Evidence map›Paper›PMID 30061529›Full record

ArticleBiomolecules2018

Understanding the Positional Binding and Substrate Interaction of a Highly Thermostable GH10 Xylanase from

Jiangke Yang, Zhenggang Han

Open access · goldAbstract read
In one paragraph

Article in Biomolecules, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.2field-weighted citation impact, top 22% 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

14 citing papers in PubMed, 24 citations in OpenAlex.

  1. Whole-genome analysis and enzymatic profiling of Bacillus spizizenii as a xylanase-producing source from Iran.International microbiology : the official journal of the Spanish Society for Microbiology · 2026
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  11. Improved secretory expression and characterization of thermostable xylanase andFrontiers in bioengineering and biotechnology · 2023
    Article
  12. A thermostable and CBM2-linked GH10 xylanase fromFrontiers in bioengineering and biotechnology · 2022
    Article
  13. Article
  14. 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

2 authors at 1 institution in 1 country.

Jiangke YangCollege of Biology and Pharmaceutical Engineering, Wuhan Polytechnic University, Wuhan 430023, China. jiangke.yang@gmail.com.
Zhenggang HanCollege of Biology and Pharmaceutical Engineering, Wuhan Polytechnic University, Wuhan 430023, China. zhengganghan@whpu.edu.cn.
Wuhan Polytechnic University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Glycoside hydrolase family 10 (GH10) xylanases are responsible for enzymatic cleavage of the internal glycosidic linkages of the xylan backbone, to generate xylooligosaccharides (XOS) and xyloses. The topologies of active-site cleft determine the substrate preferences and product profiles of xylanases. In this study, positional bindings and substrate interactions of TmxB, one of the most thermostable xylanases characterized from

Indexed as

Molecular Docking SimulationTemperatureAmino Acid SequenceCatalytic DomainEndo-1,4-beta XylanasesEnzyme StabilityGlucuronatesOligosaccharidesProtein BindingSubstrate SpecificityThermotoga maritimaEndo-1,4-beta XylanasesGlucuronatesOligosaccharidesxylooligosaccharideAutoDockglycoside hydrolase family 10molecular dockingxylanasexylooligosaccharide

Identifiers

PMID30061529
PMCPMC6163442
OpenAlexW2884177657

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.