Evidence map›Paper›PMID 11739777›Full record

ArticleMolecular biology of the cell2001

Structure-function analysis of fission yeast Hus1-Rad1-Rad9 checkpoint complex.

R Kaur, C F Kostrub, T Enoch

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
3.0field-weighted citation impact, top 8% 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

16 citing papers in PubMed, 49 citations in OpenAlex.

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  15. Molecular modeling-based analysis of interactions in the RFC-dependent clamp-loading process.Protein science : a publication of the Protein Society · 2002
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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

3 authors at 2 institutions in 1 country.

R KaurDepartment of Genetics, Harvard Medical School, Boston, MA 02115, USA. rkaur1@jhmi.edu
C F Kostrub
T Enoch
Harvard University · USJohns Hopkins University · US

Funding

MITOSIS COUPLING TO COMPLETION OF DNA REPLICATIONR01GM050015 · NIGMS · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI ENOCH, TAMAR L · 1993 to 2000
$355k
NIGMS NIH HHS GM-50015
6 · The paper itself

Abstract

Hus1, Rad1, and Rad9 are three evolutionarily conserved proteins required for checkpoint control in fission yeast. These proteins are known to form a stable complex in vivo. Recently, computational studies have predicted structural similarity between the individual proteins of Hus1-Rad1-Rad9 complex and the replication processivity factor proliferating cell nuclear antigen (PCNA). This has led to the proposal that the Hus1-Rad1-Rad9 complex may form a PCNA-like ring structure, and could function as a sliding clamp during checkpoint control. In the present study, we have attempted to test the predictions of this model by asking whether the PCNA alignment identifies functionally important residues or explains mutant phenotypes of hus1, rad1, or rad9 alleles. Although some of our results are consistent with the PCNA alignment, others indicate that the Hus1-Rad1-Rad9 complex possesses unique structural and functional features.

Indexed as

Cell CycleDNA-Binding ProteinsSchizosaccharomycesAllelesBlotting, WesternCell Cycle ProteinsEndonucleasesMacromolecular SubstancesMutationProliferating Cell Nuclear AntigenProtein BindingProtein Structure, TertiarySchizosaccharomyces pombe ProteinsSequence HomologyStructure-Activity RelationshipCell Cycle ProteinsDNA-Binding ProteinsEndonucleaseshus1 protein, S pombeMacromolecular SubstancesProliferating Cell Nuclear Antigenrad1 protein, S pomberad9 proteinSchizosaccharomyces pombe Proteins

Identifiers

PMID11739777
PMCPMC60752
OpenAlexW2157764677

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.