Evidence map›Paper›PMID 39730661›Full record

ArticleScientific reports2024

Bee pollen peptides as potent tyrosinase inhibitors with anti-melanogenesis effects in murine b16f10 melanoma cells and zebrafish embryos.

Papassara Sangtanoo, Piroonporn Srimongkol, Tanatorn Saisavoey, Songchan Puthong, Anumart Buakeaw, Rutairat Suttisuwan, Marisa Jatupornpipat, Wittaya Pimtong, Onrapak Reamtong, Aphichart Karnchanatat

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Scientific reports, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Article
  2. Article
  3. 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

10 authors.

Papassara SangtanooCenter of Excellence in Bioconversion and Bioseparation for Platform Chemical Production, Institute of Biotechnology and Genetic Engineering, Chulalongkorn University, 254 Phayathai Road, Pathumwan, Bangkok, 10330, Thailand.
Piroonporn SrimongkolCenter of Excellence in Bioconversion and Bioseparation for Platform Chemical Production, Institute of Biotechnology and Genetic Engineering, Chulalongkorn University, 254 Phayathai Road, Pathumwan, Bangkok, 10330, Thailand.
Tanatorn SaisavoeyCenter of Excellence in Bioconversion and Bioseparation for Platform Chemical Production, Institute of Biotechnology and Genetic Engineering, Chulalongkorn University, 254 Phayathai Road, Pathumwan, Bangkok, 10330, Thailand.
Songchan PuthongCenter of Excellence in Bioconversion and Bioseparation for Platform Chemical Production, Institute of Biotechnology and Genetic Engineering, Chulalongkorn University, 254 Phayathai Road, Pathumwan, Bangkok, 10330, Thailand.
Anumart BuakeawCenter of Excellence in Bioconversion and Bioseparation for Platform Chemical Production, Institute of Biotechnology and Genetic Engineering, Chulalongkorn University, 254 Phayathai Road, Pathumwan, Bangkok, 10330, Thailand.
Rutairat SuttisuwanBiodiversity and Sustainable Utilization Research Unit, Department of Biology, Faculty of Science and Technology, Rajamangala University of Technology Krungthep, 2 Nang linchi Road, Sathorn, Bangkok, 10120, Thailand.
Marisa JatupornpipatDepartment of Biology, Faculty of Science, King Mongkut's Institute of Technology, Ladkrabang, Chalongkrung Road, Ladkrabang, Bangkok, 10520, Thailand.
Wittaya PimtongNano Environmental and Health Safety Research Team, National Science and Technology Development Agency (NSTDA), 111 Thailand Science Park, Phahonyothin Road, Khlong Nueng, Khlong Luang, 12120, Pathum Thani, Thailand.
Onrapak ReamtongDepartment of Molecular Tropical Medicine and Genetics, Faculty of Tropical Medicine, Mahidol University, 420/6 Ratchawithi Road, Ratchathewi, Bangkok, 10400, Thailand.
Aphichart KarnchanatatCenter of Excellence in Bioconversion and Bioseparation for Platform Chemical Production, Institute of Biotechnology and Genetic Engineering, Chulalongkorn University, 254 Phayathai Road, Pathumwan, Bangkok, 10330, Thailand. Aphichart.K@chula.ac.th.

Funding

The Thailand Science Research and Innovation Fund Chulalongkorn University BCG66610030
6 · The paper itself

Abstract

One important functional food ingredient today, valued for its health properties and ability to prevent disease, is bee pollen, which comprises a combination of nectar, pollen from plants, and the secretions of bees. In this research, the tyrosinase (TYR) inhibiting abilities of the peptides derived from bee pollen protein hydrolysates are investigated. Various proteases were utilized to generate these peptides, followed by testing at different concentrations. Tyrosinase inhibition activity was detected in all cases, while the hydrolysate drawn from 5.0% w/v neutrase exhibited the best IC

Indexed as

Melanoma, ExperimentalMonophenol MonooxygenasePeptidesPollenZebrafishAnimalsBeesCell Line, TumorEmbryo, NonmammalianEnzyme InhibitorsMelaninsMiceMolecular Docking SimulationEnzyme InhibitorsMelaninsMonophenol MonooxygenasePeptidesB16F10 mouse melanoma cellsBee pollenMelanogenesisProtein hydrolysateTyrosinase inhibitory peptidesZebrafish

Identifiers

PMID39730661
PMCPMC11681159

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.