 69
Chinnaswamy, S., Yarbrough, I., Palaninathan, S. K., Ranjith-Kumar, C. T., Vijayaraghavan, V., Demeler, B., Lemon, S. M., Sacchettini, J. C., & Kao, C. C. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m801490200 · Cited by 68
Structural basis for processivity and antiviral drug toxicity in human mitochondrial DNA replicase
Szymański, M. R., Kuznetsov, V. B., Shumate, C. K., Meng, Q., Lee, Y., Patel, G., Patel, S. S., & Yin, Y. W. (2015) · The EMBO Journal · doi:10.15252/embj.201591520 · Cited by 69
Evolution of replication machines
Yao, N. Y., & O’Donnell, M. E. (2015) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409238.2015.1125845 · Cited by 68
Structure and mechanism of B-family DNA polymerase ζ specialized for translesion DNA synthesis
Malik, R., Kopylov, M., Gómez-Llorente, Y., Jain, R., Johnson, R. E., Prakash, L., Prakash, S., Ubarretxena‐Belandia, I., & Aggarwal, A. K. (2020) · Nature Structural & Molecular Biology · doi:10.1038/s41594-020-0476-7 · Cited by 67
Putative telomerase catalytic subunits from Giardia lamblia and Caenorhabditis elegans
Malik, H. S., Burke, W. D., & Eickbush, T. H. (2000) · Gene · doi:10.1016/s0378-1119(00)00207-9 · Cited by 68
Sigel, H. (2004) · Chemical Society Reviews · doi:10.1039/b310349h · Cited by 67
Kannan, S. R., Sachdev, S., Reddy, A. S., Kandasamy, S. L., Byrareddy, S. N., Lorson, C. L., & Singh, K. (2022) · Journal of Autoimmunity · doi:10.1016/j.jaut.2022.102928 · Cited by 65
Fiala, K. A., Abdel-Gawad, W., & Suo, Z. (2004) · Biochemistry · doi:10.1021/bi049975c · Cited by 66
Magnetic isotope and magnetic field effects on the DNA synthesis
Buchachenko, A. L., Orlov, A. P., Kuznetsov, D. A., & Breslavskaya, N. N. (2013) · Nucleic Acids Research · doi:10.1093/nar/gkt537 · Cited by 66
Telomere Lengthening and Other Functions of Telomerase
Rubtsova, M. P., Vasilkova, D. P., Malyavko, A. N., Нарайкина, Ю. В., Zvereva, M. I., & Донцова, О. А. (2012) · Acta Naturae · doi:10.32607/20758251-2012-4-2-44-61 · Cited by 66
Dpo4 is hindered in extending a G·T mismatch by a reverse wobble
Trincão, J., Johnson, R. E., Wolfle, W. T., Escalante, C. R., Prakash, S., Prakash, L., & Aggarwal, A. K. (2004) · Nature Structural & Molecular Biology · doi:10.1038/nsmb755 · Cited by 63
Metadata
- Authors
- Steitz, T. A.
- Affiliations
- Howard Hughes Medical Institute (US)
- Corresponding author
- Steitz, Thomas A.
- ORCID
- Steitz, Thomas A.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1999-06
- Volume
- 274
- Issue
- 25
- Pages
- 17395-17398
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2067371216
- Cited by
- 848
- References
- 30
- Citations by year
- 2026: 25 · 2025: 19 · 2024: 20 · 2023: 23 · 2022: 27 · 2021: 17 · 2020: 20 · 2019: 22 · 2018: 28 · 2017: 23 · 2016: 24 · 2015: 31 · 2014: 34 · 2013: 36 · 2012: 30
- FWCI
- 32.86
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA and Nucleic Acid Chemistry
- Keywords
- DNA polymerase, structural diversity, polymerase mechanism, DNA replication, replication fidelity, polynucleotide synthesis
- MeSH terms
- DNA, DNA-Directed DNA Polymerase, Escherichia coli, Metals, Models, Molecular, Templates, Genetic, Taq Polymerase, HIV Reverse Transcriptase
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review