Evidence map›Paper›PMID 22245831›Full record

ReviewSeminars in cell & developmental biology2012

Selective destruction of abnormal proteins by ubiquitin-mediated protein quality control degradation.

Eric K Fredrickson, Richard G Gardner

Abstract readReview
In one paragraph

Review in Seminars in cell & developmental biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing 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

38 citing papers in PubMed.

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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

2 authors.

Eric K FredricksonDepartment of Pharmacology, University of Washington, Seattle, WA 98195, USA.
Richard G Gardner

Funding

Pharmacological Sciences SupplementT32GM007750 · NIGMS · UNIVERSITY OF WASHINGTON · PI ATKINS, WILLIAM M · 1985 to 2023
$12.6M
Identifying and characterizing protein quality control mechanisms in the nucleusR01AG031136 · NIA · UNIVERSITY OF WASHINGTON · PI GARDNER, RICHARD GEORGE · 2009 to 2013
$1.6M
Discovery of ubiquitin ligase substrates - the development of integrated experimeR21RR025787 · NCRR · UNIVERSITY OF WASHINGTON · PI GARDNER, RICHARD GEORGE, RANDOLPH, TIMOTHY W · 2009 to 2010
$616k
NCRR NIH HHS R21 RR025787NCRR NIH HHS R21RR025787NIA NIH HHS R01 AG031136NIA NIH HHS R01AG031136NIGMS NIH HHS 5T32GM007750NIGMS NIH HHS T32 GM007750
6 · The paper itself

Abstract

Misfolded proteins are continuously produced in the cell and present an escalating detriment to cellular physiology if not managed effectively. As such, all organisms have evolved mechanisms to address misfolded proteins. One primary way eukaryotic cells handle the complication of misfolded proteins is by destroying them through the ubiquitin-proteasome system. To do this, eukaryotes possess specialized ubiquitin-protein ligases that have the capacity to recognize misfolded proteins over normally folded proteins. The strategies used by these Protein Quality Control (PQC) ligases to target the wide variety of misfolded proteins in the cell will likely be different than those used by ubiquitin-protein ligases that function in regulated degradation to target normally folded proteins. In this review, we highlight what is known about how misfolded proteins are recognized by PQC ubiquitin-protein ligases.

Indexed as

ProteolysisAnimalsExtracellular SpaceHumansProteasome Endopeptidase ComplexProteinsUbiquitinProteasome Endopeptidase ComplexProteinsUbiquitin

Identifiers

PMID22245831
PMCPMC3345107

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.