Evidence map›Paper›PMID 40647959›Full record

ArticlePlants (Basel, Switzerland)2025

The Structural Deciphering of the α3 Helix Within ZmHsfA2'S DNA-Binding Domain for the Recognition of Heat Shock Elements in Maize.

Yantao Wang, Zhenyu Ma, Guoliang Li, Xiangzhao Meng, Shuonan Duan, Zihui Liu, Min Zhao, Xiulin Guo, Huaning Zhang

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Plants (Basel, Switzerland), 2025. 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.

Yantao WangSchool of Landscape and Ecological Engineering, Hebei University of Engineering, Handan 056000, China.
Zhenyu MaHebei Key Laboratory of Plant Genetic Engineering, Institute of Biotechnology and Food Science, Hebei Academy of Agriculture and Forestry Sciences, Shijiazhuang 050051, China.
Guoliang LiHebei Key Laboratory of Plant Genetic Engineering, Institute of Biotechnology and Food Science, Hebei Academy of Agriculture and Forestry Sciences, Shijiazhuang 050051, China.ORCID 0000-0001-9384-2933
Xiangzhao MengHebei Key Laboratory of Plant Genetic Engineering, Institute of Biotechnology and Food Science, Hebei Academy of Agriculture and Forestry Sciences, Shijiazhuang 050051, China.
Shuonan DuanHebei Key Laboratory of Plant Genetic Engineering, Institute of Biotechnology and Food Science, Hebei Academy of Agriculture and Forestry Sciences, Shijiazhuang 050051, China.
Zihui LiuHebei Key Laboratory of Plant Genetic Engineering, Institute of Biotechnology and Food Science, Hebei Academy of Agriculture and Forestry Sciences, Shijiazhuang 050051, China.
Min ZhaoSchool of Landscape and Ecological Engineering, Hebei University of Engineering, Handan 056000, China.
Xiulin GuoHebei Key Laboratory of Plant Genetic Engineering, Institute of Biotechnology and Food Science, Hebei Academy of Agriculture and Forestry Sciences, Shijiazhuang 050051, China.
Huaning ZhangHebei Key Laboratory of Plant Genetic Engineering, Institute of Biotechnology and Food Science, Hebei Academy of Agriculture and Forestry Sciences, Shijiazhuang 050051, China.ORCID 0000-0003-1197-0152

Funding

Basic Research Funds of Hebei Academy of Agriculture and Forestry Sciences 2024110205Hebei Natural Science Foundation C2024301029Hebei Natural Science Foundation C2024301030
6 · The paper itself

Abstract

Heat shock transcription factor (Hsf) plays a pivotal role in regulating plant growth, development, and stress responses. Hsf activates or represses target gene transcription by binding to the heat shock element (HSE) of downstream genes. However, the specific interaction sites between Hsf and the HSE in the promoter remain unclear. In this study, the critical amino acid residues of ZmHsf17 and the paralogous ZmHsf05 involved in DNA binding were identified using molecular docking models, site-directed mutagenesis, and the electrophoretic mobility shift assay (EMSA). The results reveal that both ZmHsf17 and ZmHsf05 bind to the HSE of the

Indexed as

arginineheat shock elementheat shock transcription factormaize

Identifiers

PMID40647959
PMCPMC12251660

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.