Evidence map›Paper›PMID 42393036›Full record

ReviewNature communications2026

Comparative analysis of Cdc48-dependent proteolysis at the ER, mitochondria and chloroplasts.

Anne Sophie Lau, Sreedhar Nellaepalli, R Paul Jarvis

Abstract readComparative StudyReview
In one paragraph

Review in Nature communications, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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.

Anne Sophie LauSection of Molecular Plant Biology, Department of Biology, University of Oxford, South Parks Road, Oxford, UK.
Sreedhar NellaepalliSection of Molecular Plant Biology, Department of Biology, University of Oxford, South Parks Road, Oxford, UK.ORCID 0000-0002-9402-6951
R Paul JarvisSection of Molecular Plant Biology, Department of Biology, University of Oxford, South Parks Road, Oxford, UK. paul.jarvis@biology.ox.ac.uk.ORCID 0000-0003-2127-5671

Funding

Biotechnology and Biological Sciences Research Council BB/Z516624/1 AND UKRI719RCUK | Biotechnology and Biological Sciences Research Council (BBSRC) BB/V007300/1, BB/W015021/1, BB/X000192/1, BB/Z516624/1, UKRI719
6 · The paper itself

Abstract

The ubiquitin-proteasome system (UPS) is the preeminent proteolytic system in eukaryotes. While soluble nucleocytosolic proteins are readily accessed by the UPS, organelle-localised proteins present major, membrane-related accessibility challenges. Cells overcome this problem by employing the conserved AAA+ ATPase Cdc48 to extract organellar proteins to the cytosol, thereby enabling proteasomal degradation. Major Cdc48-dependent proteolytic systems exist at the endoplasmic reticulum, mitochondria and chloroplasts, and are uniquely adapted to deliver protein homeostasis within the respective organelles. We provide a focused comparison of these systems, analysing similarities and differences between them. Better understanding of underlying principles has important implications spanning human health and agriculture.

Indexed as

ChloroplastsEndoplasmic ReticulumMitochondriaSaccharomyces cerevisiae ProteinsValosin Containing ProteinHumansProteasome Endopeptidase ComplexProteolysisSaccharomyces cerevisiaeCDC48 protein, S cerevisiaeProteasome Endopeptidase ComplexSaccharomyces cerevisiae ProteinsValosin Containing Protein

Identifiers

PMID42393036
PMCPMC13328587

What Socratic 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 Socratic graph.