Evidence map›Paper›PMID 36348649›Full record

ArticleThe journal of poultry science2022

Repression Effects of Hydrolysates from Hen-Egg Proteins on Amyloid Fibril Formation.

Yukiko Muroi, Izumi Aburaya, Takuro Shima, Mitsuharu Matsumoto, Ryo Sasahara, Takahisa Suzuki, Keiichi Watanabe, Koji Wada, Yasushi Sugimoto

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in The journal of poultry science, 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
0.1field-weighted citation impact, top 51% 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, 1 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

9 authors at 2 institutions in 1 country.

Yukiko MuroiFaculty of Food and Nutrition, Kyushu Nutrition and Welfare University, 5-1-1 Shimoitozu, Kokura-Kitaku, Kitakyushu 803-8511, Japan.
Izumi AburayaFaculty of Food and Nutrition, Kyushu Nutrition and Welfare University, 5-1-1 Shimoitozu, Kokura-Kitaku, Kitakyushu 803-8511, Japan.
Takuro ShimaFaculty of Food and Nutrition, Kyushu Nutrition and Welfare University, 5-1-1 Shimoitozu, Kokura-Kitaku, Kitakyushu 803-8511, Japan.
Mitsuharu MatsumotoJoint Faculty of Veterinary Medicine, Kagoshima University, 1-21-24 Korimoto, Kagoshima 890-0065, Japan.
Ryo SasaharaR&D Division, Kewpie Corporation, 2-5-7 Sengawa, Chofu, Tokyo 182-0002, Japan.
Takahisa SuzukiR&D Division, Kewpie Corporation, 2-5-7 Sengawa, Chofu, Tokyo 182-0002, Japan.
Keiichi WatanabeFaculty of Food and Nutrition, Kyushu Nutrition and Welfare University, 5-1-1 Shimoitozu, Kokura-Kitaku, Kitakyushu 803-8511, Japan.
Koji WadaDepartment of Food Function Chemistry, The United Graduate School of Agricultural Sciences, Kagoshima University, 1-21-24 Korimoto, Kagoshima 890-0065, Japan.
Yasushi SugimotoFaculty of Food and Nutrition, Kyushu Nutrition and Welfare University, 5-1-1 Shimoitozu, Kokura-Kitaku, Kitakyushu 803-8511, Japan.
Kagoshima University · JPKyushu Nutrition Welfare University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Amyloid fibrils, which are formed from aggregates of aberrant proteins, can cause various forms of amyloidosis (including Alzheimer's disease). Such disorders often occur in elderly populations and are suspected to be lifestyle related. Thus, it has been speculated that some foodstuffs could be beneficial for preventing amyloidosis. In this study, we determine whether fibril formation by the hen egg white lysozyme (HEWL) could be inhibited by conducting a thioflavin T assay followed by fluorescence and electron microscopy observations. The results demonstrated that four peptide specimens prepared by the hydrolysis of crude proteins from the egg white, egg yolk, chalazae, and eggshell membrane of hen eggs effectively inhibited HEWL fibril formation. Among the four specimens, peptides from chalazae exhibited the highest preventive ability. The superiority of chalaza peptides was also observed when fibril formation was assayed using a full-length human lysozyme and human amyloid

Indexed as

amyloid fibrilamyloid β1–42chalaza hydrolysatesHEWLhuman lysozyme

Identifiers

PMID36348649
PMCPMC9596292
OpenAlexW4286886735

What OpenQuestion holds

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LicenceCC BY-NC-SA
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.