Evidence map›Paper›PMID 39854233›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2025

The

Congying Liang, Lu Lin, Tao Xu, Guoqiang Kang, Zhi-Hua Liu, Bing-Zhi Li

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing 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

11 citing papers in PubMed.

  1. Article
  2. Article
  3. Microorganisms · 2026
    Article
  4. Review
  5. Article
  6. Review
  7. Article
  8. Review
  9. Glyceraldehyde-3-phosphate dehydrogenase homologs as bifunctional gatekeepers of metabolic segregation inProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  10. Article
  11. 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

6 authors.

Congying LiangInstitute of Marine Science and Technology, Shandong University, Qingdao 266237, People's Republic of China.ORCID 0009-0000-3775-0807
Lu LinInstitute of Marine Science and Technology, Shandong University, Qingdao 266237, People's Republic of China.ORCID 0000-0002-9663-6382
Tao XuFrontiers Science Center for Synthetic Biology and Key Laboratory of Systems Bioengineering (Ministry of Education), School of Chemical Engineering and Technology, Tianjin University, Tianjin 300072, People's Republic of China.
Guoqiang KangFrontiers Science Center for Synthetic Biology and Key Laboratory of Systems Bioengineering (Ministry of Education), School of Chemical Engineering and Technology, Tianjin University, Tianjin 300072, People's Republic of China.
Zhi-Hua LiuFrontiers Science Center for Synthetic Biology and Key Laboratory of Systems Bioengineering (Ministry of Education), School of Chemical Engineering and Technology, Tianjin University, Tianjin 300072, People's Republic of China.
Bing-Zhi LiFrontiers Science Center for Synthetic Biology and Key Laboratory of Systems Bioengineering (Ministry of Education), School of Chemical Engineering and Technology, Tianjin University, Tianjin 300072, People's Republic of China.

Funding

MOST | National Key Research and Development Program of China (NKPs) 2023YFC3403500MOST | National Natural Science Foundation of China (NSFC) 32370115
6 · The paper itself

Abstract

Lignin degradation by biocatalysts is a key strategy to develop a plant-based sustainable carbon economy and thus alleviate global climate change. This process involves synergy between ligninases and auxiliary enzymes. However, auxiliary enzymes within secretomes, which are composed of thousands of enzymes, remain enigmatic, although several ligninolytic enzymes have been well characterized. Moreover, it is a challenge to understand synergistic lignin degradation via a diverse array of enzymes, especially in bacterial systems. In this study, the coexpression network of the periplasmic proteome uncovers potential accessory enzymes for B-type dye-decolorizing peroxidases (DypBs) in

Indexed as

Bacterial ProteinsLigninPeroxidasesPseudomonas putidaBiocatalysisOxidation-ReductionBacterial ProteinsLigninPeroxidasesauxiliary enzymesB-type dye-decolorizing peroxidaselignin degradationquinone redox cyclingsynthetic enzyme cocktail

Identifiers

PMID39854233
PMCPMC11789138

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.