Evidence map›Paper›PMID 31783503›Full record

ArticleInternational journal of molecular sciences2019

Crystal Structure of a GH3 β-Glucosidase from the Thermophilic Fungus

Imran Mohsin, Nirmal Poudel, Duo-Chuan Li, Anastassios C Papageorgiou

Abstract read
In one paragraph

Article in International journal of molecular sciences, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
–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

8 citing papers in PubMed.

  1. Application of Immobilized β-Glucosidase fromIndian journal of microbiology · 2024
    Article
  2. Article
  3. Lignocellulolytic extremozymes and their biotechnological applications.Extremophiles : life under extreme conditions · 2023
    Review
  4. Article
  5. Profiling of the β-glucosidases identified in the genome ofApplied and environmental microbiology · 2023
    Article
  6. Article
  7. Review
  8. Carbohydrate-Active Enzymes: Structure, Activity, and Reaction Products.International journal of molecular sciences · 2020
    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

4 authors.

Imran MohsinTurku Bioscience, University of Turku and Åbo Akademi University, 20520 Turku, Finland.
Nirmal PoudelTurku Bioscience, University of Turku and Åbo Akademi University, 20520 Turku, Finland.
Duo-Chuan LiDepartment of Mycology, Shandong Agricultural University, Taian 271018, China.
Anastassios C PapageorgiouTurku Bioscience, University of Turku and Åbo Akademi University, 20520 Turku, Finland.ORCID 0000-0002-7980-1120

Funding

Chinese National Nature Science Foundation 31571949
6 · The paper itself

Abstract

Beta-glucosidases (β-glucosidases) have attracted considerable attention in recent years for use in various biotechnological applications. They are also essential enzymes for lignocellulose degradation in biofuel production. However, cost-effective biomass conversion requires the use of highly efficient enzymes. Thus, the search for new enzymes as better alternatives of the currently available enzyme preparations is highly important. Thermophilic fungi are nowadays considered as a promising source of enzymes with improved stability. Here, the crystal structure of a family GH3 β-glucosidase from the thermophilic fungus

Indexed as

beta-GlucosidaseCatalytic DomainChaetomiumCrystallography, X-RayFungal ProteinsGlycosylationHydrolysisLigninSubstrate Specificitybeta-GlucosidaseFungal ProteinsLigninlignocellulosecellulose degradationChaetomium thermophilumfungal enzymesglycoside hydrolaseprotein structurethermophilic fungusβ-glucosidases

Identifiers

PMID31783503
PMCPMC6929035

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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.