Evidence map›Paper›PMID 39242571›Full record

ArticleNature communications2024

Cryo-EM structures of Candida albicans Cdr1 reveal azole-substrate recognition and inhibitor blocking mechanisms.

Ying Peng, Yan Lu, Hui Sun, Jinying Ma, Xiaomei Li, Xiaodan Han, Zhixiong Fang, Junming Tan, Yingchen Qiu, Tingting Qu and 2 more

Abstract read
In one paragraph

Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing 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

20 citing papers in PubMed.

  1. Article
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  3. New Acylglucoses fromPlants (Basel, Switzerland) · 2026
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  10. Flavonoids as a Potential Antifungal Alternative AgainstJournal of fungi (Basel, Switzerland) · 2026
    Article
  11. Article
  12. Review
  13. Capsaicin inhibits cariogenicJournal of oral microbiology · 2026
    Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Review
  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

12 authors.

Ying Peng *Affiliated Hospital of Hunan University/Xiangtan Central Hospital, School of Biomedical Sciences, Hunan University, Changsha, China.ORCID 0000-0002-3797-6870
Yan Lu *Affiliated Hospital of Hunan University/Xiangtan Central Hospital, School of Biomedical Sciences, Hunan University, Changsha, China.
Hui Sun *Affiliated Hospital of Hunan University/Xiangtan Central Hospital, School of Biomedical Sciences, Hunan University, Changsha, China.ORCID 0009-0006-7850-7655
Jinying Ma *School of Life Sciences, Tsinghua University, Beijing, China.ORCID 0009-0002-3893-7942
Xiaomei Li *Shanxi Academy of Advanced Research and Innovation, Taiyuan, China.ORCID 0000-0002-7662-1925
Xiaodan Han *Affiliated Hospital of Hunan University/Xiangtan Central Hospital, School of Biomedical Sciences, Hunan University, Changsha, China.ORCID 0009-0005-8619-2780
Zhixiong FangAffiliated Hospital of Hunan University/Xiangtan Central Hospital, School of Biomedical Sciences, Hunan University, Changsha, China.
Junming TanAffiliated Hospital of Hunan University/Xiangtan Central Hospital, School of Biomedical Sciences, Hunan University, Changsha, China.ORCID 0009-0005-6452-1870
Yingchen QiuAffiliated Hospital of Hunan University/Xiangtan Central Hospital, School of Biomedical Sciences, Hunan University, Changsha, China.
Tingting QuAffiliated Hospital of Hunan University/Xiangtan Central Hospital, School of Biomedical Sciences, Hunan University, Changsha, China.ORCID 0000-0002-4455-2064
Meng YinAffiliated Hospital of Hunan University/Xiangtan Central Hospital, School of Biomedical Sciences, Hunan University, Changsha, China. yinm@hnu.edu.cn.ORCID 0000-0003-2293-7112
Zhaofeng YanAffiliated Hospital of Hunan University/Xiangtan Central Hospital, School of Biomedical Sciences, Hunan University, Changsha, China. zhaofengyan@hnu.edu.cn.ORCID 0000-0001-9054-3313

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In Candida albicans, Cdr1 pumps azole drugs out of the cells to reduce intracellular accumulation at detrimental concentrations, leading to azole-drug resistance. Milbemycin oxime, a veterinary anti-parasitic drug, strongly and specifically inhibits Cdr1. However, how Cdr1 recognizes and exports azole drugs, and how milbemycin oxime inhibits Cdr1 remain unclear. Here, we report three cryo-EM structures of Cdr1 in distinct states: the apo state (Cdr1

Indexed as

Antifungal AgentsAzolesCandida albicansCryoelectron MicroscopyFungal ProteinsMembrane Transport ProteinsBinding SitesDrug Resistance, FungalFluconazoleAntifungal AgentsAzolesCDR1 protein, Candida albicansFluconazoleFungal ProteinsMembrane Transport Proteins

Identifiers

PMID39242571
PMCPMC11379888

What OpenQuestion holds

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LicenceCC BY-NC-ND
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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.