Evidence map›Paper›PMID 22119785›Full record

ArticleNature cell biology2011

Defining human ERAD networks through an integrative mapping strategy.

John C Christianson, James A Olzmann, Thomas A Shaler, Mathew E Sowa, Eric J Bennett, Caleb M Richter, Ryan E Tyler, Ethan J Greenblatt, J Wade Harper, Ron R Kopito

Open access · greenAbstract read
In one paragraph

Article in Nature cell biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 333 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
333citing papers in PubMed, 1 pooled it
13.1field-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

333 citing papers in PubMed, 1 synthesis or guideline pooled it, 506 citations in OpenAlex.

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  16. Competition between Der1 and ERAD-M substrates controls Hrd1 complex function.Proceedings of the National Academy of Sciences of the United States of America · 2025
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273 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

10 authors at 4 institutions in 2 countries.

John C ChristiansonDepartment of Biology & Bio-X Program, Stanford University, Stanford, California 94305, USA.
James A Olzmann
Thomas A Shaler
Mathew E Sowa
Eric J Bennett
Caleb M Richter
Ryan E Tyler
Ethan J Greenblatt
J Wade Harper
Ron R Kopito
Stanford University · USHarvard University · USSRI International · USUniversity of Oxford · GB

Funding

Ubiquitin Mediated Proteolysis and Cell Cycle ControlR01AG011085 · NIA · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI JEFFREY W HARPER · 1993 to 2026
$10.9M
The Ubiquitin Proteasome System in Quality ControlR01GM074874 · NIGMS · STANFORD UNIVERSITY · PI KOPITO, RON R · 2006 to 2022
$8.0M
Protein Aggregation and Inclusion Body FormationR01NS042842 · NINDS · STANFORD UNIVERSITY · PI KOPITO, RON R · 2002 to 2016
$6.1M
SYSTEMATIC ANALYSIS OF THE DUB PROTEOMER01GM054137 · NIGMS · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI HARPER, JEFFREY W · 1996 to 2012
$4.1M
SYSTEMATIC ANALYSIS OF PROTEOLYSIS PATHWAYS FOR CULLIN TARGETSR01GM070565 · NIGMS · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI HARPER, JEFFREY W · 2005 to 2012
$2.6M
Molecular mechanisms of ubiquitin-dependent Er-associated degradationF32GM086026 · NIGMS · STANFORD UNIVERSITY · PI OLZMANN, JAMES A · 2008 to 2010
$149k
NIA NIH HHS R01 AG011085NIGMS NIH HHS F32 GM086026NIGMS NIH HHS R01 GM054137NIGMS NIH HHS R01 GM070565NIGMS NIH HHS R01 GM074874NINDS NIH HHS R01 NS042842
6 · The paper itself

Abstract

Proteins that fail to correctly fold or assemble into oligomeric complexes in the endoplasmic reticulum (ER) are degraded by a ubiquitin- and proteasome-dependent process known as ER-associated degradation (ERAD). Although many individual components of the ERAD system have been identified, how these proteins are organized into a functional network that coordinates recognition, ubiquitylation and dislocation of substrates across the ER membrane is not well understood. We have investigated the functional organization of the mammalian ERAD system using a systems-level strategy that integrates proteomics, functional genomics and the transcriptional response to ER stress. This analysis supports an adaptive organization for the mammalian ERAD machinery and reveals a number of metazoan-specific genes not previously linked to ERAD.

Indexed as

Amino Acid SequenceAnimalsEndoplasmic ReticulumEndoplasmic Reticulum-Associated DegradationHEK293 CellsHeLa CellsHumansMolecular Sequence DataProteasome Endopeptidase ComplexProtein FoldingProteinsProteolysisReceptors, Autocrine Motility FactorRNA InterferenceUbiquitin-Protein LigasesAMFR protein, humanATP dependent 26S proteaseProteasome Endopeptidase ComplexProteinsReceptors, Autocrine Motility FactorSEL1L protein, humanSYVN1 protein, humanUbiquitin-Protein Ligases

Identifiers

PMID22119785
PMCPMC3250479
OpenAlexW2076100752

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.