Evidence map›Paper›PMID 41390874›Full record

ArticleAntonie van Leeuwenhoek2025

Cloning, heterologus expression and characterization of a thermophilic and salt tolerant GH11 xylanase from Allostreptomyces psammosilenae YIM DR4008

Xin-Wei Li, Dan Zhu, Lei Li, Run-Feng Yang, Shi-Yuan Fan, Zhi-Hua Lv, Meng-Di Rao, Rong-Huang Song, Peng Sang, Yi-Rui Yin and 1 more

Abstract read
PubMed Publisher
In one paragraph

Article in Antonie van Leeuwenhoek, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Article
  2. Enzymatic Treatments for Biosolids: An Outlook and Recent Trends.International journal of environmental research and public health · 2023
    Review
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

11 authors.

Xin-Wei Li *College of Agriculture and Biological Science, Dali University, Dali, 671003, People's Republic of China.
Dan Zhu *College of Agriculture and Biological Science, Dali University, Dali, 671003, People's Republic of China.
Lei LiCollege of Agriculture and Biological Science, Dali University, Dali, 671003, People's Republic of China.
Run-Feng YangCollege of Agriculture and Biological Science, Dali University, Dali, 671003, People's Republic of China.
Shi-Yuan FanCollege of Agriculture and Biological Science, Dali University, Dali, 671003, People's Republic of China.
Zhi-Hua LvCollege of Agriculture and Biological Science, Dali University, Dali, 671003, People's Republic of China.
Meng-Di RaoCollege of Agriculture and Biological Science, Dali University, Dali, 671003, People's Republic of China.
Rong-Huang SongCollege of Agriculture and Biological Science, Dali University, Dali, 671003, People's Republic of China.
Peng SangCollege of Agriculture and Biological Science, Dali University, Dali, 671003, People's Republic of China.
Yi-Rui YinCollege of Agriculture and Biological Science, Dali University, Dali, 671003, People's Republic of China. yinyirui@dali.edu.cn.
Li-Quan YangCollege of Agriculture and Biological Science, Dali University, Dali, 671003, People's Republic of China. ylqbioinfo@163.com.

Funding

National Natural Sciences Foundation of China Regional Program 31660015 and 31860243Yunnan Applied Basic Research Projects 2017FB024 and 2017FH001-032Yunnan Applied Basic Research Projects 202101AU070138
6 · The paper itself

Abstract

Xylanases are used in a wide range of applications such as food, feed, and bioenergy production. Many industrial applications need to be carried out at high temperatures, so it is important to discover new thermophilic xylanases. In this study, a xylanase gene (576 bp), denominated apxyn11a, was obtained from Allostreptomyces psammosilenae YIM DR4008

Indexed as

Endo-1,4-beta XylanasesCloning, MolecularEnzyme StabilityEscherichia coliHydrogen-Ion ConcentrationKineticsRecombinant ProteinsSalt ToleranceSubstrate SpecificityTemperatureEndo-1,4-beta XylanasesRecombinant ProteinsAllostreptomyces psammosilenaeSalt tolerantThermophilicXylanase

Identifiers

PMID41390874

What OpenQuestion holds

Textmetadata
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.