Evidence map›Paper›PMID 42588464›Full record

ArticleMolecules (Basel, Switzerland)2026

Structure and Function of Honeybee α-Amylase of Glycoside Hydrolase Family 13 Subfamily 15.

Wataru Saburi, Yushi Takahashi, Shiho Takei, Toyoyuki Ose, Haruhide Mori

Abstract read
In one paragraph

Article in Molecules (Basel, Switzerland), 2026. 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
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.

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

5 authors.

Wataru SaburiResearch Faculty of Agriculture, Hokkaido University, Kita 9, Nishi 9, Sapporo 060-8589, Hokkaido, Japan.
Yushi TakahashiJapan Food Research Laboratories, Bunkyo, Chitose 066-0052, Hokkaido, Japan.ORCID 0000-0002-9210-6413
Shiho TakeiFaculty of Advanced Life Science, Hokkaido University, Kita 10, Nishi 8, Sapporo 060-0810, Hokkaido, Japan.ORCID 0009-0001-5873-546X
Toyoyuki OseFaculty of Advanced Life Science, Hokkaido University, Kita 10, Nishi 8, Sapporo 060-0810, Hokkaido, Japan.ORCID 0000-0002-2001-9388
Haruhide MoriResearch Faculty of Agriculture, Hokkaido University, Kita 9, Nishi 9, Sapporo 060-8589, Hokkaido, Japan.ORCID 0000-0001-7346-9131

Funding

Japan Society for the Promotion of Science JPJS00420230001
6 · The paper itself

Abstract

α-Amylase, ubiquitously distributed across diverse organisms, catalyzes the hydrolysis of the internal α-(1→4)-linkage of α-(1→4)-glucan including starch as an essential energy source. Insect α-amylases, which belong to the glycoside hydrolase family 13 subfamily 15 (GH13_15), are important for optimal larval growth and adult longevity. Honeybee (

Indexed as

alpha-AmylasesGlycoside HydrolasesAmino Acid SequenceAnimalsBeesKineticsModels, MolecularOligosaccharidesStructure-Activity RelationshipSubstrate Specificityalpha-AmylasesGlycoside HydrolasesmaltooligosaccharidesOligosaccharidesGH13_15honeyhoneybeestarch granulessubsite mapα-amylase

Identifiers

PMID42588464
PMCPMC13468693

What OpenQuestion holds

Textmetadata
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.