Evidence map›Paper›PMID 40617831›Full record

ArticleNature communications2025

Harnessing protein language model for structure-based discovery of highly efficient and robust PET hydrolases.

Banghao Wu, Bozitao Zhong, Lirong Zheng, Runye Huang, Shifeng Jiang, Mingchen Li, Liang Hong, Pan Tan

Abstract read
In one paragraph

Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed, 1 pooled it
–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

15 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Pooled it
  2. Article
  3. Article
  4. Article
  5. Article
  6. Journal of chemical information and modeling · 2026
    Article
  7. Article
  8. Protein foundation models: a comprehensive survey.Science China. Life sciences · 2026
    Review
  9. Article
  10. Review
  11. EngineeringiScience · 2026
    Article
  12. Review
  13. Article
  14. Article
  15. EngineeringInternational journal of molecular sciences · 2025
    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

8 authors.

Banghao Wu *School of Life Sciences and Biotechnology, Shanghai Jiao Tong University, Shanghai, China.ORCID http://orcid.org/0009-0002-3361-161X
Bozitao Zhong *School of Life Sciences and Biotechnology, Shanghai Jiao Tong University, Shanghai, China.ORCID http://orcid.org/0000-0001-9363-6099
Lirong ZhengShanghai National Center for Applied Mathematics (SJTU Center) & Institute of Natural Sciences, Shanghai Jiao Tong University, Shanghai, China. lrzheng@umich.edu.ORCID http://orcid.org/0000-0001-6803-5048
Runye HuangSchool of Life Sciences and Biotechnology, Shanghai Jiao Tong University, Shanghai, China.
Shifeng JiangSchool of Life Sciences and Biotechnology, Shanghai Jiao Tong University, Shanghai, China.
Mingchen LiShanghai National Center for Applied Mathematics (SJTU Center) & Institute of Natural Sciences, Shanghai Jiao Tong University, Shanghai, China.ORCID http://orcid.org/0000-0001-6862-0052
Liang HongSchool of Life Sciences and Biotechnology, Shanghai Jiao Tong University, Shanghai, China. hongl3liang@sjtu.edu.cn.ORCID http://orcid.org/0000-0003-0107-336X
Pan TanSchool of Life Sciences and Biotechnology, Shanghai Jiao Tong University, Shanghai, China. tpan1039@gmail.com.ORCID http://orcid.org/0000-0003-2086-0940

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Plastic waste, particularly polyethylene terephthalate (PET), presents significant environmental challenges, driving extensive research into enzymatic biodegradation. However, existing PET hydrolases (PETases) are limited by narrow sequence diversity and suboptimal performance. This study introduces VenusMine, a protein discovery pipeline that integrates protein language models (PLMs) with a representation tree to identify PETases based on structural similarity using sequence information. Using the crystal structure of IsPETase as a template, VenusMine identifies and clusters target proteins. Candidates are further screened using PLM-based assessments of solubility and thermostability, leading to the selection of 34 proteins for biochemical validation. Results reveal that 14 candidates exhibit PET degradation activity across 30-60 °C. Notably, a PET hydrolase from Kibdelosporangium banguiense (KbPETase) demonstrates a melting temperature (T

Indexed as

HydrolasesPolyethylene TerephthalatesCrystallography, X-RayMolecular Dynamics SimulationProtein ConformationHydrolasesPolyethylene Terephthalates

Identifiers

PMID40617831
PMCPMC12228687

What OpenQuestion holds

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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.