Evidence map›Paper›PMID 32824561›Full record

ReviewInternational journal of molecular sciences2020

Current Understanding of the Emerging Role of Prolidase in Cellular Metabolism.

Magdalena Misiura, Wojciech Miltyk

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.7field-weighted citation impact, top 13% 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

17 citing papers in PubMed, 32 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Review
  8. Prolidase deficiency, a rare inborn error of immunity, clinical phenotypes, immunological features, and proposed treatments in twins.Allergy, asthma, and clinical immunology : official journal of the Canadian Society of Allergy and Clinical Immunology · 2022
    Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Extracellular Prolidase (PEPD) Induces Anabolic Processes through EGFR, βInternational journal of molecular sciences · 2021
    Article
  15. Article
  16. Article
  17. 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

2 authors at 1 institution in 1 country.

Magdalena MisiuraDepartment of Analysis and Bioanalysis of Medicines, Medical University of Bialystok, 15-089 Białystok, Poland.ORCID 0000-0002-8641-2991
Wojciech MiltykDepartment of Analysis and Bioanalysis of Medicines, Medical University of Bialystok, 15-089 Białystok, Poland.ORCID 0000-0001-5150-6093
Medical University of Białystok · PL

Funding

Narodowe Centrum Nauki 2017/25/B/NZ7/02650
6 · The paper itself

Abstract

Prolidase [EC 3.4.13.9], known as PEPD, cleaves di- and tripeptides containing carboxyl-terminal proline or hydroxyproline. For decades, prolidase has been thoroughly investigated, and several mechanisms regulating its activity are known, including the activation of the β

Indexed as

AnimalsDipeptidasesErbB ReceptorsHumansReceptors, InterferonSignal TransductionTumor Suppressor Protein p53DipeptidasesErbB Receptorsproline dipeptidaseReceptors, InterferonTumor Suppressor Protein p53cellular metabolismEGFRPEPDprolidase

Identifiers

PMID32824561
PMCPMC7460564
OpenAlexW3049474652

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.