Evidence map›Paper›PMID 31333816›Full record

ArticleComputational and structural biotechnology journal2019

Evolutionary Stability of Salt Bridges Hints Its Contribution to Stability of Proteins.

Xiaofeng Ban, Pratik Lahiri, Abhishek S Dhoble, Dan Li, Zhengbiao Gu, Caiming Li, Li Cheng, Yan Hong, Zhaofeng Li, Bhalerao Kaustubh

Abstract read
In one paragraph

Article in Computational and structural biotechnology journal, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed, 1 pooled it
–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

22 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Fidaxomicin resistance inAntimicrobial agents and chemotherapy · 2024
    Pooled it
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  18. Structural Insights of PD-1/PD-L1 Axis: AnCurrent protein & peptide science · 2024
    Article
  19. Article
  20. 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

10 authors.

Xiaofeng BanSchool of Food Science and Technology, Jiangnan University, Wuxi 214122, China.
Pratik LahiriDepartment of Agricultural and Biological Engineering, University of Illinois at Urbana-Champaign, IL-61801, USA.
Abhishek S DhobleDepartment of Agricultural and Biological Engineering, University of Illinois at Urbana-Champaign, IL-61801, USA.
Dan LiThe Second Military Medical University, Shanghai, China.
Zhengbiao GuState Key Laboratory of Food Science and Technology, Jiangnan University, Wuxi 214122, China.
Caiming LiSchool of Food Science and Technology, Jiangnan University, Wuxi 214122, China.
Li ChengSchool of Food Science and Technology, Jiangnan University, Wuxi 214122, China.
Yan HongSchool of Food Science and Technology, Jiangnan University, Wuxi 214122, China.
Zhaofeng LiState Key Laboratory of Food Science and Technology, Jiangnan University, Wuxi 214122, China.
Bhalerao KaustubhDepartment of Agricultural and Biological Engineering, University of Illinois at Urbana-Champaign, IL-61801, USA.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The contribution of newly designed salt bridges to protein stabilization remains controversial even today. In order to solve this problem, we investigated salt bridges from two aspects: spatial distribution and evolutionary characteristics of salt bridges. Firstly, we analyzed spatial distribution of salt bridges in proteins, elucidating the basic requirements of forming salt bridges. Then, from an evolutionary point of view, the evolutionary characteristics of salt bridges as well as their neighboring residues were investigated in our study. The results demonstrate that charged residues appear more frequently than other neutral residues at certain positions of sequence even under evolutionary pressure, which are able to form electrostatic interactions that could increase the evolutionary stability of corresponding amino acid regions, enhancing their importance to stability of proteins. As a corollary, we conjectured that the newly designed salt bridges with more contribution to proteins, not only, are qualified spatial distribution of salt bridges, but also, are needed to further increase the evolutionary stability of corresponding amino acid regions. Based on analysis, the 8 mutations were accordingly constructed in the 1,4-α-glucan branching enzyme (EC 2.4.1.18, GBE) from

Indexed as

Evolutionary stabilityEvolutionary traceMutagenesisSalt bridgeThermostability

Identifiers

PMID31333816
PMCPMC6620738

What OpenQuestion holds

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Registered trials

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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.