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Cited by 398

The DOI matches its Crossref record; 23 of the 23 references it cites were found in a registry or an index.

Rad53 FHA Domain Associated with Phosphorylated Rad9 in the DNA Damage Checkpoint

Sun, Zhaoxia, Hsiao, James, Fay, David S., Stern, David F.·1998·Science

Abstract

The Rad53 protein kinase of Saccharomyces cerevisiae is required for checkpoints that prevent cell division in cells with damaged or incompletely replicated DNA. The Rad9 protein was phosphorylated in response to DNA damage, and phosphorylated Rad9 interacted with the COOH-terminal forkhead homology–associated (FHA) domain of Rad53. Inactivation of this domain abolished DNA damage–dependent Rad53 phosphorylation, G 2 /M cell cycle phase arrest, and increase of RNR3 transcription but did not affect replication inhibition–dependent Rad53 phosphorylation. Thus, Rad53 integrates DNA damage signals by coupling with phosphorylated Rad9. The hitherto uncharacterized FHA domain appears to be a modular protein-binding domain.

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Metadata

Authors
Sun, Z., Hsiao, J., Fay, D. S., & Stern, D. F.
Venue
Science
Published
1998-07-10
Volume
281
Issue
5374
Pages
272-274
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W2011287943
Cited by
398
References
23
FWCI
12.61
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Rad53 FHA Domain Associated with Phosphorylated Rad9 in the DNA Damage Checkpoint. https://app.cochat.ai/papers/10.1126/science.281.5374.272
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Sun, Z., Hsiao, J., Fay, D. S., & Stern, D. F. (1998). Rad53 FHA Domain Associated with Phosphorylated Rad9 in the DNA Damage Checkpoint. Science. https://doi.org/10.1126/science.281.5374.272

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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.