Evidence map›Paper›PMID 28224255›Full record

ArticleJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry2017

Thiol oxidase ability of copper ion is specifically retained upon chelation by aldose reductase.

Francesco Balestri, Roberta Moschini, Mario Cappiello, Umberto Mura, Antonella Del-Corso

Open access · greenAbstract read
PubMed Publisher
In one paragraph

Article in Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2017. 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, 2 citations in OpenAlex.

  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

5 authors at 1 institution in 1 country.

Francesco BalestriBiochemistry Unit, Department of Biology, University of Pisa, via San Zeno, 51, 56123, Pisa, Italy.
Roberta MoschiniBiochemistry Unit, Department of Biology, University of Pisa, via San Zeno, 51, 56123, Pisa, Italy.
Mario CappielloBiochemistry Unit, Department of Biology, University of Pisa, via San Zeno, 51, 56123, Pisa, Italy.
Umberto MuraBiochemistry Unit, Department of Biology, University of Pisa, via San Zeno, 51, 56123, Pisa, Italy.
Antonella Del-CorsoBiochemistry Unit, Department of Biology, University of Pisa, via San Zeno, 51, 56123, Pisa, Italy. antonella.delcorso@unipi.it.
University of Pisa · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Bovine lens aldose reductase is susceptible to a copper-mediated oxidation, leading to the generation of a disulfide bridge with the concomitant incorporation of two equivalents of the metal and inactivation of the enzyme. The metal complexed by the protein remains redox active, being able to catalyse the oxidation of different physiological thiol compounds. The thiol oxidase activity displayed by the enzymatic form carrying one equivalent of copper ion (Cu

Indexed as

Aldehyde ReductaseAnimalsCattleChelating AgentsCopperIonsOxidoreductasesOxidoreductases Acting on Sulfur Group DonorsAldehyde ReductaseChelating AgentsCopperIonsOxidoreductasesOxidoreductases Acting on Sulfur Group DonorsAldose reductaseCopperOxidative stressThiol oxidase

Identifiers

PMID28224255
OpenAlexW2590936256

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.