Evidence map›Paper›PMID 40402396›Full record

ReviewBotanical studies2025

Analysing protein complexes in plant science: insights and limitation with AlphaFold 3.

Pei-Yu Lin, Shiang-Chin Huang, Kuan-Lin Chen, Yu-Chun Huang, Chia-Yu Liao, Guan-Jun Lin, HueyTyng Lee, Pao-Yang Chen

Abstract readReview
In one paragraph

Review in Botanical studies, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing 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

13 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Review
  6. Article
  7. The transformative power of structural predictions with AI in plant science.The Plant journal : for cell and molecular biology · 2026
    Review
  8. Review
  9. Review
  10. Article
  11. International journal of molecular sciences · 2025
    Article
  12. Review
  13. 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.

Pei-Yu LinInstitute of Plant and Microbial Biology, Academia Sinica, Taipei, 115, Taiwan.
Shiang-Chin HuangInstitute of Plant and Microbial Biology, Academia Sinica, Taipei, 115, Taiwan.
Kuan-Lin ChenInstitute of Plant and Microbial Biology, Academia Sinica, Taipei, 115, Taiwan.
Yu-Chun HuangInstitute of Plant and Microbial Biology, Academia Sinica, Taipei, 115, Taiwan.
Chia-Yu LiaoInstitute of Plant and Microbial Biology, Academia Sinica, Taipei, 115, Taiwan.
Guan-Jun LinInstitute of Plant and Microbial Biology, Academia Sinica, Taipei, 115, Taiwan.
HueyTyng LeeInstitute of Plant and Microbial Biology, Academia Sinica, Taipei, 115, Taiwan.
Pao-Yang ChenInstitute of Plant and Microbial Biology, Academia Sinica, Taipei, 115, Taiwan. paoyang@gate.sinica.edu.tw.ORCID http://orcid.org/0000-0002-7402-3075

Funding

Academia Sinica NTU-AS Innovative Joint Program AS-NTU-112-12Academia Sinica VGH-TSGH-AS Joint Research Program VTA112-T-3-2National Science and Technology Council 113-2311-B-001-002National Science and Technology Council 113-2313-B-001-005
6 · The paper itself

Abstract

AlphaFold 3 (AF3), an artificial intelligence (AI)-based software for protein complex structure prediction, represents a significant advancement in structural biology. Its flexibility and enhanced scalability have unlocked new applications in various fields, specifically in plant science, including improving crop resilience and predicting the structures of plant-specific proteins involved in stress responses, signalling pathways, and immune responses. Comparisons with existing tools, such as ClusPro and AlphaPulldown, highlight AF3's unique strengths in sequence-based interaction predictions and its greater adaptability to various biomolecular structures. However, limitations persist, including challenges in modelling large complexes, protein dynamics, and structures from underrepresented plant proteins with limited evolutionary data. Additionally, AF3 encounters difficulties in predicting mutation effects on protein interactions and DNA binding, which can be improved with molecular dynamics and experimental validation. This review presents an overview of AF3's advancements, using examples in plant and fungal research, and comparisons with existing tools. It also discusses current limitations and offers perspectives on integrating molecular dynamics and experimental validation to enhance its capabilities.

Indexed as

AlphaFold 3Crop resilienceProtein complexProtein–protein interactionProtein structureStructure biology

Identifiers

PMID40402396
PMCPMC12098255

What OpenQuestion holds

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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.