Evidence map›Paper›PMID 32549280›Full record

ArticleBiomolecules2020

Structural Basis of Specific Glucoimidazole and Mannoimidazole Binding by Os3BGlu7.

Bodee Nutho, Salila Pengthaisong, Anupong Tankrathok, Vannajan Sanghiran Lee, James R Ketudat Cairns, Thanyada Rungrotmongkol, Supot Hannongbua

Open access · goldAbstract read
In one paragraph

Article in Biomolecules, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.8field-weighted citation impact, top 16% 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

12 citing papers in PubMed, 19 citations in OpenAlex.

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  5. 3,4,3'-Tri-RSC advances · 2022
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  8. TheBiomolecules · 2022
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  9. Article
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  12. 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 3 institutions in 2 countries.

Bodee NuthoCenter of Excellence in Computational Chemistry (CECC), Department of Chemistry, Faculty of Science, Chulalongkorn University, Bangkok 10330, Thailand.
Salila PengthaisongSchool of Chemistry, Institute of Science, Suranaree University of Technology, Nakhon Ratchasima 30000, Thailand.
Anupong TankrathokSchool of Chemistry, Institute of Science, Suranaree University of Technology, Nakhon Ratchasima 30000, Thailand.
Vannajan Sanghiran LeeDepartment of Chemistry, Faculty of Science, University of Malaya, Kuala Lumpur 50603, Malaysia.
James R Ketudat CairnsSchool of Chemistry, Institute of Science, Suranaree University of Technology, Nakhon Ratchasima 30000, Thailand.ORCID 0000-0003-3042-1626
Thanyada RungrotmongkolBiocatalyst and Environmental Biotechnology Research Unit, Department of Biochemistry, Faculty of Science, Chulalongkorn University, Bangkok 10330, Thailand.
Supot HannongbuaCenter of Excellence in Computational Chemistry (CECC), Department of Chemistry, Faculty of Science, Chulalongkorn University, Bangkok 10330, Thailand.
Chulalongkorn University · THSuranaree University of Technology · THUniversity of Malaya · MY

Funding

Second Century Fund C2FSuranaree University of Technology BRG5980015Thailand Research Fund TRF
6 · The paper itself

Abstract

β-Glucosidases and β-mannosidases hydrolyze substrates that differ only in the epimer of the nonreducing terminal sugar moiety, but most such enzymes show a strong preference for one activity or the other. Rice Os3BGlu7 and Os7BGlu26 β-glycosidases show a less strong preference, but Os3BGlu7 and Os7BGlu26 prefer glucosides and mannosides, respectively. Previous studies of crystal structures with glucoimidazole (GIm) and mannoimidazole (MIm) complexes and metadynamic simulations suggested that Os7BGlu26 hydrolyzes mannosides via the

Indexed as

GlycosidesImidazolesAmino Acid Sequencebeta-GlucosidaseBinding SitesCrystallography, X-RayGlucoseHydrolysisMannoseModels, MolecularMolecular Docking SimulationMolecular Dynamics SimulationOryzaProtein BindingProtein ConformationSubstrate Specificitybeta-GlucosidaseGlucoseGlycosidesimidazoleImidazolesMannoseMD simulationREMDtransition state mimicsX-ray crystallographyβ-glycosidase

Identifiers

PMID32549280
PMCPMC7356692
OpenAlexW3034312421

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.