Evidence map›Paper›PMID 36291150›Full record

ArticleCells2022

The Highly Efficient Expression System of Recombinant Human Prolidase and the Effect of N-Terminal His-Tag on the Enzyme Activity.

Justyna Czyrko-Horczak, Magdalena Nizioł, Antonella Forlino, Roberta Besio, Wojciech Miltyk

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Cells, 2022. 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 79% 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. 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 3 institutions in 2 countries.

Justyna Czyrko-HorczakDepartment of Structural Chemistry, Faculty of Chemistry, University of Bialystok, 15-245 Bialystok, Poland.
Magdalena NiziołDepartment of Analysis and Bioanalysis of Medicines, Medical University of Bialystok, 15-089 Bialystok, Poland.
Antonella ForlinoBiochemistry Unit, Department of Molecular Medicine, University of Pavia, 27100 Pavia, Italy.
Roberta BesioBiochemistry Unit, Department of Molecular Medicine, University of Pavia, 27100 Pavia, Italy.
Wojciech MiltykDepartment of Analysis and Bioanalysis of Medicines, Medical University of Bialystok, 15-089 Bialystok, Poland.ORCID 0000-0001-5150-6093
Medical University of Białystok · PLUniversity of Pavia · ITUniversity of Białystok · PL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Prolidase is an enzyme hydrolyzing dipeptides containing proline or hydroxyprolineat the C-terminus and plays an important role in collagen turnover. Human prolidase is active as a dimer with the C-terminal domain containing two Mn

Indexed as

CollagenProlineDipeptidasesDipeptidesErbB ReceptorsHumansCollagenDipeptidasesDipeptidesErbB ReceptorsProlineproline dipeptidasehuman recombinant prolidaseprolidase activityprotein expression system

Identifiers

PMID36291150
PMCPMC9600000
OpenAlexW4306849146

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.