Evidence map›Paper›PMID 36568514›Full record

ReviewOpen medicine (Warsaw, Poland)2022

Physiological and modulatory role of thioredoxins in the cellular function.

Luis Omar Xinastle-Castillo, Abraham Landa

Open access · goldAbstract readReview
In one paragraph

Review in Open medicine (Warsaw, Poland), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.2field-weighted citation impact, top 21% 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

11 citing papers in PubMed, 17 citations in OpenAlex.

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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

2 authors at 1 institution in 1 country.

Luis Omar Xinastle-CastilloDepartamento de Microbiología y Parasitología, Facultad de Medicina, Universidad Nacional Autónoma de México, Edificio A, 2o Piso. Ciudad Universitaria, Ciudad de México, 04510, México.
Abraham LandaDepartamento de Microbiología y Parasitología, Facultad de Medicina, Universidad Nacional Autónoma de México, Edificio A, 2o Piso. Ciudad Universitaria, Ciudad de México, 04510, México.
Universidad Nacional Autónoma de México · MX

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Thioredoxins (TRXs) are a class of ubiquitous and multifunctional protein. Mammal cells present three isoforms: a cytosolic and extracellular called thioredoxin 1 (TRX1), a mitochondrial (TRX2), and one specific in spermatozoids (TRX3). Besides, a truncated form called TRX80 exists, which results from the post-translational cleavage performed on TRX1. TRXs' main function is to maintain the reduction-oxidation homeostasis of the cell, reducing the proteins through a thiol-disulfide exchange that depends on two cysteines located in the active site of the protein (Cys32-X-X-Cys35 in humans). In addition, TRX1 performs S-nitrosylation, a post-translational modification of proteins that depends on cysteines of its C-terminal region (Cys62, Cys69, and Cys73 in human TRX1). These modifications allow the TRXs to modulate the protein function and participate in regulating diverse cellular processes, such as oxidative stress, transcription, signaling cascades, apoptosis, inflammation, and immunologic response. This points out the crucial relevance of TRXs for cell function, signaling it as a strategic target for the treatment of many diseases and its possible use as a therapeutic factor.

Indexed as

immune responseredox statesignaling cascadeS-nitrosylationtranscription factor

Identifiers

PMID36568514
PMCPMC9746700
OpenAlexW4312212001

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.