Evidence map›Paper›PMID 34301892›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2021

Structural basis for ligand binding modes of CTP synthase.

Xian Zhou, Chen-Jun Guo, Chia-Chun Chang, Jiale Zhong, Huan-Huan Hu, Guang-Ming Lu, Ji-Long Liu

Open access · hybridAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
5.5field-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

35 citing papers in PubMed, 80 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Filamentation of hCTPS1 with CTP.Cell & bioscience · 2025
    Article
  7. Article
  8. Cytoophidium complexes resonate with cell fates.Cellular and molecular life sciences : CMLS · 2025
    Article
  9. Article
  10. Structural Basis of Bifunctional CTP/dCTP Synthase.Journal of molecular biology · 2024
    Article
  11. Article
  12. Differential Cytoophidium Assembly betweenInternational journal of molecular sciences · 2024
    Article
  13. Article
  14. Article
  15. Dynamic Cytoophidia during Late-StageInternational journal of molecular sciences · 2024
    Article
  16. Connecting Hippo Pathway and Cytoophidia inInternational journal of molecular sciences · 2024
    Article
  17. Cytoophidia Influence Cell Cycle and Size inInternational journal of molecular sciences · 2024
    Article
  18. Article
  19. Article
  20. 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

7 authors at 2 institutions in 2 countries.

Xian ZhouSchool of Life Science and Technology, ShanghaiTech University, Shanghai, 201210, China.ORCID 0000-0002-0000-2415
Chen-Jun GuoSchool of Life Science and Technology, ShanghaiTech University, Shanghai, 201210, China.ORCID 0000-0001-5342-4761
Chia-Chun ChangSchool of Life Science and Technology, ShanghaiTech University, Shanghai, 201210, China.ORCID 0000-0001-7942-6300
Jiale ZhongSchool of Life Science and Technology, ShanghaiTech University, Shanghai, 201210, China.ORCID 0000-0001-5873-0450
Huan-Huan HuSchool of Life Science and Technology, ShanghaiTech University, Shanghai, 201210, China.ORCID 0000-0002-5997-530X
Guang-Ming LuSchool of Life Science and Technology, ShanghaiTech University, Shanghai, 201210, China.ORCID 0000-0002-6607-2264
Ji-Long LiuSchool of Life Science and Technology, ShanghaiTech University, Shanghai, 201210, China; liujl3@shanghaitech.edu.cn.ORCID 0000-0002-4834-8554
Chinese Academy of Sciences · CNShanghaiTech University · CN

Funding

Medical Research Council MC_U137788471Medical Research Council MC_UU_12021/3
6 · The paper itself

Abstract

Cytidine triphosphate synthase (CTPS), which comprises an ammonia ligase domain and a glutamine amidotransferase domain, catalyzes the final step of de novo CTP biosynthesis. The activity of CTPS is regulated by the binding of four nucleotides and glutamine. While glutamine serves as an ammonia donor for the ATP-dependent conversion of UTP to CTP, the fourth nucleotide GTP acts as an allosteric activator. Models have been proposed to explain the mechanisms of action at the active site of the ammonia ligase domain and the conformational changes derived by GTP binding. However, actual GTP/ATP/UTP binding modes and relevant conformational changes have not been revealed fully. Here, we report the discovery of binding modes of four nucleotides and a glutamine analog 6-diazo-5-oxo-L-norleucine in

Indexed as

Adenosine TriphosphateAllosteric RegulationAmmoniaAnimalsBinding SitesCarbon-Nitrogen LigasesCatalysisCryoelectron MicroscopyDrosophila melanogasterGlutamineHydrolysisKineticsLigandsProtein ConformationUridine TriphosphateAdenosine TriphosphateAmmoniaCarbon-Nitrogen LigasesCTP synthetaseGlutamineLigandsUridine Triphosphateallosteric regulationcryo–electron microscopyCTP synthasecytoophidium

Identifiers

PMID34301892
PMCPMC8325340
OpenAlexW3185611713

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.