ArticleEukaryotic cell2007
Structure and function analysis of CaMdr1p, a major facilitator superfamily antifungal efflux transporter protein of Candida albicans: identification of amino acid residues critical for drug/H+ transport.
Article in Eukaryotic cell, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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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.
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Who cites it
41 citing papers in PubMed, 91 citations in OpenAlex.
- Genomic Analysis Reveals Diversified and Stress-Responsive Transport Repertoire inJournal of fungi (Basel, Switzerland) · 2026Article
- Functional characterization ofFrontiers in microbiology · 2026Article
- Exploring the Arsenal of Novel Antifungal Drug Targets for Combating Fungal Infections.Current pharmaceutical biotechnology · 2025Review
- Targeting yeast topoisomerase II by imidazo and triazoloacridinone derivatives resulting in their antifungal activity.Scientific reports · 2024Article
- Review
- Inhibition of Multidrug Efflux Pumps Belonging to the Major Facilitator Superfamily in Bacterial Pathogens.Biomedicines · 2023Review
- The Major Facilitator Superfamily and Antimicrobial Resistance Efflux Pumps of the ESKAPEE PathogenAntibiotics (Basel, Switzerland) · 2023Review
- Spontaneous Suppressors against Debilitating Transmembrane Mutants ofJournal of fungi (Basel, Switzerland) · 2022Article
- Palmarumycin P3 Reverses Mrr1-Mediated Azole Resistance by Blocking the Efflux Pump Mdr1.Antimicrobial agents and chemotherapy · 2022Article
- Directed Mutational Strategies Reveal Drug Binding and Transport by the MDR Transporters ofJournal of fungi (Basel, Switzerland) · 2021Review
- Transcriptome Signatures Predict Phenotypic Variations ofFrontiers in cellular and infection microbiology · 2021Article
- The Genetic Architecture of Emerging Fungicide Resistance in Populations of a Global Wheat Pathogen.Genome biology and evolution · 2020Article
- Dynamical Behavior of the Human Ferroportin Homologue fromInternational journal of molecular sciences · 2020Article
- Functional and Structural Roles of the Major Facilitator Superfamily Bacterial Multidrug Efflux Pumps.Microorganisms · 2020Review
- Synthesis of new piperazinyl-pyrrolo[1,2-RSC advances · 2020Article
- Fungicidal action of geraniol against Candida albicans is potentiated by abrogated CaCdr1p drug efflux and fluconazole synergism.PloS one · 2018Article
- A New Endogenous Overexpression System of Multidrug Transporters of Candida albicans Suitable for Structural and Functional Studies.Frontiers in microbiology · 2016Article
- Substrate-bound structure of the E. coli multidrug resistance transporter MdfA.Cell research · 2015Article
- Mutational Analysis of Intracellular Loops Identify Cross Talk with Nucleotide Binding Domains of Yeast ABC Transporter Cdr1p.Scientific reports · 2015Article
- Multidrug efflux pumps from Enterobacteriaceae, Vibrio cholerae and Staphylococcus aureus bacterial food pathogens.International journal of environmental research and public health · 2015Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We have cloned and overexpressed multidrug transporter CaMdr1p as a green fluorescent protein-tagged protein to show its capability to extrude drug substrates. The drug extrusion was sensitive to pH and energy inhibitors and displayed selective substrate specificity. CaMdr1p has a unique and conserved antiporter motif, also called motif C [G(X6)G(X3)GP(X2)GP(X2)G], in its transmembrane segment 5 (TMS 5). Alanine scanning of all the amino acids of the TMS 5 by site-directed mutagenesis highlighted the importance of the motif, as well as that of other residues of TMS 5, in drug transport. The mutant variants of TMS 5 were placed in four different categories. The first category had four residues, G244, G251, G255, and G259, which are part of the conserved motif C, and their substitution with alanine resulted in increased sensitivity to drugs and displayed impaired efflux of drugs. Interestingly, first category mutants, when replaced with leucine, resulted in more dramatic loss of drug resistance and efflux. Notwithstanding the location in the core motif, the second category included residues which are part of the motif, such as P260, and those which were not part of the motif, such as L245, W248, P256, and F262, whose substitution with alanine resulted in a severe loss of drug resistance and efflux. The third category included G263, which is a part of motif C, but unlike other conserved glycines, its replacement with alanine or leucine showed no change in the phenotype. The replacement of the remaining 11 residues of the fourth category did not result in any change. The putative helical wheel projection showed clustering of functionally critical residues to one side and thus suggests an asymmetric nature of TMS 5.
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