Evidence map›Paper›PMID 30675527›Full record

ArticleCommunications biology2019

The Cdc48 unfoldase prepares well-folded protein substrates for degradation by the 26S proteasome.

Michal M Olszewski, Cameron Williams, Ken C Dong, Andreas Martin

Open access · goldAbstract read
In one paragraph

Article in Communications biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 89 papers.

0numbers the graph read from it
0cells of the map it votes in
89citing papers in PubMed
6.5field-weighted citation impact, top 2% 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

89 citing papers in PubMed, 137 citations in OpenAlex.

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29 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

4 authors at 1 institution in 1 country.

Michal M Olszewski1Department of Molecular and Cell Biology, University of California, Berkeley, CA 94720 USA.
Cameron Williams1Department of Molecular and Cell Biology, University of California, Berkeley, CA 94720 USA.
Ken C Dong1Department of Molecular and Cell Biology, University of California, Berkeley, CA 94720 USA.
Andreas Martin1Department of Molecular and Cell Biology, University of California, Berkeley, CA 94720 USA.ORCID 0000-0003-0923-3284
QB3 · US

Funding

MOLECULAR BIOPHYSICS TRAINING GRANTT32GM008295 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI HURLEY, JAMES H, WEMMER, DAVID E · 1989 to 2022
$8.1M
ATP-Dependent Protein Unfolding and Translocation by the Eukaryotic ProteasomeR01GM094497 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI MARTIN, ANDREAS · 2011 to 2024
$3.7M
Howard Hughes Medical InstituteNIGMS NIH HHS R01 GM094497NIGMS NIH HHS T32 GM008295
6 · The paper itself

Abstract

Cdc48/p97 is an essential and highly conserved AAA+ ATPase that uses its protein-unfoldase activity to extract ubiquitinated polypeptides from macromolecular complexes and membranes. This motor has also been implicated in protein-degradation pathways, yet its exact role in acting upstream of the 26S proteasome remains elusive. Ubiquitinated proteins destined for degradation by the proteasome require an unstructured initiation region to engage with the proteasomal translocation machinery, and Cdc48 was proposed to generate these unfolded segments, yet direct evidence has been missing. Here, we used an in vitro reconstituted system to demonstrate the collaboration of Cdc48 and the 26S proteasome from

Indexed as

Protein FoldingProtein UnfoldingModels, BiologicalProteasome Endopeptidase ComplexProtein BindingProteolysisSubstrate SpecificityUbiquitinValosin Containing ProteinATP dependent 26S proteaseProteasome Endopeptidase ComplexUbiquitinValosin Containing Protein

Identifiers

PMID30675527
PMCPMC6340886
OpenAlexW2908579890

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.