The DOI matches its Crossref record; 7 of the 7 references it cites were found in a registry or an index.
The catalytic domain of avian sarcoma virus integrase: conformation of the active-site residues in the presence of divalent cations
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Citations
Cites
Dyda, F., Hickman, A. B., Jenkins, T. M., Engelman, A., Craigie, R., & Davies, D. R. (1994) · Science · doi:10.1126/science.7801124 · Cited by 810
HIV-1 DNA integration: Mechanism of viral DNA cleavage and DNA strand transfer
Engelman, A., Mizuuchi, K., & Craigie, R. (1991) · Cell · doi:10.1016/0092-8674(91)90297-c · Cited by 655
Crystal structure of the ribonuclease H domain of HIV-1 reverse transcriptase
Davies, J. F., Hostomska, Z., Hostomsky, Z., Jordan, S. R., & Matthews, D. A. (1991) · Science · doi:10.1126/science.1707186 · Cited by 570
Engelman, A., & Craigie, R. (1992) · Journal of Virology · doi:10.1128/jvi.66.11.6361-6369.1992 · Cited by 519
Three-dimensional structure of ribonuclease H from E. coli
Katayanagi, K., Miyagawa, M., Matsushima, M., Ishikawa, M., Kanaya, S., Ikehara, M., Matsuzaki, T., & Morikawa, K. (1990) · Nature · doi:10.1038/347306a0 · Cited by 349
Katzman, M., Katz, R. A., Skalka, A. M., & Leis, J. (1989) · Journal of Virology · doi:10.1128/jvi.63.12.5319-5327.1989 · Cited by 311
Self-citationRecombining the structures of HIV integrase, RuvC and RNase H
Yang, W., & Steitz, T. A. (1995) · Structure · doi:10.1016/s0969-2126(01)00142-3 · Cited by 246
Cited by
Recent Advances in Zinc Enzymology
Lipscomb, W. N., & Sträter, N. (1996) · Chemical Reviews · doi:10.1021/cr950042j · Cited by 1,366
INHIBITORS OF HIV-1 PROTEASE: A Major Success of Structure-Assisted Drug Design
Wlodawer, A., & Vondrasek, J. (1998) · Annual Review of Biophysics and Biomolecular Structure · doi:10.1146/annurev.biophys.27.1.249 · Cited by 734
Self-citationMetal Activation of Enzymes in Nucleic Acid Biochemistry
Cowan, J. A. (1998) · Chemical Reviews · doi:10.1021/cr960436q · Cited by 406
Grobler, J. A., Stillmock, K., Hu, B., Witmer, M., Felock, P., Espeseth, A. S., Wolfe, A., Egbertson, M., Bourgeois, M., Melamed, J., et al. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.092056199 · Cited by 399
Wang, J.-Y. (2001) · The EMBO Journal · doi:10.1093/emboj/20.24.7333 · Cited by 335
Metadata
- Authors
- Bujacz, G., Jaskólski, M., Alexandratos, J., Wlodawer, A., Merkel, G., Katz, R. A., & Skalka, A. M.
- Venue
- Structure
- Publisher
- Elsevier BV
- Published
- 1996-01
- Volume
- 4
- Issue
- 1
- Pages
- 89-96
- ISSN
- 0969-2126 (ISSN-L)
- OpenAlex
- W2074176676
- Cited by
- 170
- References
- 7
- FWCI
- 20.94
- Type
- journal article
- Language
- en
- Open access
- bronze
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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.
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How to cite
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- This page
- CoChat. (2026). Citation check: The catalytic domain of avian sarcoma virus integrase: conformation of the active-site residues in the presence of divalent cations. https://app.cochat.ai/papers/10.1016/s0969-2126(96)00012-3
- The paper
- Bujacz, G., Jaskólski, M., Alexandratos, J., Wlodawer, A., Merkel, G., Katz, R. A., & Skalka, A. M. (1996). The catalytic domain of avian sarcoma virus integrase: conformation of the active-site residues in the presence of divalent cations. Structure. https://doi.org/10.1016/s0969-2126(96)00012-3
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
