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Amphotericin primarily kills yeast by simply binding ergosterol
Open accessAbstract
Amphotericin B (AmB) is a prototypical small molecule natural product that can form ion channels in living eukaryotic cells and has remained refractory to microbial resistance despite extensive clinical utilization in the treatment of life-threatening fungal infections for more than half a century. It is now widely accepted that AmB kills yeast primarily via channel-mediated membrane permeabilization. Enabled by the iterative cross-coupling-based synthesis of a functional group deficient derivative of this natural product, we have discovered that channel formation is not required for potent fungicidal activity. Alternatively, AmB primarily kills yeast by simply binding ergosterol, a lipid that is vital for many aspects of yeast cell physiology. Membrane permeabilization via channel formation represents a second complementary mechanism that further increases drug potency and the rate of yeast killing. Collectively, these findings ( i ) reveal that the binding of a physiologically important microbial lipid is a powerful and clinically validated antimicrobial strategy that may be inherently refractory to resistance, ( ii ) illuminate a more straightforward path to an improved therapeutic index for this clinically vital but also highly toxic antifungal agent, and ( iii ) suggest that the capacity for AmB to form protein-like ion channels might be separable from its cytocidal effects.
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In the citing paper
“AmB binds to ergosterol, forming microporous channels on the cell membrane and enabling the drug’s fungicidal activity.”
From Antifungal persistence: Clinical relevance and mechanisms (2025) · cites this paper as [64]
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“Downregulation of ergosterol may therefore reduce the exposure of AmB drug targets [64].”
From Antifungal persistence: Clinical relevance and mechanisms (2025) · cites this paper as [64]
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“These amphipathic compounds act as a sponge extracting ergosterol from the fungal cell membrane, leading to the formation of pores, causing leakage of cellular components and ultimately death of the fungal cell [32,33].”
From Antifungal therapy of Candida biofilms: Past, present and future (2023) · cites this paper as [33]
In the citing paper
“Amphotericin B (AMB), a polyene class of antifungal drug, irreversibly binds to ergosterol, resulting in fungal cell death.”
From Aspergillus fumigatus and Aspergillosis in 2019 (2019) · cites this paper as [615]
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Cites
Antibiotic resistance is ancient
D’Costa, V. M., King, C. E., Kalan, L., Morar, M., Sung, W. W. L., Schwarz, C., Froese, D., Zazula, G., Calmels, F., Debruyne, R., et al. (2011) · Nature · doi:10.1038/nature10388 · Cited by 2,720
Comparison of Caspofungin and Amphotericin B for Invasive Candidiasis
Mora-Duarte, J., Betts, R., Rotstein, C., Colombo, A. L., Thompson-Moya, L., Smietana, J., Lupinacci, R., Sable, C., Kartsonis, N., & Perfect, J. (2002) · New England Journal of Medicine · doi:10.1056/nejmoa021585 · Cited by 1,380
Global analysis of the yeast lipidome by quantitative shotgun mass spectrometry
Ejsing, C. S., Sampaio, J. L., Surendranath, V., Duchoslav, E., Ekroos, K., Klemm, R. W., Simons, K., & Shevchenko, A. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0811700106 · Cited by 1,053
Antibacterial agents based on the cyclic d,l-α-peptide architecture
Fernandez‐Lopez, S., Kim, H.-S., Choi, E. C., Delgado, M., Granja, J. R., Khasanov, A. B., Kraehenbuehl, K., Long, G. V., Weinberger, D. A., Wilcoxen, K., et al. (2001) · Nature · doi:10.1038/35086601 · Cited by 938
Taubes, G. (2008) · Science · doi:10.1126/science.321.5887.356 · Cited by 757
How do the polyene macrolide antibiotics affect the cellular membrane properties?
Bolard, J. (1986) · Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes · doi:10.1016/0304-4157(86)90002-x · Cited by 757
KRUIJFF, B. D., & DEMEL, R. A. (1974) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/0005-2736(74)90332-0 · Cited by 609
Knapp, D. M., Gillis, E. P., & Burke, M. D. (2009) · Journal of the American Chemical Society · doi:10.1021/ja901416p · Cited by 559
Self-citationAn Alternative Bactericidal Mechanism of Action for Lantibiotic Peptides That Target Lipid II
Hasper, H. E., Kramer, N. E., Smith, L., Hillman, J. D., Zachariah, C., Kuipers, O. P., KRUIJFF, B. D., & Breukink, E. J. (2006) · Science · doi:10.1126/science.1129818 · Cited by 502
Gillis, E. P., & Burke, M. D. (2007) · Journal of the American Chemical Society · doi:10.1021/ja0716204 · Cited by 488
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Items 201–300 of 612
Kumar, M., Singh, A., Kumari, S., Kumar, P., Wasi, M., Mondal, A. K., Rudramurthy, S. M., Chakrabarti, A., Gaur, N. A., Gow, N. A. R., et al. (2020) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2020.158815 · Cited by 33
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Pal, R., Teli, G., Akhtar, M. J., & Matada, G. S. P. (2023) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2023.115927 · Cited by 31
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Cremer, K. D., Staes, I., Delattin, N., Cammue, B. P. A., Thevissen, K., & Brucker, K. D. (2015) · Expert Review of Anti-infective Therapy · doi:10.1586/14787210.2015.1056162 · Cited by 31
Tan, T. R. M., Hoi, K. M., Zhang, P., & Ng, S. K. (2016) · PLoS ONE · doi:10.1371/journal.pone.0152112 · Cited by 31
Yao, J., Zhi, H., Shi, Q., Zhang, Y., Feng, J., Liu, J., Huang, H., & Xie, X. (2023) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.3c07761 · Cited by 31
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Hetta, H. F., Melhem, T., Aljohani, H. M., Salama, A., Ahmed, R., Elfadil, H., Alanazi, F. E., Ramadan, Y. N., Battah, B., Rottura, M., et al. (2025) · Pharmaceuticals · doi:10.3390/ph18030364 · Cited by 32
Yang, L., Guo, G., Tian, Z., Zhou, L., Zhu, L., Peng, J., Sun, C., & Huang, M. (2021) · Journal of Proteomics · doi:10.1016/j.jprot.2021.104385 · Cited by 31
Efficacy of low doses of amphotericin B plus allicin against experimental visceral leishmaniasis
Corral, M. J., Serrano, D. R., Moreno, I., Torrado, J. J., Domínguez, M., & Alunda, J. M. (2014) · Journal of Antimicrobial Chemotherapy · doi:10.1093/jac/dku290 · Cited by 30
Nakagawa, Y., Umegawa, Y., Matsushita, N., Yamamoto, T., Tsuchikawa, H., Hanashima, S., Oishi, T., Matsumori, N., & Murata, M. (2016) · Biochemistry · doi:10.1021/acs.biochem.6b00193 · Cited by 30
Abbasi, E., & Saeedi, S. (2025) · The Pediatric Infectious Disease Journal · doi:10.1097/inf.0000000000004876 · Cited by 29
Rane, H. S., Bernardo, S. M., Hayek, S. R., Binder, J., Parra, K. J., & Lee, S. A. (2014) · Eukaryotic Cell · doi:10.1128/ec.00135-14 · Cited by 30
Delhom, R., Nelson, A. R. J., Laux, V., Haertlein, M., Knecht, W., Fragneto, G., & Wacklin, H. P. (2020) · Nanomaterials · doi:10.3390/nano10122439 · Cited by 29
Roth, C., Murray, D., Scott, A., Fu, C., Averette, A. F., Sun, S., Heitman, J., & Magwene, P. M. (2021) · PLoS Genetics · doi:10.1371/journal.pgen.1009313 · Cited by 30
Wang, J., Zhang, J., Ma, J., Liu, L., Li, J., Shen, T., & Tian, Y. (2022) · Journal of Applied Microbiology · doi:10.1111/jam.15458 · Cited by 28
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Quantifying membrane permeability of amphotericin B ion channels in single living cells
Yang, T., Ou, K., Peng, P., Liou, B.-C., Wang, W., Huang, Y.-C., Tsai, C., & Su, C. (2013) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2013.03.021 · Cited by 29
Neumann, A., Wieczór, M., Zielińska, J., Bagiński, M., & Czub, J. (2016) · Langmuir · doi:10.1021/acs.langmuir.5b04433 · Cited by 29
Chemogenomic Profiling of the Fungal Pathogen Candida albicans
Chen, Y., Mallick, J., Maqnas, A., Sun, Y., Choudhury, B. I., Côte, P., Yan, L., Ni, T., Li, Y., Zhang, D., et al. (2017) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.02365-17 · Cited by 35
Han, X., Wang, J., Liu, L., Shen, F., Meng, Q., Li, X., Li, Y., & Liu, D. (2021) · Applied and Environmental Microbiology · doi:10.1128/aem.03157-20 · Cited by 28
Kamiński, D. M., Czernel, G., Murphy, B. M., Runge, B., Magnussen, O. M., & Gagoś, M. (2014) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2014.08.004 · Cited by 28
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Barbu, E. M., Shirazi, F., McGrath, D. M., Albert, N. D., Sidman, R. L., Pasqualini, R., Arap, W., & Kontoyiannis, D. P. (2013) · PLoS ONE · doi:10.1371/journal.pone.0076981 · Cited by 28
Topical and systemic antifungals in dermatology practice
Durdu, M., İlkit, M., Tamaddon, Y., Tolooe, A., Rafati, H., & Seyedmousavi, S. (2016) · Expert Review of Clinical Pharmacology · doi:10.1080/17512433.2017.1263564 · Cited by 28
Zoysa, G. H. D., Glossop, H. D., & Sarojini, V. (2018) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2018.01.023 · Cited by 28
Arima, A. A., Pavinatto, F. J., Oliveira, O. N., & Gonzales, E. R. P. (2014) · Colloids and Surfaces B Biointerfaces · doi:10.1016/j.colsurfb.2014.06.058 · Cited by 27
Restored Physiology in Protein-Deficient Yeast by a Small Molecule Channel
Cioffi, A. G., Hou, J. C., Grillo, A. S., Diaz, K. A., & Burke, M. D. (2015) · Journal of the American Chemical Society · doi:10.1021/jacs.5b05765 · Cited by 27
Self-citationStigmasterol as a potential biomarker for amphotericin B resistance in Leishmania donovani
Bansal, R., Sen, S. S., Muthuswami, R., & Madhubala, R. (2019) · Journal of Antimicrobial Chemotherapy · doi:10.1093/jac/dkz515 · Cited by 27
Recent advances in the synthesis and reactivity of MIDA boronates
Aich, D., Kumar, P., Ghorai, D., Das, K. K., & Panda, S. (2022) · Chemical Communications · doi:10.1039/d2cc04893k · Cited by 27
Peridinin Is an Exceptionally Potent and Membrane-Embedded Inhibitor of Bilayer Lipid Peroxidation
Haley, H. M. S., Hill, A. G., Greenwood, A. I., Woerly, E. M., Rienstra, C. M., & Burke, M. D. (2018) · Journal of the American Chemical Society · doi:10.1021/jacs.8b06933 · Cited by 27
Self-citationSqualene lipotoxicity in a lipid droplet‐less yeast mutant is linked to plasma membrane dysfunction
Csáky, Z., Garaiová, M., Kodedová, M., Valachovič, M., Sychrová, H., & Hapala, I. (2019) · Yeast · doi:10.1002/yea.3454 · Cited by 27
Feng, M., Jin, Y., Yang, S., Joachim, A. M., Yu, N., Mori‐Quiroz, L. M., Fromm, J., Perera, C., Zhang, K., Werbovetz, K. A., et al. (2022) · International Journal for Parasitology Drugs and Drug Resistance · doi:10.1016/j.ijpddr.2022.07.003 · Cited by 26
Antibiofilm effects of berberine-loaded chitosan nanoparticles against Candida albicans biofilm
Lin, Q., Li, Y., Sheng, M., Xu, J., Xu, X., Lee, J., & Tan, Y. (2022) · LWT · doi:10.1016/j.lwt.2022.114237 · Cited by 26
Holden, W. M., Ebert, A. R., Canning, P. F., & Rollins‐Smith, L. A. (2014) · Applied and Environmental Microbiology · doi:10.1128/aem.04171-13 · Cited by 26
Serhan, G., Stack, C. M., Perrone, G. G., & Morton, C. O. (2014) · Annals of Clinical Microbiology and Antimicrobials · doi:10.1186/1476-0711-13-18 · Cited by 26
Müller, C., Neugebauer, T., Zill, P., Lass‐Flörl, C., Bracher, F., & Binder, U. (2018) · Molecules · doi:10.3390/molecules23051218 · Cited by 26
Foglia, F., Lawrence, M. J., Demé, B., Fragneto, G., & Barlow, D. J. (2012) · Scientific Reports · doi:10.1038/srep00778 · Cited by 25
Mantil, E., Crippin, T., & Avis, T. J. (2019) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2019.01.003 · Cited by 25
Szomek, M., Reinholdt, P., Walther, H.-L., Scheidt, H. A., Müller, P. K., Obermaier, S., Poolman, B., Kongsted, J., & Wüstner, D. (2022) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2022.184012 · Cited by 25
Tevyashova, A. N., Efimova, S. S., Alexandrov, A. I., Omelchuk, O. A., Ghazy, E. S. M. O., Бычкова, Е. Н., Zatonsky, G. V., Grammatikova, N. E., Dezhenkova, L. G., Solovieva, S. E., et al. (2023) · Antibiotics · doi:10.3390/antibiotics12010151 · Cited by 25
Qasim, M. H., Baipaywad, P., Udomluck, N., Na, D., & Park, H. (2014) · Macromolecular Research · doi:10.1007/s13233-014-2162-2 · Cited by 25
Singh, V. K., Tiwari, R., Rajneesh, Kumar, A., Chauhan, S. B., Sudarshan, M., Mehrotra, S., Gautam, V., Sundar, S., & Kumar, R. (2024) · ACS Infectious Diseases · doi:10.1021/acsinfecdis.4c00693 · Cited by 24
Xu, L., Ding, S., & Li, P. (2014) · Angewandte Chemie · doi:10.1002/ange.201309546 · Cited by 24
Tang, X., Dai, J., Xie, J., Zhu, Y., Zhu, M., Wang, Z., Xie, C., Yao, A., Liu, T., Wang, X., et al. (2015) · Nanoscale Research Letters · doi:10.1186/s11671-015-0969-1 · Cited by 24
Linearmycins are lytic membrane-targeting antibiotics
Stubbendieck, R. M., Brock, D. J., Pellois, J., Gill, J. J., & Straight, P. D. (2018) · The Journal of Antibiotics · doi:10.1038/s41429-017-0005-z · Cited by 24
Die molekulare industrielle Revolution: zur automatisierten Synthese organischer Verbindungen
Trobe, M., & Burke, M. D. (2018) · Angewandte Chemie · doi:10.1002/ange.201710482 · Cited by 23
Self-citationSegura, T., Puga, A. M., Burillo, G., Llovo, J., Brackman, G., Coenye, T., Concheiro, Á., & Alvarez‐Lorenzo, C. (2014) · Biomacromolecules · doi:10.1021/bm500257s · Cited by 23
Dalhoff, A. (2017) · Journal of Global Antimicrobial Resistance · doi:10.1016/j.jgar.2017.10.024 · Cited by 26
Alfatah, M., Bari, V. K., Nahar, A. S., Bijlani, S., & Ganesan, K. (2017) · Scientific Reports · doi:10.1038/srep40281 · Cited by 22
Hoo, L. S. (2017) · Journal of Liposome Research · doi:10.1080/08982104.2017.1360345 · Cited by 21
Direct observation of nystatin binding to the plasma membrane of living cells
Szomek, M., Reinholdt, P., Petersen, D., Caci, A., Kongsted, J., & Wüstner, D. (2020) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2020.183528 · Cited by 22
Chen, D., Forster, H., & Adaskaveg, J. E. (2020) · Plant Disease · doi:10.1094/pdis-07-20-1421-re · Cited by 22
Suchodolski, J., Muraszko, J., Bernat, P., & Krasowska, A. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22105219 · Cited by 22
A novel performing PEG-cholane nanoformulation for Amphotericin B delivery
Alonso, C. L., Torrado, J. J., Ballesteros, M. P., Malfanti, A., Bersani, S., Salmaso, S., & Caliceti, P. (2015) · International Journal of Pharmaceutics · doi:10.1016/j.ijpharm.2015.08.070 · Cited by 22
Nakagawa, Y., Umegawa, Y., Nonomura, K., Matsushita, N., Takano, T., Tsuchikawa, H., Hanashima, S., Oishi, T., Matsumori, N., & Murata, M. (2014) · Biochemistry · doi:10.1021/bi5012942 · Cited by 21
Samie, S., Trollope, K. M., Joubert, L., Makunga, N. P., & Volschenk, H. (2019) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2019.02.008 · Cited by 22
Morphology and dynamics of domains in ergosterol or cholesterol containing membranes
Galván‐Hernández, A., Kobayashi, N., Hernández‐Cobos, J., Antillón, A., Nakabayashi, S., & Ortega‐Blake, I. (2019) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2019.183101 · Cited by 22
Wang, X. (2021) · Infectious diseases · doi:10.5772/intechopen.87410 · Cited by 22
Suchodolski, J., Derkacz, D., Bernat, P., & Krasowska, A. (2021) · Scientific Reports · doi:10.1038/s41598-021-86012-9 · Cited by 21
Effects of cholesterol on the mechanism of fengycin, a biofungicide
Sur, S., & Grossfield, A. M. (2022) · Biophysical Journal · doi:10.1016/j.bpj.2022.04.006 · Cited by 21
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de Sousa, N. S. O., de Almeida, J. D. R., Frickmann, H., Lacerda, M., & de Souza, J. V. B. (2023) · Revista da Sociedade Brasileira de Medicina Tropical · doi:10.1590/0037-8682-0121-2023 · Cited by 24
Navarro-Mendoza, M. I., Arques, C. P., Parker, J. E., Xu, Z., Kelly, S. L., & Heitman, J. (2024) · mBio · doi:10.1128/mbio.01661-24 · Cited by 20
Folk, A., Cotoraci, C. A., Baltă, C., Suciu, M., Herman, H., Boldura, O. M., Dinescu, S., Păiuşan, L., Ardelean, A., & Hermenean, A. O. (2016) · BioMed Research International · doi:10.1155/2016/5398730 · Cited by 21
Kim, J. Y., Lee, I. H., Kim, D.-W., Kim, S. H., Kwon, Y., Han, G.-H., Cho, G., Choi, E. H., & Lee, G. J. (2016) · RSC Advances · doi:10.1039/c5ra28107e · Cited by 21
Nesbitt, J. R., Steves, E., Schonhofer, C., Cait, A., Manku, S., Yeung, J. H. F., Bennet, A. J., McNagny, K. M., Choy, J. C., Hughes, M. R., et al. (2018) · Frontiers in Microbiology · doi:10.3389/fmicb.2017.02706 · Cited by 20
Pountain, A. W., & Barrett, M. P. (2019) · Wellcome Open Research · doi:10.12688/wellcomeopenres.15452.1 · Cited by 19
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de Sá, N. P., Taouil, A. K., Kim, J., Clement, T., Hoffmann, R. M., Burke, J. E., Rizzo, R. C., Ojima, I., Poeta, M. D., & Airola, M. V. (2021) · Nature Communications · doi:10.1038/s41467-021-26163-5 · Cited by 20
The antimicrobial and immunomodulatory effects of Ionophores for the treatment of human infection
Li, G., Oliveira, D. M. P. D., & Walker, M. J. (2021) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2021.111661 · Cited by 21
Pezzotti, G., Kobara, M., Nakaya, T., Imamura, H., Asai, T., Miyamoto, N., Adachi, T., Yamamoto, T., Kanamura, N., Ohgitani, E., et al. (2022) · Frontiers in Microbiology · doi:10.3389/fmicb.2022.896359 · Cited by 20
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Amphotericin B from antifungal to antiviral therapy: promising modern therapeutic branch
Al-Khikani, F. H. O. (2020) · Research Results in Pharmacology · doi:10.3897/rrpharmacology.6.53649 · Cited by 20
Pruitt, H. M., Zhu, J., Riley, S. P., & Shi, M. (2025) · Journal of Fungi · doi:10.3390/jof11030236 · Cited by 20
Butyrolactol A enhances caspofungin efficacy via flippase inhibition in drug-resistant fungi
Chen, X., Duan, H. D., Hoy, M. J., Koteva, K. K., Spitzer, M., Guitor, A. K., Puumala, E., Fiebig‐Comyn, A., Hu, G., Yiu, B., et al. (2025) · Cell · doi:10.1016/j.cell.2025.11.036 · Cited by 23
Tulloch, L. B., Tinti, M., Wall, R. J., Weidt, S. K., Corpas‐López, V., Dey, G., Smith, T., Fairlamb, A. H., Barrett, M. P., & Wyllie, S. (2024) · PLoS Pathogens · doi:10.1371/journal.ppat.1012382 · Cited by 19
Becucci, L., Innocenti, M., Bellandi, S., & Guidelli, R. (2013) · Electrochimica Acta · doi:10.1016/j.electacta.2013.09.027 · Cited by 19
The Use of α-fetoprotein for the Delivery of Cytotoxic Payloads to Cancer Cells
Pak, V. N. (2014) · Therapeutic Delivery · doi:10.4155/tde.14.59 · Cited by 19
Minematsu, A., Miyazaki, T., Shimamura, S., Nishikawa, H., Nakayama, H., Takazono, T., Saijo, T., Yamamoto, K., Imamura, Y., Yanagihara, K., et al. (2019) · PLoS ONE · doi:10.1371/journal.pone.0210883 · Cited by 22
Bansal, R., Sen, S. S., Muthuswami, R., & Madhubala, R. (2019) · PLoS neglected tropical diseases · doi:10.1371/journal.pntd.0007260 · Cited by 19
Recent insights on nanomedicine for augmented infection control
Singh, S., Hussain, A., Shakeel, F., Ahsan, M. J., Alshehri, S., Webster, T. J., & Lal, U. R. (2019) · International Journal of Nanomedicine · doi:10.2147/ijn.s170280 · Cited by 19
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Guirao-Abad, J. P., Sánchez-Fresneda, R., Román, E., Plá, J., Argüelles, J. C., & Alonso‐Monge, R. (2019) · Fungal Genetics and Biology · doi:10.1016/j.fgb.2019.103302 · Cited by 21
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Zamith‐Miranda, D., Heyman, H. M., Burnet, M., Couvillion, S., Zheng, X., Munoz, N., Nelson, W. C., Kyle, J. E., Zink, E. M., Weitz, K. K., et al. (2021) · mBio · doi:10.1128/mbio.02972-21 · Cited by 20
Serum albumin promotes ATP-binding cassette transporter-dependent sterol uptake in yeast
Marek, M., Silvestro, D., Fredslund, M. D., Andersen, T. G., & Pomorski, T. G. (2014) · FEMS Yeast Research · doi:10.1111/1567-1364.12219 · Cited by 20
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Davis, S. A., Ripa, L. A. D., Hu, L., Cioffi, A. G., Pogorelov, T. V., Rienstra, C. M., & Burke, M. D. (2015) · Journal of the American Chemical Society · doi:10.1021/jacs.5b05766 · Cited by 18
Self-citationMolecular Umbrella–Amphotericin B Conjugates
Janout, V., Bienvenu, C., Schell, W. A., Perfect, J. R., & Regen, S. L. (2014) · Bioconjugate Chemistry · doi:10.1021/bc500277v · Cited by 18
Mantil, E., Crippin, T., & Avis, T. J. (2019) · Colloids and Surfaces B Biointerfaces · doi:10.1016/j.colsurfb.2019.02.050 · Cited by 18
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Reeßing, F., Bispo, M., Alvarez, M. L., van Oosten, M., Feringa, B. L., van Dijl, J. M., & Szymański, W. (2020) · ACS Omega · doi:10.1021/acsomega.0c02094 · Cited by 18
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Baghirova, A. A., & Kasumov, K. M. (2022) · Biochemistry (Moscow) Supplement Series B Biomedical Chemistry · doi:10.1134/s1990750822010024 · Cited by 17
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Carlson, T., Lupinacci, E., Moseley, K., & Chandrasekaran, S. (2021) · FEMS Microbiology Letters · doi:10.1093/femsle/fnab040 · Cited by 17
He, L., Schulz‐Senft, M., Thiedemann, B., Linshoeft, J., Gates, P. J., & Staubitz, A. (2015) · European Journal of Organic Chemistry · doi:10.1002/ejoc.201500138 · Cited by 17
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Zhang, Y., Kong, W.-L., Wu, X., & Li, P.-S. (2022) · Phytopathology · doi:10.1094/phyto-10-21-0442-r · Cited by 16
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Halbandge, S. D., MORTALE, S. P., & Karuppayil, S. M. (2017) · The Open Nanomedicine Journal · doi:10.2174/1875933501704010001 · Cited by 16
Han, Y., Liu, Y., Ma, X., Shen, A., Liu, Y., Weeranoppanant, N., Dong, H., Li, Y., Ren, T., Kuai, L., et al. (2021) · Biomaterials · doi:10.1016/j.biomaterials.2021.120849 · Cited by 16
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Self-citation
Metadata
- Authors
- Gray, K. C., Palacios, D. S., Dailey, I., Endo, M. M., Uno, B. E., Wilcock, B. C., & Burke, M. D.
- Affiliations
- Howard Hughes Medical Institute (US)
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2012-01-17
- Volume
- 109
- Issue
- 7
- Pages
- 2234-2239
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC3289339
- OpenAlex
- W1987640473
- Cited by
- 608
- References
- 50
- Citations by year
- 2026: 42 · 2025: 42 · 2024: 34 · 2023: 49 · 2022: 45 · 2021: 56 · 2020: 53 · 2019: 50 · 2018: 32 · 2017: 44 · 2016: 44 · 2015: 40 · 2014: 36 · 2013: 30 · 2012: 11
- FWCI
- 24.34
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Howard Hughes Medical Institute
- Bristol-Myers Squibb
- National Institutes of Health
- National Institute of General Medical Sciences (R01GM080436, GM080436)
- Topics
- Health Sciences › Medicine › Infectious Diseases › Antifungal resistance and susceptibility
- Life Sciences › Immunology and Microbiology › Applied Microbiology and Biotechnology › Antimicrobial agents and applications
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Lipid Membrane Structure and Behavior
- Keywords
- amphotericin B, ergosterol binding, yeast cell death, antifungal mechanism, ion channel formation, membrane permeabilization, fungal drug resistance, natural product derivatives, therapeutic index, antifungal toxicity
- MeSH terms
- Amphotericin B, Antifungal Agents, Ergosterol, Saccharomyces cerevisiae
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