Evidence map›Paper›PMID 32270446›Full record

ReviewBiophysical reviews2020

Theoretical identification of thermostabilizing amino acid mutations for G-protein-coupled receptors.

Takeshi Murata, Satoshi Yasuda, Tomohiko Hayashi, Masahiro Kinoshita

Open access · bronzeAbstract readReview
PubMed Full text at PMC Publisher
In one paragraph

Review in Biophysical reviews, 2020. 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
0.4field-weighted citation impact, top 41% 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

1 citing paper in PubMed, 6 citations in OpenAlex.

  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

4 authors at 3 institutions in 1 country.

Takeshi MurataGraduate School of Science, Chiba University, 1-33 Yayoi-cho, Inage, Chiba, 263-8522, Japan.
Satoshi YasudaGraduate School of Science, Chiba University, 1-33 Yayoi-cho, Inage, Chiba, 263-8522, Japan.
Tomohiko HayashiInstitute of Advanced Energy, Kyoto University, Uji, Kyoto, 611-0011, Japan.
Masahiro KinoshitaInstitute of Advanced Energy, Kyoto University, Uji, Kyoto, 611-0011, Japan. kinoshit@iae.kyoto-u.ac.jp.
Chiba University · JPKyoto University · JPNiigata University · JP

Funding

Cabinet Office, Government of Japan JP18am0101083Japan Agency for Medical Research and Development JP19am0101083Japan Society for the Promotion of Science 17H03663Japan Society for the Promotion of Science 17K15099Japan Society for the Promotion of Science 18H05425Japan Society for the Promotion of Science 19K14674
6 · The paper itself

Abstract

Thermostabilization of a membrane proteins, especially G-protein-coupled receptors (GPCRs), is often necessary for biochemical applications and pharmaceutical studies involving structure-based drug design. Here we review our theoretical, physics-based method for identifying thermostabilizing amino acid mutations. Its novel aspects are the following: The entropic effect originating from the translational displacement of hydrocarbon groups within the lipid bilayer is treated as a pivotal factor; a reliable measure of thermostability is introduced and a mutation which enlarges the measure to a significant extent is chosen; and all the possible mutations can be examined with moderate computational effort. It was shown that mutating the residue at a position of N

Indexed as

G-protein-coupled receptorIntegral equation theoryLipid bilayerMembrane proteinMorphometric approachProtein foldingSolvation thermodynamicsThermostabilizing mutation

Identifiers

PMID32270446
PMCPMC7242571
OpenAlexW3015262651

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.