Evidence map›Paper›PMID 12917350›Full record

ArticleMolecular and cellular biology2003

Rad53 phosphorylation site clusters are important for Rad53 regulation and signaling.

Soo-Jung Lee, Marc F Schwartz, Jimmy K Duong, David F Stern

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.

0numbers the graph read from it
0cells of the map it votes in
54citing papers in PubMed
2.8field-weighted citation impact, top 9% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

54 citing papers in PubMed, 106 citations in OpenAlex.

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  12. Activation of Tel1The Journal of biological chemistry · 2019
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 1 institution in 1 country.

Soo-Jung LeeDepartment of Pathology, Yale University School of Medicine, New Haven, Connecticut 06510,USA.
Marc F Schwartz
Jimmy K Duong
David F Stern
Yale University · US

Funding

Skill Development for Diverse Scientific Careers: A New Course Predoctoral Program in Cellular and Molecular BiologyT32GM007223 · NIGMS · YALE UNIVERSITY · PI BASERGA, SUSAN J · 1985 to 2019
$31.0M
PROTEIN KINASES IN YEAST DNA CHECKPOINT PATHWAYSR01CA082257 · NCI · YALE UNIVERSITY · PI STERN, DAVID F · 1999 to 2009
$2.3M
NCI NIH HHS R01 CA082257NCI NIH HHS R01CA82257NIGMS NIH HHS T32 GM007223NIGMS NIH HHS T32GM07223
6 · The paper itself

Abstract

Budding yeast Rad53 is an essential protein kinase that is phosphorylated and activated in a MEC1- and TEL1-dependent manner in response to DNA damage. We studied the role of Rad53 phosphorylation through mutation of consensus phosphorylation sites for upstream kinases Mec1 and Tel1. Alanine substitution of the Rad53 amino-terminal TQ cluster region reduced viability and impaired checkpoint functions. These substitution mutations spared the basal interaction with Asf1 and the DNA damage-induced interactions with Rad9. However, they caused a decrease in DNA damage-induced Rad53 kinase activity and an impaired interaction with the protein kinase Dun1. The Dun1 FHA (Forkhead-associated) domain recognized the amino-terminal TQ cluster of Rad53 after DNA damage or replication blockade. Thus, the phosphorylation of Rad53 by upstream kinases is important not only for Rad53 activation but also for creation of an interface between Rad53 and Dun1.

Indexed as

MAP Kinase Kinase 1Saccharomyces cerevisiae ProteinsAlanineAmino Acid SubstitutionBinding SitesCell Cycle ProteinsCheckpoint Kinase 2DNA DamageFungal ProteinsIntracellular Signaling Peptides and ProteinsMitogen-Activated Protein Kinase KinasesMutationPhosphorylationProtein KinasesProtein Serine-Threonine KinasesProtein Structure, TertiaryAlanineCell Cycle ProteinsCheckpoint Kinase 2DUN1 protein, S cerevisiaeFungal ProteinsIntracellular Signaling Peptides and ProteinsMAP Kinase Kinase 1Mek1 protein, S pombeMitogen-Activated Protein Kinase KinasesProtein KinasesProtein Serine-Threonine KinasesRAD53 protein, S cerevisiaerad9 proteinSaccharomyces cerevisiae ProteinsSchizosaccharomyces pombe ProteinsTEL1 protein, S cerevisiaetel1 protein, S pombe

Identifiers

PMID12917350
PMCPMC180918
OpenAlexW2161460305

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.