Evidence map›Paper›PMID 39715753›Full record

ArticleNature communications2024

Generating a mirror-image monobody targeting MCP-1 via TRAP display and chemical protein synthesis.

Gosuke Hayashi, Toshinori Naito, Sayaka Miura, Naoya Iwamoto, Yusuke Usui, Mika Bando-Shimizu, Sae Suzuki, Katsuaki Higashi, Motohiro Nonaka, Shinya Oishi and 1 more

Abstract read
In one paragraph

Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing 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

7 citing papers in PubMed.

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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

11 authors.

Gosuke HayashiDepartment of Biomolecular Engineering, Graduate School of Engineering, Nagoya University, Nagoya, Japan. hayashi@chembio.nagoya-u.ac.jp.
Toshinori NaitoDepartment of Biomolecular Engineering, Graduate School of Engineering, Nagoya University, Nagoya, Japan.
Sayaka MiuraDepartment of Biomolecular Engineering, Graduate School of Engineering, Nagoya University, Nagoya, Japan.
Naoya IwamotoGraduate School of Pharmaceutical Sciences, Kyoto University, Kyoto, Japan.ORCID 0009-0003-6664-8117
Yusuke UsuiGraduate School of Pharmaceutical Sciences, Kyoto University, Kyoto, Japan.
Mika Bando-ShimizuHuman Health Sciences, Graduate School of Medicine, Kyoto University, Kyoto, Japan.
Sae SuzukiDepartment of Biomolecular Engineering, Graduate School of Engineering, Nagoya University, Nagoya, Japan.
Katsuaki HigashiHuman Health Sciences, Graduate School of Medicine, Kyoto University, Kyoto, Japan.
Motohiro NonakaHuman Health Sciences, Graduate School of Medicine, Kyoto University, Kyoto, Japan. nonaka.motohiro.4r@kyoto-u.ac.jp.ORCID 0000-0002-8487-6485
Shinya OishiGraduate School of Pharmaceutical Sciences, Kyoto University, Kyoto, Japan. soishi@mb.kyoto-phu.ac.jp.ORCID 0000-0002-2833-2539
Hiroshi MurakamiDepartment of Biomolecular Engineering, Graduate School of Engineering, Nagoya University, Nagoya, Japan. murah@chembio.nagoya-u.ac.jp.ORCID 0000-0003-2089-9263

Funding

Japan Agency for Medical Research and Development (AMED) JP20ak0101144Japan Agency for Medical Research and Development (AMED) JP21zf0127004Japan Agency for Medical Research and Development (AMED) JP22ama121009MEXT | Japan Society for the Promotion of Science (JSPS) JP20H04704, JP 21H00278, JP 22KK0128, JP24H01893MEXT | Japan Society for the Promotion of Science (JSPS) JP20K21252, JP22H02747, JP22K19376, JP22KJ1842, JP24K01628MEXT | Japan Society for the Promotion of Science (JSPS) JP23H05456MEXT | JST | Precursory Research for Embryonic Science and Technology (PRESTO) JST PRESTO
6 · The paper itself

Abstract

Biologically produced protein drugs are generally susceptible to degradation by proteases and often exhibit immunogenicity. To address this issue, mirror-image peptide/protein binders consisting of D-amino acids have been developed so far through the mirror-image phage display technique. Here, we develop a mirror-image protein binder derived from a monobody, one of the promising protein scaffolds, utilizing two notable technologies: chemical protein synthesis and TRAP display, an improved version of mRNA display. A sequential workflow of initial screening followed by affinity maturation, facilitated by TRAP display, generates an L-monobody with high affinity (K

Indexed as

Chemokine CCL2Peptide LibraryAnimalsCell MovementDrug DiscoveryHumansMicePeptidesProtein BindingStereoisomerismCCL2 protein, humanChemokine CCL2Peptide LibraryPeptides

Identifiers

PMID39715753
PMCPMC11666718

What OpenQuestion holds

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LicenceCC BY-NC-ND
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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.