Evidence map›Paper›PMID 42028693›Full record

ArticleDalton transactions (Cambridge, England : 2003)2026

Uncovering the copper(I) binding abilities of a unique fungal metallothionein: characterization of

Aleksandra Hecel, Mariano Briccola, Eva Freisinger

Abstract read
In one paragraph

Article in Dalton transactions (Cambridge, England : 2003), 2026. 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
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. 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

3 authors.

Aleksandra HecelFaculty of Chemistry, University of Wrocław, 50-383 Wrocław, Poland.
Mariano BriccolaDepartment of Chemistry, University of Zurich, 8057 Zurich, Switzerland. freisinger@chem.uzh.ch.
Eva FreisingerDepartment of Chemistry, University of Zurich, 8057 Zurich, Switzerland. freisinger@chem.uzh.ch.ORCID http://orcid.org/0000-0003-3102-6329

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Metallothioneins (MTs) are a superfamily of cysteine-rich proteins essential for metal homeostasis and detoxification. While mammalian and plant MTs have been extensively characterized, fungal MTs remain comparatively understudied despite their remarkable sequence diversity. In particular, members of the fungal-IV MT family from

Indexed as

CopperFungal ProteinsMetallothioneinYarrowiaAmino Acid SequenceBinding SitesModels, MolecularMutationProtein BindingCopperFungal ProteinsMetallothionein

Identifiers

PMID42028693
PMCPMC13107397

What OpenQuestion holds

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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.