Evidence map›Paper›PMID 32640464›Full record

ArticleNature2020

Structures of fungal and plant acetohydroxyacid synthases.

Thierry Lonhienne, Yu Shang Low, Mario D Garcia, Tristan Croll, Yan Gao, Quan Wang, Lou Brillault, Craig M Williams, James A Fraser, Ross P McGeary and 5 more

Open access · greenAbstract read
PubMed Publisher
In one paragraph

Article in Nature, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
3.0field-weighted citation impact, top 8% 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

32 citing papers in PubMed, 70 citations in OpenAlex.

  1. Article
  2. Article
  3. Development ofBiotechnology reports (Amsterdam, Netherlands) · 2026
    Article
  4. Synthesis and Herbicidal Activity of NovelMolecules (Basel, Switzerland) · 2026
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. 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

15 authors at 5 institutions in 3 countries.

Thierry Lonhienne *School of Chemistry and Molecular Biosciences, The University of Queensland, Brisbane, Queensland, Australia. t.lonhienne@uq.edu.au.ORCID http://orcid.org/0000-0001-8788-2840
Yu Shang Low *School of Chemistry and Molecular Biosciences, The University of Queensland, Brisbane, Queensland, Australia.
Mario D GarciaSchool of Chemistry and Molecular Biosciences, The University of Queensland, Brisbane, Queensland, Australia.ORCID http://orcid.org/0000-0001-8378-7475
Tristan CrollCambridge Institute for Medical Research, University of Cambridge, Cambridge, UK.
Yan GaoShanghai Institute for Advanced Immunochemical Studies, School of Life Science and Technology, ShanghaiTech University, Shanghai, China.
Quan WangShanghai Institute for Advanced Immunochemical Studies, School of Life Science and Technology, ShanghaiTech University, Shanghai, China.ORCID http://orcid.org/0000-0001-5148-5210
Lou BrillaultCentre for Microscopy and Microanalysis, The University of Queensland, Brisbane, Queensland, Australia.
Craig M WilliamsSchool of Chemistry and Molecular Biosciences, The University of Queensland, Brisbane, Queensland, Australia.
James A FraserSchool of Chemistry and Molecular Biosciences, The University of Queensland, Brisbane, Queensland, Australia.
Ross P McGearySchool of Chemistry and Molecular Biosciences, The University of Queensland, Brisbane, Queensland, Australia.
Nicholas P WestSchool of Chemistry and Molecular Biosciences, The University of Queensland, Brisbane, Queensland, Australia.
Michael J LandsbergSchool of Chemistry and Molecular Biosciences, The University of Queensland, Brisbane, Queensland, Australia.ORCID http://orcid.org/0000-0002-2464-990X
Zihe RaoShanghai Institute for Advanced Immunochemical Studies, School of Life Science and Technology, ShanghaiTech University, Shanghai, China.ORCID http://orcid.org/0000-0001-9866-2384
Gerhard SchenkSchool of Chemistry and Molecular Biosciences, The University of Queensland, Brisbane, Queensland, Australia.ORCID http://orcid.org/0000-0001-8619-0631
Luke W GuddatSchool of Chemistry and Molecular Biosciences, The University of Queensland, Brisbane, Queensland, Australia. luke.guddat@uq.edu.au.ORCID http://orcid.org/0000-0002-8204-8408
The University of Queensland · AUShanghaiTech University · CNNankai University · CNQueensland University of Technology · AUUniversity of Cambridge · GB

Funding

Wellcome Trust 209407/Z/17/Z
6 · The paper itself

Abstract

Acetohydroxyacid synthase (AHAS), also known as acetolactate synthase, is a flavin adenine dinucleotide-, thiamine diphosphate- and magnesium-dependent enzyme that catalyses the first step in the biosynthesis of branched-chain amino acids

Indexed as

Acetolactate SynthaseAdenosine TriphosphateAmino Acids, Branched-ChainArabidopsisCatalytic DomainEnzyme ActivationEvolution, MolecularFeedback, PhysiologicalModels, MolecularMultiprotein ComplexesMycobacterium tuberculosisProtein BindingProtein ConformationProtein SubunitsSaccharomyces cerevisiaeValineAcetolactate SynthaseAdenosine TriphosphateAmino Acids, Branched-ChainMultiprotein ComplexesProtein SubunitsValine

Identifiers

PMID32640464
OpenAlexW3041233297

What OpenQuestion holds

Textmetadata
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.