Evidence map›Paper›PMID 37861467›Full record

ArticleProtein science : a publication of the Protein Society2023

Conformation state-specific monobodies regulate the functions of flexible proteins through conformation trapping.

Ibuki Nakamura, Hiroshi Amesaka, Mizuho Hara, Kento Yonezawa, Keisuke Okamoto, Hironari Kamikubo, Shun-Ichi Tanaka, Takashi Matsuo

Open access · bronzeAbstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
1.1field-weighted citation impact, top 21% 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

3 citing papers in PubMed, 5 citations in OpenAlex.

  1. Article
  2. Article
  3. 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 at 3 institutions in 1 country.

Ibuki NakamuraDivision of Materials Science, Graduate School of Science and Technology, Nara Institute of Science and Technology (NAIST), Nara, Japan.ORCID 0000-0002-7274-1137
Hiroshi AmesakaGraduate School of Life and Environmental Sciences, Kyoto Prefectural University, Kyoto, Japan.ORCID 0000-0003-1688-7796
Mizuho HaraGraduate School of Life and Environmental Sciences, Kyoto Prefectural University, Kyoto, Japan.ORCID 0000-0003-0941-0279
Kento YonezawaDivision of Materials Science, Graduate School of Science and Technology, Nara Institute of Science and Technology (NAIST), Nara, Japan.ORCID 0000-0002-6656-0313
Keisuke OkamotoGraduate School of Life and Environmental Sciences, Kyoto Prefectural University, Kyoto, Japan.ORCID 0009-0009-8124-3680
Hironari KamikuboDivision of Materials Science, Graduate School of Science and Technology, Nara Institute of Science and Technology (NAIST), Nara, Japan.ORCID 0000-0002-0878-6488
Shun-Ichi TanakaGraduate School of Life and Environmental Sciences, Kyoto Prefectural University, Kyoto, Japan.ORCID 0000-0003-4270-0374
Takashi MatsuoDivision of Materials Science, Graduate School of Science and Technology, Nara Institute of Science and Technology (NAIST), Nara, Japan.ORCID 0000-0002-5646-6251
Nara Institute of Science and Technology · JPKyoto Prefectural University · JPRitsumeikan University · JP

Funding

Japan Society for the Promotion of ScienceMurata Science Foundation
6 · The paper itself

Abstract

Synthetic binding proteins have emerged as modulators of protein functions through protein-protein interactions (PPIs). Because PPIs are influenced by the structural dynamics of targeted proteins, investigating whether the synthetic-binders-based strategy is applicable for proteins with large conformational changes is important. This study demonstrates the applicability of monobodies (fibronectin type-III domain-based synthetic binding proteins) in regulating the functions of proteins that undergo tens-of-angstroms-scale conformational changes, using an example of the A55C/C77S/V169C triple mutant (Adk

Indexed as

Carrier ProteinsBinding SitesChromatographyCrystallography, X-RayProtein BindingProtein ConformationScattering, Small AngleX-Ray DiffractionCarrier Proteinsadenylate kinaseconformational changemonobodyprotein-protein interaction (PPI)pyreneSEC-SAXSsynthetic binding protein

Identifiers

PMID37861467
PMCPMC10659937
OpenAlexW4387798434

What OpenQuestion holds

Textmetadata
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.