Evidence map›Paper›PMID 32184021›Full record

ArticleBiochemical and biophysical research communications2020

Crystal structure and transient dimerization for the FKBP12 protein from the pathogenic fungus Candida auris.

Qamar Bashir, Zhong Li, Hongmin Li, David M LeMaster, Griselda Hernández

Open access · hybridAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Biochemical and biophysical research communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.1field-weighted citation impact, top 57% 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

1 citing paper in PubMed, 4 citations in OpenAlex.

  1. Bioactive structures for inhibitors ofFuture medicinal chemistry · 2025
    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

5 authors at 1 institution in 1 country.

Qamar BashirWadsworth Center, New York State Department of Health, Empire State Plaza, Albany, NY, 12201, USA.
Zhong LiWadsworth Center, New York State Department of Health, Empire State Plaza, Albany, NY, 12201, USA.
Hongmin LiWadsworth Center, New York State Department of Health, Empire State Plaza, Albany, NY, 12201, USA.
David M LeMasterWadsworth Center, New York State Department of Health, Empire State Plaza, Albany, NY, 12201, USA.
Griselda HernándezWadsworth Center, New York State Department of Health, Empire State Plaza, Albany, NY, 12201, USA. Electronic address: griselda.hernandez@health.ny.gov.
New York State Department of Health · US

Funding

Resource for Biocomputing Visualization and InformaticsP41GM103311 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI FERRIN, THOMAS E · 2012 to 2017
$8.2M
High throughput screening of the Prp8 intein splicing inhibitors for pathogenic fungiR01AI140726 · NIAID · WADSWORTH CENTER · PI LI, HONGMIN · 2019 to 2022
$2.4M
Coupled transitions of FK506-binding domains in molecular design and signalingR01GM119152 · NIGMS · WADSWORTH CENTER · PI HERNANDEZ, GRISELDA · 2017 to 2020
$1.2M
Discovery of therapeutics against Cryptococcosis by Repurposing Pharmaceutical LibrariesR21AI141178 · NIAID · WADSWORTH CENTER · PI LI, HONGMIN · 2019 to 2020
$441k
NIAID NIH HHS R01 AI140726NIAID NIH HHS R21 AI141178NIGMS NIH HHS P41 GM103311NIGMS NIH HHS R01 GM119152
6 · The paper itself

Abstract

International concern over the recent emergence of Candida auris infections reflects not only its comparative ease of transmission and substantial mortality but the increasing level of resistance observed to all three major classes of antifungal drugs. Diminution in virulence has been reported for a wide range of fungal pathogens when the FK506-binding protein FKBP12 binds to that immunosuppressant drug and the binary complex then inhibits the fungal calcineurin signaling pathway. Structure-based drug design efforts have described modifications of FK506 which modestly reduce virulence for a number of fungal pathogens while also lessening the side effect of suppressing the tissue immunity response in the patient. To aid in such studies, we report the crystal structure of Candida auris FKBP12. As physiological relevance has been proposed for transient homodimerization interactions of distantly related fungal FKBP12 proteins, we report the solution NMR characterization of the homodimerization interactions of the FKBP12 proteins from both Candida auris and Candida glabrata.

Indexed as

CandidaCandida glabrataCrystallography, X-RayDimerizationFungal ProteinsMagnetic Resonance SpectroscopyTacrolimusTacrolimus Binding Protein 1AFungal ProteinsTacrolimusTacrolimus Binding Protein 1ACandida aurisCandida glabrataChemical shift perturbationCrystal structureFKBP12Multi-drug resistance

Identifiers

PMID32184021
PMCPMC7566232
OpenAlexW3010928736

What OpenQuestion holds

Textmetadata
LicenceTDM
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.