Evidence map›Paper›PMID 10471701›Full record

ArticleGenetics1999

Pleiotropic defects caused by loss of the proteasome-interacting factors Rad23 and Rpn10 of Saccharomyces cerevisiae.

D Lambertson, L Chen, K Madura

Open access · bronzeAbstract read
In one paragraph

Article in Genetics, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 papers.

0numbers the graph read from it
0cells of the map it votes in
62citing papers in PubMed
3.4field-weighted citation impact, top 7% 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

62 citing papers in PubMed, 153 citations in OpenAlex.

  1. Review
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  12. Loss of RAD-23 Protects Against Models of Motor Neuron Disease by Enhancing Mutant Protein Clearance.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2015
    Article
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  19. Cdc48: a swiss army knife of cell biology.Journal of amino acids · 2013
    Review
  20. Article

2 more citing papers are in PubMed but not listed here.

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 1 institution in 1 country.

D LambertsonRobert Wood Johnson Medical School-UMDNJ, Piscataway, New Jersey 08854-5635, USA.
L Chen
K Madura
Johnson University · US

Funding

NIGMS NIH HHS GM52058
6 · The paper itself

Abstract

Rad23 is a member of a novel class of proteins that contain unprocessed ubiquitin-like (UbL) domains. We showed recently that a small fraction of Rad23 can form an interaction with the 26S proteasome. Similarly, a small fraction of Rpn10 is a component of the proteasome. Rpn10 can bind multiubiquitin chains in vitro, but genetic studies have not clarified its role in vivo. We report here that the loss of both Rad23 and Rpn10 results in pleiotropic defects that are not observed in either single mutant. rad23Delta rpn10Delta displays slow growth, cold sensitivity, and a pronounced G2/M phase delay, implicating overlapping roles for Rad23 and Rpn10. Although rad23Delta rpn10Delta displays similar sensitivity to DNA damage as a rad23Delta single mutant, deletion of RAD23 in rpn10Delta significantly increased sensitivity to canavanine, a phenotype associated with an rpn10Delta single mutant. A mutant Rad23 that is unable to bind the proteasome ((DeltaUbL)rad23) does not suppress the canavanine or cold-sensitive defects of rad23Delta rpn10Delta, demonstrating that Rad23/proteasome interaction is related to these effects. Finally, the accumulation of multiubiquitinated proteins and the stabilization of a specific proteolytic substrate in rad23Delta rpn10Delta suggest that proteasome function is altered.

Indexed as

Carrier ProteinsGene DeletionProteasome Endopeptidase ComplexSaccharomyces cerevisiae ProteinsCanavanineCell CycleCold TemperatureDNA-Binding ProteinsDNA RepairFungal ProteinsGenes, EssentialGenes, FungalGenetic Complementation TestPeptide HydrolasesPhenotypeProtein BindingATP dependent 26S proteaseCanavanineCarrier ProteinsDNA-Binding ProteinsFungal ProteinsPeptide HydrolasesProteasome Endopeptidase ComplexRAD23 protein, S cerevisiaeRecombinant Fusion ProteinsRepressor ProteinsRPN10 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsUbiquitins

Identifiers

PMID10471701
PMCPMC1460738
OpenAlexW2134108276

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.