Evidence map›Paper›PMID 11500370›Full record

ArticleThe EMBO journal2001

Cic1, an adaptor protein specifically linking the 26S proteasome to its substrate, the SCF component Cdc4.

S Jäger, J Strayle, W Heinemeyer, D H Wolf

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

21 citing papers in PubMed, 47 citations in OpenAlex.

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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.

S JägerInstitut für Biochemie der Universität Stuttgart, Pfaffenwaldring 55, D-70569 Stuttgart, Germany.
J Strayle
W Heinemeyer
D H Wolf
Bayer (Germany) · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In eukaryotes, the ubiquitin-proteasome system plays a major role in selective protein breakdown for cellular regulation. Here we report the discovery of a new essential component of this degradation machinery. We found the Saccharomyces cerevisiae protein Cic1 attached to 26S proteasomes playing a crucial role in substrate specificity for proteasomal destruction. Whereas degradation of short-lived test proteins is not affected, cic1 mutants stabilize the F-box proteins Cdc4 and Grr1, substrate recognition subunits of the SCF complex. Cic1 interacts in vitro and in vivo with Cdc4, suggesting a function as a new kind of substrate recruiting factor or adaptor associated with the proteasome.

Indexed as

F-Box ProteinsProteasome Endopeptidase ComplexSaccharomyces cerevisiae ProteinsUbiquitin-Protein LigasesAmino Acid SequenceCarrier ProteinsCell Cycle ProteinsF-Box-WD Repeat-Containing Protein 7Fungal ProteinsHumansMolecular Sequence DataPeptide HydrolasesPeptide SynthasesSKP Cullin F-Box Protein LigasesSubstrate SpecificityUbiquitinsATP dependent 26S proteaseCarrier ProteinsCell Cycle ProteinsCic1 protein, S cerevisiaeF-Box ProteinsF-Box-WD Repeat-Containing Protein 7FBXW7 protein, humanFungal ProteinsGRR1 protein, S cerevisiaePeptide HydrolasesPeptide SynthasesProteasome Endopeptidase ComplexSaccharomyces cerevisiae ProteinsSKP Cullin F-Box Protein LigasesUbiquitin-Protein LigasesUbiquitins

Identifiers

PMID11500370
PMCPMC125261
OpenAlexW2008598849

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.