Evidence map›Paper›PMID 31687556›Full record

ArticleHeliyon2019

Catalytides derived from the Box A region in the ANA/BTG3 protein cleave amyloid-β fragment peptide.

Yusuke Hatakawa, Rina Nakamura, Motomi Konishi, Toshiyasu Sakane, Motoaki Saito, Toshifumi Akizawa

Open access · goldAbstract read
In one paragraph

Article in Heliyon, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
0.5field-weighted citation impact, top 35% 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

8 citing papers in PubMed, 11 citations in OpenAlex.

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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

6 authors at 3 institutions in 1 country.

Yusuke HatakawaPharmaceutical Technology, Kobe Pharmaceutical University, 4-19-1, Motoyamakita, Higashinada, Kobe, 658-8558, Japan.
Rina NakamuraO-Force Co., Ltd, 3454 Irino Kuroshio-cho, Hata-gun, Kochi 789-1931, Japan.
Motomi KonishiLaboratory of Clinical Analytical Chemistry, Faculty of Pharmaceutical Sciences, Setsunan University, 45-1 Nagaotoge-cho, Hirakata, Osaka 573-0101, Japan.
Toshiyasu SakanePharmaceutical Technology, Kobe Pharmaceutical University, 4-19-1, Motoyamakita, Higashinada, Kobe, 658-8558, Japan.
Motoaki SaitoLaboratory of Pharmacology, School of Medicine, Kochi University, Kohasu, Oko-cho, Nankoku, Kochi, 783-0047, Japan.
Toshifumi AkizawaO-Force Co., Ltd, 3454 Irino Kuroshio-cho, Hata-gun, Kochi 789-1931, Japan.
Kōchi University · JPKobe Pharmaceutical University · JPSetsunan University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We have recently reported about shorter proteolytic peptides termed Catalytide as general name. JAL-TA9 (YKGSGFRMI), a fragment peptide derived from Box A region of Tob1 protein, is the first Catalytide and cleaves Aβ42 and its fragment peptides. Herein, we demonstrate the enzymatic properties of ANA-TA9 corresponding region to JAL-TA9 in ANA/BTG3 protein. ANA-TA9 showed the auto-proteolytic activity and cleaved 3 kinds of synthetic fragment peptides derived from Aβ42, especially on the central region of Aβ42 with a serine protease like activity. Interestingly, 2 kinds of components, ANA-SA5 (SKGQA) and ANA-YA4 (YRMI), also showed similar proteolytic activity. These results indicate that ANA-TA9 is composed of two different Catalytides.

Indexed as

Alzheimer's diseaseAmyloid-β peptideANA/BTG3Analytical chemistryBiochemistryBiophysical chemistryBiotechnologyBox A regionCatalytideChromatographyDevelopmental biologyHydrolase activityMolecular biologyMolecular modelingPeptidesStructural biologyTob/BTG

Identifiers

PMID31687556
PMCPMC6819762
OpenAlexW2975952610

What OpenQuestion holds

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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.