Evidence map›Paper›PMID 41258083›Full record

ArticleNature communications2025

A UBH-UBX module amplifies p97/VCP's unfolding power to facilitate protein extraction and degradation.

Xin-Yu Huo, Di Liu, Rong Zou, Zhao-Peng Li, Yunxia Li, Lifeng Pan, Yaoyang Zhang, Zai-Rong Zhang

Abstract read
In one paragraph

Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing 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

9 citing papers in PubMed.

  1. Regulation of cellular proteostasis via mitochondrial protein import.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2026
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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

8 authors.

Xin-Yu Huo *Interdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, 100 Haike Road, Bldg. 13, Rm. 340, Pudong New District, Shanghai, China.
Di Liu *Interdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, 100 Haike Road, Bldg. 13, Rm. 340, Pudong New District, Shanghai, China.
Rong Zou *Interdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, 100 Haike Road, Bldg. 13, Rm. 340, Pudong New District, Shanghai, China.
Zhao-Peng LiInterdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, 100 Haike Road, Bldg. 13, Rm. 340, Pudong New District, Shanghai, China.
Yunxia LiInterdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, 100 Haike Road, Bldg. 13, Rm. 340, Pudong New District, Shanghai, China.ORCID http://orcid.org/0000-0001-6377-1281
Lifeng PanState Key Laboratory of Chemical Biology, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, Shanghai, China.ORCID http://orcid.org/0000-0002-9229-6288
Yaoyang ZhangInterdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, 100 Haike Road, Bldg. 13, Rm. 340, Pudong New District, Shanghai, China.ORCID http://orcid.org/0000-0001-5363-9834
Zai-Rong ZhangInterdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, 100 Haike Road, Bldg. 13, Rm. 340, Pudong New District, Shanghai, China. zrzhang@sioc.ac.cn.ORCID http://orcid.org/0000-0001-9768-0548

Funding

National Natural Science Foundation of China (National Science Foundation of China) 32270824National Natural Science Foundation of China (National Science Foundation of China) 32570911
6 · The paper itself

Abstract

The p97-UFD1L-NPLOC4 ATPase unfolds numerous proteins for proteasomal degradation, but whether it suffices to pull proteins out of lipid bilayer remains unclear. Here, we identify a conserved ubiquitin-binding helix (UBH) in many UBX-containing p97 adapters, including FAF2, across yeast, plants, and metazoans. The UBH-UBX substantially facilitates the engagement of ubiquitinated substrates with p97-UFD1L-NPLOC4, and enhances p97 motor's working ATPase and unfolding activities by approximately twofold. Using purified p97-UFD1L-NPLOC4-FAF2

Indexed as

Adenosine TriphosphatasesUbiquitinValosin Containing ProteinAdaptor Proteins, Signal TransducingAnimalsHumansMembrane ProteinsNuclear ProteinsProtein BindingProtein UnfoldingProteolysisSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsUbiquitinationAdaptor Proteins, Signal TransducingAdenosine TriphosphatasesMembrane ProteinsNPLOC4 protein, humanNuclear Proteinsp97 ATPaseSaccharomyces cerevisiae ProteinsUbiquitinValosin Containing ProteinVCP protein, human

Identifiers

PMID41258083
PMCPMC12630741

What OpenQuestion holds

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LicenceCC BY-NC-ND
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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.