Evidence map›Paper›PMID 38785993›Full record

ArticleBiomolecules2024

SKGQA, a Peptide Derived from the ANA/BTG3 Protein, Cleaves Amyloid-β with Proteolytic Activity.

Yusuke Hatakawa, Rina Nakamura, Toshifumi Akizawa, Motomi Konishi, Akira Matsuda, Tomoyuki Oe, Motoaki Saito, Fumiaki Ito

Abstract read
In one paragraph

Article in Biomolecules, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. Article
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

8 authors.

Yusuke HatakawaDepartment of Bio-Analytical Chemistry, Graduate School of Pharmaceutical Sciences, Tohoku University, 6-3 Aramaki-Aoba, Aoba-ku, Sendai 980-8578, Miyagi, Japan.
Rina NakamuraO-Force Co., Ltd., 3454 Irino Kuroshio-cho, Hata-gun 789-1931, Kochi, Japan.ORCID 0000-0003-1745-2225
Toshifumi AkizawaO-Force Co., Ltd., 3454 Irino Kuroshio-cho, Hata-gun 789-1931, Kochi, Japan.ORCID 0000-0002-3440-0905
Motomi KonishiDepartment of Integrative Pharmacy, Faculty of Pharmaceutical Sciences, Setsunan University, 45-1 Nagaotoge-cho, Hirakata 573-0101, Osaka, Japan.ORCID 0000-0001-5516-4270
Akira MatsudaLaboratory of Medicinal and Biochemical Analysis, Faculty of Pharmaceutical Sciences, Hiroshima International University, 5-1-1 Hirokoshinkai, Kure 737-0112, Hiroshima, Japan.
Tomoyuki OeDepartment of Bio-Analytical Chemistry, Graduate School of Pharmaceutical Sciences, Tohoku University, 6-3 Aramaki-Aoba, Aoba-ku, Sendai 980-8578, Miyagi, Japan.
Motoaki SaitoDepartment of Pharmacology, Kochi Medical School, Kochi University, Kohasu, Oko-cho, Nankoku 783-8505, Kochi, Japan.
Fumiaki ItoO-Force Co., Ltd., 3454 Irino Kuroshio-cho, Hata-gun 789-1931, Kochi, Japan.ORCID 0000-0002-4129-4899

Funding

Japan Agency for Medical Research and Development 22ym0126810j0001Japan Agency for Medical Research and Development JP20lm0203008Japan Society for the Promotion of Science 15K07908Japan Society for the Promotion of Science 19K22499The Kochi Shimbun and Kochi Broadcasting Charitable trust " Fund of Life (Inochi)"
6 · The paper itself

Abstract

Despite the extensive research conducted on Alzheimer's disease (AD) over the years, no effective drug for AD treatment has been found. Therefore, the development of new drugs for the treatment of AD is of the utmost importance. We recently reported the proteolytic activities of JAL-TA9 (YKGSGFRMI) and ANA-TA9 (SKGQAYRMA), synthetic peptides of nine amino acids each, derived from the Box A region of Tob1 and ANA/BTG3 proteins, respectively. Furthermore, two components of ANA-TA9, ANA-YA4 (YRMI) at the C-terminus end and ANA-SA5 (SKGQA) at the N-terminus end of ANA-TA9, exhibited proteolytic activity against amyloid-β (Aβ) fragment peptides. In this study, we identified the active center of ANA-SA5 using AEBSF, a serine protease inhibitor, and a peptide in which the Ser residue of ANA-SA5 was replaced with Leu. In addition, we demonstrate the proteolytic activity of ANA-SA5 against the soluble form Aβ42 (

Indexed as

Amyloid beta-PeptidesProteolysisAlzheimer DiseaseCell Cycle ProteinsCell Line, TumorHumansPeptide FragmentsPeptidesAmyloid beta-PeptidesBTG3 protein, humanCell Cycle ProteinsPeptide FragmentsPeptidesAlzheimer’s diseaseamyloid-βANA-SA5ANA-TA9CatalytideJAL-TA9neurodegenerative diseasepeptide drugproteolytic peptideserine proteases

Identifiers

PMID38785993
PMCPMC11118129

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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.