Comparative Ploidy Proteomics of Candida albicans Biofilms Unraveled the Role of the AHP1 Gene in the Biofilm Persistence Against Amphotericin B
Open accessAbstract
Candida albicans is a major fungal pathogen causing lethal infections in immunocompromised patients. C. albicans forms antifungal tolerant biofilms contributing significantly to therapeutic failure. The recently established haploid C. albicans biofilm model provides a new toolbox to uncover the mechanism governing the higher antifungal tolerance of biofilms. Here, we comprehensively examined the proteomics and antifungal susceptibility of standard diploid (SC5314 and BWP17) and stable haploid (GZY792 and GZY803) strains of C. albicans biofilms. Subsequent downstream analyses identified alkyl hydroperoxide reductase 1 (AHP1) as a critical determinant of C. albicans biofilm's tolerance of amphotericin B. At 32 μg/ml of amphotericin B, GZY803 haploid biofilms showed 0.1% of persister population as compared with 1% of the diploid biofilms. AHP1 expression was found to be lower in GZY803 biofilms, and AHP1 overexpression in GZY803 restored the percentage of persister population. Consistently, deleting AHP1 in the diploid strain BWP17 caused a similar increase in amphotericin B susceptibility. AHP1 expression was also positively correlated with the antioxidant potential. Furthermore, C. albicans ira2Δ/Δ biofilms were susceptible to amphotericin B and had a diminished antioxidant capacity. Interestingly, AHP1 overexpression in the ira2Δ/Δ strain restored the antioxidant potential and enhanced the persister population against amphotericin B, and shutting down the AHP1 expression in ira2Δ/Δ biofilms reversed the effect. In conclusion, we provide evidence that the AHP1 gene critically determines the amphotericin B tolerance of C. albicans biofilms possibly by maintaining the persisters' antioxidant capacity. This finding will open up new avenues for developing therapies targeting the persister population of C. albicans biofilms. The mass spectrometry proteomics data are available via ProteomeXchange with identifier PXD004274.
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Ahp1 can be directly or indirectly regulated by Ira2, an inhibitory regulator of the RAS-cAMP pathway.
“Studies indicate that Ahp1 can be directly or indirectly regulated by Ira2, an inhibitory regulator of the RAS-cAMP pathway [70].”
From Antifungal persistence: Clinical relevance and mechanisms (2025) · cites this paper as [70]
Cites
Cytoscape: A software Environment for integrated models of biomolecular interaction networks
Shannon, P., Markiel, A., Ozier, O., Baliga, N. S., Wang, J. T., Ramage, D., Amin, N., Schwikowski, B., & Ideker, T. (2003) · Genome Research · doi:10.1101/gr.1239303 · Cited by 51,888 · see citing works
Understanding the Warburg Effect: The Metabolic Requirements of Cell Proliferation
Vander Heiden, M. G., Cantley, L. C., & Thompson, C. B. (2009) · Science · doi:10.1126/science.1160809 · Cited by 16,197 · see citing works
National Committee for Clinical Laboratory Standards
Bruck, E. (1980) · PEDIATRICS · doi:10.1542/peds.65.1.187 · Cited by 14,736 · see citing works
Cluster analysis and display of genome-wide expression patterns
Eisen, M. B., Spellman, P. T., Brown, P. O., & Botstein, D. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.25.14863 · Cited by 12,617 · see citing works
Wisplinghoff, H., Bischoff, T., Tallent, S. M., Seifert, H., Wenzel, R. P., & Edmond, M. B. (2004) · Clinical Infectious Diseases · doi:10.1086/421946 · Cited by 4,496 · see citing works
Maere, S., Heymans, K., & Kuiper, M. (2005) · Bioinform. · doi:10.1093/bioinformatics/bti551 · Cited by 4,251 · see citing works
2016 update of the PRIDE database and its related tools
Vizcaíno, J. A., Csordás, A., del‐Toro, N., Dianes, J. A., Griss, J., Lavidas, I., Mayer, G., Pérez‐Riverol, Y., Reisinger, F., Ternent, T., et al. (2015) · Nucleic Acids Research · doi:10.1093/nar/gkv1145 · Cited by 3,466 · see citing works
Aerobic glycolysis: Meeting the metabolic requirements of cell proliferation
Lunt, S. Y., & Vander Heiden, M. G. (2011) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-092910-154237 · Cited by 3,057 · see citing works
Chandra, J., Kuhn, D. M., Mukherjee, P. K., Hoyer, L. L., McCormick, T., & Ghannoum, M. A. (2001) · Journal of Bacteriology · doi:10.1128/jb.183.18.5385-5394.2001 · Cited by 1,578 · see citing works
Protein labeling by iTRAQ: A new tool for quantitative mass spectrometry in proteome research
Wiese, S., Reidegeld, K. A., Meyer, H. E., & Warscheid, B. (2006) · PROTEOMICS · doi:10.1002/pmic.200600422 · Cited by 803 · see citing works
Cell Wall and Secreted Proteins of<i>Candida albicans</i>: Identification, Function, and Expression
Chaffin, W. L., López-Ribot, J. L., Casanova, M., Gozalbo, D., & Martínez, J. P. (1998) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.62.1.130-180.1998 · Cited by 726 · see citing works
<i>Candida</i>Biofilms: an Update
Ramage, G., Saville, S. P., Thomas, D. P., & López-Ribot, J. L. (2005) · Eukaryotic Cell · doi:10.1128/ec.4.4.633-638.2005 · Cited by 678 · see citing works
<i>Candida albicans</i> Biofilms Produce Antifungal-Tolerant Persister Cells
LaFleur, M. D., Kumamoto, C. A., & Lewis, K. (2006) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.00684-06 · Cited by 521 · see citing works
Resistance of Candida albicans biofilms to antifungal agents in vitro
Hawser, S., & Douglas, L. (1995) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.39.9.2128 · Cited by 407 · see citing works
Gan, C. S., Chong, P. K., Pham, T. K., & Wright, P. C. (2007) · Journal of Proteome Research · doi:10.1021/pr060474i · Cited by 404 · see citing works
Apoptosis induced by environmental stresses and amphotericin B in <i>Candida albicans</i>
Phillips, A. J., Sudbery, I., & Ramsdale, M. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2332326100 · Cited by 398 · see citing works
Baillie, G. S. (2000) · Journal of Antimicrobial Chemotherapy · doi:10.1093/jac/46.3.397 · Cited by 389 · see citing works
Invasive candidiasis as a cause of sepsis in the critically ill patient
Delaloye, J., & Calandra, T. (2013) · Virulence · doi:10.4161/viru.26187 · Cited by 380 · see citing works
Biofilm lifestyle of <i>Candida:</i> a mini review
Seneviratne, C., Jin, L., & Samaranayake, L. (2008) · Oral Diseases · doi:10.1111/j.1601-0825.2007.01424.x · Cited by 317 · see citing works
Self-citationTanaka, K., Nakafuku, M., Tamanoi, F., Kaziro, Y., Matsumoto, K., & Toh‐e, A. (1990) · Molecular and Cellular Biology · doi:10.1128/mcb.10.8.4303 · Cited by 292 · see citing works
The ‘obligate diploid’ Candida albicans forms mating-competent haploids
Hickman, M. A., Zeng, G., Forche, A., Hirakawa, M. P., Abbey, D., Harrison, B. D., Wang, Y.-M., Su, C.-H., Bennett, R. J., Wang, Y., et al. (2013) · Nature · doi:10.1038/nature11865 · Cited by 284 · see citing works
Self-citationOxidative Stress Responses in the Human Fungal Pathogen, Candida albicans
Dantas, A., Day, A., Ikeh, M., Kos, I., Achan, B., & Quinn, J. (2015) · Biomolecules · doi:10.3390/biom5010142 · Cited by 281 · see citing works
Recent insights into Candida albicans biofilm resistance mechanisms
Mathé, L., & Van Dijck, P. (2013) · Current Genetics · doi:10.1007/s00294-013-0400-3 · Cited by 271 · see citing works
Crm1p mediates regulated nuclear export of a yeast AP‐1‐like transcription factor
Yan, C. T., Lee, L. H., & Davis, L. I. (1998) · The EMBO Journal · doi:10.1093/emboj/17.24.7416 · Cited by 264 · see citing works
Mavor, A., Thewes, S., & Hube, B. (2005) · Current Drug Targets · doi:10.2174/138945005774912735 · Cited by 252 · see citing works
Mesa-Arango, A. C., Trevijano-Contador, N., Román, E., Sánchez-Fresneda, R., Casas, C., Herrero, E., Argüelles, J. C., Pla, J., Cuenca-Estrella, M., & Zaragoza, O. (2014) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.03570-14 · Cited by 232 · see citing works
Social evolution in multispecies biofilms
Mitri, S., Xavier, J. B., & Foster, K. R. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1100292108 · Cited by 222 · see citing works
Alberts, A. S., Bouquin, N., Johnston, L. H., & Treisman, R. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.15.8616 · Cited by 208 · see citing works
Tetracycline-Inducible Gene Expression and Gene Deletion in Candida albicans
Park, Y.-N., & Morschhäuser, J. (2005) · Eukaryotic Cell · doi:10.1128/ec.4.8.1328-1342.2005 · Cited by 205 · see citing works
Signalling and oxidant adaptation in Candida albicans and Aspergillus fumigatus
Chauhan, N., Latgé, J., & Calderone, R. (2006) · Nature Reviews Microbiology · doi:10.1038/nrmicro1426 · Cited by 197 · see citing works
The Ras Superfamily of Small GTPases: The Unlocked Secrets
Goitre, L., Trapani, E., Trabalzini, L., & Retta, S. F. (2013) · Methods in molecular biology · doi:10.1007/978-1-62703-791-4_1 · Cited by 186 · see citing works
A New Antioxidant with Alkyl Hydroperoxide Defense Properties in Yeast
Lee, J., Spector, D., Godon, C., Labarre, J., & Tolédano, M. B. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.8.4537 · Cited by 179 · see citing works
Chauhan, N., Inglis, D., Roman, E., Pla, J., Li, D., Calera, J. A., & Calderone, R. (2003) · Eukaryotic Cell · doi:10.1128/ec.2.5.1018-1024.2003 · Cited by 159 · see citing works
Gullo, A. (2009) · Drugs · doi:10.2165/11315530-000000000-00000 · Cited by 127 · see citing works
Superoxide dismutases are involved in Candida albicans biofilm persistence against miconazole
Bink, A., Vandenbosch, D., Coenye, T., Nelis, H., Cammue, B. P. A., & Thevissen, K. (2011) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.00280-11 · Cited by 119 · see citing works
IRA2, an upstream negative regulator of RAS in yeast, is a RAS GTPase-activating protein.
Tanaka, K., Lin, B. K., Wood, D. R., & Tamanoi, F. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.2.468 · Cited by 112 · see citing works
Proteomic and Transcriptomic Analysis of Aspergillus fumigatus on Exposure to Amphotericin B
Gautam, P., Shankar, J., Madan, T., Sirdeshmukh, R., Sundaram, C. S., Gade, W. N., Basir, S. F., & Sarma, P. U. (2008) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.01431-07 · Cited by 109 · see citing works
Cell Density and Cell Aging as Factors Modulating Antifungal Resistance ofCandida albicansBiofilms
Seneviratne, C. J., Jin, L., Samaranayake, Y. H., & Samaranayake, L. P. (2008) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.00541-08 · Cited by 107 · see citing works
Self-citationSeneviratne, C. J., Wang, Y., Jin, L., Abiko, Y., & Samaranayake, L. P. (2008) · PROTEOMICS · doi:10.1002/pmic.200701097 · Cited by 104 · see citing works
Self-citationLi, P., Seneviratne, C. J., Alpi, E., Vizcaino, J. A., & Jin, L. (2015) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.00543-15 · Cited by 95 · see citing works
Self-citationWu, N., He, L., Cui, P., Wang, W., Yuan, Y., Liu, S., Xu, T., Zhang, S., Wu, J., Zhang, W., et al. (2015) · Frontiers in Microbiology · doi:10.3389/fmicb.2015.01003 · Cited by 91 · see citing works
Vylkova, S., Jang, W. S., Li, W., Nayyar, N., & Edgerton, M. (2007) · Eukaryotic Cell · doi:10.1128/ec.00039-07 · Cited by 88 · see citing works
Zhang, L. (2002) · Journal of Antimicrobial Chemotherapy · doi:10.1093/jac/dkf001 · Cited by 84 · see citing works
Sarosi, G. A. (1990) · Postgraduate Medicine · doi:10.1080/00325481.1990.11716368 · Cited by 71 · see citing works
Ghosh, D., Li, Z., Tan, X. F., Lim, T. K., Mao, Y., & Lin, Q. (2013) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m112.023085 · Cited by 71 · see citing works
Unraveling the resistance of microbial biofilms: Has proteomics been helpful?
Seneviratne, C. J., Wang, Y., Jin, L., Wong, S. S. W., Herath, T. D. K., & Samaranayake, L. P. (2012) · PROTEOMICS · doi:10.1002/pmic.201100356 · Cited by 56 · see citing works
Self-citationTranscriptomic and Proteomic Profile of Aspergillus fumigatus on Exposure to Artemisinin
Gautam, P., Upadhyay, S. K., Hassan, W., Madan, T., Sirdeshmukh, R., Sundaram, C. S., Gade, W. N., Basir, S. F., Singh, Y. P., & Sarma, P. U. (2011) · Mycopathologia · doi:10.1007/s11046-011-9445-3 · Cited by 53 · see citing works
Iwai, K., Naganuma, A., & Kuge, S. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.090142 · Cited by 45 · see citing works
Gao, Y., Lim, T. K., Lin, Q., & Li, S. F. Y. (2016) · Journal of Proteomics · doi:10.1016/j.jprot.2016.03.012 · Cited by 40 · see citing works
Mechanism of Chorismate Synthase
Kitzing, K., Auweter, S., Amrhein, N., & Macheroux, P. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m312471200 · Cited by 40 · see citing works
Wimhurst, J. M., & Manchester, K. L. (1973) · Biochemical Journal · doi:10.1042/bj1340143 · Cited by 30 · see citing works
One-step targeted gene deletion in Candida albicans haploids
Zeng, G., Wang, Y., Chan, F. Y., & Wang, Y. (2014) · Nature Protocols · doi:10.1038/nprot.2014.029 · Cited by 24 · see citing works
Self-citationHolland, M. J., & Westhead, E. W. (1973) · Biochemistry · doi:10.1021/bi00736a013 · Cited by 24 · see citing works
New “haploid biofilm model” unravels IRA2 as a novel regulator of Candida albicans biofilm formation
Seneviratne, C. J., Zeng, G., Truong, T., Wong, S. S. W., Wong, S. S. W., Samaranayake, L. P., Chan, F. Y., Wang, Y., Wang, H., Gao, J., et al. (2015) · Scientific Reports · doi:10.1038/srep12433 · Cited by 19 · see citing works
Self-citationSun, X., Lu, H., Jiang, Y., & Cao, Y. (2013) · Current Microbiology · doi:10.1007/s00284-013-0366-x · Cited by 5 · see citing works
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Development and regulation of single- and multi-species Candida albicans biofilms
Lohse, M. B., Gulati, M., Johnson, A. D., & Nobile, C. J. (2018) · Nature Reviews Microbiology · doi:10.1038/nrmicro.2017.107 · Cited by 643 · see citing works
<i>Candida albicans</i> biofilms and polymicrobial interactions
Ponde, N. O., Lortal, L., Ramage, G., Naglik, J. R., & Richardson, J. P. (2021) · Critical Reviews in Microbiology · doi:10.1080/1040841x.2020.1843400 · Cited by 281 · see citing works
Fungal persister cells: The basis for recalcitrant infections?
Wuyts, J., Van Dijck, P., & Holtappels, M. (2018) · PLOS Pathogens · doi:10.1371/journal.ppat.1007301 · Cited by 136 · see citing works
Ellepola, K., Truong, T., Liu, Y., Lin, Q., Lim, T. K., Lee, Y. M., Cao, T., Koo, H., & Seneviratne, C. J. (2019) · Infection and Immunity · doi:10.1128/iai.00339-19 · Cited by 122 · see citing works
Self-citationBacterial GtfB Augments Candida albicans Accumulation in Cross-Kingdom Biofilms
Ellepola, K., Liu, Y., Cao, T., Koo, H., & Seneviratne, C. J. (2017) · Journal of Dental Research · doi:10.1177/0022034517714414 · Cited by 94 · see citing works
Self-citationMulti-omics tools for studying microbial biofilms: current perspectives and future directions
Seneviratne, C. J., Suriyanarayanan, T., Widyarman, A. S., Lee, L. S., Lau, M., Ching, J., Delaney, C., & Ramage, G. (2020) · Critical Reviews in Microbiology · doi:10.1080/1040841x.2020.1828817 · Cited by 89 · see citing works
Self-citationBall, B., Bermas, A., Carruthers‐Lay, D., & Geddes‐McAlister, J. (2019) · Journal of Fungi · doi:10.3390/jof5020052 · Cited by 62 · see citing works
Gaining Insights from Candida Biofilm Heterogeneity: One Size Does Not Fit All
Kean, R., Delaney, C., Rajendran, R., Sherry, L., Metcalfe, R., Thomas, R., McLean, W., Williams, C., & Ramage, G. (2018) · Journal of Fungi · doi:10.3390/jof4010012 · Cited by 53 · see citing works
Specific Enrichment and Proteomics Analysis ofEscherichia coliPersisters from Rifampin Pretreatment
Sulaiman, J. E., Hao, C., & Lam, H. (2018) · Journal of Proteome Research · doi:10.1021/acs.jproteome.8b00625 · Cited by 50 · see citing works
<i>Candida albicans</i> Biofilms Are Generally Devoid of Persister Cells
Denega, I., d’Enfert, C., & Bachellier-Bassi, S. (2019) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.01979-18 · Cited by 32 · see citing works
Oxidative imbalance in Candida tropicalis biofilms and its relation with persister cells
da Silva, M. A., Baronetti, J. L., Páez, P. L., & Paraje, M. G. (2021) · Frontiers in Microbiology · doi:10.3389/fmicb.2020.598834 · Cited by 28 · see citing works
A mitochondrial proteomics view of complex I deficiency in Candida albicans
She, X., Zhang, P., Gao, Y., Zhang, L., Wang, Q., Chen, H., Calderone, R., Liu, W., & Li, D. (2018) · Mitochondrion · doi:10.1016/j.mito.2017.08.003 · Cited by 26 · see citing works
Proteome analysis of biofilm produced by a Fusarium falciforme keratitis infectious agent
Calvillo‐Medina, R. P., Reyes‐Grajeda, J. P., Escoto, L. B., Bautista-Hernández, L. A., Campos‐Guillén, J., Jones, G. H., & Lucio, V. M. B. (2019) · Microbial Pathogenesis · doi:10.1016/j.micpath.2019.03.001 · Cited by 24 · see citing works
Mixed Fungal Biofilms: From Mycobiota to Devices, a New Challenge on Clinical Practice
Costa, P. D. S., Prado, A., Bagon, N. P., Negri, M., & Svidzinski, T. I. E. (2022) · Microorganisms · doi:10.3390/microorganisms10091721 · Cited by 24 · see citing works
El Meouche, I., Jain, P., Jolly, M. K., & Capp, J.-P. (2024) · Translational Oncology · doi:10.1016/j.tranon.2024.102069 · Cited by 22 · see citing works
Application of proteomics in studying bacterial persistence
Sulaiman, J. E., & Lam, H. (2019) · Expert Review of Proteomics · doi:10.1080/14789450.2019.1575207 · Cited by 20 · see citing works
Sulaiman, J. E., & Lam, H. (2022) · PROTEOMICS · doi:10.1002/pmic.202100409 · Cited by 19 · see citing works
Das, P. P., Chua, G. M., Lin, Q., & Wong, S. (2019) · Journal of Proteomics · doi:10.1016/j.jprot.2019.02.002 · Cited by 19 · see citing works
Use of Haploid Model of Candida albicans to Uncover Mechanism of Action of a Novel Antifungal Agent
Truong, T., Suriyanarayanan, T., Zeng, G., Le, T. D., Liu, L., Li, J., Tong, C., Wang, Y., & Seneviratne, C. J. (2018) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2018.00164 · Cited by 16 · see citing works
Self-citationThe effects of cigarette smoking and exercise on total salivary antioxidant activity
Munther, S. (2018) · The Saudi Dental Journal · doi:10.1016/j.sdentj.2018.09.002 · Cited by 16 · see citing works
Brantl, V., Boysen, J. M., Yap, A., Golubtsov, E., Ruf, D., Heinekamp, T., Straßburger, M., Dichtl, K., Haas, H., Hillmann, F., et al. (2021) · mBio · doi:10.1128/mbio.00976-21 · Cited by 15 · see citing works
Truong, T., Zeng, G., Lim, T. K., Cao, T., Pang, L. M., Lee, Y. M., Lin, Q., Wang, Y., & Seneviratne, C. J. (2019) · PROTEOMICS · doi:10.1002/pmic.201900240 · Cited by 14 · see citing works
Self-citationAşkun, T. (2022) · IntechOpen eBooks · doi:10.5772/intechopen.100869 · Cited by 15 · see citing works
Sdd3 regulates the biofilm formation of Candida albicans via the Rho1-PKC-MAPK pathway
Pang, L. M., Zeng, G., Chow, E. W. L., Xu, X., Li, N., Kok, Y. J., Chong, S. C., Bi, X., Gao, J., Seneviratne, C. J., et al. (2024) · mBio · doi:10.1128/mbio.03283-24 · Cited by 13 · see citing works
Self-citationThe role of Npt1 in regulating antifungal protein activity in filamentous fungi
Wang, Y., Wang, S., Chen, Y., Xie, C., Xu, H., Lin, Y., Lin, R., Zeng, W., Chen, X., Nie, X., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-58230-6 · Cited by 13 · see citing works
Self-citationAboualigalehdari, E., Tahmasebi Birgani, M., Fatahinia, M., & Hosseinzadeh, M. (2021) · Frontiers in Microbiology · doi:10.3389/fmicb.2021.651221 · Cited by 11 · see citing works
Zeng, G., Xu, X., Kok, Y. J., Deng, F.-S., Chow, E. W. L., Gao, J., Bi, X., & Wang, Y. (2023) · Cell Reports · doi:10.1016/j.celrep.2023.113473 · Cited by 12 · see citing works
Self-citationWei, T., Zheng, N., Zheng, H., Chen, Y., Hong, P., Liu, W., & Liu, M. (2022) · Medical Mycology · doi:10.1093/mmy/myac084 · Cited by 10 · see citing works
Antifungal persistence: Clinical relevance and mechanisms
Wang, R., Lv, J., Chen, L., Zhao, Y., & Du, H. (2025) · PLoS pathogens · doi:10.1371/journal.ppat.1013456 · Cited by 12 · see citing works
“Studies indicate that Ahp1 can be directly or indirectly regulated by Ira2, an inhibitory regulator of the RAS-cAMP pathway [70].”
Owens, R. A., & Doyle, S. (2021) · Expert Review of Proteomics · doi:10.1080/14789450.2021.1912601 · Cited by 8 · see citing works
Shoukat, I., Frazer, C., & Allingham, J. S. (2019) · mSphere · doi:10.1128/msphere.00610-19 · Cited by 7 · see citing works
Zeng, G., Xu, X., Gao, J., Dantas, A. D. S., Gow, N. A. R., & Wang, Y. (2021) · The Cell Surface · doi:10.1016/j.tcsw.2021.100057 · Cited by 8 · see citing works
Self-citationSun, Y., Roy, S., Yang, Q., Tang, Y., & Ren, D. (2025) · Frontiers in Pharmacology · doi:10.3389/fphar.2025.1634627 · Cited by 6 · see citing works
Chauhan, A., Gow, N. A. R., & Prasad, R. (2026) · The Cell Surface · doi:10.1016/j.tcsw.2026.100168 · Cited by 6 · see citing works
Romero, O., & Geddes‐McAlister, J. (2025) · mBio · doi:10.1128/mbio.02303-24 · Cited by 5 · see citing works
Studying Bacterial Persistence: Established Methods and Current Advances
Louwagie, E., Verstraete, L., Michiels, J. J., & Verstraeten, N. (2021) · Methods in molecular biology · doi:10.1007/978-1-0716-1621-5_1 · Cited by 4 · see citing works
Biçer, M. (2023) · Archives of Microbiology · doi:10.1007/s00203-023-03744-0 · Cited by 4 · see citing works
Truong, T., Pang, L. M., Rajan, S., Wong, S. S. W., Fung, Y. M. E., Samaranayake, L. P., & Seneviratne, C. J. (2020) · Microorganisms · doi:10.3390/microorganisms8101541 · Cited by 3 · see citing works
Self-citationClinical Significance, Molecular Formation, and Natural Antibiofilm Agents of Candida albicans
Abdulghani, M. M. M., & Zore, G. B. (2024) · Springer eBooks · doi:10.1007/978-981-97-5165-5_9 · Cited by 1 · see citing works
Cytrynbaum, E. G., & McClean, M. N. (2025) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2025.115740 · Cited by 1 · see citing works
Dutta, D., Manuri, S., Sidhu, V. K., & Kumar, P. (2022) · IntechOpen eBooks · doi:10.5772/intechopen.108054 · Cited by 1 · see citing works
Methodologies and Applications of Proteomics for Study of Yeast Strains: An Update
Lacerda, M. P. F., Marcelino, M., Lourencetti, N. M. S., Neto, Á. D. B., Gattás, E. A. D. L., Mendes‐Giannini, M. J. S., & Fusco‐Almeida, A. M. (2019) · Current Protein and Peptide Science · doi:10.2174/1389203720666190715145131 · Cited by 1 · see citing works
Al-Ameri, H. A. (2021) · Mağallaẗ al-tarbiyaẗ wa-al-ʻilm · doi:10.33899/edusj.2021.168652 · Cited by 1 · see citing works
Etude structurale du remodeleur de la chromatine RSC chez Candida albicans
Dupeyron, R. (2023) · theses.fr (ABES) · doi:10.70675/5f7d1879zcfb3z42d7z91e1z9a2a37a29c1f
- Authors
- Truong, T., Zeng, G., Qingsong, L., Kwang, L. T., Tong, C., Chan, F. Y., Wang, Y., & Seneviratne, C. J.
- Affiliations
- National University of Singapore (SG)
- Agency for Science, Technology and Research (SG)
- Corresponding author
- Wang, Yue
- Seneviratne, Chaminda Jayampath
- Venue
- Molecular & Cellular Proteomics
- Publisher
- Elsevier BV
- Published
- 2016-11
- Volume
- 15
- Issue
- 11
- Pages
- 3488-3500
- ISSN
- 1535-9476 (ISSN-L)
- PMC
- PMC5098045
- OpenAlex
- W2522661577
- Cited by
- 45
- References
- 57
- Citations by year
- 2026: 1 · 2025: 5 · 2024: 3 · 2023: 3 · 2022: 5 · 2021: 8 · 2020: 3 · 2019: 9 · 2018: 5 · 2017: 3
- FWCI
- 5.23
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Molecular & Cellular Proteomics (publishedVersion, cc-by)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Medical Research Council (R-221–000-073–511)
- NUS-Start-up (R-221–000- 064–133)
- Agency for Science, Technology, and Research
- Topics
- Health Sciences › Medicine › Infectious Diseases › Antifungal resistance and susceptibility
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Fungal and yeast genetics research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Bacterial biofilms and quorum sensing
- Keywords
- Candida albicans, biofilm, antifungal tolerance, amphotericin B, alkyl hydroperoxide reductase, persister cells, antioxidant capacity, IRA2, ploidy, antifungal susceptibility, proteomics
- MeSH terms
- Amphotericin B, Antifungal Agents, Candida albicans, Diploidy, Fungal Proteins, Polyploidy, Down-Regulation, Gene Expression Regulation, Fungal, Biofilms, Drug Resistance, Bacterial, Proteomics, Peroxiredoxins
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