Evidence map›Paper›PMID 32512945›Full record

ArticleInternational journal of molecular sciences2020

In-Silico Characterization of Glycosyl Hydrolase Family 1 β-Glucosidase from

Mohamad Farhan Mohamad Sobri, Suraini Abd-Aziz, Farah Diba Abu Bakar, Norhayati Ramli

Abstract read
In one paragraph

Article in International journal of molecular sciences, 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
–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

4 citing papers in PubMed.

  1. Characterization of a New Glucose-Tolerant GH1 β-Glycosidase fromInternational journal of molecular sciences · 2023
    Article
  2. Review
  3. 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

4 authors.

Mohamad Farhan Mohamad SobriDepartment of Bioprocess Technology, Faculty of Biotechnology and Biomolecular Sciences, Universiti Putra Malaysia, Serdang 43400 UPM, Selangor, Malaysia.
Suraini Abd-AzizDepartment of Bioprocess Technology, Faculty of Biotechnology and Biomolecular Sciences, Universiti Putra Malaysia, Serdang 43400 UPM, Selangor, Malaysia.ORCID 0000-0002-4202-9069
Farah Diba Abu BakarSchool of Biosciences and Biotechnology, Faculty of Science and Technology, Universiti Kebangsaan Malaysia, Bangi 43600 UKM, Selangor, Malaysia.
Norhayati RamliDepartment of Bioprocess Technology, Faculty of Biotechnology and Biomolecular Sciences, Universiti Putra Malaysia, Serdang 43400 UPM, Selangor, Malaysia.ORCID 0000-0002-8015-8654

Funding

Universiti Putra Malaysia GP-IPM/2013/9402000Universiti Putra Malaysia GP-IPS/2014/9429400
6 · The paper itself

Abstract

β-glucosidases (Bgl) are widely utilized for releasing non-reducing terminal glucosyl residues. Nevertheless, feedback inhibition by glucose end product has limited its application. A noticeable exception has been found for β-glucosidases of the glycoside hydrolase (GH) family 1, which exhibit tolerance and even stimulation by glucose. In this study, using local isolate

Indexed as

Models, MolecularProtein ConformationAmino Acid SequenceBase Sequencebeta-GlucosidaseChemical PhenomenaHydrophobic and Hydrophilic InteractionsHypocrealesN-Glycosyl HydrolasesPhylogenyStructure-Activity Relationshipbeta-GlucosidaseN-Glycosyl Hydrolasesglycosyl hydrolase family 1in-silico analysesTrichoderma asperellumβ-glucosidase

Identifiers

PMID32512945
PMCPMC7311958

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.