Evidence map›Paper›PMID 39525645›Full record

ArticleData in brief2024

Data on the crystal structures of β-glucosidase from

Ki Hyun Nam

Abstract read
In one paragraph

Article in Data in brief, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing 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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

1 author.

Ki Hyun NamCollege of General Education, Kookmin University, Seoul 02707, Republic of Korea.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

β-Glucosidase (Bgl) is a biomass-degrading enzyme that hydrolyzes cellobiose and glucose-substituted polysaccharides into glucose, playing a crucial role in enzymatic saccharification during biofuel production. Despite the wealth of structural information available on Bgl, the molecular properties of the loops above the substrate-binding pocket remain unexplored. In previous study, to better understand the molecular functions of these loop regions, four crystal structures of

Indexed as

Loop structureStructural dynamicsTemperature factorβ-glucosidase (Bgl)

Identifiers

PMID39525645
PMCPMC11546679

What OpenQuestion holds

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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.