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Cited by 347

The DOI matches its Crossref record; 24 of the 24 references it cites were found in a registry or an index.

HMG-domain proteins specifically inhibit the repair of the major DNA adduct of the anticancer drug cisplatin by human excision nuclease.

Open access
Huang, J C, Zamble, D B, Reardon, J T, Lippard, S J, Sancar, A·1994·Proceedings of the National Academy of Sciences

Abstract

The most frequent DNA adduct made by the anticancer drug cisplatin, the 1,2-intrastrand d(GpG) cross-link, as well as the minor 1,3-intrastrand d(GpTpG) adduct, were both repaired by an in vitro human excision repair system. Fragments of 27-29 nt containing the platinum damage were excised. The high mobility group (HMG)-domain proteins HMG1 and human mitochondrial transcription factor specifically inhibited repair of the 1,2-intrastrand cross-link by the human excision nuclease. These results suggest that the types and levels of HMG-domain proteins in a given tumor may influence the responsiveness of that cancer to cisplatin chemotherapy and they provide a rational basis for the synthesis of new platinum anticancer drug candidates.

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Metadata

Authors
Huang, J. C., Zamble, D. B., Reardon, J. T., Lippard, S. J., & Sancar, A.
Venue
Proceedings of the National Academy of Sciences
Published
1994-10-25
Volume
91
Issue
22
Pages
10394-10398
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
OpenAlex
W2022631460
Cited by
347
References
24
FWCI
5.39
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: HMG-domain proteins specifically inhibit the repair of the major DNA adduct of the anticancer drug cisplatin by human excision nuclease. https://app.cochat.ai/papers/10.1073/pnas.91.22.10394
The paper
Huang, J. C., Zamble, D. B., Reardon, J. T., Lippard, S. J., & Sancar, A. (1994). HMG-domain proteins specifically inhibit the repair of the major DNA adduct of the anticancer drug cisplatin by human excision nuclease. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.91.22.10394

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

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