Evidence map›Paper›PMID 32102340›Full record

ArticleMolecules (Basel, Switzerland)2020

Novel Chaperones

Chunmeng Xu, Lingjun Tang, Youxiang Liang, Song Jiao, Huimin Yu, Hui Luo

Open access · goldAbstract read
In one paragraph

Article in Molecules (Basel, Switzerland), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
1.0field-weighted citation impact, top 29% 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

4 citing papers in PubMed, 15 citations in OpenAlex.

  1. Article
  2. Article
  3. Phe-140 Determines the Catalytic Efficiency of Arylacetonitrilase fromInternational journal of molecular sciences · 2020
    Article
  4. 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 2 institutions in 1 country.

Chunmeng XuKey Laboratory of Industrial Biocatalysis, Ministry of Education, Beijing 100084, China.
Lingjun TangKey Laboratory of Industrial Biocatalysis, Ministry of Education, Beijing 100084, China.
Youxiang LiangKey Laboratory of Industrial Biocatalysis, Ministry of Education, Beijing 100084, China.
Song JiaoKey Laboratory of Industrial Biocatalysis, Ministry of Education, Beijing 100084, China.
Huimin YuKey Laboratory of Industrial Biocatalysis, Ministry of Education, Beijing 100084, China.
Hui LuoDepartment of Biological Science and Engineering, University of Science and Technology Beijing, Beijing 100083, China.
Tsinghua University · CNUniversity of Science and Technology Beijing · CN

Funding

National Key R&D Program of China 2018YFA0901700Natural Science Foundation of China No. 21776157; No. 21476126
6 · The paper itself

Abstract

For large-scale bioproduction, thermal stability is a crucial property for most industrial enzymes. A new method to improve both the thermal stability and activity of enzymes is of great significance. In this work, the novel chaperones

Indexed as

Genome, BacterialAminohydrolasesBacterial ProteinsChaperonin 60Cloning, MolecularCRISPR-Cas SystemsEnzyme StabilityEscherichia coliGene EditingGene ExpressionGenetic EngineeringHumansKineticsModels, MolecularPlasmidsProtein Conformation, alpha-HelicalAminohydrolasesBacterial ProteinsChaperonin 60nitrilaseRecombinant Fusion ProteinschaperoneE. colinitrilaseR. ruberstability

Identifiers

PMID32102340
PMCPMC7070999
OpenAlexW3008794332

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.