Evidence map›Paper›PMID 15326225›Full record

ArticleNucleic acids research2004

The human Rad9 checkpoint protein stimulates the carbamoyl phosphate synthetase activity of the multifunctional protein CAD.

Laura A Lindsey-Boltz, Eric M Wauson, Lee M Graves, Aziz Sancar

Open access · bronzeAbstract read
In one paragraph

Article in Nucleic acids research, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
0.8field-weighted citation impact, top 29% 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

20 citing papers in PubMed, 28 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Article
  6. Review
  7. Review
  8. Article
  9. Review
  10. A pathway map of glutamate metabolism.Journal of cell communication and signaling · 2016
    Article
  11. Article
  12. Review
  13. Contributions of Rad9 to tumorigenesis.Journal of cellular biochemistry · 2012
    Review
  14. The role of RAD9 in tumorigenesis.Journal of molecular cell biology · 2011
    Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article
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.

Laura A Lindsey-BoltzDepartment of Biochemistry and Biophysics, and Lineberger Comprehensive Cancer Center, University of North Carolina, Chapel Hill, NC 27599, USA.
Eric M Wauson
Lee M Graves
Aziz Sancar
University of North Carolina at Chapel Hill · US

Funding

STRUCTURE AND FUNCTION OF UVRABC EXCISION NUCLEASER01GM032833 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI SANCAR, AZIZ · 1985 to 2015
$8.9M
REGULATION OF CARBAMYL PHOSPH SYNTHETASES BY MAP KINASER01GM059767 · NIGMS · UNIVERSITY OF NORTH CAROLINA CHAPEL HILL · PI GRAVES, LEE M · 1999 to 2002
$608k
ANALYSIS OF HRAD17: A DNA DAMAGE CHECKPOINT PROTEINF32GM020830 · NIGMS · UNIVERSITY OF NORTH CAROLINA CHAPEL HILL · PI LINDSEY-BOLTZ, LAURA A · 2001 to 2002
$79k
NIGMS NIH HHS F32 GM020830NIGMS NIH HHS F32-GM20830NIGMS NIH HHS GM32833NIGMS NIH HHS R01 GM032833NIGMS NIH HHS R01-GM59767
6 · The paper itself

Abstract

The human Rad9 checkpoint protein is a subunit of the heterotrimeric Rad9-Rad1-Hus1 (9-1-1) complex that plays a role as a damage sensor in the DNA damage checkpoint response. Rad9 has been found to interact with several other proteins outside the context of the 9-1-1 complex with no obvious checkpoint functions. During our studies on the 9-1-1 complex, we found that Rad9 immunoprecipitates contained a 240 kDa protein that was identified as carbamoyl phosphate synthetase/aspartate transcarbamoylase/dihydroorotase (CAD), a multienzymatic protein required for the de novo synthesis of pyrimidine nucleotides and cell growth. Further investigations revealed that only free Rad9, but not Rad9 within the 9-1-1 complex, bound to CAD. The rate-limiting step in de novo pyrimidine nucleotide synthesis is catalyzed by the carbamoyl phosphate synthetase II (CPSase) domain of CAD. We find that Rad9 binds to the CPSase domain, and, moreover, this binding results in a 2-fold stimulation of the CPSase activity of CAD. Similar results were also obtained with an N-terminal Rad9 fragment. These findings suggest that Rad9 may play a role in ribonucleotide biosynthesis.

Indexed as

Aspartate CarbamoyltransferaseBinding SitesCarbamoyl-Phosphate Synthase (Glutamine-Hydrolyzing)Cell Cycle ProteinsCell LineDihydroorotaseEnzyme ActivationHumansMacromolecular SubstancesProtein Structure, TertiaryAspartate CarbamoyltransferaseCAD trifunctional enzymeCarbamoyl-Phosphate Synthase (Glutamine-Hydrolyzing)Cell Cycle ProteinsDihydroorotaseMacromolecular Substancesrad9 protein

Identifiers

PMID15326225
PMCPMC516061
OpenAlexW2135005899

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.