Evidence map›Paper›PMID 37804695›Full record

ArticleRedox biology2023

TXNL1 has dual functions as a redox active thioredoxin-like protein as well as an ATP- and redox-independent chaperone.

Attila Andor, Mahendravarman Mohanraj, Zsuzsanna Anna Pató, Katalin Úri, Beáta Biri-Kovács, Qing Cheng, Elias S J Arnér

Abstract read
In one paragraph

Article in Redox biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
–field-weighted citation impact
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

15 citing papers in PubMed.

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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

7 authors.

Attila AndorDepartment of Selenoprotein Research and the National Tumor Biology Laboratory, National Institute of Oncology, 1122, Budapest, Hungary; Division of Biochemistry, Department of Medical Biochemistry, Karolinska Institutet, SE-171 77, Stockholm, Sweden.
Mahendravarman MohanrajDepartment of Selenoprotein Research and the National Tumor Biology Laboratory, National Institute of Oncology, 1122, Budapest, Hungary; Division of Biochemistry, Department of Medical Biochemistry, Karolinska Institutet, SE-171 77, Stockholm, Sweden.
Zsuzsanna Anna PatóDepartment of Selenoprotein Research and the National Tumor Biology Laboratory, National Institute of Oncology, 1122, Budapest, Hungary; Division of Biochemistry, Department of Medical Biochemistry, Karolinska Institutet, SE-171 77, Stockholm, Sweden.
Katalin ÚriDepartment of Selenoprotein Research and the National Tumor Biology Laboratory, National Institute of Oncology, 1122, Budapest, Hungary; Division of Biochemistry, Department of Medical Biochemistry, Karolinska Institutet, SE-171 77, Stockholm, Sweden.
Beáta Biri-KovácsDepartment of Selenoprotein Research and the National Tumor Biology Laboratory, National Institute of Oncology, 1122, Budapest, Hungary; Division of Biochemistry, Department of Medical Biochemistry, Karolinska Institutet, SE-171 77, Stockholm, Sweden.
Qing ChengDivision of Biochemistry, Department of Medical Biochemistry, Karolinska Institutet, SE-171 77, Stockholm, Sweden.
Elias S J ArnérDepartment of Selenoprotein Research and the National Tumor Biology Laboratory, National Institute of Oncology, 1122, Budapest, Hungary; Division of Biochemistry, Department of Medical Biochemistry, Karolinska Institutet, SE-171 77, Stockholm, Sweden. Electronic address: elias.arner@ki.se.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

TXNL1 (also named TRP32, for thioredoxin related protein of 32 kDa) is a cytosolic thioredoxin-fold protein expressed in all cell types and conserved from yeast to mammals, but with yet poorly known function. Here, we expressed and purified human TXNL1 together with several Cys-to-Ser variants, characterizing their enzymatic properties. TXNL1 could reduce disulfides in insulin, cystine and glutathione disulfide (GSSG) in reactions coupled to thioredoxin reductase (TXNRD1, TrxR1) using NADPH, similarly to thioredoxin (TXN, Trx1), but with lower catalytic efficacy due to at least one order of magnitude higher K

Indexed as

CystineInsulinsAdenosine TriphosphateAnimalsHumansMammalsNADPOxidation-ReductionThioredoxin-Disulfide ReductaseThioredoxinsAdenosine TriphosphateCystineInsulinsNADPThioredoxin-Disulfide ReductaseThioredoxinsChaperoneDisulfideInsulinReductionThioredoxin

Identifiers

PMID37804695
PMCPMC10570131

What OpenQuestion holds

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Registered trials

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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.