Evidence map›Paper›PMID 34944526›Full record

ArticleBiomolecules2021

Improving the Substrate Affinity and Catalytic Efficiency of β-Glucosidase Bgl3A from

Wei Xia, Yingguo Bai, Pengjun Shi

Open access · goldAbstract read
In one paragraph

Article in Biomolecules, 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
1.3field-weighted citation impact, top 21% 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, 18 citations in OpenAlex.

  1. Review
  2. Article
  3. Site-Directed Mutagenesis Increased the Catalytic Activity and Stability ofInternational journal of molecular sciences · 2025
    Article
  4. Review
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

3 authors at 2 institutions in 1 country.

Wei XiaInstitute of Food Science and Technology, Chinese Academy of Agricultural Sciences, Beijing 100081, China.ORCID 0000-0001-8820-5833
Yingguo BaiInstitute of Animal Science, Chinese Academy of Agricultural Sciences, Beijing 100193, China.
Pengjun ShiInstitute of Food Science and Technology, Chinese Academy of Agricultural Sciences, Beijing 100081, China.
Institute of Food Science and Technology · CNChinese Academy of Agricultural Sciences · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Improving the substrate affinity and catalytic efficiency of β-glucosidase is necessary for better performance in the enzymatic saccharification of cellulosic biomass because of its ability to prevent cellobiose inhibition on cellulases. Bgl3A from

Indexed as

Mutationbeta-GlucosidaseBinding SitesBiocatalysisCellobioseFungal ProteinsHydrogen BondingHydrogen-Ion ConcentrationModels, MolecularMolecular Dynamics SimulationProtein ConformationSubstrate SpecificityTalaromycesbeta-GlucosidaseCellobioseFungal Proteinscellobioseenzyme engineeringmolecular dynamics simulationsubstrate affinityβ-glucosidase

Identifiers

PMID34944526
PMCPMC8699594
OpenAlexW4200206396

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.