Evidence map›Paper›PMID 26945625›Full record

ReviewGene2016

Structure and function of the AAA+ ATPase p97/Cdc48p.

Di Xia, Wai Kwan Tang, Yihong Ye

Abstract readReview
In one paragraph

Review in Gene, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 111 papers.

0numbers the graph read from it
0cells of the map it votes in
111citing papers in PubMed
14.6field-weighted citation impact, top 1% 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

111 citing papers in PubMed, 162 citations in OpenAlex.

  1. Review
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  15. Article
  16. Allosteric activation of VCP, an AAA unfoldase, by small molecule mimicry.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  17. Article
  18. Article
  19. Article
  20. Article

51 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

3 authors at 2 institutions in 1 country.

Di XiaLaboratory of Cell Biology, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892, United States. Electronic address: xiad@mail.nih.gov.
Wai Kwan TangLaboratory of Cell Biology, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892, United States.
Yihong YeLaboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, United States. Electronic address: yihongy@mail.nih.gov.
National Institutes of Health · USCenter for Cancer Research · US

Funding

Study of AAA proteins by X-ray protein crystallographyZIABC010600 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI XIA, DI S · 2009 to 2025
$6.8M
The Gene Wiki: Community intelligence applied to gene annotationR01GM089820 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI SU, ANDREW I · 2010 to 2021
$5.2M
Study of AAA proteins by X-ray protein crystallographyZ01BC010600 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI XIA, DI S · 2004 to 2008
$330k
Intramural NIH HHS Z01 BC010600NIGMS NIH HHS GM089820NIGMS NIH HHS R01 GM089820
6 · The paper itself

Abstract

p97 (also known as valosin-containing protein (VCP) in mammals or Cdc48p in Saccharomyces cerevisiae) is an evolutionarily conserved ATPase present in all eukaryotes and archaebacteria. In conjunction with a collection of cofactors and adaptors, p97/Cdc48p performs an array of biological functions mostly through modulating the stability of 'client' proteins. Using energy from ATP hydrolysis, p97/Cdc48p segregates these molecules from immobile cellular structures such as protein assemblies, membrane organelles, and chromatin. Consequently, the released polypeptides can be efficiently degraded by the ubiquitin proteasome system or recycled. This review summarizes our current understanding of the structure and function of this essential cellular chaperoning system.

Indexed as

Adenosine TriphosphatasesAdenosine TriphosphateAnimalsCell Cycle ProteinsChromatinHomeostasisHumansHydrolysisMembrane FusionMiceMolecular Targeted TherapyMutationNeoplasmsProtein ConformationSaccharomyces cerevisiae ProteinsValosin Containing ProteinAdenosine TriphosphatasesAdenosine TriphosphateCDC48 protein, S cerevisiaeCell Cycle ProteinsChromatinSaccharomyces cerevisiae ProteinsValosin Containing ProteinVCP protein, humanVcp protein, mouseAAA+ ATPaseChromatin-associated degradationER-associated degradationMembrane fusionMitochondria-associated degradationp97/CDC48ProteasomeProtein quality controlRibosome-associated degradationSegregaseUbiquitinUnfoldase

Identifiers

PMID26945625
PMCPMC4821690
OpenAlexW2293268779

What OpenQuestion holds

Textmetadata
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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.