Evidence map›Paper›PMID 39574306›Full record

ArticleThe journal of physical chemistry. B2024

Why Bestatin Prefers Human Carnosinase 2 (CN2) to Human Carnosinase 1 (CN1).

Borvornwat Toviwek, Skorn Koonawootrittriron, Thanathip Suwanasopee, Danai Jattawa, Prapasiri Pongprayoon

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in The journal of physical chemistry. B, 2024. 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. Review
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.

Borvornwat ToviwekDepartment of Chemistry, Faculty of Science, Kasetsart University, Chatuchak, Bangkok 10900, Thailand.
Skorn KoonawootrittrironDepartment of Animal Science, Faculty of Agriculture, Kasetsart University, Chatuchak, Bangkok 10900, Thailand.
Thanathip SuwanasopeeDepartment of Animal Science, Faculty of Agriculture, Kasetsart University, Chatuchak, Bangkok 10900, Thailand.
Danai JattawaDepartment of Animal Science, Faculty of Agriculture, Kasetsart University, Chatuchak, Bangkok 10900, Thailand.
Prapasiri PongprayoonDepartment of Chemistry, Faculty of Science, Kasetsart University, Chatuchak, Bangkok 10900, Thailand.ORCID 0000-0002-1472-8241

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Human carnosinases (CNs) are Xaa-His metal-ion-activated aminopeptidases that break down bioactive carnosine and other histidine-containing dipeptides. Carnosine is a bioactive peptide found in meat and prevalently used as a supplement and in functional food formulation. Nonetheless, carnosine is digested by CNs rapidly after ingestion. CNs have two isoforms (carnosinase 1 (CN1) and carnosinase 2 (CN2)), where CN1 is the main player in carnosine digestion. CNs contain a catalytic metal ion pair (Zn

Indexed as

DipeptidasesLeucineMolecular Dynamics SimulationCarnosineHumansSubstrate Specificityaminoacyl-histidine dipeptidaseCarnosineCNDP1 protein, humanDipeptidasesLeucineubenimex

Identifiers

PMID39574306
PMCPMC11626516

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.