Evidence map›Paper›PMID 30373305›Full record

ReviewInternational journal of molecular sciences2018

Linking Enzymatic Oxidative Degradation of Lignin to Organics Detoxification.

Xiaolu Wang, Bin Yao, Xiaoyun Su

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
9.5field-weighted citation impact, top 2% 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

38 citing papers in PubMed, 137 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Phytoremediation of Wastewater From Oil Well Drilling: Potential of Different Plant Species.Water environment research : a research publication of the Water Environment Federation · 2026
    Article
  5. Article
  6. Review
  7. Review
  8. Review
  9. Asphaltene biotransformation by a novel enzyme thiol peroxidase fromApplied and environmental microbiology · 2025
    Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Review
  15. Article
  16. Recent Progress on Peroxidase Modification and Application.Applied biochemistry and biotechnology · 2024
    Review
  17. Contribution of Microbiota to Bioactivity Exerted by Bee Bread.Pharmaceuticals (Basel, Switzerland) · 2024
    Article
  18. Article
  19. Review
  20. 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

3 authors at 2 institutions in 1 country.

Xiaolu WangKey Laboratory for Feed Biotechnology of the Ministry of Agriculture, Feed Research Institute, Chinese Academy of Agricultural Sciences, Beijing 100081, China. xiaolu4444@126.com.
Bin YaoKey Laboratory for Feed Biotechnology of the Ministry of Agriculture, Feed Research Institute, Chinese Academy of Agricultural Sciences, Beijing 100081, China. binyao@caas.cn.
Xiaoyun SuKey Laboratory for Feed Biotechnology of the Ministry of Agriculture, Feed Research Institute, Chinese Academy of Agricultural Sciences, Beijing 100081, China. suxiaoyun@caas.cn.
Feed Research Institute · CNChinese Academy of Agricultural Sciences · CN

Funding

China Modern Agriculture Research System CARS-41Elite Youth Program of Chinese Academy of Agricultural Sciences n/aNational Key Research and Development Program of China 2016YFD0501409-02National Natural Science Foundation of China 31672458
6 · The paper itself

Abstract

The major enzymes involved in lignin degradation are laccase, class II peroxidases (lignin peroxidase, manganese peroxidase, and versatile peroxidase) and dye peroxidase, which use an oxidative or peroxidative mechanism to deconstruct the complex and recalcitrant lignin. Laccase and manganese peroxidase directly oxidize phenolic lignin components, while lignin peroxidase and versatile peroxidase can act on the more recalcitrant non-phenolic lignin compounds. Mediators or co-oxidants not only increase the catalytic ability of these enzymes, but also largely expand their substrate scope to those with higher redox potential or more complicated structures. Neither laccase nor the peroxidases are stringently selective of substrates. The promiscuous nature in substrate preference can be employed in detoxification of a range of organics.

Indexed as

BiocatalysisBiodegradation, EnvironmentalHydrolysisLigninOxidation-ReductionPeroxidaseLigninPeroxidasedetoxificationdye-decolorization peroxidase (DyP)laccaseligninlignin peroxidase (LiP)manganese peroxidase (MnP)versatile peroxidase (VP)

Identifiers

PMID30373305
PMCPMC6274955
OpenAlexW2898315493

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.