Evidence map›Paper›PMID 25434464›Full record

ArticleNature cell biology2014

Rsp5/Nedd4 clears cells of heat-damaged proteins.

Thomas Sommer, Annika Weber, Ernst Jarosch

Abstract readComment
PubMed Publisher
In one paragraph

Article in Nature cell biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.3field-weighted citation impact, top 40% 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

5 citing papers in PubMed, 11 citations in OpenAlex.

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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

3 authors at 1 institution in 1 country.

Thomas SommerMax-Delbrück-Center for Molecular Medicine, Robert-Rössle-Str. 10, D-13125 Berlin, Germany.
Annika WeberMax-Delbrück-Center for Molecular Medicine, Robert-Rössle-Str. 10, D-13125 Berlin, Germany.
Ernst JaroschMax-Delbrück-Center for Molecular Medicine, Robert-Rössle-Str. 10, D-13125 Berlin, Germany.
Max Delbrück Center · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein quality control systems protect cells from proteotoxicity caused by the accumulation of aberrantly folded polypeptides. The Rsp5 ubiquitin ligase (mammalian homologue Nedd4) is now identified as a major constituent of a clearance pathway that degrades misfolded cytosolic proteins after exposure to heat.

Indexed as

Protein FoldingAnimalsEndosomal Sorting Complexes Required for TransportHeat-Shock ResponseHSP40 Heat-Shock ProteinsHumansNedd4 Ubiquitin Protein LigasesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsUbiquitin-Protein Ligase ComplexesUbiquitin-Protein LigasesEndosomal Sorting Complexes Required for TransportHSP40 Heat-Shock ProteinsNedd4 protein, humanNedd4 Ubiquitin Protein LigasesRSP5 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsUbiquitin-Protein Ligase ComplexesUbiquitin-Protein LigasesYDJ1 protein, S cerevisiae

Identifiers

PMID25434464
OpenAlexW2047749760

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.