Evidence map›Paper›PMID 33388824›Full record

ReviewCurrent genetics2021

Cdc48/Shp1 participates in dissociation of protein complexes to regulate their activity.

Linda Lauinger, Karin Flick, Peter Kaiser

Abstract readReview
PubMed Full text at PMC Publisher
In one paragraph

Review in Current genetics, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.4field-weighted citation impact, top 46% 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

3 citing papers in PubMed, 4 citations in OpenAlex.

  1. Article
  2. Quality control of cytoplasmic proteins inside the nucleus.Computational and structural biotechnology journal · 2022
    Review
  3. HJournal of fungi (Basel, Switzerland) · 2021
    Article
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 1 institution in 1 country.

Linda LauingerDepartment of Biological Chemistry, School of Medicine, University of California Irvine, 240D Med Sci I, Irvine, CA 92697-1700, USA.
Karin FlickDepartment of Biological Chemistry, School of Medicine, University of California Irvine, 240D Med Sci I, Irvine, CA 92697-1700, USA.
Peter KaiserDepartment of Biological Chemistry, School of Medicine, University of California Irvine, 240D Med Sci I, Irvine, CA 92697-1700, USA. pkaiser@uci.edu.ORCID http://orcid.org/0000-0002-3326-0090
University of California, Irvine · US

Funding

Ubiquitin SignalingR01GM066164 · NIGMS · UNIVERSITY OF CALIFORNIA-IRVINE · PI KAISER, PETER · 2002 to 2022
$7.4M
Molecular concepts that monitor methionine metabolismR01GM128432 · NIGMS · UNIVERSITY OF CALIFORNIA-IRVINE · PI KAISER, PETER · 2018 to 2021
$1.3M
Regulation by Proteolysis-Independent UbiquitinationR56GM066164 · NIGMS · UNIVERSITY OF CALIFORNIA-IRVINE · PI KAISER, PETER · 2007 to 2007
$265k
NIGMS NIH HHS GM-066164NIGMS NIH HHS GM128432NIGMS NIH HHS R01 GM066164NIGMS NIH HHS R01 GM128432
6 · The paper itself

Abstract

The AAA-ATPase p97/Cdc48 is one of the most abundant proteins in eukaryotes, and owing to its multiple functions, is considered the swiss army knife of cells. Recent findings demonstrate that p97/Cdc48 and its cofactor p47/Shp1 control the heavy metal stress response by active, signal-triggered disassembly of a multisubunit ubiquitin ligase. Here we review this pathway and describe recently achieved mechanistic insight into the role of p47/Shp1 in this process.

Indexed as

Adenosine TriphosphateCell Cycle ProteinsIntracellular Signaling Peptides and ProteinsMultiprotein ComplexesProteasome Endopeptidase ComplexProtein BindingSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsUbiquitinValosin Containing ProteinAdenosine TriphosphateCDC48 protein, S cerevisiaeCell Cycle ProteinsIntracellular Signaling Peptides and ProteinsMultiprotein ComplexesProteasome Endopeptidase ComplexSaccharomyces cerevisiae ProteinsSHP1 protein, S cerevisiaeUbiquitinValosin Containing ProteinCadmium responseCdc48/p97SCF ubiquitin ligaseShp1/p47

Identifiers

PMID33388824
PMCPMC12674453
OpenAlexW3120136175

What OpenQuestion holds

Textmetadata
LicenceTDM
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.