The DOI matches its Crossref record; 24 of the 24 references it cites were found in a registry or an index.
An open and closed case for all polymerases
Open accessAbstract
The recently determined structures of HIV-1 reverse transcriptase and Taq DNA polymerase in complex with DNA primer-template and an incoming nucleotide have shown that a large conformational change configures the polymerase active site for nucleotidyl transfer. The structure of reverse transcriptase in the catalytic complex will open the path to the rational design of novel nucleoside analog inhibitors of viral replication.
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 [18]
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 [18]
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
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
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
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
Self-citationLi, 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
Self-citation
Cited by
Sorted by citations
Items 101–200 of 316
Savino, C., Federici, L., Johnson, K. A., Vallone, B., Nastopoulos, V., Rossi, M., Pisani, F. M., & Tsernoglou, D. (2004) · Structure · doi:10.1016/j.str.2004.09.007 · Cited by 56
In Silico Evidence for DNA Polymerase-β’s Substrate-Induced Conformational Change
Arora, K., & Tamar Schlick, A. (2004) · Biophysical Journal · doi:10.1529/biophysj.104.040915 · Cited by 55
Structural Basis for Dimerization and Activity of Human PAPD1, a Noncanonical Poly(A) Polymerase
Bai, Y., Srivastava, S. K., Chang, J. H., Manley, J. L., & Tong, L. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.01.013 · Cited by 54
Molecular Dynamics Study of the Opening Mechanism for DNA Polymerase I
Miller, B. R., Parish, C. A., & Wu, E. Y. (2014) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1003961 · Cited by 54
Yang, L., Beard, W. A., Wilson, S. H., Roux, B., Broyde, S. B., & Tamar Schlick, A. (2002) · Journal of Molecular Biology · doi:10.1016/s0022-2836(02)00617-4 · Cited by 53
Osheroff, W. P., Beard, W. A., Yin, S., Wilson, S. H., & Kunkel, T. A. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m003462200 · Cited by 54
Chinnaswamy, S., Murali, A., Li, P., Fujisaki, K., & Kao, C. C. (2010) · Journal of Virology · doi:10.1128/jvi.02446-09 · 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
Self-citationTarbouriech, N., Ducournau, C., Hutin, S., Mas, P. J., Man, P., Forest, É., Hart, D. J., Peyrefitte, C. N., Burmeister, W. P., & Iseni, F. (2017) · Nature Communications · doi:10.1038/s41467-017-01542-z · Cited by 51
Davey, M. J., & O’Donnell, M. E. (2000) · Current Opinion in Chemical Biology · doi:10.1016/s1367-5931(00)00134-4 · 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
Self-citationDiscovery of a small-molecule inhibitor that traps Polθ on DNA and synergizes with PARP inhibitors
Fried, W., Tyagi, M., Станиславович, М. Л., Chandramouly, G., Tredinnick, T., Ramanjulu, M. M., Auerbacher, W., Calbert, M. L., Rusanov, T., Hoàng, T., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-46593-1 · Cited by 53
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
Challenges at the frontiers of structural biology
Šali, A., & Kuriyan, J. (1999) · Trends in Cell Biology · doi:10.1016/s0962-8924(99)01685-2 · Cited by 49
Characterization of the Metal Ion Binding Properties of the Hepatitis C Virus RNA Polymerase
Bougie, I., Charpentier, S., & Bisaillon, M. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m209785200 · Cited by 48
How a homolog of high-fidelity replicases conducts mutagenic DNA synthesis
Lee, Y., Gao, Y., & Yang, W. (2015) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2985 · Cited by 48
Structural insights into eukaryotic DNA replication
Doublié, S., & Zahn, K. E. (2014) · Frontiers in Microbiology · doi:10.3389/fmicb.2014.00444 · Cited by 47
Self-citationProgress Toward a Semi-Synthetic Organism with an Unrestricted Expanded Genetic Alphabet
Dien, V. T., Holcomb, M., Feldman, A. W., Fischer, E. C., Dwyer, T. J., & Romesberg, F. E. (2018) · Journal of the American Chemical Society · doi:10.1021/jacs.8b08416 · Cited by 47
Yang, L., Beard, W. A., Wilson, S. H., Broyde, S. B., & Tamar Schlick, A. (2004) · Biophysical Journal · doi:10.1529/biophysj.103.036012 · Cited by 47
A unique error signature for human DNA polymerase ν
Arana, M. E., Takata, K., García–Díaz, M., Wood, R. D., & Kunkel, T. A. (2006) · DNA repair · doi:10.1016/j.dnarep.2006.09.012 · Cited by 46
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
Litosh, V. A., Wu, W., Stupi, B. P., Wang, J., Morris, S. E., Hersh, M. N., & Metzker, M. L. (2011) · Nucleic Acids Research · doi:10.1093/nar/gkq1293 · Cited by 46
Evans, G. W., Hohlbein, J., Craggs, T. D., Aigrain, L., & Kapanidis, A. N. (2015) · Nucleic Acids Research · doi:10.1093/nar/gkv547 · Cited by 45
A Unified Kinetic Mechanism Applicable to Multiple DNA Polymerases,
Bakhtina, M., Roettger, M. P., Kumar, S., & Tsai, M. (2007) · Biochemistry · doi:10.1021/bi700084w · Cited by 45
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
Bougie, I., & Bisaillon, M. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m308917200 · Cited by 44
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
Wu, S., Beard, W. A., Pedersen, L. G., & Wilson, S. H. (2013) · Chemical Reviews · doi:10.1021/cr3005179 · Cited by 46
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
Hold Tight (but Not Too Tight) to Get It Right
Brieba, L. G., & Ellenberger, T. (2003) · Structure · doi:10.1016/s0969-2126(02)00917-6 · Cited by 41
Self-citationThe Closing Mechanism of DNA Polymerase I at Atomic Resolution
Miller, B. R., Beese, L. S., Parish, C. A., & Wu, E. Y. (2015) · Structure · doi:10.1016/j.str.2015.06.016 · Cited by 40
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
Scholl, D., Adhya, S. L., & Merril, C. R. (2002) · Journal of Bacteriology · doi:10.1128/jb.184.10.2833-2836.2002 · Cited by 40
Tuning and switching a DNA polymerase motor with mechanical tension
Goel, A., Astumian, R. D., & Herschbach, D. R. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1033134100 · 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
Repasky, J. A. E., Corbett, E., Boboilă, C., & Schatz, D. G. (2004) · The Journal of Immunology · doi:10.4049/jimmunol.172.9.5478 · Cited by 40
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
Minnick, D. T., Liu, L., Grindley, N. D. F., Kunkel, T. A., & Joyce, C. M. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.032457899 · Cited by 37
Surface plasmon field-enhanced fluorescence spectroscopy studies of primer extension reactions
Stengel, G. (2005) · Nucleic Acids Research · doi:10.1093/nar/gni067 · Cited by 37
Structure and function relationships in mammalian DNA polymerases
Hoitsma, N. M., Whitaker, A. M., Schaich, M. A., Smith, M. R., Fairlamb, M. S., & Freudenthal, B. (2019) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-019-03368-y · Cited by 37
Perlow-Poehnelt, R. A., Likhterov, I., Scicchitano, D. A., Geacintov, N. E., & Broyde, S. B. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m404332200 · Cited by 35
Bermek, O., Grindley, N. D. F., & Joyce, C. M. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.167593 · Cited by 34
Multiple deprotonation paths of the nucleophile 3′-OH in the DNA synthesis reaction
Gregory, M., Gao, Y., Cui, Q., & Yang, W. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2103990118 · Cited by 27
Zhang, H., & Guengerich, F. P. (2009) · Journal of Molecular Biology · doi:10.1016/j.jmb.2009.11.071 · Cited by 32
Brenlla, A., Markiewicz, R. P., Rueda, D., & Romano, L. J. (2013) · Nucleic Acids Research · doi:10.1093/nar/gkt1149 · Cited by 33
Götte, M. (2006) · Current Pharmaceutical Design · doi:10.2174/138161206776873626 · Cited by 32
Molecular basis of transcriptional fidelity and DNA lesion-induced transcriptional mutagenesis
Xu, L., Da, L., Plouffe, S. W., Chong, J. P. C., Kool, E. T., & Wang, D. (2014) · DNA repair · doi:10.1016/j.dnarep.2014.03.024 · Cited by 32
Wang, L., Broyde, S. B., & Zhang, Y. (2009) · Journal of Molecular Biology · doi:10.1016/j.jmb.2009.04.029 · Cited by 31
Shivalingam, A., Tyburn, A. E. S., El-Sagheer, A. H., & Brown, T. P. (2017) · Journal of the American Chemical Society · doi:10.1021/jacs.6b11530 · Cited by 31
RETRACTED: Human DNA polymerase θ harbors DNA end-trimming activity critical for DNA repair
Zahn, K. E., Jensen, R. B., Wood, R. D., & Doublié, S. (2021) · Molecular Cell · doi:10.1016/j.molcel.2021.01.021 · Cited by 32
Self-citationRetractedFlorián, J., Warshel, A., & Goodman, M. F. (2002) · The Journal of Physical Chemistry B · doi:10.1021/jp020791m · Cited by 31
Genotyping of simple sequence repeat factors implicated in shadow band generation revisited
Olejniczak, M., & Krzyżosiak, W. J. (2006) · Electrophoresis · doi:10.1002/elps.200600136 · Cited by 31
DNA polymerase beta and other gap-filling enzymes in mammalian base excision repair
Beard, W. A., & Wilson, S. H. (2019) · The Enzymes · doi:10.1016/bs.enz.2019.08.002 · Cited by 30
Ligand-induced changes in hepatitis C virus NS5B polymerase structure
Rigat, K. L., Wang, Y., Hudyma, T. W., Ding, M., Zheng, X., Gentles, R. G., Beno, B. R., Gao, M., & Roberts, S. B. (2010) · Antiviral Research · doi:10.1016/j.antiviral.2010.08.014 · Cited by 30
Xu, L., Wang, W., Chong, J. P. C., Shin, J. H., Xu, J., & Wang, D. (2015) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409238.2015.1087960 · Cited by 28
Contribution of the Reverse Rate of the Conformational Step to Polymerase β Fidelity
Bakhtina, M., Roettger, M. P., & Tsai, M. (2009) · Biochemistry · doi:10.1021/bi802119f · Cited by 28
D’Abramo, C. M., Cellai, L., & Götte, M. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.01.030 · Cited by 27
Kumari, S., Chakraborty, S., Ahmad, M., Kumar, V., Tailor, P. B., & Biswal, B. K. (2022) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2022.12.252 · Cited by 26
RetractedBorden, J., Crans, D. C., & Florián, J. (2006) · The Journal of Physical Chemistry B · doi:10.1021/jp060168s · Cited by 27
Perlow, R. A., & Broyde, S. B. (2003) · Journal of Molecular Biology · doi:10.1016/s0022-2836(03)00187-6 · Cited by 27
Balbo, P., Toth, J., & Bohm, A. (2006) · Journal of Molecular Biology · doi:10.1016/j.jmb.2006.12.030 · Cited by 27
Substrate-induced DNA Polymerase β Activation
Beard, W. A., Shock, D. D., Batra, V. K., Prasad, R., & Wilson, S. H. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.607432 · Cited by 26
Mechanisms of Hepatitis B Virus Resistance Development
Warner, N., & LOCARNINI, S. A. (2014) · Intervirology · doi:10.1159/000360940 · Cited by 26
Gardner, A. F., Wang, J., Wu, W., Karouby, J., Li, H., Stupi, B. P., Jack, W. E., Hersh, M. N., & Metzker, M. L. (2012) · Nucleic Acids Research · doi:10.1093/nar/gks330 · Cited by 26
Back-priming mode of ϕ6 RNA-dependent RNA polymerase
Laurila, M. R. L., Salgado, P. S., Stuart, D. I., Grimes, J. M., & Bamford, D. H. (2005) · Journal of General Virology · doi:10.1099/vir.0.80492-0 · Cited by 26
Wang, X., Ma, L., Li, N., & Gao, N. (2023) · Molecular Cell · doi:10.1016/j.molcel.2023.10.038 · Cited by 24
Wu, E. Y., Walsh, A. R., Materne, E., Hiltner, E. P., Zielinski, B., Miller, B. R., Mawby, L., Modeste, E. S., Parish, C. A., Barnes, W. M., et al. (2014) · Biochemistry · doi:10.1021/bi501198f · Cited by 27
DNA polymerase β catalytic efficiency mirrors the Asn279–dCTP H‐bonding strength
Martínek, V., Bren, U., Goodman, M. F., Warshel, A., & Florián, J. (2007) · FEBS Letters · doi:10.1016/j.febslet.2007.01.042 · Cited by 25
Mechanism of Hepatitis C Virus RNA Polymerase Inhibition with Dihydroxypyrimidines
Powdrill, M. H., Deval, J., Narjes, F., Francesco, R. D., & Götte, M. (2009) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.01216-09 · Cited by 25
Nedumpully-Govindan, P., Monticelli, L., & Salonen, E. (2012) · The Journal of Physical Chemistry B · doi:10.1021/jp3046577 · Cited by 25
Maxwell, B. A., & Suo, Z. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.459982 · Cited by 24
Yang, Q., Nausch, L., Martin, G., Keller, W., & Doublié, S. (2013) · Journal of Molecular Biology · doi:10.1016/j.jmb.2013.09.025 · Cited by 24
Self-citationComputational Simulation Strategies for Analysis of Multisubunit RNA Polymerases
Wang, B., Feig, M., Cukier, R., & Burton, Z. (2013) · Chemical Reviews · doi:10.1021/cr400046x · Cited by 25
Kinetic Analysis of 3′–5′ Nucleotide Addition Catalyzed by Eukaryotic tRNAHis Guanylyltransferase
Smith, B. A., & Jackman, J. E. (2011) · Biochemistry · doi:10.1021/bi201397f · Cited by 25
Effect of Metal Ion Binding on the Structural Stability of the Hepatitis C Virus RNA Polymerase
Benzaghou, I., Bougie, I., & Bisaillon, M. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m409657200 · Cited by 24
Mechanisms of nucleotide selection by telomerase
Schaich, M. A., Sanford, S. L., Welfer, G. A., Johnson, S. A., Khoang, T. H., Opresko, P. L., & Freudenthal, B. (2020) · eLife · doi:10.7554/elife.55438 · Cited by 24
Federley, R., & Romano, L. J. (2010) · Journal of Nucleic Acids · doi:10.4061/2010/457176 · Cited by 23
Structural and Molecular Biology of a Protein-Polymerizing Nanomachine for Pilus Biogenesis
Waksman, G. (2017) · Journal of Molecular Biology · doi:10.1016/j.jmb.2017.05.016 · Cited by 23
Kinetic Mechanism of Active Site Assembly and Chemical Catalysis of DNA Polymerase β
Balbo, P., Wang, E. C.-W., & Tsai, M. (2011) · Biochemistry · doi:10.1021/bi200954r · Cited by 23
Replication across Template T/U by Human DNA Polymerase-ι
Jain, R., Nair, D. T., Johnson, R. E., Prakash, L., Prakash, S., & Aggarwal, A. K. (2009) · Structure · doi:10.1016/j.str.2009.04.011 · Cited by 22
Biological and Therapeutic Relevance of Nonreplicative DNA Polymerases to Cancer
Parsons, J. L., Nicolay, N. H., & Sharma, R. A. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.4203 · Cited by 24
Biochemical Activities of the HCV NS5B RNA-Dependent RNA Polymerase
Ranjith-Kumar, C. T., & Kao, C.-H. (2006) · Cited by 22
Insight into the mechanism of DNA synthesis by human terminal deoxynucleotidyltransferase
Кузнецова, А. А., Tyugashev, T. E., Alekseeva, I. V., Timofeyeva, N. A., Fedorova, O. S., & Kuznetsov, N. A. (2022) · Life Science Alliance · doi:10.26508/lsa.202201428 · Cited by 21
Vooradi, V., & Romano, L. (2009) · Biochemistry · doi:10.1021/bi9000722 · Cited by 21
Eckenroth, B. E., Towle-Weicksel, J. B., Sweasy, J. B., & Doublié, S. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.510891 · Cited by 20
Self-citationKao, & Chinnaswamy (2010) · Virus Adaptation and Treatment · doi:10.2147/vaat.s9641 · Cited by 20
DNA Polymerase θ: A Cancer Drug Target with Reverse Transcriptase Activity
Chen, X. S., & Pomerantz, R. T. (2021) · Genes · doi:10.3390/genes12081146 · Cited by 20
Role of the C-terminal Residue of the DNA Polymerase of Bacteriophage T7
Kumar, J. K., Tabor, S., & Richardson, C. C. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m104151200 · Cited by 20
Martín, M. J., García‐Ortiz, M. V., Gomez-Bedoya, A., Esteban, V., Guerra, S., & Blanco, L. (2013) · Nucleic Acids Research · doi:10.1093/nar/gkt681 · Cited by 21
Bartl, S., Miracle, A. L., Rumfelt, L. L., Kepler, T. B., Mochon, E., Litman, G. W., & Flajnik, M. F. (2003) · Immunogenetics · doi:10.1007/s00251-003-0608-3 · Cited by 21
Rappaport, H. P. (2004) · Biochemical Journal · doi:10.1042/bj20031776 · Cited by 20
Characterization of terminal deoxynucleotidyl transferase and polymerase μ in zebrafish
Beetz, S., Diekhoff, D., & Steiner, L. A. (2007) · Immunogenetics · doi:10.1007/s00251-007-0241-7 · Cited by 21
Cryo-EM structure of translesion DNA synthesis polymerase ζ with a base pair mismatch
Malik, R., Johnson, R. E., Prakash, L., Prakash, S., Ubarretxena‐Belandia, I., & Aggarwal, A. K. (2022) · Nature Communications · doi:10.1038/s41467-022-28644-7 · Cited by 19
Elucidation of kinetic mechanisms of human translesion DNA polymerase κ using tryptophan mutants
Zhao, L., Pence, M. G., Eoff, R. L., Yuan, S., Fercu, C. A., & Guengerich, F. P. (2014) · FEBS Journal · doi:10.1111/febs.12947 · Cited by 19
Garforth, S., Kim, T. W., Parniak, M. A., Kool, E. T., & Prasad, V. R. (2006) · Journal of Molecular Biology · doi:10.1016/j.jmb.2006.09.057 · Cited by 19
Expression and Structural Analyses of Human DNA Polymerase θ (POLQ)
Malaby, A. W., Martin, S. K., Wood, R. D., & Doublié, S. (2017) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2017.03.026 · Cited by 18
Self-citationWang, L., Wu, M., Yan, S. F., Patel, D. J., Geacintov, N. E., & Broyde, S. B. (2005) · Chemical Research in Toxicology · doi:10.1021/tx049786v · Cited by 17
Xu, L., Vaidyanathan, V. G., & Cho, B. P. (2014) · Chemical Research in Toxicology · doi:10.1021/tx500252z · Cited by 17
Metadata
- Authors
- Doublié, S., Sawaya, M. R., & Ellenberger, T.
- Affiliations
- University of Vermont (US)
- Harvard University (US)
- Corresponding author
- Ellenberger, Tom
- Venue
- Structure
- Publisher
- Elsevier BV
- Published
- 1999-02
- Volume
- 7
- Issue
- 2
- Pages
- R31-R35
- ISSN
- 0969-2126 (ISSN-L)
- OpenAlex
- W2036894316
- Cited by
- 314
- References
- 24
- Citations by year
- 2026: 4 · 2025: 4 · 2024: 8 · 2023: 5 · 2022: 6 · 2021: 7 · 2020: 6 · 2019: 4 · 2018: 6 · 2017: 11 · 2016: 9 · 2015: 8 · 2014: 19 · 2013: 13 · 2012: 8
- FWCI
- 13.72
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Structure (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
- Health Sciences › Medicine › Infectious Diseases › HIV/AIDS drug development and treatment
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Keywords
- polymerase active site, HIV-1 reverse transcriptase, Taq DNA polymerase, nucleotidyl transfer, conformational change, primer-template complex, rational drug design, polymerase structure
- MeSH terms
- Binding Sites, DNA-Directed DNA Polymerase, Models, Molecular, HIV-1, Protein Structure, Secondary, DNA Primers, 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