Evidence map›Paper›PMID 24566305›Full record

ReviewMolecules (Basel, Switzerland)2014

Carnosinases, their substrates and diseases.

Francesco Bellia, Graziella Vecchio, Enrico Rizzarelli

Open access · goldAbstract readReview
In one paragraph

Review in Molecules (Basel, Switzerland), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.

0numbers the graph read from it
0cells of the map it votes in
52citing papers in PubMed
3.6field-weighted citation impact, top 7% 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

52 citing papers in PubMed, 102 citations in OpenAlex.

  1. Trial
  2. Carnosine-Related Metabolism in Rat Cardiomyocytes and Human Heart Tissue.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2026
    Article
  3. Review
  4. Review
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  6. Article
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  8. Review
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  10. Review
  11. The Possible Roles ofCurrent medicinal chemistry · 2025
    Review
  12. Article
  13. Article
  14. Research progress on intranasal treatment for Parkinson's disease.Neuroprotection (Chichester, England) · 2024
    Review
  15. Article
  16. Review
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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

3 authors at 2 institutions in 1 country.

Francesco BelliaInstitute of Biostructure and Bioimaging, CNR, viale A. Doria 6, 95125 Catania, Italy. francesco.bellia@cnr.it.
Graziella VecchioDepartment of Chemical Sciences, University of Catania, viale A. Doria 6, 95125 Catania, Italy. gr.vecchio@unict.it.
Enrico RizzarelliInstitute of Biostructure and Bioimaging, CNR, viale A. Doria 6, 95125 Catania, Italy. erizzarelli@unict.it.
University of Catania · ITInstitute of Biostructure and Bioimaging · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Carnosinases are Xaa-His dipeptidases that play diverse functions throughout all kingdoms of life. Human isoforms of carnosinase (CN1 and CN2) under appropriate conditions catalyze the hydrolysis of the dipeptides carnosine (β-alanyl-L-histidine) and homocarnosine (γ-aminobutyryl-L-histidine). Alterations of serum carnosinase (CN1) activity has been associated with several pathological conditions, such as neurological disorders, chronic diseases and cancer. For this reason the use of carnosinase levels as a biomarker in cerebrospinal fluid (CSF) has been questioned. The hydrolysis of imidazole-related dipeptides in prokaryotes and eukaryotes is also catalyzed by aminoacyl-histidine dipeptidases like PepD (EC 3.4.13.3), PepV (EC 3.4.13.19) and anserinase (EC 3.4.13.5). The review deals with the structure and function of this class of enzymes in physiological and pathological conditions. The main substrates of these enzymes, i.e., carnosine, homocarnosine and anserine (β-alanyl-3-methyl-L-histidine) will also be described.

Indexed as

CarnosineDipeptidasesDipeptidesHumansNeoplasmsNervous System DiseasesProtein ConformationStructure-Activity RelationshipSubstrate SpecificityCarnosineCNDP1 protein, humanDipeptidasesDipeptideshomocarnosine

Identifiers

PMID24566305
PMCPMC6271292
OpenAlexW2065731270

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.