Evidence map›Paper›PMID 19002207›Full record

ReviewNature reviews. Molecular cell biology2008

One step at a time: endoplasmic reticulum-associated degradation.

Shruthi S Vembar, Jeffrey L Brodsky

Abstract readReview
In one paragraph

Review in Nature reviews. Molecular cell biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 765 papers.

0numbers the graph read from it
0cells of the map it votes in
765citing 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

765 citing papers in PubMed.

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705 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

2 authors.

Shruthi S VembarDepartment of Biological Sciences, University of Pittsburgh, Pittsburgh, Pennsylvania 15260, USA.
Jeffrey L Brodsky

Funding

ER Associated Degradation of Membrane Proteins in YeastR01GM075061 · NIGMS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI BRODSKY, JEFFREY L. · 2006 to 2019
$3.2M
NIGMS NIH HHS R01 GM075061
6 · The paper itself

Abstract

Protein folding in the endoplasmic reticulum (ER) is monitored by ER quality control (ERQC) mechanisms. Proteins that pass ERQC criteria traffic to their final destinations through the secretory pathway, whereas non-native and unassembled subunits of multimeric proteins are degraded by the ER-associated degradation (ERAD) pathway. During ERAD, molecular chaperones and associated factors recognize and target substrates for retrotranslocation to the cytoplasm, where they are degraded by the ubiquitin-proteasome machinery. The discovery of diseases that are associated with ERAD substrates highlights the importance of this pathway. Here, we summarize our current understanding of each step during ERAD, with emphasis on the factors that catalyse distinct activities.

Indexed as

AnimalsCytoplasmEndoplasmic ReticulumHumansMolecular ChaperonesProteasome Endopeptidase ComplexProtein FoldingProteinsProtein TransportSecretory PathwaySubstrate SpecificityUbiquitinUbiquitinationMolecular ChaperonesProteasome Endopeptidase ComplexProteinsUbiquitin

Identifiers

PMID19002207
PMCPMC2654601

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.