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
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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Citations
Cites
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Cited by
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The ATM-Chk2-Cdc25A checkpoint pathway guards against radioresistant DNA synthesis
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Control of the DNA damage checkpoint by Chk1 and Rad53 protein kinases through distinct mechanisms
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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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- 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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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).
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