Evidence map›Paper›PMID 36173170›Full record

ArticleProtein science : a publication of the Protein Society2022

A methodology for creating mutants of G-protein coupled receptors stabilized in active state by combining statistical thermodynamics and evolutionary molecular engineering.

Taisei Yamamoto, Satoshi Yasuda, Rinshi S Kasai, Ryosuke Nakano, Simon Hikiri, Kanna Sugaya, Tomohiko Hayashi, Satoshi Ogasawara, Mitsunori Shiroishi, Takahiro K Fujiwara and 2 more

Open access · greenAbstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2022. 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
0.5field-weighted citation impact, top 38% 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, 7 citations in OpenAlex.

  1. Journal of the American Chemical Society · 2026
    Article
  2. Recovery of the histamine HScientific reports · 2023
    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

12 authors at 4 institutions in 1 country.

Taisei YamamotoDepartment of Chemistry, Graduate School of Science, Chiba University, Chiba, Japan.
Satoshi YasudaDepartment of Chemistry, Graduate School of Science, Chiba University, Chiba, Japan.ORCID 0000-0003-3555-1083
Rinshi S KasaiInstitute for Glyco-core Research (iGCORE), Gifu University, Gifu, Japan.ORCID 0000-0002-9234-3283
Ryosuke NakanoDepartment of Chemistry, Graduate School of Science, Chiba University, Chiba, Japan.
Simon HikiriGraduate School of Engineering Science, Osaka University, Osaka, Japan.
Kanna SugayaDepartment of Chemistry, Graduate School of Science, Chiba University, Chiba, Japan.
Tomohiko HayashiInterdisciplinary Program of Biomedical Engineering, Assistive Technology, and Art and Sports Sciences, Faculty of Engineering, Niigata University, Niigata, Japan.
Satoshi OgasawaraDepartment of Chemistry, Graduate School of Science, Chiba University, Chiba, Japan.
Mitsunori ShiroishiDepartment of Biological Science and Technology, Tokyo University of Science, Tokyo, Japan.ORCID 0000-0002-3133-157X
Takahiro K FujiwaraInstitute for Integrated Cell-Material Sciences (WPI-iCeMS), Kyoto University, Kyoto, Japan.ORCID 0000-0001-5576-759X
Masahiro KinoshitaDepartment of Chemistry, Graduate School of Science, Chiba University, Chiba, Japan.ORCID 0000-0001-8060-045X
Takeshi MurataDepartment of Chemistry, Graduate School of Science, Chiba University, Chiba, Japan.
Chiba University · JPKyoto University · JPOsaka Health Science University · JPTokyo University of Science · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We challenged the stabilization of a G-protein coupled receptor (GPCR) in the active state solely by multiple amino-acid mutations without the agonist binding. For many GPCRs, the free energy of the active state is higher than that of the inactive state. When the inactive state is stabilized through the lowering of its free energy, the apparent midpoint temperature of thermal denaturation T

Indexed as

GTP-Binding ProteinsReceptor, Adenosine A2AMutationThermodynamicsGTP-Binding ProteinsReceptor, Adenosine A2Aactive stateagonistamino-acid mutationconfigurational entropyG proteinG-protein coupled receptorhydrocarbon grouphydrogen bondlipid moleculesite-directed saturation mutagenesis

Identifiers

PMID36173170
PMCPMC9490800
OpenAlexW4296959560

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.