Evidence map›Paper›PMID 41290551›Full record

ArticleJournal of integrative plant biology2026

The PbrMADS1-PbrMYB169 complex has uniquely emerged to regulate lignification of stone cells in pear.

Yongsong Xue, Shulin Chen, Yingyu Hao, Meng Shan, Pengfei Zheng, Runze Wang, Mingyue Zhang, Jun Wu, Cheng Xue

Abstract read
In one paragraph

Article in Journal of integrative plant biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. 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

9 authors.

Yongsong XueAnhui Province Key Laboratory of Horticultural Crop Quality Biology, School of Horticulture, Anhui Agricultural University, Hefei, 230036, China.ORCID https://orcid.org/0009-0008-6315-1099
Shulin ChenCollege of Horticulture Science and Engineering, Shandong Agricultural University, Tai-An, 271018, China.ORCID https://orcid.org/0009-0007-7289-0195
Yingyu HaoAnhui Province Key Laboratory of Horticultural Crop Quality Biology, School of Horticulture, Anhui Agricultural University, Hefei, 230036, China.ORCID https://orcid.org/0009-0001-1460-5516
Meng ShanAnhui Province Key Laboratory of Horticultural Crop Quality Biology, School of Horticulture, Anhui Agricultural University, Hefei, 230036, China.ORCID https://orcid.org/0009-0005-7557-7124
Pengfei ZhengCollege of Horticulture Science and Engineering, Shandong Agricultural University, Tai-An, 271018, China.ORCID https://orcid.org/0009-0008-3433-2878
Runze WangAnhui Province Key Laboratory of Horticultural Crop Quality Biology, School of Horticulture, Anhui Agricultural University, Hefei, 230036, China.ORCID https://orcid.org/0009-0004-4767-6152
Mingyue ZhangCollege of Life Sciences, South China Agricultural University, Guangzhou, 510642, China.ORCID https://orcid.org/0000-0002-2293-8847
Jun WuAnhui Province Key Laboratory of Horticultural Crop Quality Biology, School of Horticulture, Anhui Agricultural University, Hefei, 230036, China.ORCID https://orcid.org/0000-0002-1566-5115
Cheng XueCollege of Horticulture Science and Engineering, Shandong Agricultural University, Tai-An, 271018, China.ORCID https://orcid.org/0000-0002-3541-9958

Funding

National Science Foundation of China 32472689
6 · The paper itself

Abstract

Lignified stone cells are a unique feature of pear fruit, significantly affecting fruit texture. Even though some research efforts have already been made, the stone cell formation mechanism is complex, with many aspects yet to be elucidated. Here, through a genome-wide association analysis of stone cell traits, we identified PbrMADS1, a member of the SEPALLATA3 (SEP3) subfamily, as a candidate gene specifically expressed in stone cells during early fruit development. Functional studies confirmed that PbrMADS1 promotes stone cell formation; however, it does not directly activate lignin-related genes. Instead, PbrMADS1 interacts with PbrMYB169, enhancing PbrMYB169's binding to AC elements and amplifying downstream gene activation. Notably, homologous MADS1 and MYB169 proteins from closely related species such as apple and loquat do not form a similar complex. Sequence analysis revealed that the protein sequence of PbrMADS1 contains methionine (M) at the 63

Indexed as

LigninPlant ProteinsPyrusAmino Acid SequenceFruitGene Expression Regulation, PlantPhylogenyLigninPlant Proteinsfunctional divergencePbrMADS1–PbrMYB169 complexpearstone cells

Identifiers

PMID41290551
PMCPMC12782895

What OpenQuestion holds

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Registered trials

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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.