Evidence map›Paper›PMID 36012226›Full record

ArticleInternational journal of molecular sciences2022

Discovery of the Key Mutation Site Influencing the Thermostability of

Enheng Zhu, Xia Xiang, Sidi Wan, Huabiao Miao, Nanyu Han, Zunxi Huang

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in International journal of molecular sciences, 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
0.6field-weighted citation impact, top 36% 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, 9 citations in OpenAlex.

  1. Chemical Modification ofInternational journal of molecular sciences · 2025
    Article
  2. Review
  3. Improving the Thermostability ofInternational journal of molecular sciences · 2023
    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

6 authors at 1 institution in 1 country.

Enheng ZhuSchool of Life Sciences, Yunnan Normal University, Kunming 650500, China.
Xia XiangSchool of Life Sciences, Yunnan Normal University, Kunming 650500, China.
Sidi WanSchool of Life Sciences, Yunnan Normal University, Kunming 650500, China.
Huabiao MiaoSchool of Life Sciences, Yunnan Normal University, Kunming 650500, China.
Nanyu HanSchool of Life Sciences, Yunnan Normal University, Kunming 650500, China.
Zunxi HuangSchool of Life Sciences, Yunnan Normal University, Kunming 650500, China.
Yunnan Normal University · CN

Funding

Fundamental Research Founding of Yunnan Province 202201AT070033
6 · The paper itself

Abstract

Lipases are remarkable biocatalysts and are broadly applied in many industry fields because of their versatile catalytic capabilities. Considering the harsh biotechnological treatment of industrial processes, the activities of lipase products are required to be maintained under extreme conditions. In our current study, Gibbs free energy calculations were performed to predict potent thermostable

Indexed as

DEETEurotialesLipaseMutationDEETLipaseGibbs free energylipaseRosettathermostability

Identifiers

PMID36012226
PMCPMC9408933
OpenAlexW4290952099

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.