The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
XRCC1 Polypeptide Interacts with DNA Polymerase and Possibly Poly (ADP-Ribose) Polymerase, and DNA Ligase III Is a Novel Molecular 'Nick-Sensor' In Vitro
Open accessAbstract
The DNA repair proteins XRCC1 and DNA ligase III are physically associated in human cells and directly interact in vitro and in vivo. Here, we demonstrate that XRCC1 is additionally associated with DNA polymerase-beta in human cells and that these polypeptides also directly interact. We also present data suggesting that poly (ADP-ribose) polymerase can interact with XRCC1. Finally, we demonstrate that DNA ligase III shares with poly (ADP-ribose) polymerase the novel function of a molecular DNA nick-sensor, and that the DNA ligase can inhibit activity of the latter polypeptide in vitro. Taken together, these data suggest that the activity of the four polypeptides described above may be co-ordinated in human cells within a single multiprotein complex.
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Citations
Cites
Excision of Deoxyribose Phosphate Residues by DNA Polymerase β During DNA Repair
Matsumoto, Y., & Kim, K. (1995) · Science · doi:10.1126/science.7624801 · Cited by 683
Masutani, C., Sugasawa, K., Yanagisawa, J., Sonoyama, T., Ui, M., Enomoto, T., Takio, K., Tanaka, K., van der Spek, P. J., & Bootsma, D. (1994) · The EMBO Journal · doi:10.1002/j.1460-2075.1994.tb06452.x · Cited by 400
Cited by
Advances in autism genetics: on the threshold of a new neurobiology
Abrahams, B. S., & Geschwind, D. H. (2008) · Nature Reviews Genetics · doi:10.1038/nrg2346 · Cited by 1,866
New insights into the molecular and cellular functions of poly(ADP-ribose) and PARPs
Gibson, B. A., & Kraus, W. L. (2012) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3376 · Cited by 1,226
El-Khamisy, S. F. (2003) · Nucleic Acids Research · doi:10.1093/nar/gkg761 · Cited by 659
Whitehouse, C. J., Taylor, R. M., Thistlethwaite, A., Zhang, H., Karimi-Busheri, F., Lasko, D. D., Weinfeld, M., & Caldecott, K. W. (2001) · Cell · doi:10.1016/s0092-8674(01)00195-7 · Cited by 608
Self-citationMammalian DNA double-strand break repair protein XRCC4 interacts with DNA ligase IV
Critchlow, S. E., Bowater, R. P., & Jackson, S. P. (1997) · Current Biology · doi:10.1016/s0960-9822(06)00258-2 · Cited by 470
Metadata
- Authors
- Caldecott, K. W., Aoufouchi, S., Johnson, P., & Shall, S.
- Venue
- Nucleic Acids Research
- Publisher
- Oxford University Press (OUP)
- Published
- 1996-11-01
- Volume
- 24
- Issue
- 22
- Pages
- 4387-4394
- ISSN
- 0305-1048 (ISSN-L)
- 1362-4962
- OpenAlex
- W2134831636
- Cited by
- 620
- References
- 2
- FWCI
- 6.80
- Type
- journal article
- Language
- en
- Open access
- bronze
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- CoChat. (2026). Citation check: XRCC1 Polypeptide Interacts with DNA Polymerase and Possibly Poly (ADP-Ribose) Polymerase, and DNA Ligase III Is a Novel Molecular 'Nick-Sensor' In Vitro. https://app.cochat.ai/papers/10.1093/nar/24.22.4387
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- Caldecott, K. W., Aoufouchi, S., Johnson, P., & Shall, S. (1996). XRCC1 Polypeptide Interacts with DNA Polymerase and Possibly Poly (ADP-Ribose) Polymerase, and DNA Ligase III Is a Novel Molecular 'Nick-Sensor' In Vitro. Nucleic Acids Research. https://doi.org/10.1093/nar/24.22.4387
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