Evidence map›Paper›PMID 36555186›Full record

ArticleInternational journal of molecular sciences2022

Detection and pH-Thermal Characterization of Proteinases Exclusive of Honeybee Worker-Fate Larvae (

Simona Sagona, Chiara D'Onofrio, Vincenzo Miragliotta, Antonio Felicioli

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact, top 90% 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

0 citing papers in PubMed, 0 citations in OpenAlex.

No citing paper in PubMed yet.

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

4 authors at 1 institution in 2 countries.

Simona SagonaDepartment of Veterinary Sciences, Pisa University, Viale delle Piagge 2, 56124 Pisa, Italy.ORCID 0000-0003-1592-7522
Chiara D'OnofrioDepartment of Veterinary Sciences, Pisa University, Viale delle Piagge 2, 56124 Pisa, Italy.ORCID 0000-0001-5586-6694
Vincenzo MiragliottaDepartment of Veterinary Sciences, Pisa University, Viale delle Piagge 2, 56124 Pisa, Italy.ORCID 0000-0001-7896-5695
Antonio FelicioliDepartment of Veterinary Sciences, Pisa University, Viale delle Piagge 2, 56124 Pisa, Italy.ORCID 0000-0002-0808-3037
University of Pisa · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The occurrence of the honeybee caste polyphenism arises when a change in diet is transduced into cellular metabolic responses, resulting in a developmental shift mediated by gene expression. The aim of this investigation was to detect and describe the expression profile of water-soluble proteases during the ontogenesis of honeybee worker-fate larvae. The extraction of insect homogenates was followed by the electrophoretic separation of the protein extract in polyacrylamide gels under semi-denaturing condition, precast with gelatin, pollen, or royal jelly protein extracts. The worker-fate honeybee larva showed a proteolytic pattern that varied with aging, and a protease with the highest activity at 72 h after hatching was named PS4. PS4 has a molecular weight of 45 kDa, it remained active until cell sealing, and its enzymatic properties suggest a serine-proteinase nature. To define the process that originates a queen-fate larvae, royal jelly and pollen were analysed, but PS4 was not detected in either of them. The effect of food on the PS4 was investigated by mixing crude extracts of queen and worker-fate larvae with pollen and royal jelly, respectively. Only royal jelly inhibited PS4 in worker-fate larvae. Taken together, our data suggest that PS4 could be involved in caste differentiation.

Indexed as

EndopeptidasesSerine ProteasesAnimalsBeesElectrophoresisHydrogen-Ion ConcentrationInsect ProteinsLarvaEndopeptidasesInsect ProteinsSerine ProteasesApis melliferabee larvaepolyphenismproteasezymography

Identifiers

PMID36555186
PMCPMC9779378
OpenAlexW4311952989

What OpenQuestion holds

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LicenceCC BY
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Registered trials

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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.