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.
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“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
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Crystal structure of a bacteriophage T7 DNA replication complex at 2.2 Å resolution
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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
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Structure of large fragment of Escherichia coli DNA polymerase I complexed with dTMP
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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
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Signal Transduction in the Escherichia coli SOS Response
Beuning, P. J., & Walker, G. C. (2003) · Elsevier eBooks · doi:10.1016/b978-012124546-7/50661-6
The mechano-chemistry of a monomeric reverse transcriptasePreprint
Malik, O., Khamis, H., Rudnizky, S., & Kaplan, A. (2017) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/194159
Pal, S. (2019) · Elsevier eBooks · doi:10.1016/b978-0-12-814855-6.00008-0
Friedberg, E. C., Walker, G. C., Siede, W., Wood, R. D., Schultz, R. A., & Ellenberger, T. E. (2014) · ASM Press eBooks · doi:10.1128/9781555816704.ch3
Self-citationHosmane, R. S. (2003) · Wiley eBooks · doi:10.1002/0471238961.0114200918052201.a01.pub2 · Cited by 1
Li, Y., & Waksman, G. (2001) · Wiley eBooks · doi:10.1038/npg.els.0001043
Structural Features of Bypass Polymerases
Kisker, C. (2005) · CRC Press eBooks · doi:10.1201/9780849352683.ch25
Comparison of Bacterial and Eukaryotic Replisome Components
Yao, N. Y., & O’Donnell, M. E. (2022) · Elsevier eBooks · doi:10.1016/b978-0-12-821618-7.00097-3
Minimal Polymerase-Containing Precursor Required for Chikungunya Virus RNA Synthesis
Aponte-Diaz, D., Jain, A., Harris, J. M., Arnold, J. J., & Cameron, C. E. (2025) · Viruses · doi:10.3390/v17121556
Sawyer, D. L., Eckenroth, B. E., Chavira, C., Alnajjar, K. S., Hanley, J. P., Dragon, J. A., Doublié, S., & Sweasy, J. B. (2026) · Biochemistry · doi:10.1021/acs.biochem.5c00628
Self-citationYadav, L. R., Tiwari, P., Dubey, J. K., & Mande, S. C. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.06.02.729529
Hall, S. D., Cordero, C., Hashemian, M. H., Ngo, M. B., David, S. S., Roberts, S. A., Sweasy, J. B., & Doublié, S. (2026) · International Journal of Radiation Biology · doi:10.1080/09553002.2026.2686689
Self-citationMissoury, S., Lucas‐Staat, S., Sieskind, R., & Delarue, M. H. (2026) · Nucleic Acids Research · doi:10.1093/nar/gkag1018
BindingDB Entry 50037487: Control of hepatitis C: a medicinal chemistry perspective.
BindingDB (2012) · UC San Diego · doi:10.7270/q2xp75q1
BindingDB (2011) · UC San Diego · doi:10.7270/q29p31wh
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
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