Evidence map›Paper›PMID 23037595›Full record

ArticleNature structural & molecular biology2012

Making the cut: intramembrane cleavage by a rhomboid protease promotes ERAD.

Ethan J Greenblatt, James A Olzmann, Ron R Kopito

Abstract readComment
In one paragraph

Article in Nature structural & molecular biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing 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

14 citing papers in PubMed.

  1. The Dsc complex and its role in Golgi quality control.Biochemical Society transactions · 2024
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

3 authors.

Ethan J GreenblattHoward Hughes Medical Institute Research Laboratories, Department of Embryology, Carnegie Institution of Washington, Baltimore, Maryland, USA.
James A Olzmann
Ron R Kopito

Funding

The Ubiquitin Proteasome System in Quality ControlR01GM074874 · NIGMS · STANFORD UNIVERSITY · PI KOPITO, RON R · 2006 to 2022
$8.0M
NIGMS NIH HHS R01 GM074874
6 · The paper itself

Abstract

Endoplasmic reticulum–associated degradation (ERAD) is a cellular protein quality-control process that disposes of proteasomal substrates from the early secretory pathway. Recent work shows that the endoplasmic reticulum–resident rhomboid protease RHBDL4 facilitates ERAD by recognizing and cleaving integral membrane substrates. The work indicates that intramembrane proteolysis may have a general role in the extraction of misfolded membrane proteins from the endoplasmic reticulum.

Indexed as

Endoplasmic ReticulumEndoplasmic Reticulum-Associated DegradationHumansMembrane ProteinsPeptide HydrolasesUbiquitinMembrane ProteinsPeptide HydrolasesUbiquitin

Identifiers

PMID23037595
PMCPMC3616633

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.