Evidence map›Paper›PMID 33374996›Full record

ReviewJournal of fungi (Basel, Switzerland)2020

Sterol 14α-Demethylase Ligand-Binding Pocket-Mediated Acquired and Intrinsic Azole Resistance in Fungal Pathogens.

Katharina Rosam, Brian C Monk, Michaela Lackner

Open access · goldAbstract readReview
In one paragraph

Review in Journal of fungi (Basel, Switzerland), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
0.8field-weighted citation impact, top 16% 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

40 citing papers in PubMed, 67 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. The molecular basis of intrinsic resistance to azoles inAntimicrobial agents and chemotherapy · 2026
    Article
  12. Article
  13. Rising antifungal resistance inFrontiers in microbiology · 2026
    Review
  14. Azole Resistance inJournal of fungi (Basel, Switzerland) · 2025
    Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Journal of fungi (Basel, Switzerland) · 2024
    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

3 authors at 2 institutions in 2 countries.

Katharina RosamInstitute of Hygiene and Medical Microbiology, Medical University of Innsbruck, Schöpfstrasse 41, 6020 Innsbruck, Austria.ORCID 0000-0002-4170-558X
Brian C MonkSir John Walsh Research Institute and Department of Oral Biology, Faculty of Dentistry, University of Otago, PO Box 56, 9054 Dunedin, New Zealand.ORCID 0000-0003-2264-3480
Michaela LacknerInstitute of Hygiene and Medical Microbiology, Medical University of Innsbruck, Schöpfstrasse 41, 6020 Innsbruck, Austria.ORCID 0000-0001-9073-2886
Innsbruck Medical University · ATUniversity of Otago · NZ

Funding

Austrian Science Fund FWF P32329-B
6 · The paper itself

Abstract

The fungal cytochrome P450 enzyme sterol 14α-demethylase (SDM) is a key enzyme in the ergosterol biosynthesis pathway. The binding of azoles to the active site of SDM results in a depletion of ergosterol, the accumulation of toxic intermediates and growth inhibition. The prevalence of azole-resistant strains and fungi is increasing in both agriculture and medicine. This can lead to major yield loss during food production and therapeutic failure in medical settings. Diverse mechanisms are responsible for azole resistance. They include amino acid (AA) substitutions in SDM and overexpression of SDM and/or efflux pumps. This review considers AA affecting the ligand-binding pocket of SDMs with a primary focus on substitutions that affect interactions between the active site and the substrate and inhibitory ligands. Some of these interactions are particularly important for the binding of short-tailed azoles (e.g., voriconazole). We highlight the occurrence throughout the fungal kingdom of some key AA substitutions. Elucidation of the role of these AAs and their substitutions may assist drug design in overcoming some common forms of innate and acquired azole resistance.

Indexed as

amino acid substitutionantifungal resistanceazole agrochemicalsazole drugscross-kingdom pathogenscytochrome P450ergosterol biosynthesisheme-containing active siteimidazolelanosterol 14α-demethylasepan-fungal kingdom mutationpoint mutationspromotor regionprophylaxissterol 14α-demethylasesubstrate entry channeltandem repeattherapytreatmenttriazolewater-mediated hydrogen bond network

Identifiers

PMID33374996
PMCPMC7822023
OpenAlexW3116171444

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.