Evidence map›Paper›PMID 28077573›Full record

ArticleThe Journal of biological chemistry2017

A Cdc48 "Retrochaperone" Function Is Required for the Solubility of Retrotranslocated, Integral Membrane Endoplasmic Reticulum-associated Degradation (ERAD-M) Substrates.

Sonya Neal, Raymond Mak, Eric J Bennett, Randolph Hampton

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
2.5field-weighted citation impact, top 11% 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

26 citing papers in PubMed, 44 citations in OpenAlex.

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  13. Assays for studying normalSTAR protocols · 2021
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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

4 authors at 1 institution in 1 country.

Sonya NealDivision of Biological Sciences, Section of Cell and Developmental Biology, University of California, San Diego, La Jolla, California 92093.
Raymond MakDivision of Biological Sciences, Section of Cell and Developmental Biology, University of California, San Diego, La Jolla, California 92093.
Eric J BennettDivision of Biological Sciences, Section of Cell and Developmental Biology, University of California, San Diego, La Jolla, California 92093.
Randolph HamptonDivision of Biological Sciences, Section of Cell and Developmental Biology, University of California, San Diego, La Jolla, California 92093. Electronic address: rhampton@ucsd.edu.
University of California, San Diego · US

Funding

Protein degradation and cholesterol regulationR37DK051996 · NIDDK · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI HAMPTON, RANDOLPH Y. · 2012 to 2020
$3.2M
Manipulating Protein Homeostasis through Specialized Quality Control RibosomesDP2GM119132 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI BENNETT, ERIC J · 2015 to 2015
$2.3M
Discovering the machinery and mechanism of ERAD-M retrotranslocationF32GM111024 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI NEAL, SONYA ELINA · 2014 to 2016
$164k
NIDDK NIH HHS R37 DK051996NIGMS NIH HHS DP2 GM119132NIGMS NIH HHS F32 GM111024
6 · The paper itself

Abstract

A surprising feature of endoplasmic reticulum (ER)-associated degradation (ERAD) is the movement, or retrotranslocation, of ubiquitinated substrates from the ER lumen or membrane to the cytosol where they are degraded by the 26S proteasome. Multispanning ER membrane proteins, called ERAD-M substrates, are retrotranslocated to the cytosol as full-length intermediates during ERAD, and we have investigated how they maintain substrate solubility. Using an

Indexed as

Endoplasmic Reticulum-Associated DegradationAdenosine TriphosphatasesCell Cycle ProteinsEndoplasmic ReticulumHydroxymethylglutaryl CoA ReductasesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSolubilityUbiquitinUbiquitinationValosin Containing ProteinAdenosine TriphosphatasesCDC48 protein, S cerevisiaeCell Cycle ProteinsHMG2 protein, S cerevisiaeHydroxymethylglutaryl CoA ReductasesSaccharomyces cerevisiae ProteinsUbiquitinValosin Containing ProteinCdc48E3 ubiquitin ligaseendoplasmic-reticulum-associated protein degradation (ERAD)endoplasmic reticulum (ER)Hmg2Npl4Retrotranslocationubiquitinubiquitin ligaseUfd1

Identifiers

PMID28077573
PMCPMC5336148
OpenAlexW2578983077

What OpenQuestion holds

Textmetadata
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.