Evidence map›Paper›PMID 33808840›Full record

ArticleMolecules (Basel, Switzerland)2021

Two Key Amino Acids Variant of α-l-arabinofuranosidase from

Ru Zhang, Shi Quan Tan, Bian Ling Zhang, Zi Yu Guo, Liang Yu Tian, Pei Weng, Zhi Yong Luo

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

Article in Molecules (Basel, Switzerland), 2021. 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
0.6field-weighted citation impact, top 34% 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, 11 citations in OpenAlex.

  1. Review
  2. Review
  3. Review
  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

7 authors at 2 institutions in 1 country.

Ru ZhangCollege of Materials and Chemical Engineering, Hunan Institute of Engineering, Xiangtan 411104, China.
Shi Quan TanCollege of Materials and Chemical Engineering, Hunan Institute of Engineering, Xiangtan 411104, China.
Bian Ling ZhangCollege of Materials and Chemical Engineering, Hunan Institute of Engineering, Xiangtan 411104, China.
Zi Yu GuoCollege of Materials and Chemical Engineering, Hunan Institute of Engineering, Xiangtan 411104, China.
Liang Yu TianCollege of Materials and Chemical Engineering, Hunan Institute of Engineering, Xiangtan 411104, China.
Pei WengCollege of Materials and Chemical Engineering, Hunan Institute of Engineering, Xiangtan 411104, China.
Zhi Yong LuoMolecular Biology Research Center, School of Life Sciences, Central South University, Changsha 410078, China.
Hunan Institute of Engineering · CNCentral South University · CN

Funding

National Natural Science Foundation of China 81874332, 81973710Natural Science Foundation of Hunan Province 2020JJ2012Postdoctoral Science Foundation of China 2017T100601, 2016M590746
6 · The paper itself

Abstract

α-l-arabinofuranosidase is a subfamily of glycosidases involved in the hydrolysis of l-arabinofuranosidic bonds, especially in those of the terminal non-reducing arabinofuranosyl residues of glycosides, from which efficient glycoside hydrolases can be screened for the transformation of ginsenosides. In this study, the ginsenoside Rc-hydrolyzing α-l-arabinofuranosidase gene,

Indexed as

Amino Acid SubstitutionBacillus subtilisBacterial ProteinsGlycoside HydrolasesMutagenesis, Site-DirectedGinsenosidesMutation, MissenseRecombinant Fusion Proteinsalpha-N-arabinofuranosidaseBacterial Proteinsginsenoside Rcginsenoside RdGinsenosidesGlycoside HydrolasesRecombinant Fusion ProteinsBacilus subtilisbiotransformationginsenoside Rcginsenoside Rdmolecular dockingsite-directed mutagenesisα-l-arabinofuranosidase

Identifiers

PMID33808840
PMCPMC8003784
OpenAlexW3136804618

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.