Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Rad53 FHA domain associated with phosphorylated Rad9 in the DNA damage checkpoint.

Science (New York, N.Y.) - 10 Jul 1998

Sun Z, Hsiao J, Fay D S, Stern D F

Abstract excerpt

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,...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Amino Acid Sequence
Share to DNA Damage
Share to DNA Replication

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Fungal Proteins

Share to Mutation

Share to Phosphorylation

Share to Saccharomyces cerevisiae

Share to Saccharomyces cerevisiae Proteins

Source

Identifiers

PMID: 9657725
DOI: 10.1126/science.281.5374.272

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Rad53 FHA domain associated with phosphorylated Rad9 in the DNA damage checkpoint.PMID 9657725Read ↗

FHA domain-mediated DNA checkpoint regulation of Rad53.Semantic proximity Read ↗

Rad9 phosphorylation sites couple Rad53 to the Saccharomyces cerevisiae DNA damage checkpoint.Semantic proximity Read ↗

Rad53 kinase activation-independent replication checkpoint function of the N-terminal forkhead-associated (FHA1) domain.Semantic proximity Read ↗

Diverse but overlapping functions of the two forkhead-associated (FHA) domains in Rad53 checkpoint kinase activation.Semantic proximity Read ↗

Rad53 phosphorylation site clusters are important for Rad53 regulation and signaling.Semantic proximity Read ↗

Role of the N-terminal forkhead-associated domain in the cell cycle checkpoint function of the Rad53 kinase.Semantic proximity Read ↗

A domain of Rad9 specifically required for activation of Chk1 in budding yeast.Semantic proximity Read ↗

Association of Rad9 with double-strand breaks through a Mec1-dependent mechanism.Semantic proximity Read ↗

The budding yeast Rad9 checkpoint protein is subjected to Mec1/Tel1-dependent hyperphosphorylation and interacts with Rad53 after DNA damage.Semantic proximity Read ↗

Direct kinase-to-kinase signaling mediated by the FHA phosphoprotein recognition domain of the Dun1 DNA damage checkpoint kinase.Semantic proximity Read ↗

NFBD1, a Novel Nuclear Protein with Signature Motifs of FHA and BRCT, and an Internal 41-Amino Acid Repeat Sequence, Is an Early Participant in DNA Damage ResponseSemantic proximity Read ↗

The molecular basis of FHA domain:phosphopeptide binding specificity and implications for phospho-dependent signaling mechanisms.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.