Evidence map›Paper›PMID 28974575›Full record

ArticleThe Journal of biological chemistry2017

Insights into the roles of non-catalytic residues in the active site of a GH10 xylanase with activity on cellulose.

Yindi Chu, Tao Tu, Leena Penttinen, Xianli Xue, Xiaoyu Wang, Zhuolin Yi, Li Gong, Juha Rouvinen, Huiying Luo, Nina Hakulinen and 2 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.8field-weighted citation impact, top 15% 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

20 citing papers in PubMed, 45 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. A thermostable and CBM2-linked GH10 xylanase fromFrontiers in bioengineering and biotechnology · 2022
    Article
  8. Review
  9. Article
  10. Article
  11. Xylanase from Marine Filamentous FungusJournal of applied glycoscience · 2021
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. 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

12 authors at 4 institutions in 2 countries.

Yindi ChuFrom the Key Laboratory for Feed Biotechnology of the Ministry of Agriculture, Feed Research Institute, Chinese Academy of Agricultural Sciences, Beijing 100081, China.
Tao TuFrom the Key Laboratory for Feed Biotechnology of the Ministry of Agriculture, Feed Research Institute, Chinese Academy of Agricultural Sciences, Beijing 100081, China.
Leena Penttinenthe Department of Chemistry, University of Eastern Finland, Joensuu Campus, Joensuu FIN-80101, Finland.
Xianli XueFrom the Key Laboratory for Feed Biotechnology of the Ministry of Agriculture, Feed Research Institute, Chinese Academy of Agricultural Sciences, Beijing 100081, China.
Xiaoyu WangFrom the Key Laboratory for Feed Biotechnology of the Ministry of Agriculture, Feed Research Institute, Chinese Academy of Agricultural Sciences, Beijing 100081, China.
Zhuolin Yithe Chengdu Institute of Biology, Chinese Academy of Sciences, Chengdu 610041, China, and.
Li GongFrom the Key Laboratory for Feed Biotechnology of the Ministry of Agriculture, Feed Research Institute, Chinese Academy of Agricultural Sciences, Beijing 100081, China.
Juha Rouvinenthe Department of Chemistry, University of Eastern Finland, Joensuu Campus, Joensuu FIN-80101, Finland.
Huiying LuoFrom the Key Laboratory for Feed Biotechnology of the Ministry of Agriculture, Feed Research Institute, Chinese Academy of Agricultural Sciences, Beijing 100081, China.
Nina Hakulinenthe Department of Chemistry, University of Eastern Finland, Joensuu Campus, Joensuu FIN-80101, Finland, nina.hakulinen@uef.fi.
Bin YaoFrom the Key Laboratory for Feed Biotechnology of the Ministry of Agriculture, Feed Research Institute, Chinese Academy of Agricultural Sciences, Beijing 100081, China, binyao@caas.cn.
Xiaoyun SuFrom the Key Laboratory for Feed Biotechnology of the Ministry of Agriculture, Feed Research Institute, Chinese Academy of Agricultural Sciences, Beijing 100081, China, suxiaoyun@caas.cn.
Chinese Academy of Agricultural Sciences · CNFeed Research Institute · CNUniversity of Eastern Finland · FIChinese Academy of Sciences · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Bifunctional glycoside hydrolases have potential for cost-savings in enzymatic decomposition of plant cell wall polysaccharides for biofuels and bio-based chemicals. The N-terminal GH10 domain of a bifunctional multimodular enzyme

Indexed as

Amino Acid SequenceBacillotaBiocatalysisCatalytic DomainCelluloseCrystallography, X-RayEndo-1,4-beta XylanasesHydrolysisModels, MolecularMutagenesis, Site-DirectedMutationProtein BindingProtein ConformationSequence HomologySubstrate SpecificityCelluloseEndo-1,4-beta Xylanasesbifunctionalbiofuelscellulasecrystal structureGH10glycoside hydrolasemolecular dockingmutagenesisxylanase

Identifiers

PMID28974575
PMCPMC5702671
OpenAlexW2761123924

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.