Evidence map›Paper›PMID 28848693›Full record

ArticlePeerJ2017

Acetylation of N-terminus and two internal amino acids is dispensable for degradation of a protein that aberrantly engages the endoplasmic reticulum translocon.

Sarah M Engle, Justin J Crowder, Sheldon G Watts, Christopher J Indovina, Samuel Z Coffey, Eric M Rubenstein

Open access · goldAbstract read
In one paragraph

Article in PeerJ, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.2field-weighted citation impact, top 44% 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

4 citing papers in PubMed, 4 citations in OpenAlex.

  1. Article
  2. Article
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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

6 authors at 3 institutions in 1 country.

Sarah M Engle *Department of Biology, Ball State University, Muncie, IN, United States of America.
Justin J Crowder *Department of Biology, Ball State University, Muncie, IN, United States of America.
Sheldon G WattsDepartment of Biology, Ball State University, Muncie, IN, United States of America.
Christopher J IndovinaDepartment of Biology, Ball State University, Muncie, IN, United States of America.
Samuel Z CoffeyDepartment of Biology, Ball State University, Muncie, IN, United States of America.
Eric M RubensteinDepartment of Biology, Ball State University, Muncie, IN, United States of America.
Ball State University · USEli Lilly (United States) · USIndiana University School of Medicine

Funding

Regulation of Endoplasmic Reticulum Protein Quality Control by Microtubule-Associated ProteinsR15GM111713 · NIGMS · BALL STATE UNIVERSITY · PI Eric Meyer Rubenstein · 2014 to 2026
$1.8M
NIGMS NIH HHS R15 GM111713
6 · The paper itself

Abstract

Conserved homologues of the Hrd1 ubiquitin ligase target for degradation proteins that persistently or aberrantly engage the endoplasmic reticulum translocon, including mammalian apolipoprotein B (apoB; the major protein component of low-density lipoproteins) and the artificial yeast protein

Indexed as

AcetylationApolipoprotein BEndoplasmic reticulum-associated degradationHrd1Nat3Protein degradationProtein quality controlTransloconUbiquitin-proteasome system

Identifiers

PMID28848693
PMCPMC5571791
OpenAlexW2748272197

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.