Evidence map›Paper›PMID 29475957›Full record

ArticleThe Journal of biological chemistry2018

An isomerase completes the circuit for a redox switch.

Gustavo Salinas

Open access · hybridAbstract readComment
In one paragraph

Article in The Journal of biological chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact, top 98% 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

1 citing paper in PubMed, 1 citations in OpenAlex.

  1. ERp57/PDIA3: new insight.Cellular & molecular biology letters · 2022
    Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

1 author at 1 institution in 1 country.

Gustavo SalinasDepartamento de Biociencias, Facultad de Química, Universidad de la República, Montevideo 11800, Uruguay; Institut Pasteur de Montevideo, Mataojo 2020, Montevideo 11400, Uruguay. Electronic address: gsalin@fq.edu.uy.
Universidad de la República · UY

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The activity of human transglutaminase 2 (TG2), which forms protein cross-links between glutamine and lysine residues, is controlled by an allosteric disulfide bond. However, the mechanism by which this bond is formed, like many systems regulated by oxidative cysteine modifications, was not clear. A new study from Khosla and colleagues shows that TG2 is oxidatively inactivated by the protein disulfide isomerase ERp57, providing the first example of a defined and reversible protein-controlled redox switch and pointing to new strategies to inhibit undesirable TG2 activity in pathological states.

Indexed as

Endoplasmic Reticulum StressProtein Disulfide-IsomerasesGTP-Binding ProteinsHumansOxidation-ReductionProtein Glutamine gamma Glutamyltransferase 2TransglutaminasesGTP-Binding ProteinsProtein Disulfide-IsomerasesProtein Glutamine gamma Glutamyltransferase 2Transglutaminases

Identifiers

PMID29475957
PMCPMC5827431
OpenAlexW2791146710

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.