Evidence map›Paper›PMID 34799726›Full record

ArticleCell research2022

Structural basis of ALMT1-mediated aluminum resistance in Arabidopsis.

Jiangqin Wang, Xiafei Yu, Zhong Jie Ding, Xiaokang Zhang, Yanping Luo, Ximing Xu, Yuan Xie, Xiaoxiao Li, Tian Yuan, Shao Jian Zheng and 2 more

Open access · bronzeAbstract read
In one paragraph

Article in Cell research, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
8.2field-weighted citation impact, top 3% of its field
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

30 citing papers in PubMed, 54 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Structural insights into a citrate transporter that mediates aluminum tolerance in barley.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  7. Article
  8. Article
  9. Review
  10. Frontiers in plant science · 2025
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Investigating the involvement of potato (Frontiers in plant science · 2024
    Article
  19. Review
  20. Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

12 authors at 5 institutions in 1 country.

Jiangqin Wang *Department of Biophysics, and Department of Pathology of Sir Run Run Shaw Hospital, Zhejiang University School of Medicine, Hangzhou, Zhejiang, China.
Xiafei Yu *Department of Biophysics and Department of Neurosurgery, The First Affiliated Hospital, Zhejiang University School of Medicine, Hangzhou, Zhejiang, China.
Zhong Jie Ding *State Key Laboratory of Plant Physiology and Biochemistry, College of Life Sciences, Zhejiang University, Hangzhou, Zhejiang, China.
Xiaokang Zhang *Interdisciplinary Center for Brain Information, The Brain Cognition and Brain Disease Institute, Faculty of Life and Health Sciences, Shenzhen Institute of Advanced Technology, Chinese Academy of Sciences, Shenzhen, Guangdong, China.ORCID http://orcid.org/0000-0001-5073-2582
Yanping LuoDepartment of Biophysics and Department of Neurosurgery, The First Affiliated Hospital, Zhejiang University School of Medicine, Hangzhou, Zhejiang, China.
Ximing XuKey Laboratory of Marine Drugs of Ministry of Education, School of Medicine and Pharmacy, Ocean University of China, Qingdao, Shandong, China.
Yuan XieDepartment of Biophysics, and Department of Pathology of Sir Run Run Shaw Hospital, Zhejiang University School of Medicine, Hangzhou, Zhejiang, China.ORCID http://orcid.org/0000-0001-6982-8525
Xiaoxiao LiDepartment of Biophysics, and Department of Pathology of Sir Run Run Shaw Hospital, Zhejiang University School of Medicine, Hangzhou, Zhejiang, China.ORCID http://orcid.org/0000-0002-2372-6192
Tian YuanState Key Laboratory of Plant Physiology and Biochemistry, College of Life Sciences, Zhejiang University, Hangzhou, Zhejiang, China.
Shao Jian ZhengState Key Laboratory of Plant Physiology and Biochemistry, College of Life Sciences, Zhejiang University, Hangzhou, Zhejiang, China. sjzheng@zju.edu.cn.ORCID http://orcid.org/0000-0002-3336-8165
Wei YangDepartment of Biophysics and Department of Neurosurgery, The First Affiliated Hospital, Zhejiang University School of Medicine, Hangzhou, Zhejiang, China. yangwei@zju.edu.cn.
Jiangtao GuoDepartment of Biophysics, and Department of Pathology of Sir Run Run Shaw Hospital, Zhejiang University School of Medicine, Hangzhou, Zhejiang, China. jiangtaoguo@zju.edu.cn.
Sir Run Run Shaw Hospital · CNFirst Affiliated Hospital Zhejiang University · CNZhejiang University · CNChinese Academy of Sciences · CNOcean University of China · CN

Funding

Chinese Ministry of Science and Technology | Department of S and T for Social Development (Department of S&T for Social Development) 2016YFA0501100Chinese Ministry of Science and Technology | Department of S and T for Social Development (Department of S&T for Social Development) 2018YFA0508100Chinese Ministry of Science and Technology | Department of S and T for Social Development (Department of S&T for Social Development) 2020YFA0908501National Natural Science Foundation of China (National Science Foundation of China) 31600606National Natural Science Foundation of China (National Science Foundation of China) 31730006National Natural Science Foundation of China (National Science Foundation of China) 31870724National Natural Science Foundation of China (National Science Foundation of China) 31872796National Natural Science Foundation of China (National Science Foundation of China) 81571127National Natural Science Foundation of China (National Science Foundation of China) 82030108
6 · The paper itself

Abstract

The plant aluminum (Al)-activated malate transporter ALMT1 mediates the efflux of malate to chelate the Al in acidic soils and underlies the plant Al resistance. Here we present cryo-electron microscopy (cryo-EM) structures of Arabidopsis thaliana ALMT1 (AtALMT1) in the apo, malate-bound, and Al-bound states at neutral and/or acidic pH at up to 3.0 Å resolution. The AtALMT1 dimer assembles an anion channel and each subunit contains six transmembrane helices (TMs) and six cytosolic α-helices. Two pairs of Arg residues are located in the center of the channel pore and contribute to malate recognition. Al binds at the extracellular side of AtALMT1 and induces conformational changes of the TM1-2 loop and the TM5-6 loop, resulting in the opening of the extracellular gate. These structures, along with electrophysiological measurements, molecular dynamic simulations, and mutagenesis study in Arabidopsis, elucidate the structural basis for Al-activated malate transport by ALMT1.

Indexed as

ArabidopsisArabidopsis ProteinsOrganic Anion TransportersAluminumCryoelectron MicroscopyGene Expression Regulation, PlantPlant RootsAluminumArabidopsis ProteinsOrganic Anion Transporters

Identifiers

PMID34799726
PMCPMC8724285
OpenAlexW3213338226

What OpenQuestion holds

Textmetadata
Read underepoch 390

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.