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 201–300 of 855
Structure–Function Studies of DNA Polymerase λ
Bębenek, K., Pedersen, L. C., & Kunkel, T. A. (2014) · Biochemistry · doi:10.1021/bi4017236 · Cited by 70
Nair, D. T., Johnson, R. E., Prakash, L., Prakash, S., & Aggarwal, A. K. (2006) · Structure · doi:10.1016/j.str.2006.01.010 · Cited by 65
Sosunov, V. V. (2005) · Nucleic Acids Research · doi:10.1093/nar/gki688 · Cited by 65
Weston, J. (2009) · Patai's chemistry of functional groups · doi:10.1002/9780470682531.pat0407 · Cited by 67
Liu, X., Yin, Y., Wu, J., & Liu, Z. (2014) · Nature Communications · doi:10.1038/ncomms5244 · Cited by 64
Using structural motif templates to identify proteins with DNA binding function
Jones, S. (2003) · Nucleic Acids Research · doi:10.1093/nar/gkg386 · Cited by 64
Nair, D. T., Johnson, R. E., Prakash, L., Prakash, S., & Aggarwal, A. K. (2008) · Structure · doi:10.1016/j.str.2007.12.009 · Cited by 64
Zhu, H., Nandakumar, J., Aniukwu, J., Wang, L., Glickman, M. S., Lima, C. D., & Shuman, S. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0509083103 · Cited by 63
Polymerization and editing modes of a high-fidelity DNA polymerase are linked by a well-defined path
Dodd, T., Botto, M. M., Paul, F., Fernández-Leiro, R., Lamers, M. H., & Ivanov, I. N. (2020) · Nature Communications · doi:10.1038/s41467-020-19165-2 · Cited by 62
Structural Mechanisms for Replicating DNA in Eukaryotes
Attali, I., Botchan, M. R., & Berger, J. M. (2021) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-090120-125407 · Cited by 65
Activation of Trans Geometry in Bifunctional Mononuclear Platinum Complexes by a Piperidine Ligand
Kašpárková, J., Nováková, O., Marini, V., Najajreh, Y., Gibson, D., Perez, J. M. G., & Brabec, V. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m304720200 · Cited by 62
Conformational Dynamics of DNA Polymerase Probed with a Novel Fluorescent DNA Base Analogue
Stengel, G., Gill, J. P., Sandin, P., Wilhelmsson, L. M., Albinsson, B., Nordén, B., & Millar, D. P. (2007) · Biochemistry · doi:10.1021/bi700755m · Cited by 61
The p12 Subunit of Human Polymerase δ Modulates the Rate and Fidelity of DNA Synthesis
Meng, X., Zhou, Y., Lee, E. Y. C., Lee, M., & Frick, D. N. (2010) · Biochemistry · doi:10.1021/bi100042b · Cited by 61
Structure of Human DNA Polymerase κ Inserting dATP Opposite an 8-OxoG DNA Lesion
Carpio, R. V., Silverstein, T. D., Lone, S., Swan, M. K., Choudhury, J. R., Johnson, R. E., Prakash, S., Prakash, L., & Aggarwal, A. K. (2009) · PLoS ONE · doi:10.1371/journal.pone.0005766 · Cited by 60
A new paradigm of DNA synthesis: three-metal-ion catalysis
Yang, W., Weng, P. J., & Gao, Y. (2016) · Cell & Bioscience · doi:10.1186/s13578-016-0118-2 · Cited by 60
Single-molecule microscopy reveals new insights into nucleotide selection by DNA polymerase I
Markiewicz, R. P., Vrtis, K. B., Rueda, D., & Romano, L. J. (2012) · Nucleic Acids Research · doi:10.1093/nar/gks523 · Cited by 59
Singh, A. K., & Das, K. (2022) · Viruses · doi:10.3390/v14051027 · Cited by 58
Bumps in the road: how replicative DNA polymerases see DNA damage
Hogg, M., Wallace, S. S., & Doublié, S. (2005) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2005.01.014 · Cited by 58
Y265H Mutator Mutant of DNA Polymerase β
Shah, A. M., Li, S., Anderson, K. S., & Sweasy, J. B. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m008680200 · Cited by 58
Stevens, D. R., & Hammes-Schiffer, S. (2018) · Journal of the American Chemical Society · doi:10.1021/jacs.8b05177 · Cited by 52
Enzyme screening with synthetic multifunctional pores: Focus on biopolymers
Sordé, N., Das, G. C., & Matile, S. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2132894100 · Cited by 56
Zhu, X. Q., & Ye, K. (2012) · FEBS Letters · doi:10.1016/j.febslet.2012.02.036 · Cited by 55
An Unexplored Diversity of Reverse Transcriptases in Bacteria
Zimmerly, S., & Wu, L. (2015) · Microbiology Spectrum · doi:10.1128/microbiolspec.mdna3-0058-2014 · Cited by 57
Mutations in human DNA polymerase η motif II alter bypass of DNA lesions
Glick, E., Vigna, K. L., & Loeb, L. A. (2001) · The EMBO Journal · doi:10.1093/emboj/20.24.7303 · Cited by 54
Domingo, E. (2007) · Wiley eBooks · doi:10.1002/9780470015902.a0000436.pub2 · Cited by 54
Kašpárková, J., Suchánková, T., Halámiková, A., Zerzánková, L., Vrána, O., Margiotta, N., Natile, G., & Brabec, V. (2009) · Biochemical Pharmacology · doi:10.1016/j.bcp.2009.09.019 · Cited by 54
Automated Structural Comparisons Clarify the Phylogeny of the Right-Hand-Shaped Polymerases
Mönttinen, H. A. M., Ravantti, J., Stuart, D. I., & Poranen, M. M. (2014) · Molecular Biology and Evolution · doi:10.1093/molbev/msu219 · Cited by 55
Polymerase-Directed Synthesis of 2‘-Deoxy-2‘-fluoro-β- D -arabinonucleic Acids
Peng, C. G., & Damha, M. J. (2007) · Journal of the American Chemical Society · doi:10.1021/ja069100g · Cited by 54
Structures of the Noncanonical RNA Ligase RtcB Reveal the Mechanism of Histidine Guanylylation
Desai, K. K., Bingman, C. A., Phillips, G. N., & Raines, R. T. (2013) · Biochemistry · doi:10.1021/bi4002375 · Cited by 53
DNA Adduct Structure–Function Relationships: Comparing Solution with Polymerase Structures
Broyde, S. B., Wang, L., Zhang, L., Rechkoblit, O., Geacintov, N. E., & Patel, D. J. (2007) · Chemical Research in Toxicology · doi:10.1021/tx700193x · Cited by 56
Jackman, J. E., & Phizicky, E. M. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0603068103 · Cited by 53
Lehmann, A. R. (2000) · Gene · doi:10.1016/s0378-1119(00)00250-x · Cited by 52
Tuning DNA “strings”: Modulating the rate of DNA replication with mechanical tension
Goel, A., Frank-Kamenetskii, M. D., Ellenberger, T., & Herschbach, D. R. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.151261198 · Cited by 52
Evolutionary innovations and the organization of protein functions in genotype space
Ferrada, E., & Wagner, A. (2010) · PLoS ONE · doi:10.1371/journal.pone.0014172 · Cited by 51
Turner, R. M., Grindley, N. D. F., & Joyce, C. M. (2003) · Biochemistry · doi:10.1021/bi026566c · Cited by 51
Ito, N., Nureki, O., Shirouzu, M., Yokoyama, S., & Hanaoka, F. (2003) · Genes to Cells · doi:10.1111/j.1365-2443.2003.00693.x · Cited by 51
Hyde, S. J., Eckenroth, B. E., Smith, B. A., Eberley, W. A., Heintz, N. H., Jackman, J. E., & Doublié, S. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1010436107 · Cited by 51
The Conserved Active Site Motif A of Escherichia coliDNA Polymerase I Is Highly Mutable
Shinkai, A., Patel, P. H., & Loeb, L. A. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m011472200 · Cited by 51
Structures of dNTP Intermediate States during DNA Polymerase Active Site Assembly
Freudenthal, B., Beard, W. A., & Wilson, S. H. (2012) · Structure · doi:10.1016/j.str.2012.08.008 · Cited by 50
Common structural features of nucleic acid polymerases
Cramer, P. (2002) · BioEssays · doi:10.1002/bies.10127 · Cited by 50
Current Developments in HIV Chemotherapy
Meadows, D. C., & Gervay‐Hague, J. (2005) · ChemMedChem · doi:10.1002/cmdc.200500026 · Cited by 50
RB69 DNA Polymerase Structure, Kinetics, and Fidelity
Xia, S., & Konigsberg, W. H. (2014) · Biochemistry · doi:10.1021/bi4014215 · Cited by 49
Bioinformatics and Molecular Modeling in Chemical Enzymology. Active Sites of Hydrolases
Varfolomeev, S. D., Uporov, I. V., & Fedorov, E. V. (2002) · Biochemistry (Moscow) · doi:10.1023/a:1020907122341 · Cited by 49
A proposal: Evolution of PCNA's role as a marker of newly replicated DNA
Georgescu, R. E., Langston, L. D., & O’Donnell, M. E. (2015) · DNA repair · doi:10.1016/j.dnarep.2015.01.015 · Cited by 48
The Replication System of Bacteriophage T7
Kulczyk, A., & Richardson, C. C. (2016) · The Enzymes · doi:10.1016/bs.enz.2016.02.001 · Cited by 48
Plant organellar DNA polymerases are replicative and translesion DNA synthesis polymerases
Baruch‐Torres, N., & Brieba, L. G. (2017) · Nucleic Acids Research · doi:10.1093/nar/gkx744 · Cited by 48
Masaoka, A., Terato, H., Kobayashi, M., Ohyama, Y., & Ide, H. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m008598200 · Cited by 47
Structural insights into eukaryotic DNA replication
Doublié, S., & Zahn, K. E. (2014) · Frontiers in Microbiology · doi:10.3389/fmicb.2014.00444 · Cited by 47
Quasispecies structure, cornerstone of hepatitis B virus infection: Mass sequencing approach
Rodríguez‐Frias, F. (2013) · World Journal of Gastroenterology · doi:10.3748/wjg.v19.i41.6995 · Cited by 47
Schauer, G. D., Huber, K. D., Leuba, S. H., & Sluis‐Cremer, N. (2014) · Nucleic Acids Research · doi:10.1093/nar/gku819 · Cited by 46
Francklyn, C. S. (2008) · Biochemistry · doi:10.1021/bi801500z · Cited by 46
Acidic Residues Critical for the Activity and Biological Function of Yeast DNA Polymerase η
Kondratick, C. M., Washington, M. T., Prakash, S., & Prakash, L. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.6.2018-2025.2001 · Cited by 46
HCV Genetic Variability: From Quasispecies Evolution to Genotype Classification
Argentini, C., Genovese, D., Dettori, S., & Rapicetta, M. (2009) · Future Microbiology · doi:10.2217/fmb.09.8 · Cited by 46
Accuracy, lesion bypass, strand displacement and translocation by DNA polymerases
Steitz, T. A., & Yin, Y. W. (2004) · Philosophical Transactions of the Royal Society B Biological Sciences · doi:10.1098/rstb.2003.1374 · Cited by 45
Self-citationDzantiev, L., Alekseyev, Y. O., Morales, J. C., Kool, E. T., & Romano, L. J. (2001) · Biochemistry · doi:10.1021/bi002569i · Cited by 45
Electronic Measurements of Single-Molecule Processing by DNA Polymerase I (Klenow Fragment)
Olsen, T. J., Choi, Y., Sims, P. C., Gul, O. T., Corso, B. L., Dong, C., Brown, W. A., Collins, P. G., & Weiss, G. A. (2013) · Journal of the American Chemical Society · doi:10.1021/ja311603r · Cited by 44
Marini, V. (2005) · Nucleic Acids Research · doi:10.1093/nar/gki884 · Cited by 44
Tchertanov, L., & Mouscadet, J. F. (2007) · Journal of Medicinal Chemistry · doi:10.1021/jm061375j · Cited by 44
Structural mechanism of LINE-1 target-primed reverse transcription
Ghanim, G. E., Hu, H., Boulanger, J., & Nguyen, T. H. D. (2025) · Science · doi:10.1126/science.ads8412 · Cited by 49
PCNA accelerates the nucleotide incorporation rate by DNA polymerase δ
Mondol, T., Stodola, J. L., Galletto, R., & Burgers, P. (2018) · Nucleic Acids Research · doi:10.1093/nar/gky1321 · Cited by 43
Structure and Function of RNA Polymerase II
Cramer, P. (2004) · Advances in protein chemistry · doi:10.1016/s0065-3233(04)67001-x · Cited by 43
Substrate-induced Conformational Fit and Headpiece Closure in the Ca2+ATPase (SERCA)
Ma, H., Inesi, G., & Toyoshima, C. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m304120200 · Cited by 43
Wang, Y., & Tamar Schlick, A. (2008) · Journal of the American Chemical Society · doi:10.1021/ja802215c · Cited by 42
Wu, S., Beard, W. A., Pedersen, L. G., & Wilson, S. H. (2013) · Chemical Reviews · doi:10.1021/cr3005179 · Cited by 46
Sharma, A. S., Kottur, J., Narayanan, N., & Nair, D. T. (2013) · Nucleic Acids Research · doi:10.1093/nar/gkt146 · Cited by 42
Programmed Allelic Mutagenesis of a DNA Polymerase with Single Amino Acid Resolution
Nikoomanzar, A., Vallejo, D., Yik, E. J., & Chaput, J. C. (2020) · ACS Synthetic Biology · doi:10.1021/acssynbio.0c00236 · Cited by 42
Graupner, M., Xu, H., & White, R. H. (2002) · Biochemistry · doi:10.1021/bi011937v · Cited by 42
In Vivo Mutagenesis by Escherichia coliDNA Polymerase I
Shinkai, A., & Loeb, L. A. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m104780200 · Cited by 42
Seifert, M., van Nies, P., Papini, F. S., Arnold, J. J., Poranen, M. M., Cameron, C. E., Depken, M., & Dulin, D. (2020) · Nucleic Acids Research · doi:10.1093/nar/gkaa233 · Cited by 40
Recent Insight into the Kinetic Mechanisms and Conformational Dynamics of Y-Family DNA Polymerases
Maxwell, B. A., & Suo, Z. (2014) · Biochemistry · doi:10.1021/bi5000405 · Cited by 41
RNA-dependent RNA polymerases of dsRNA bacteriophages
Makeyev, E. V., & Grimes, J. M. (2004) · Virus Research · doi:10.1016/j.virusres.2003.12.005 · Cited by 40
The Eukaryotic Replication Machine
Zhang, D., & O’Donnell, M. E. (2016) · The Enzymes · doi:10.1016/bs.enz.2016.03.004 · Cited by 39
Regulation and Modulation of Human DNA Polymerase δ Activity and Function
Lee, M., Wang, X., Zhang, S., Zhang, Z., & Lee, E. (2017) · Genes · doi:10.3390/genes8070190 · Cited by 42
Conservative transcription in three steps visualized in a double-stranded RNA virus
Cui, Y., Zhang, Y., Zhou, K., Sun, J., & Zhou, Z. H. (2019) · Nature Structural & Molecular Biology · doi:10.1038/s41594-019-0320-0 · Cited by 41
Dual role of the RNA substrate in selectivity and catalysis by terminal uridylyl transferases
Stagno, J. R., Aphasizheva, I., Aphasizhev, R., & Luecke, H. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0704259104 · Cited by 41
Crystallographic Analysis of a Novel Complex of Actinomycin D Bound to the DNA Decamer CGATCGATCG
Robinson, H. H., Gao, Y., Yang, X., Sanishvili, R., Joachimiak, A., & Wang, A. H. ‐. (2001) · Biochemistry · doi:10.1021/bi002859z · Cited by 41
Perlow, R. A., & Broyde, S. B. (2001) · Journal of Molecular Biology · doi:10.1006/jmbi.2001.4674 · Cited by 41
Human DNA Polymerase η Is Pre-Aligned for dNTP Binding and Catalysis
Ummat, A., Silverstein, T. D., Jain, R., Buku, A., Johnson, R. E., Prakash, L., Prakash, S., & Aggarwal, A. K. (2011) · Journal of Molecular Biology · doi:10.1016/j.jmb.2011.11.038 · Cited by 40
Structural and Molecular Kinetic Features of Activities of DNA Polymerases
Кузнецова, А. А., Fedorova, O. S., & Kuznetsov, N. A. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23126373 · Cited by 41
Dynamic mechanism of nick recognition by DNA ligase
Cherepanov, A. V., & de Vries, S. (2002) · European Journal of Biochemistry · doi:10.1046/j.1432-1033.2002.03309.x · Cited by 40
RNA-editing Terminal Uridylyl Transferase 1
Aphasizheva, I., Aphasizhev, R., & Simpson, L. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m401234200 · Cited by 40
Villani, G. (2002) · Nucleic Acids Research · doi:10.1093/nar/gkf463 · Cited by 40
Da, L., Chao, E., Duan, B., Zhang, C., Zhou, X., & Yu, J. H. (2015) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1004624 · Cited by 40
Computer simulation studies of the fidelity of DNA polymerases
Florián, J., Goodman, M. F., & Warshel, A. (2003) · Biopolymers · doi:10.1002/bip.10244 · Cited by 40
Chen, X., Qin, S., Chen, S., Li, J., Li, L., Wang, Z., Wang, Q., Lin, J., Yang, C., & Shui, W. (2015) · Scientific Reports · doi:10.1038/srep08361 · Cited by 41
Lior-Hoffmann, L., Wang, L., Wang, S., Geacintov, N. E., Broyde, S. B., & Zhang, Y. (2012) · Nucleic Acids Research · doi:10.1093/nar/gks653 · Cited by 39
Therminator DNA Polymerase: Modified Nucleotides and Unnatural Substrates
Gardner, A. F., Jackson, K. M., Boyle, M. M., Buss, J. A., Potapov, V., Gehring, A. M., Zatopek, K. M., Junior, I. R. C., Ong, J. L., & Jack, W. E. (2019) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2019.00028 · Cited by 42
Rungrotmongkol, T., Mulholland, A. J., & Hannongbua, S. (2006) · Journal of Molecular Graphics and Modelling · doi:10.1016/j.jmgm.2006.09.004 · Cited by 39
Comparative Kinetics of Nucleotide Analog Incorporation by Vent DNA Polymerase
Gardner, A. F., Joyce, C. M., & Jack, W. E. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m308286200 · Cited by 39
Functional Analysis of RNA Binding by the Hepatitis C Virus RNA-dependent RNA Polymerase
Kim, Y. C., Russell, W. K., Ranjith-Kumar, C. T., Thomson, M., Russell, D. H., & Kao, C. C. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m508145200 · Cited by 38
Zhang, H., Cao, W., Zakharova, E., Konigsberg, W. H., & Cruz, E. M. D. L. (2007) · Nucleic Acids Research · doi:10.1093/nar/gkm587 · Cited by 38
Bojin, M. D., & Tamar Schlick, A. (2007) · The Journal of Physical Chemistry B · doi:10.1021/jp071838c · Cited by 38
Human DNA polymerase α in binary complex with a DNA:DNA template-primer
y Coloma, J. P. D. S., Johnson, R. E., Prakash, L., Prakash, S., & Aggarwal, A. K. (2016) · Scientific Reports · doi:10.1038/srep23784 · Cited by 38
Bienstock, R. J., & Copeland, W. C. (2004) · Mitochondrion · doi:10.1016/j.mito.2004.05.018 · Cited by 38
Following replicative DNA synthesis by time-resolved X-ray crystallography
Chim, N., Meza, R. A., Trinh, A. M., Yang, K., & Chaput, J. C. (2021) · Nature Communications · doi:10.1038/s41467-021-22937-z · Cited by 34
Single-Molecule Study of DNA Polymerization Activity of HIV-1 Reverse Transcriptase on DNA Templates
Kim, S., Schroeder, C. M., & Xie, X. S. (2009) · Journal of Molecular Biology · doi:10.1016/j.jmb.2009.11.072 · Cited by 37
The three-component helicase/primase complex of herpes simplex virus-1
Bermek, O., & Williams, R. S. (2021) · Open Biology · doi:10.1098/rsob.210011 · Cited by 37
High-level expression and purification of untagged and histidine-tagged HIV-1 reverse transcriptase
Hou, E. W., Prasad, R., Beard, W. A., & Wilson, S. H. (2003) · Protein Expression and Purification · doi:10.1016/j.pep.2003.10.018 · Cited by 37
HIV-1 Integrase: From Biology to Chemotherapeutics
Loizidou, E. Z., Nicolaou, C. A., Nicolaides, A. V., & Kostrikis, L. G. (2007) · Current HIV Research · doi:10.2174/157016207781023965 · Cited by 37
Magnetic control of the DNA synthesis
Buchachenko, A. L., Orlov, A. P., Kuznetsov, D. A., & Breslavskaya, N. N. (2013) · Chemical Physics Letters · doi:10.1016/j.cplett.2013.07.056 · Cited by 37
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