Evidence map›Paper›PMID 31709055›Full record

ArticleIUCrJ2019

Mutagenesis facilitated crystallization of GLP-1R.

Yueming Xu, Yuxia Wang, Yang Wang, Kaiwen Liu, Yao Peng, Deqiang Yao, Houchao Tao, Haiguang Liu, Gaojie Song

Open access · goldAbstract read
In one paragraph

Article in IUCrJ, 2019. 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
2.4field-weighted citation impact, top 11% 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

7 citing papers in PubMed, 17 citations in OpenAlex.

  1. Article
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  4. Article
  5. Review
  6. Current Trends in GPCR Allostery.The Journal of membrane biology · 2021
    Article
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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

9 authors at 3 institutions in 1 country.

Yueming XuShanghai Key Laboratory of Regulatory Biology, Institute of Biomedical Sciences and School of Life Sciences, East China Normal University, Shanghai 200241, People's Republic of China.
Yuxia WangiHuman Institute, ShanghaiTech University, 393 Middle Huaxia Road, Shanghai 201210, People's Republic of China.
Yang WangComplex Systems Division, Beijing Computational Science Research Center, Beijing 100193, People's Republic of China.
Kaiwen LiuiHuman Institute, ShanghaiTech University, 393 Middle Huaxia Road, Shanghai 201210, People's Republic of China.
Yao PengiHuman Institute, ShanghaiTech University, 393 Middle Huaxia Road, Shanghai 201210, People's Republic of China.
Deqiang YaoiHuman Institute, ShanghaiTech University, 393 Middle Huaxia Road, Shanghai 201210, People's Republic of China.
Houchao TaoiHuman Institute, ShanghaiTech University, 393 Middle Huaxia Road, Shanghai 201210, People's Republic of China.
Haiguang LiuComplex Systems Division, Beijing Computational Science Research Center, Beijing 100193, People's Republic of China.ORCID https://orcid.org/0000-0001-7324-6632
Gaojie SongShanghai Key Laboratory of Regulatory Biology, Institute of Biomedical Sciences and School of Life Sciences, East China Normal University, Shanghai 200241, People's Republic of China.
ShanghaiTech University · CNEast China Normal University · CNBeijing Computational Science Research Center · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The class B family of G-protein-coupled receptors (GPCRs) has long been a paradigm for peptide hormone recognition and signal transduction. One class B GPCR, the glucagon-like peptide-1 receptor (GLP-1R), has been considered as an anti-diabetes drug target and there are several peptidic drugs available for the treatment of this overwhelming disease. The previously determined structures of inactive GLP-1R in complex with two negative allosteric modulators include ten thermal-stabilizing mutations that were selected from a total of 98 designed mutations. Here we systematically summarize all 98 mutations we have tested and the results suggest that the mutagenesis strategy that strengthens inter-helical hydro-phobic interactions shows the highest success rate. We further investigate four back mutations by thermal-shift assay, crystallization and molecular dynamic simulations, and conclude that mutation I196

Indexed as

crystallizationglucagon-like peptide-1 receptorG-protein-coupled receptorsmembrane proteinsmolecular dynamic simulationsmutations

Identifiers

PMID31709055
PMCPMC6830218
OpenAlexW2980701319

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.