Evidence map›Paper›PMID 33134321›Full record

ArticleFrontiers in molecular biosciences2020

Resolving the TorsinA Oligomerization Conundrum: The Glycan Hypothesis.

Christian Fercher, Lucía F Zacchi

Open access · goldAbstract read
In one paragraph

Article in Frontiers in molecular biosciences, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.3field-weighted citation impact, top 45% 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

2 citing papers in PubMed, 4 citations in OpenAlex.

  1. Article
  2. TorsinA folding and N-linked glycosylation are sensitive to redox homeostasis.Biochimica et biophysica acta. Molecular cell research · 2021
    Article
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 at 2 institutions in 1 country.

Christian FercherAustralian Research Council (ARC), Training Centre for Biopharmaceutical Innovation, The University of Queensland, St Lucia, QLD, Australia.
Lucía F ZacchiAustralian Research Council (ARC), Training Centre for Biopharmaceutical Innovation, The University of Queensland, St Lucia, QLD, Australia.
Australian Research Council · AUUniversity of Queensland · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

TorsinA is a AAA+ ATPase involved in the severe neurological disease Early Onset Torsion Dystonia. Despite the impressive progress in the field in the recent years, the structural organization and function of this intriguing molecule is still not clear. One outstanding difference between torsinA and other AAA+ ATPases is that torsinA is a glycoprotein. TorsinA

Indexed as

AAA ATPaseglycansmodelingstructuretorsinA

Identifiers

PMID33134321
PMCPMC7567157
OpenAlexW3089467463

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.