Cited by 172Fungal and yeast genetics researchBioinformatics and Genomic NetworksMicrobial Metabolic Engineering and Bioproduction

The DOI matches its Crossref record; 50 of the 50 references it cites were found in a registry or an index.

High-resolution chemical dissection of a model eukaryote reveals targets, pathways and gene functions

Open access

Hoepfner, Dominic, Helliwell, Stephen B., Sadlish, Heather, Schuierer, Sven, Filipuzzi, Ireos, Brachat, Sophie, Bhullar, Bhupinder, Plikat, Uwe, Abraham, Yann, Altorfer, Marc, Aust, Thomas, Baeriswyl, Lukas, Cerino, Raffaele, Chang, Lena, Estoppey, David, Eichenberger, Juerg, Frederiksen, Mathias, Hartmann, Nicole, Hohendahl, Annika, Knapp, Britta, Krastel, Philipp, Melin, Nicolas, Nigsch, Florian, Oakeley, Edward J., Petitjean, Virginie, Petersen, Frank, Riedl, Ralph, Schmitt, Esther K., Staedtler, Frank, Studer, Christian, Tallarico, John A., Wetzel, Stefan, Fishman, Mark C., Porter, Jeffrey A., Movva, N. Rao·2014·Microbiological Research

DOI 10.1016/j.micres.2013.11.004

Open this paper in CoChat — free account Open PDF

Abstract

Due to evolutionary conservation of biology, experimental knowledge captured from genetic studies in eukaryotic model organisms provides insight into human cellular pathways and ultimately physiology. Yeast chemogenomic profiling is a powerful approach for annotating cellular responses to small molecules. Using an optimized platform, we provide the relative sensitivities of the heterozygous and homozygous deletion collections for nearly 1800 biologically active compounds. The data quality enables unique insights into pathways that are sensitive and resistant to a given perturbation, as demonstrated with both known and novel compounds. We present examples of novel compounds that inhibit the therapeutically relevant fatty acid synthase and desaturase (Fas1p and Ole1p), and demonstrate how the individual profiles facilitate hypothesis-driven experiments to delineate compound mechanism of action. Importantly, the scale and diversity of tested compounds yields a dataset where the number of modulated pathways approaches saturation. This resource can be used to map novel biological connections, and also identify functions for unannotated genes. We validated hypotheses generated by global two-way hierarchical clustering of profiles for (i) novel compounds with a similar mechanism of action acting upon microtubules or vacuolar ATPases, and (ii) an un-annotated ORF, YIL060w, that plays a role in respiration in the mitochondria. Finally, we identify and characterize background mutations in the widely used yeast deletion collection which should improve the interpretation of past and future screens throughout the community. This comprehensive resource of cellular responses enables the expansion of our understanding of eukaryotic pathway biology.

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Integrity signals

Registry

Crossref · 10.1016/j.micres.2013.11.004

Cites

50 of 50 references verified0 citation errors · 0 not checkable

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Functional Characterization of the S. cerevisiae Genome by Gene Deletion and Parallel Analysis
Winzeler, E. A., Shoemaker, D. D., Astromoff, A., Liang, H., Anderson, K., Andre, B., Bangham, R., Benito, R., Boeke, J. D., Bussey, H., et al. (1999) · Science · doi:10.1126/science.285.5429.901 · Cited by 3,953
The Genetic Landscape of a Cell
Costanzo, M., Baryshnikova, A., Bellay, J., Kim, Y., Spear, E. D., Sevier, C. S., Ding, H., Koh, J. L. Y., Toufighi, K., Mostafavi, S., et al. (2010) · Science · doi:10.1126/science.1180823 · Cited by 2,162
Crystal Structure of an Hsp90–Geldanamycin Complex: Targeting of a Protein Chaperone by an Antitumor Agent
Stebbins, C. E., Russo, A. A., Schneider, C. B., Rosen, N. X., Hartl, F. U., & Pavletich, N. P. (1997) · Cell · doi:10.1016/s0092-8674(00)80203-2 · Cited by 1,370
The Chemical Genomic Portrait of Yeast: Uncovering a Phenotype for All Genes
Hillenmeyer, M. E., Fung, E., Wildenhain, J., Pierce, S. E., Hoon, S. S., Lee, W., Proctor, M. J., St.Onge, R. P., Tyers, M., Koller, D., et al. (2008) · Science · doi:10.1126/science.1150021 · Cited by 978
Exploration of the Function and Organization of the Yeast Early Secretory Pathway through an Epistatic Miniarray Profile
Schuldiner, M., Collins, S. R., Thompson, N. J., Denic, V., Bhamidipati, A., Punna, T., Ihmels, J., Andrews, B., Boone, C., Greenblatt, J. F., et al. (2005) · Cell · doi:10.1016/j.cell.2005.08.031 · Cited by 870
Inhibition of actin polymerization by latrunculin A
Coué, M., Brenner, S. L., Spector, I., & Korn, E. D. (1987) · FEBS Letters · doi:10.1016/0014-5793(87)81513-2 · Cited by 824
Integration of chemical-genetic and genetic interaction data links bioactive compounds to cellular target pathways
Parsons, A. B., Brost, R. L., Ding, H., Li, Z., Zhang, C., Sheikh, B., Brown, G. W., Kane, P. M., Hughes, T. R., & Boone, C. M. (2003) · Nature Biotechnology · doi:10.1038/nbt919 · Cited by 651
hsp82 is an essential protein that is required in higher concentrations for growth of cells at higher temperatures.
Borkovich, K. A., Farrelly, F. W., Finkelstein, D. B., Taulien, J., & Lindquist, S. (1989) · Molecular and Cellular Biology · doi:10.1128/mcb.9.9.3919 · Cited by 641
An Antifungal Agent Inhibits an Aminoacyl-tRNA Synthetase by Trapping tRNA in the Editing Site
Rock, F. L., Mao, W., Yaremchuk, A. D., Tukalo, M. A., Crépin, T., Zhou, H., Zhang, Y.-K., Hernandez, V. S., Akama, T., Baker, S. J., et al. (2007) · Science · doi:10.1126/science.1142189 · Cited by 639
Structural comparison of anticancer drug-DNA complexes: adriamycin and daunomycin
Frederick, C. A., Williams, L. D., Ughetto, G., MAREL, G. A. V. D., BOOM, J. H. V., Rich, A., & Wang, A. H. ‐. (1990) · Biochemistry · doi:10.1021/bi00462a016 · Cited by 578

Show all 50 references

Sorted by citations

Items 101–172 of 172

Bridging the Gap to Non-toxic Fungal Control: Lupinus-Derived Blad-Containing Oligomer as a Novel Candidate to Combat Human Pathogenic Fungi
Pinheiro, A. M., Carreira, A., Prescott, T. A. K., Ferreira, R. B., & Monteiro, S. (2017) · Frontiers in Microbiology · doi:10.3389/fmicb.2017.01182 · Cited by 8
The putative transient receptor potential channel protein encoded by the orf19.4805 gene is involved in cation sensitivity, antifungal tolerance, and filamentation in Candida albicans
Jiang, L., & Yang, Y. (2018) · Canadian Journal of Microbiology · doi:10.1139/cjm-2018-0048 · Cited by 7
Hijacking Transposable Elements for Saturation Mutagenesis in Fungi
Schrevens, S., & Sanglard, D. (2021) · Frontiers in Fungal Biology · doi:10.3389/ffunb.2021.633876 · Cited by 7
Systematic Mapping of Chemical–Genetic Interactions in Saccharomyces cerevisiaePreprint
Suresh, S., Schlecht, U., Xu, W., Bray, W. M., Miranda, M., Davis, R. W., Nislow, C., Giaever, G. N., Lokey, R. S., & St.Onge, R. P. (2016) · Cold Spring Harbor Protocols · doi:10.1101/pdb.top077701 · Cited by 7
Predicting bioprocess targets of chemical compounds through integration of chemical-genetic and genetic interaction networksPreprint
Simpkins, S. W., Nelson, J., Deshpande, R., Li, S. C., Piotrowski, J. S., Wilson, E. H., Gebre, A. A., Okamoto, R., Yoshimura, M., Costanzo, M., et al. (2017) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/111252 · Cited by 7
The Path towards Predicting Evolution as Illustrated in Yeast Cell Polarity
Daalman, W. K.-G., Sweep, E., & Laan, L. (2020) · Cells · doi:10.3390/cells9122534 · Cited by 6
Cytotoxicity of Extracts from Petiveria alliacea Leaves on Yeast
Cal, B. B. F., Araújo, L. B. D. N., Nunes, B. M., da Silva, C. R., Oliveira, M. B. N., Soares, B. O., Leitão, Á. A. C., de Padula, M., Nascimento, D., Chaves, D. S. D. A., et al. (2022) · Plants · doi:10.3390/plants11233263 · Cited by 6
Utilizing yeast chemogenomic profiles for the prediction of pharmacogenomic associations in humans
Silberberg, Y., Kupiec, M., & Sharan, R. (2016) · Scientific Reports · doi:10.1038/srep23703 · Cited by 6
Identification of Yeast Mutants Exhibiting Altered Sensitivity to Valinomycin and Nigericin Demonstrate Pleiotropic Effects of Ionophores on Cellular Processes
Jakúbková, M., Džugasová, V., Fričová, D., Abelovska, L., Bhatia‐Kiššová, I., Valachovič, M., Klobučnı́ková, V., Zeiselová, L., Griač, P., Nosek, J., et al. (2016) · PLoS ONE · doi:10.1371/journal.pone.0164175 · Cited by 8
Use of Chemical Genomics to Investigate the Mechanism of Action for Inhibitory Bioactive Natural Compounds
Burnside, D. J., Moteshareie, H., Márquez, I. G., Hooshyar, M., Samanfar, B., Shostak, K., Omidi, K., Peery, H. E., Smith, M. L., & Golshani, A. (2014) · Wiley eBooks · doi:10.1002/9783527684403.ch2 · Cited by 6
Hoi1 targets BLTP2 to ER–PM contact sites to regulate lipid homeostasis
Dziurdzik, S. K., Sridhar, V., Eng, H. L., Neuman, S. D., Yan, J., Davey, M., Taubert, S., Bashirullah, A., & Conibear, E. (2026) · The Journal of Cell Biology · doi:10.1083/jcb.202502131 · Cited by 5
Synthetic refactor of essential genes decodes functionally constrained sequences in yeast genome
Liang, Z., Luo, Z., Zhang, W., Kang, Y., Wang, H., Geng, B., Yang, Q., Ni, Z., Zeng, C., Zheng, Y., et al. (2022) · iScience · doi:10.1016/j.isci.2022.104982 · Cited by 5
Using Functional Genetics in Haploid Cells for Drug Target Identification
Volz, J. C., Schuller, N., & Elling, U. (2019) · Methods in Molecular Biology · doi:10.1007/978-1-4939-9145-7_1 · Cited by 4
Small molecule inhibitors of fungal Δ(9) fatty acid desaturase as antifungal agents against Candida auris
Tebbji, F., Menon, A. C. T., Khemiri, I., St‐Cyr, D. J., Villeneuve, L. R., Vincent, A. T., & Sellam, A. (2024) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2024.1434939 · Cited by 4
A Chemogenomic Screening Platform Used to Identify Chemotypes Perturbing HSP90 Pathways
Thomas, F. M., Goode, K. M., Rajwa, B. P., Bieberich, A. A., Avramova, L. V., Hazbun, T. R., & Davisson, V. J. (2017) · SLAS DISCOVERY · doi:10.1177/2472555216687525 · Cited by 4
Drug toxicity profiling of a Saccharomyces cerevisiae deubiquitinase deletion panel shows that acetaminophen mimics tyrosine
Huseinovic, A., van Dijk, M., Vermeulen, N. P. E., van Leeuwen, F., Kooter, J. M., & Vos, J. C. (2017) · Toxicology in Vitro · doi:10.1016/j.tiv.2017.12.007 · Cited by 4
A Yeast Chronological Lifespan Assay to Assess Activity of Proteasome Stimulators
Maresh, M. E., Chen, P., Hazbun, T. R., & Trader, D. J. (2021) · ChemBioChem · doi:10.1002/cbic.202100117 · Cited by 4
LI Detector: a framework for sensitive colony-based screens regardless of the distribution of fitness effects
Parikh, S. B., Coelho, N. C., & Carvunis, A. (2021) · G3 Genes Genomes Genetics · doi:10.1093/g3journal/jkaa068 · Cited by 5
Identification of Chemical–Genetic Interactions via Parallel Analysis of Barcoded Yeast StrainsPreprint
Suresh, S., Schlecht, U., Xu, W., Miranda, M., Davis, R. W., Nislow, C., Giaever, G. N., & St.Onge, R. P. (2016) · Cold Spring Harbor Protocols · doi:10.1101/pdb.prot088054 · Cited by 4
Jlp2 is a non-canonical release factor that protects cells during ribosome stallingPreprint
Iyer, K. V., Kraft, A.-A., Walter, C. A., Müller, M., Tittel, L. S., Stampa, G. F., & Winz, M. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.09.04.673968 · Cited by 4
Barcode sequencing: a robust, platform-agnostic method for massively parallel cell-based screens
Barazandeh, M., Gaikani, H. K., Pattanshetti, R., Ogbede, J. U., Sinha, S., Moore, R. A., Carr, C. E., Giaever, G. N., & Nislow, C. (2025) · G3 Genes Genomes Genetics · doi:10.1093/g3journal/jkaf166 · Cited by 3
Yeast-based high-throughput screens for discovery of kinase inhibitors for neglected diseases
Tavella, T. A., Cassiano, G. C., Costa, F. T. M., Sunnerhagen, P., & Bilsland, E. (2020) · Advances in protein chemistry and structural biology · doi:10.1016/bs.apcsb.2020.09.007 · Cited by 3
Involvement of lipid-translocating exporter family proteins in determination of myriocin sensitivity in budding yeast
Kawaguchi, T., Ishibashi, Y., Matsuzaki, M., Yamagata, S., & Tani, M. (2024) · Biochemistry and Biophysics Reports · doi:10.1016/j.bbrep.2024.101785 · Cited by 3
Panspecies Small-Molecule Disruptors of Heterochromatin-Mediated Transcriptional Gene Silencing
Castonguay, E., White, S. A., Kagansky, A., St‐Cyr, D. J., Castillo, A. G., Brugger, C., White, R., Bonilla, C., Spitzer, M., Earnshaw, W. C., et al. (2014) · Molecular and Cellular Biology · doi:10.1128/mcb.01102-14 · Cited by 3
Integrating yeast chemical genomics and mammalian cell pathway analysis
Zhou, F.-L., Li, S. C., Zhu, Y., Guo, W.-J., Shao, L.-J., Nelson, J., Simpkins, S. W., Yang, D., Liu, Q., Yashiroda, Y., et al. (2019) · Acta Pharmacologica Sinica · doi:10.1038/s41401-019-0231-y · Cited by 3
From Yeast to Humans: Leveraging New Approaches in Yeast to Accelerate Discovery of Therapeutic Targets for Synucleinopathies
Piotrowski, J. S., & Tardiff, D. F. (2019) · Methods in molecular biology · doi:10.1007/978-1-4939-9736-7_24 · Cited by 3
Contemporary Techniques for Target Deconvolution and Mode of Action Elucidation
Schirle, M., & Jenkins, J. L. (2020) · Royal Society of Chemistry eBooks · doi:10.1039/9781839160721-00083 · Cited by 3
Fast-evolving cofactors regulate the role of HEATR5 complexes in intra-Golgi trafficking
Marmorale, L. J., Jin, H., Reidy, T. G., Palomino-Alonso, B., Zysnarski, C. J., Jordan-Javed, F., Lahiri, S., & Duncan, M. C. (2023) · The Journal of Cell Biology · doi:10.1083/jcb.202309047 · Cited by 2
Inhibiting Mrt4-rRNA interaction with fumaramidmycin-based derivatives as an antifungal strategy
Cao, H., Tu, J., Chen, J., Chen, B., Huang, Z., Wang, Y., Shen, J., Hu, X., Bo, J., Rao, L., et al. (2026) · Nature Communications · doi:10.1038/s41467-026-70226-4 · Cited by 3
A simplified and easy‐to‐use HIP HOP assay provides insights into chalcone antifungal mechanisms of action
Prescott, T. A. K., Anaissi‐Afonso, L., Fox, K. R., Maxwell, A., Panaretou, B., & Machín, F. (2022) · FEBS Letters · doi:10.1002/1873-3468.14483 · Cited by 2
Interrelationship between the Non-Vesicular Transport of Sterols and Their Distribution between the Rafts and the Non-Raft Phase of the Plasma Membrane
Соколов, С. С., Zyrina, A. N., Akimov, S. A., & Severin, F. F. (2025) · Biochemistry (Moscow) · doi:10.1134/s0006297924604313 · Cited by 2
CRISPR/Cas9-Based Chemogenomic Profiling in Mammalian Cells
Hoepfner, D., McAllister, G., & Hoffman, G. R. (2018) · Methods in molecular biology · doi:10.1007/978-1-4939-8891-4_9 · Cited by 2
Self-citation
Elucidating the anti-cancer mechanisms for transition-state structure inhibitors of nucleoside phosphorylases methylthioadenosine-DADMe-immucillin A and forodesine
Coorey, N. (2017) · doi:10.26686/wgtn.17067545.v1 · Cited by 2
The kinesin Kar3 is required for endoplasmic reticulum–associated degradation
Akoto, E., Doss, E. M., Claypool, K. P., Owutey, S. L., Richards, K. A., Lehman, K. M., Daraghmi, M. M., Turk, S. M., Indovina, C. J., Avaala, J. A., et al. (2025) · Molecular Biology of the Cell · doi:10.1091/mbc.e24-10-0437 · Cited by 1
New hit compounds against Trypanosoma cruzi derived from mining yeast chemogenomic profiling data
Garnham, M. D., Landaburu, L. U., Salas‐Sarduy, E., & Agüero, F. (2026) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.00117-26 · Cited by 1
Chemogenomic Profiling: Past, Present and Beyond
Pries, V., & Hoepfner, D. (2016) · Cellular & Molecular Medicine Open access · doi:10.21767/2573-5365.100017 · Cited by 1
Self-citation
A Chemogenomic Toolkit to Evaluate the “Ins and Outs” of Yeast Plasma Membrane Transporters
Prasad, R., & Banerjee, A. (2022) · mBio · doi:10.1128/mbio.00955-22 · Cited by 1
SATAY-based chemogenomic screening uncovers antifungal resistance mechanisms and key determinants of ATI-2307 and chitosan sensitivityPreprint
Karadzas, M. T., Michel, A. H., Mosbach, A., Giannakopoulos, G., McGettigan, R., Scalliet, G., & Kornmann, B. (2025) · eLife · doi:10.7554/elife.105333.1 · Cited by 1
A Chemical-Genetic Interaction Matrix Reveals Drug Mechanism and Genetic ArchitecturePreprint
Coulombe‐Huntington, J., Bertomeu, T., Huard, C., Chatr‐aryamontri, A., St‐Cyr, D. J., Sánchez‐Osuna, M., Papadopoli, D. J., Normandin, K., Paydar, M., McLaughlan, S., et al. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.01.28.701823 · Cited by 1
Role of Occludin in the Regulation of Epithelial Tight Junctions
Manda, B. (2016) · doi:10.21007/etd.cghs.2016.0415
Mitochondria Remodeling in Cancer
Dornfeld, K. J., & Skildum, A. J. (2018) · Springer eBooks · doi:10.1007/978-3-319-73344-9_9
Unbiased Forward Genetic Screening with Chemical Mutagenesis to Uncover Drug–Target Interactions
Horn, M., Metge, F., & Denzel, M. S. (2019) · Methods in molecular biology · doi:10.1007/978-1-4939-9145-7_2
The persistence of haploinsufficiency and its role in genome evolution
Morrill, S. A. (2020) · DSpace@MIT (Massachusetts Institute of Technology)
Functional Applications of Systems Biology Tools: Identification of Novel DNA Repair Factors and Peptide Design
Burnside, D. J. (2019) · Carleton University's Institutional Repository (MacOdrum Library, Carleton University) · doi:10.22215/etd/2019-13862
Environmental Signaling through the Target of Rapamycin Complex 1 (TORC1) and the Regulation of Epigenetic Mechanisms
Workman, J. (2016) · doi:10.21007/etd.cghs.2016.0577
Large Scale Investigation in Yeast, to Identify Novel Gene(s) Involved in Translation Pathway
Samanfar, B. (2015) · doi:10.22215/etd/2015-10737
Investigating the Quantitative Trait Loci Contributing to Individual Variation in Drug Response
Roberts, C. A. (2015) · doi:10.26686/wgtn.17014628
Mithramycin-A Induced Toxicity in HepG2 Cells is mediated by Disruption of Calcium Homeostasis
(2019) · doi:10.31038/jppr.2019211
Avaliação "in vitro" e "in vivo" do potencial antimalárico da Epirrubicina
Ferreira, L. T. (2019) · doi:10.47749/t/unicamp.2019.1162431
Saccharomyces cerevisiae, a platform for drug discovery
Almeida, L. D. (2022) · doi:10.47749/t/unicamp.2022.1265921
SATAY-Based Chemogenomic Screening uncovers Antifungal Resistance Mechanisms and Key Determinants of ATI-2307 and Chitosan SensitivityPreprint
Karadzas, M. T., Michel, A. H., Mosbach, A., Giannakopoulos, G., McGettigan, R., Scalliet, G., & Kornmann, B. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.09.20.614104
SATAY-based chemogenomic screening uncovers antifungal resistance mechanisms and key determinants of ATI-2307 and chitosan sensitivityPreprint
Karadzas, M. T., Michel, A. H., Mosbach, A., Giannakopoulos, G., McGettigan, R., Scalliet, G., & Kornmann, B. (2025) · eLife · doi:10.7554/elife.105333
Leveraging synthetic genetic array screening to identify therapeutic targets and inhibitors for combatting azole resistance in Candida glabrata
Williams, C. C., & Usher, J. (2025) · Microbiology Spectrum · doi:10.1128/spectrum.02522-24
Additional file 12 of Natural variation in yeast reveals multiple paths for acquiring higher stress resistance
Scholes, A. N., Stuecker, T. N., Hood, S. E., Locke, C. J., Stacy, C. L., Zhang, Q., & Lewis, J. A. (2024) · Figshare · doi:10.6084/m9.figshare.26743436
Additional file 5 of Natural variation in yeast reveals multiple paths for acquiring higher stress resistance
Scholes, A. N., Stuecker, T. N., Hood, S. E., Locke, C. J., Stacy, C. L., Zhang, Q., & Lewis, J. A. (2024) · Figshare · doi:10.6084/m9.figshare.26743415
Additional file 2 of Natural variation in yeast reveals multiple paths for acquiring higher stress resistance
Scholes, A. N., Stuecker, T. N., Hood, S. E., Locke, C. J., Stacy, C. L., Zhang, Q., & Lewis, J. A. (2024) · Figshare · doi:10.6084/m9.figshare.26182341
Additional file 3 of The cellular response to drug perturbation is limited: comparison of large-scale chemogenomic fitness signatures
Barazandeh, M., Kriti, D., Nislow, C., & Giaever, G. N. (2022) · Figshare · doi:10.6084/m9.figshare.19350018
Additional file 10 of Natural variation in yeast reveals multiple paths for acquiring higher stress resistance
Scholes, A. N., Stuecker, T. N., Hood, S. E., Locke, C. J., Stacy, C. L., Zhang, Q., & Lewis, J. A. (2024) · Figshare · doi:10.6084/m9.figshare.26743430
Additional file 1 of Natural variation in yeast reveals multiple paths for acquiring higher stress resistance
Scholes, A. N., Stuecker, T. N., Hood, S. E., Locke, C. J., Stacy, C. L., Zhang, Q., & Lewis, J. A. (2024) · Figshare · doi:10.6084/m9.figshare.26182226
Additional file 1 of The cellular response to drug perturbation is limited: comparison of large-scale chemogenomic fitness signatures
Barazandeh, M., Kriti, D., Nislow, C., & Giaever, G. N. (2022) · Figshare · doi:10.6084/m9.figshare.19350012
Additional file 7 of Natural variation in yeast reveals multiple paths for acquiring higher stress resistance
Scholes, A. N., Stuecker, T. N., Hood, S. E., Locke, C. J., Stacy, C. L., Zhang, Q., & Lewis, J. A. (2024) · Figshare · doi:10.6084/m9.figshare.26743421
Additional file 2 of The cellular response to drug perturbation is limited: comparison of large-scale chemogenomic fitness signatures
Barazandeh, M., Kriti, D., Nislow, C., & Giaever, G. N. (2022) · Figshare · doi:10.6084/m9.figshare.19350015
Additional file 8 of Natural variation in yeast reveals multiple paths for acquiring higher stress resistance
Scholes, A. N., Stuecker, T. N., Hood, S. E., Locke, C. J., Stacy, C. L., Zhang, Q., & Lewis, J. A. (2024) · Figshare · doi:10.6084/m9.figshare.26743424
Additional file 4 of Natural variation in yeast reveals multiple paths for acquiring higher stress resistance
Scholes, A. N., Stuecker, T. N., Hood, S. E., Locke, C. J., Stacy, C. L., Zhang, Q., & Lewis, J. A. (2024) · Figshare · doi:10.6084/m9.figshare.26743412
Additional file 6 of Natural variation in yeast reveals multiple paths for acquiring higher stress resistance
Scholes, A. N., Stuecker, T. N., Hood, S. E., Locke, C. J., Stacy, C. L., Zhang, Q., & Lewis, J. A. (2024) · Figshare · doi:10.6084/m9.figshare.26743418
Additional file 9 of Natural variation in yeast reveals multiple paths for acquiring higher stress resistance
Scholes, A. N., Stuecker, T. N., Hood, S. E., Locke, C. J., Stacy, C. L., Zhang, Q., & Lewis, J. A. (2024) · Figshare · doi:10.6084/m9.figshare.26743427
Additional file 3 of Natural variation in yeast reveals multiple paths for acquiring higher stress resistance
Scholes, A. N., Stuecker, T. N., Hood, S. E., Locke, C. J., Stacy, C. L., Zhang, Q., & Lewis, J. A. (2024) · Figshare · doi:10.6084/m9.figshare.26743409
Additional file 4 of The cellular response to drug perturbation is limited: comparison of large-scale chemogenomic fitness signatures
Barazandeh, M., Kriti, D., Nislow, C., & Giaever, G. N. (2022) · Figshare · doi:10.6084/m9.figshare.19350021
Additional file 11 of Natural variation in yeast reveals multiple paths for acquiring higher stress resistance
Scholes, A. N., Stuecker, T. N., Hood, S. E., Locke, C. J., Stacy, C. L., Zhang, Q., & Lewis, J. A. (2024) · Figshare · doi:10.6084/m9.figshare.26743433
Etude de facteurs impliqués dans le contrôle-qualité de l'expression des gènes, chez Saccharomyces cerevisiae
Zhang, E. (2017) · doi:10.70675/aaeb9850z28c0z4d8cz9822z75767636cb47
Building bridges: BLTP2 forms ER–plasma membrane contact sites
Fröhlich, F. (2026) · The Journal of Cell Biology · doi:10.1083/jcb.202603182
BindingDB Entry 18: Direct Interaction of Chivosazole F with Actin Elicits Cell Responses Similar to Latrunculin A but Distinct from Chondramide.
BindingDB (2018) · UC San Diego · doi:10.7270/q25b00mp

Authors: Hoepfner, D., Helliwell, S. B., Sadlish, H., Schuierer, S., Filipuzzi, I., Brachat, S., Bhullar, B., Plikat, U., Abraham, Y., Altorfer, M., Aust, T., Baeriswyl, L., Cerino, R., Chang, L., Estoppey, D., Eichenberger, J., Frederiksen, M., Hartmann, N., Hohendahl, A., Knapp, B., Krastel, P., Melin, N., Nigsch, F., Oakeley, E. J., Petitjean, V., Petersen, F., Riedl, R., Schmitt, E. K., Staedtler, F., Studer, C., Tallarico, J. A., Wetzel, S., Fishman, M. C., Porter, J. A., & Movva, N. R.
Affiliations: Novartis (Switzerland) (CH)
Corresponding author: Hoepfner, Dominic
ORCID: Hoepfner, Dominic
Helliwell, Stephen B.
Schuierer, Sven
Filipuzzi, Ireos
Brachat, Sophie
Abraham, Yann
Altorfer, Marc
Estoppey, David
Frederiksen, Mathias
Hohendahl, Annika
Krastel, Philipp
Nigsch, Florian
Oakeley, Edward J.
Schmitt, Esther K.
Studer, Christian
Tallarico, John A.
Fishman, Mark C.
Venue: Microbiological Research
Publisher: Elsevier BV
Published: 2014-02
Volume: 169
Issue: 2-3
Pages: 107-120
ISSN: 0944-5013 (ISSN-L)
DOI: 10.1016/j.micres.2013.11.004
OpenAlex: W2013242034
Cited by: 166
References: 50
Citations by year: 2026: 5 · 2025: 11 · 2024: 12 · 2023: 6 · 2022: 13 · 2021: 6 · 2020: 11 · 2019: 23 · 2018: 20 · 2017: 23 · 2016: 12 · 2015: 18 · 2014: 5
FWCI: 5.38
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/open-access/userlicense/1.0/ (vor, 589 d)
Locations: Microbiological Research (publishedVersion)
PubMed (publishedVersion)
Funders: Novartis Institutes for BioMedical Research
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Fungal and yeast genetics research
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Bioinformatics and Genomic Networks
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Microbial Metabolic Engineering and Bioproduction
Keywords: chemogenomics, fatty acid synthase inhibition, microtubule inhibitors, mitochondrial respiration, background mutations, Saccharomyces cerevisiae
MeSH terms: Antifungal Agents, Molecular Sequence Data, Phylogeny, Saccharomyces cerevisiae, Gene Expression Regulation, Fungal, Drug Resistance, Fungal, Saccharomyces cerevisiae Proteins, Biosynthetic Pathways, High-Throughput Screening Assays

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

High-resolution chemical dissection of a model eukaryote reveals targets, pathways and gene functions

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Self-check

Citations

Cites

Cited by

Related

Metadata

Record

About these checks