Evidence map›Paper›PMID 36846372›Full record

ArticleRSC medicinal chemistry2023

Inactivation of myostatin by photooxygenation using functionalized d-peptides.

Hideyuki Okamoto, Shuko Amber Murano, Kaoru Ikekawa, Masahiro Katsuyama, Sho Konno, Akihiro Taguchi, Kentaro Takayama, Atsuhiko Taniguchi, Yoshio Hayashi

Abstract read
In one paragraph

Article in RSC medicinal chemistry, 2023. 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

9 authors.

Hideyuki OkamotoDepartment of Medicinal Chemistry, School of Pharmacy, Tokyo University of Pharmacy and Life Sciences Hachioji Tokyo 192-0392 Japan atani@toyaku.ac.jp yhayashi@toyaku.ac.jp.
Shuko Amber MuranoDepartment of Medicinal Chemistry, School of Pharmacy, Tokyo University of Pharmacy and Life Sciences Hachioji Tokyo 192-0392 Japan atani@toyaku.ac.jp yhayashi@toyaku.ac.jp.
Kaoru IkekawaDepartment of Medicinal Chemistry, School of Pharmacy, Tokyo University of Pharmacy and Life Sciences Hachioji Tokyo 192-0392 Japan atani@toyaku.ac.jp yhayashi@toyaku.ac.jp.
Masahiro KatsuyamaDepartment of Medicinal Chemistry, School of Pharmacy, Tokyo University of Pharmacy and Life Sciences Hachioji Tokyo 192-0392 Japan atani@toyaku.ac.jp yhayashi@toyaku.ac.jp.
Sho KonnoDepartment of Medicinal Chemistry, School of Pharmacy, Tokyo University of Pharmacy and Life Sciences Hachioji Tokyo 192-0392 Japan atani@toyaku.ac.jp yhayashi@toyaku.ac.jp.
Akihiro TaguchiDepartment of Medicinal Chemistry, School of Pharmacy, Tokyo University of Pharmacy and Life Sciences Hachioji Tokyo 192-0392 Japan atani@toyaku.ac.jp yhayashi@toyaku.ac.jp.
Kentaro TakayamaDepartment of Medicinal Chemistry, School of Pharmacy, Tokyo University of Pharmacy and Life Sciences Hachioji Tokyo 192-0392 Japan atani@toyaku.ac.jp yhayashi@toyaku.ac.jp.
Atsuhiko TaniguchiDepartment of Medicinal Chemistry, School of Pharmacy, Tokyo University of Pharmacy and Life Sciences Hachioji Tokyo 192-0392 Japan atani@toyaku.ac.jp yhayashi@toyaku.ac.jp.ORCID https://orcid.org/0000-0002-5857-3093
Yoshio HayashiDepartment of Medicinal Chemistry, School of Pharmacy, Tokyo University of Pharmacy and Life Sciences Hachioji Tokyo 192-0392 Japan atani@toyaku.ac.jp yhayashi@toyaku.ac.jp.ORCID https://orcid.org/0000-0002-7010-6914

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Inhibition of myostatin is an attractive strategy for the treatment of muscular atrophic diseases such as muscular dystrophy. For the efficient inhibition of myostatin, functionalized peptides were developed by the conjugation of a 16-mer myostatin-binding d-peptide with a photooxygenation catalyst. These peptides induced myostatin-selective photooxygenation and inactivation under near-infrared irradiation, and were associated with little cytotoxicity or phototoxicity. The peptides are resistant to enzymatic digestion due to their d-peptide chains. These properties could contribute to the

Identifiers

PMID36846372
PMCPMC9945861

What OpenQuestion holds

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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.