A Systems Biology Approach Reveals the Role of a Novel Methyltransferase in Response to Chemical Stress and Lipid Homeostasis
Using small molecule probes to understand gene function is an attractive approach that allows functional characterization of genes that are dispensable in standard laboratory conditions and provides insight into the mode of action of these compounds. Using chemogenomic assays we previously identifie...
Saved in:
| Published in | PLoS genetics Vol. 7; no. 10; p. e1002332 |
|---|---|
| Main Authors | , , , , , , , , , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
United States
Public Library of Science
01.10.2011
Public Library of Science (PLoS) |
| Subjects | |
| Online Access | Get full text |
| ISSN | 1553-7404 1553-7390 1553-7404 |
| DOI | 10.1371/journal.pgen.1002332 |
Cover
Loading…
| Abstract | Using small molecule probes to understand gene function is an attractive approach that allows functional characterization of genes that are dispensable in standard laboratory conditions and provides insight into the mode of action of these compounds. Using chemogenomic assays we previously identified yeast Crg1, an uncharacterized SAM-dependent methyltransferase, as a novel interactor of the protein phosphatase inhibitor cantharidin. In this study we used a combinatorial approach that exploits contemporary high-throughput techniques available in Saccharomyces cerevisiae combined with rigorous biological follow-up to characterize the interaction of Crg1 with cantharidin. Biochemical analysis of this enzyme followed by a systematic analysis of the interactome and lipidome of CRG1 mutants revealed that Crg1, a stress-responsive SAM-dependent methyltransferase, methylates cantharidin in vitro. Chemogenomic assays uncovered that lipid-related processes are essential for cantharidin resistance in cells sensitized by deletion of the CRG1 gene. Lipidome-wide analysis of mutants further showed that cantharidin induces alterations in glycerophospholipid and sphingolipid abundance in a Crg1-dependent manner. We propose that Crg1 is a small molecule methyltransferase important for maintaining lipid homeostasis in response to drug perturbation. This approach demonstrates the value of combining chemical genomics with other systems-based methods for characterizing proteins and elucidating previously unknown mechanisms of action of small molecule inhibitors. |
|---|---|
| AbstractList | Using small molecule probes to understand gene function is an attractive approach that allows functional characterization of genes that are dispensable in standard laboratory conditions and provides insight into the mode of action of these compounds. Using chemogenomic assays we previously identified yeast Crg1, an uncharacterized SAM-dependent methyltransferase, as a novel interactor of the protein phosphatase inhibitor cantharidin. In this study we used a combinatorial approach that exploits contemporary high-throughput techniques available in Saccharomyces cerevisiae combined with rigorous biological follow-up to characterize the interaction of Crg1 with cantharidin. Biochemical analysis of this enzyme followed by a systematic analysis of the interactome and lipidome of CRG1 mutants revealed that Crg1, a stress-responsive SAM-dependent methyltransferase, methylates cantharidin in vitro. Chemogenomic assays uncovered that lipidrelated processes are essential for cantharidin resistance in cells sensitized by deletion of the CRG1 gene. Lipidome-wide analysis of mutants further showed that cantharidin induces alterations in glycerophospholipid and sphingolipid abundance in a Crg1-dependent manner. We propose that Crg1 is a small molecule methyltransferase important for maintaining lipid homeostasis in response to drug perturbation. This approach demonstrates the value of combining chemical genomics with other systems-based methods for characterizing proteins and elucidating previously unknown mechanisms of action of small molecule inhibitors. Using small molecule probes to understand gene function is an attractive approach that allows functional characterization of genes that are dispensable in standard laboratory conditions and provides insight into the mode of action of these compounds. Using chemogenomic assays we previously identified yeast Crg1, an uncharacterized SAM-dependent methyltransferase, as a novel interactor of the protein phosphatase inhibitor cantharidin. In this study we used a combinatorial approach that exploits contemporary high-throughput techniques available in Saccharomyces cerevisiae combined with rigorous biological follow-up to characterize the interaction of Crg1 with cantharidin. Biochemical analysis of this enzyme followed by a systematic analysis of the interactome and lipidome of CRG1 mutants revealed that Crg1, a stress-responsive SAM-dependent methyltransferase, methylates cantharidin in vitro. Chemogenomic assays uncovered that lipid-related processes are essential for cantharidin resistance in cells sensitized by deletion of the CRG1 gene. Lipidome-wide analysis of mutants further showed that cantharidin induces alterations in glycerophospholipid and sphingolipid abundance in a Crg1-dependent manner. We propose that Crg1 is a small molecule methyltransferase important for maintaining lipid homeostasis in response to drug perturbation. This approach demonstrates the value of combining chemical genomics with other systems-based methods for characterizing proteins and elucidating previously unknown mechanisms of action of small molecule inhibitors. Using small molecule probes to understand gene function is an attractive approach that allows functional characterization of genes that are dispensable in standard laboratory conditions and provides insight into the mode of action of these compounds. Using chemogenomic assays we previously identified yeast Crg1, an uncharacterized SAM-dependent methyltransferase, as a novel interactor of the protein phosphatase inhibitor cantharidin. In this study we used a combinatorial approach that exploits contemporary high-throughput techniques available in Saccharomyces cerevisiae combined with rigorous biological follow-up to characterize the interaction of Crg1 with cantharidin. Biochemical analysis of this enzyme followed by a systematic analysis of the interactome and lipidome of CRG1 mutants revealed that Crg1, a stress-responsive SAM-dependent methyltransferase, methylates cantharidin in vitro . Chemogenomic assays uncovered that lipid-related processes are essential for cantharidin resistance in cells sensitized by deletion of the CRG1 gene. Lipidome-wide analysis of mutants further showed that cantharidin induces alterations in glycerophospholipid and sphingolipid abundance in a Crg1-dependent manner. We propose that Crg1 is a small molecule methyltransferase important for maintaining lipid homeostasis in response to drug perturbation. This approach demonstrates the value of combining chemical genomics with other systems-based methods for characterizing proteins and elucidating previously unknown mechanisms of action of small molecule inhibitors. Chemical genetics uses small molecules to perturb biological systems to study gene function. By analogy with genetic lesions, chemical probes act as fast-acting, reversible, and “tunable” conditional alleles. Furthermore, small molecules can target multiple protein targets and target pathways simultaneously to uncover phenotypes that may be masked by genes encoding partially redundant proteins. Finally, potent chemical probes can be useful starting points for the development of human therapeutics. Here, we used cantharidin, a natural toxin, to uncover otherwise “hidden” phenotypes for a methyltransferase that has resisted characterization. This enzyme, Crg1, has no phenotype in standard conditions but is indispensible for survival in the presence of cantharidin. Using this chemical genetic relationship, we characterized novel functions of Crg1, and by combining diverse genomic assays with small molecule perturbation we characterized the mechanism of cantharidin cytotoxicity. These observations are relevant beyond yeast Crg1 because cantharidin and its analogues have potent anticancer activity, yet its therapeutic use has been limited to topical applications because of its cytotoxicity. Considering that methyltransferases are an extremely abundant and diverse class of cellular proteins, chemical probes such as cantharidin are critical for understanding their cellular roles and defining potential points of therapeutic intervention. Using small molecule probes to understand gene function is an attractive approach that allows functional characterization of genes that are dispensable in standard laboratory conditions and provides insight into the mode of action of these compounds. Using chemogenomic assays we previously identified yeast Crg1, an uncharacterized SAM-dependent methyltransferase, as a novel interactor of the protein phosphatase inhibitor cantharidin. In this study we used a combinatorial approach that exploits contemporary high-throughput techniques available in Saccharomyces cerevisiae combined with rigorous biological follow-up to characterize the interaction of Crg1 with cantharidin. Biochemical analysis of this enzyme followed by a systematic analysis of the interactome and lipidome of CRG1 mutants revealed that Crg1, a stress-responsive SAM-dependent methyltransferase, methylates cantharidin in vitro. Chemogenomic assays uncovered that lipid-related processes are essential for cantharidin resistance in cells sensitized by deletion of the CRG1 gene. Lipidome-wide analysis of mutants further showed that cantharidin induces alterations in glycerophospholipid and sphingolipid abundance in a Crg1-dependent manner. We propose that Crg1 is a small molecule methyltransferase important for maintaining lipid homeostasis in response to drug perturbation. This approach demonstrates the value of combining chemical genomics with other systems-based methods for characterizing proteins and elucidating previously unknown mechanisms of action of small molecule inhibitors. Using small molecule probes to understand gene function is an attractive approach that allows functional characterization of genes that are dispensable in standard laboratory conditions and provides insight into the mode of action of these compounds. Using chemogenomic assays we previously identified yeast Crg1, an uncharacterized SAM-dependent methyltransferase, as a novel interactor of the protein phosphatase inhibitor cantharidin. In this study we used a combinatorial approach that exploits contemporary high-throughput techniques available in Saccharomyces cerevisiae combined with rigorous biological follow-up to characterize the interaction of Crg1 with cantharidin. Biochemical analysis of this enzyme followed by a systematic analysis of the interactome and lipidome of CRG1 mutants revealed that Crg1, a stress-responsive SAM-dependent methyltransferase, methylates cantharidin in vitro. Chemogenomic assays uncovered that lipid-related processes are essential for cantharidin resistance in cells sensitized by deletion of the CRG1 gene. Lipidome-wide analysis of mutants further showed that cantharidin induces alterations in glycerophospholipid and sphingolipid abundance in a Crg1-dependent manner. We propose that Crg1 is a small molecule methyltransferase important for maintaining lipid homeostasis in response to drug perturbation. This approach demonstrates the value of combining chemical genomics with other systems-based methods for characterizing proteins and elucidating previously unknown mechanisms of action of small molecule inhibitors.Using small molecule probes to understand gene function is an attractive approach that allows functional characterization of genes that are dispensable in standard laboratory conditions and provides insight into the mode of action of these compounds. Using chemogenomic assays we previously identified yeast Crg1, an uncharacterized SAM-dependent methyltransferase, as a novel interactor of the protein phosphatase inhibitor cantharidin. In this study we used a combinatorial approach that exploits contemporary high-throughput techniques available in Saccharomyces cerevisiae combined with rigorous biological follow-up to characterize the interaction of Crg1 with cantharidin. Biochemical analysis of this enzyme followed by a systematic analysis of the interactome and lipidome of CRG1 mutants revealed that Crg1, a stress-responsive SAM-dependent methyltransferase, methylates cantharidin in vitro. Chemogenomic assays uncovered that lipid-related processes are essential for cantharidin resistance in cells sensitized by deletion of the CRG1 gene. Lipidome-wide analysis of mutants further showed that cantharidin induces alterations in glycerophospholipid and sphingolipid abundance in a Crg1-dependent manner. We propose that Crg1 is a small molecule methyltransferase important for maintaining lipid homeostasis in response to drug perturbation. This approach demonstrates the value of combining chemical genomics with other systems-based methods for characterizing proteins and elucidating previously unknown mechanisms of action of small molecule inhibitors. Using small molecule probes to understand gene function is an attractive approach that allows functional characterization of genes that are dispensable in standard laboratory conditions and provides insight into the mode of action of these compounds. Using chemogenomic assays we previously identified yeast Crg1, an uncharacterized SAM-dependent methyltransferase, as a novel interactor of the protein phosphatase inhibitor cantharidin. In this study we used a combinatorial approach that exploits contemporary high-throughput techniques available in Saccharomyces cerevisiae combined with rigorous biological follow-up to characterize the interaction of Crg1 with cantharidin. Biochemical analysis of this enzyme followed by a systematic analysis of the interactome and lipidome of CRG1 mutants revealed that Crg1, a stress-responsive SAM-dependent methyltransferase, methylates cantharidin in vitro. Chemogenomic assays uncovered that lipid-related processes are essential for cantharidin resistance in cells sensitized by deletion of the CRG1 gene. Lipidome-wide analysis of mutants further showed that cantharidin induces alterations in glycerophospholipid and sphingolipid abundance in a Crg1-dependent manner. We propose that Crg1 is a small molecule methyltransferase important for maintaining lipid homeostasis in response to drug perturbation. This approach demonstrates the value of combining chemical genomics with other systems-based methods for characterizing proteins and elucidating previously unknown mechanisms of action of small molecule inhibitors. Chemical genetics uses small molecules to perturb biological systems to study gene function. By analogy with genetic lesions, chemical probes act as fast-acting, reversible, and "tunable" conditional alleles. Furthermore, small molecules can target multiple protein targets and target pathways simultaneously to uncover phenotypes that may be masked by genes encoding partially redundant proteins. Finally, potent chemical probes can be useful starting points for the development of human therapeutics. Here, we used cantharidin, a natural toxin, to uncover otherwise "hidden" phenotypes for a methyltransferase that has resisted characterization. This enzyme, Crg1, has no phenotype in standard conditions but is indispensible for survival in the presence of cantharidin. Using this chemical genetic relationship, we characterized novel functions of Crg1, and by combining diverse genomic assays with small molecule perturbation we characterized the mechanism of cantharidin cytotoxicity. These observations are relevant beyond yeast Crg1 because cantharidin and its analogues have potent anticancer activity, yet its therapeutic use has been limited to topical applications because of its cytotoxicity. Considering that methyltransferases are an extremely abundant and diverse class of cellular proteins, chemical probes such as cantharidin are critical for understanding their cellular roles and defining potential points of therapeutic intervention. |
| Audience | Academic |
| Author | Nislow, Corey Lowenson, Jonathan Giaever, Guri Clarke, Steven G. Riezman, Howard Riezman, Isabelle Baryshnikova, Anastasia Guan, Xue Li Hoon, Shawn Michaut, Magali Wenk, Markus R. Young, Brian Lissina, Elena Cowen, Leah E. Urbanus, Malene L. |
| AuthorAffiliation | 3 Department of Chemistry and Biochemistry and the Molecular Biology Institute, University of California Los Angeles, Los Angeles, California, United States of America 1 Department of Molecular Genetics, University of Toronto, Toronto, Canada HudsonAlpha Institute for Biotechnology, United States of America 5 Department of Biological Sciences, Yong Loo Lin School of Medicine, National University of Singapore, Singapore, Singapore 2 Terrence Donnelly Centre for Cellular and Biomolecular Research, University of Toronto, Toronto, Canada 7 Molecular Engineering Lab, Agency for Science, Technology, and Research, Singapore, Singapore 8 Department of Pharmacy and Pharmaceutical Sciences, University of Toronto, Toronto, Canada 4 Banting and Best Department of Medical Research, University of Toronto, Toronto, Canada 6 Department of Biochemistry, University of Geneva, Geneva, Switzerland |
| AuthorAffiliation_xml | – name: HudsonAlpha Institute for Biotechnology, United States of America – name: 1 Department of Molecular Genetics, University of Toronto, Toronto, Canada – name: 4 Banting and Best Department of Medical Research, University of Toronto, Toronto, Canada – name: 8 Department of Pharmacy and Pharmaceutical Sciences, University of Toronto, Toronto, Canada – name: 3 Department of Chemistry and Biochemistry and the Molecular Biology Institute, University of California Los Angeles, Los Angeles, California, United States of America – name: 7 Molecular Engineering Lab, Agency for Science, Technology, and Research, Singapore, Singapore – name: 2 Terrence Donnelly Centre for Cellular and Biomolecular Research, University of Toronto, Toronto, Canada – name: 5 Department of Biological Sciences, Yong Loo Lin School of Medicine, National University of Singapore, Singapore, Singapore – name: 6 Department of Biochemistry, University of Geneva, Geneva, Switzerland |
| Author_xml | – sequence: 1 givenname: Elena surname: Lissina fullname: Lissina, Elena – sequence: 2 givenname: Brian surname: Young fullname: Young, Brian – sequence: 3 givenname: Malene L. surname: Urbanus fullname: Urbanus, Malene L. – sequence: 4 givenname: Xue Li surname: Guan fullname: Guan, Xue Li – sequence: 5 givenname: Jonathan surname: Lowenson fullname: Lowenson, Jonathan – sequence: 6 givenname: Shawn surname: Hoon fullname: Hoon, Shawn – sequence: 7 givenname: Anastasia surname: Baryshnikova fullname: Baryshnikova, Anastasia – sequence: 8 givenname: Isabelle surname: Riezman fullname: Riezman, Isabelle – sequence: 9 givenname: Magali surname: Michaut fullname: Michaut, Magali – sequence: 10 givenname: Howard surname: Riezman fullname: Riezman, Howard – sequence: 11 givenname: Leah E. surname: Cowen fullname: Cowen, Leah E. – sequence: 12 givenname: Markus R. surname: Wenk fullname: Wenk, Markus R. – sequence: 13 givenname: Steven G. surname: Clarke fullname: Clarke, Steven G. – sequence: 14 givenname: Guri surname: Giaever fullname: Giaever, Guri – sequence: 15 givenname: Corey surname: Nislow fullname: Nislow, Corey |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/22028670$$D View this record in MEDLINE/PubMed |
| BookMark | eNqVk9uO0zAQhiO0iD3AGyCwhATiosWHJE72AqlUwFYqu1IL3FquM2lcOXGI3Ype8O44tEUtQhzki1jON__Y_8xcRmeNbSCKHhM8JIyTVyu77hpphu0SmiHBmDJG70UXJEnYgMc4Pjvan0eXzq0wZkmW8wfROaWYZinHF9G3EZpvnYfaoTfaGrvcolHbdlaqCs1gA9I45CtAM2sA2RJJdGs3YNAH8NXW-E42roROOkC6CQGutU3Ye4vGFdRaSYPmvgPnkGwKNNWtLtCNrcE6L512D6P7ZcgAj_bfq-jTu7cfxzeD6d37yXg0HShOcz8gJWY8zmSScZaXUqWESc5TSKCguEjSmJG0LHCyoJxki4JRzIuCZlneryRV7Cp6utNtjXVi75wThBEW55yQJBCTHVFYuRJtp2vZbYWVWvw4sN1SyM5rZUAAS7jCuVosykUMmOZSEhqXwVueAYMyaL3eZ1svaigUNMEncyJ6-qfRlVjajWAk5ynvL_NiL9DZL2twXtTaKTBGNmDXTuThgXmM8_zvJMY8WMhJIJ_tyKUMb9BNaUNq1dNiRDllwcS01xv-hgqr6KsZGrDU4fwk4OVJQGA8fPVLuXZOTOaz_2Bv_529-3zKPj9iq9CzvnLWrL0OzXgKPjkuzM-KHMYhANc7QHXWuQ5KobSXvU6wQRtBsOhn79BBop89sZ-9EBz_EnzQ_2PYd6NdMag |
| CitedBy_id | crossref_primary_10_1371_journal_pgen_1004019 crossref_primary_10_1021_cb400607h crossref_primary_10_1364_AO_416943 crossref_primary_10_1534_genetics_113_160291 crossref_primary_10_1007_s00248_016_0885_7 crossref_primary_10_1371_journal_pcbi_1003514 crossref_primary_10_1021_acs_biochem_8b01277 crossref_primary_10_1074_jbc_RA118_003890 crossref_primary_10_1039_c2np20029e crossref_primary_10_1016_j_plipres_2014_06_001 crossref_primary_10_1007_s00253_023_12863_z crossref_primary_10_1002_2211_5463_13196 crossref_primary_10_1093_molbev_msx151 crossref_primary_10_1016_j_bbrc_2021_03_074 crossref_primary_10_1155_2014_904958 |
| Cites_doi | 10.1073/pnas.0407170102 10.1016/0006-291X(89)92189-X 10.1021/bi049784+ 10.1128/EC.1.6.1021-1031.2002 10.1002/yea.320090306 10.1146/annurev.physiol.65.092101.142517 10.1128/JB.182.22.6509-6513.2000 10.1128/AAC.34.6.989 10.1007/s00726-007-0500-9 10.1093/nar/gkm683 10.1038/nrm1891 10.1016/S0092-8674(03)01035-3 10.1021/bi7018157 10.1016/S0076-6879(10)70015-X 10.1016/S0076-6879(02)50957-5 10.1016/S0076-6879(10)70010-0 10.1073/pnas.89.24.11867 10.1073/pnas.0811700106 10.1007/978-1-60761-322-0_18 10.1126/science.1150021 10.1038/nmeth.1534 10.1021/ja00751a040 10.1016/S0021-9258(17)42470-7 10.1038/nchembio762 10.1023/A:1014460818734 10.1016/S0021-9258(17)40373-5 10.1128/AAC.35.8.1532 10.1073/pnas.0610354104 10.1016/0006-3223(93)90256-D 10.1016/0014-5793(93)80889-3 10.1091/mbc.11.12.4241 10.1016/j.bcp.2003.12.025 10.1016/0006-2944(81)90084-3 10.1074/jbc.M412454200 10.1016/S0968-0004(03)00090-2 10.1126/science.1180823 10.1021/bi011380j 10.1016/0378-8741(89)90062-7 10.1186/1471-2105-3-35 10.1074/mcp.M900025-MCP200 10.1038/nature00935 10.1016/S0165-6147(03)00225-6 10.1038/nchembio.186 10.1002/cbf.913 10.1074/jbc.M800401200 10.5507/bp.2010.017 10.1016/0048-3575(86)90038-6 10.1016/j.abb.2004.08.037 10.1007/s00294-001-0259-6 10.1016/j.cell.2006.06.040 10.1091/mbc.E08-11-1126 10.1074/jbc.274.2.814 10.1074/mcp.M300037-MCP200 10.1042/BST0340330 10.1101/gad.1362105 10.1016/S0300-483X(00)00185-2 10.1128/MMBR.69.2.262-291.2005 10.1038/nchembio.100 10.1016/S0022-3565(24)36543-7 10.1096/fasebj.10.4.8647346 10.1371/journal.pone.0012671 10.1126/science.1065810 10.1074/jbc.M400299200 10.1016/j.bbalip.2005.05.006 10.1074/jbc.M806391200 10.1016/S0092-8674(00)00015-5 10.1128/MMBR.62.4.1264-1300.1998 10.1002/0471142727.mb1312s23 10.1038/nrm1434 10.1111/j.1600-0854.2006.00465.x 10.1128/MMBR.70.1.37-120.2006 10.1016/j.febslet.2004.10.057 10.1016/j.bcp.2004.12.003 10.1158/1541-7786.MCR-07-0373 10.1073/pnas.0307490100 10.1046/j.1365-2958.2003.03284.x 10.1002/yea.1362 10.1038/nprot.2007.427 10.1001/archderm.137.10.1357 10.1016/S0009-9120(88)80002-X 10.1074/jbc.M600365200 10.1139/o03-086 10.1074/jbc.M800830200 10.1371/journal.pgen.0010024 |
| ContentType | Journal Article |
| Copyright | COPYRIGHT 2011 Public Library of Science Lissina et al. 2011 2011 Lissina et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited: Lissina E, Young B, Urbanus ML, Guan XL, Lowenson J, et al. (2011) A Systems Biology Approach Reveals the Role of a Novel Methyltransferase in Response to Chemical Stress and Lipid Homeostasis. PLoS Genet 7(10): e1002332. doi:10.1371/journal.pgen.1002332 |
| Copyright_xml | – notice: COPYRIGHT 2011 Public Library of Science – notice: Lissina et al. 2011 – notice: 2011 Lissina et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited: Lissina E, Young B, Urbanus ML, Guan XL, Lowenson J, et al. (2011) A Systems Biology Approach Reveals the Role of a Novel Methyltransferase in Response to Chemical Stress and Lipid Homeostasis. PLoS Genet 7(10): e1002332. doi:10.1371/journal.pgen.1002332 |
| DBID | AAYXX CITATION CGR CUY CVF ECM EIF NPM IOV ISN ISR 7X8 7TM 8FD FR3 P64 RC3 5PM DOA |
| DOI | 10.1371/journal.pgen.1002332 |
| DatabaseName | CrossRef Medline MEDLINE MEDLINE (Ovid) MEDLINE MEDLINE PubMed Gale In Context: Opposing Viewpoints Gale In Context: Canada Gale In Context: Science MEDLINE - Academic Nucleic Acids Abstracts Technology Research Database Engineering Research Database Biotechnology and BioEngineering Abstracts Genetics Abstracts PubMed Central (Full Participant titles) DOAJ Directory of Open Access Journals |
| DatabaseTitle | CrossRef MEDLINE Medline Complete MEDLINE with Full Text PubMed MEDLINE (Ovid) MEDLINE - Academic Genetics Abstracts Engineering Research Database Technology Research Database Nucleic Acids Abstracts Biotechnology and BioEngineering Abstracts |
| DatabaseTitleList | MEDLINE - Academic Genetics Abstracts MEDLINE |
| Database_xml | – sequence: 1 dbid: DOA name: DOAJ Directory of Open Access Journals url: https://www.doaj.org/ sourceTypes: Open Website – sequence: 2 dbid: NPM name: PubMed url: https://proxy.k.utb.cz/login?url=http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed sourceTypes: Index Database – sequence: 3 dbid: EIF name: MEDLINE url: https://proxy.k.utb.cz/login?url=https://www.webofscience.com/wos/medline/basic-search sourceTypes: Index Database |
| DeliveryMethod | fulltext_linktorsrc |
| Discipline | Biology |
| DocumentTitleAlternate | Characterizing Crg1-Cantharidin Interaction |
| EISSN | 1553-7404 |
| ExternalDocumentID | 1313497115 oai_doaj_org_article_e357c09cbbfb4e029aa124f35878e3ef PMC3197675 A272364369 22028670 10_1371_journal_pgen_1002332 |
| Genre | Research Support, Non-U.S. Gov't Journal Article Research Support, N.I.H., Extramural |
| GeographicLocations | Canada |
| GeographicLocations_xml | – name: Canada |
| GrantInformation_xml | – fundername: NHGRI NIH HHS grantid: R01 HG003317 – fundername: CIHR grantid: 81340 – fundername: NIGMS NIH HHS grantid: GM026020 – fundername: NIGMS NIH HHS grantid: R37 GM026020 – fundername: NIGMS NIH HHS grantid: R01 GM026020 – fundername: CIHR grantid: 84305 – fundername: NHGRI NIH HHS grantid: HG00317 |
| GroupedDBID | --- 123 29O 2WC 53G 5VS 7X7 88E 8FE 8FH 8FI 8FJ AAFWJ AAUCC AAWOE AAYXX ABDBF ABUWG ACGFO ACIHN ACIWK ACPRK ACUHS ADBBV ADRAZ AEAQA AENEX AFKRA AFPKN AHMBA ALIPV ALMA_UNASSIGNED_HOLDINGS AOIJS B0M BAWUL BBNVY BCNDV BENPR BHPHI BPHCQ BVXVI BWKFM C1A CCPQU CITATION CS3 DIK DU5 E3Z EAP EAS EBD EBS EJD EMK EMOBN ESX F5P FPL FYUFA GROUPED_DOAJ GX1 HCIFZ HMCUK HYE IAO IGS IHR IHW INH INR IOV ISN ISR ITC KQ8 LK8 M1P M48 M7P O5R O5S OK1 OVT P2P PHGZM PHGZT PIMPY PQQKQ PROAC PSQYO QN7 RNS RPM SV3 TR2 TUS UKHRP WOW XSB ~8M CGR CUY CVF ECM EIF H13 IPNFZ NPM PJZUB PPXIY PQGLB PV9 QF4 RIG RZL WOQ PMFND 7X8 7TM 8FD FR3 P64 RC3 5PM PUEGO 3V. AAPBV ABPTK M~E |
| ID | FETCH-LOGICAL-c729t-1f03748a58739fac613a776e5ed20d564316fd05b2718bd3207dd2889898956c3 |
| IEDL.DBID | M48 |
| ISSN | 1553-7404 1553-7390 |
| IngestDate | Sun Oct 01 00:20:35 EDT 2023 Wed Aug 27 01:30:13 EDT 2025 Thu Aug 21 14:05:28 EDT 2025 Tue Aug 05 09:42:27 EDT 2025 Thu Jul 10 21:59:58 EDT 2025 Tue Jun 17 21:33:32 EDT 2025 Tue Jun 10 20:20:16 EDT 2025 Fri Jun 27 04:30:40 EDT 2025 Fri Jun 27 03:49:52 EDT 2025 Fri Jun 27 04:36:11 EDT 2025 Thu May 22 21:20:10 EDT 2025 Mon Jul 21 06:03:35 EDT 2025 Sun Jul 06 05:04:26 EDT 2025 Thu Apr 24 22:53:56 EDT 2025 |
| IsDoiOpenAccess | true |
| IsOpenAccess | true |
| IsPeerReviewed | true |
| IsScholarly | true |
| Issue | 10 |
| Language | English |
| License | This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited. Creative Commons Attribution License |
| LinkModel | DirectLink |
| MergedId | FETCHMERGED-LOGICAL-c729t-1f03748a58739fac613a776e5ed20d564316fd05b2718bd3207dd2889898956c3 |
| Notes | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 Conceived and designed the experiments: EL BY JL MLU SGC GG CN. Performed the experiments: EL BY XLG IR. Analyzed the data: EL BY XLG HR GG CN. Contributed reagents/materials/analysis tools: MLU AB JL SH MM MRW HR LEC. Wrote the paper: EL GG CN. |
| OpenAccessLink | http://journals.scholarsportal.info/openUrl.xqy?doi=10.1371/journal.pgen.1002332 |
| PMID | 22028670 |
| PQID | 900772971 |
| PQPubID | 23479 |
| ParticipantIDs | plos_journals_1313497115 doaj_primary_oai_doaj_org_article_e357c09cbbfb4e029aa124f35878e3ef pubmedcentral_primary_oai_pubmedcentral_nih_gov_3197675 proquest_miscellaneous_920794099 proquest_miscellaneous_900772971 gale_infotracmisc_A272364369 gale_infotracacademiconefile_A272364369 gale_incontextgauss_ISR_A272364369 gale_incontextgauss_ISN_A272364369 gale_incontextgauss_IOV_A272364369 gale_healthsolutions_A272364369 pubmed_primary_22028670 crossref_citationtrail_10_1371_journal_pgen_1002332 crossref_primary_10_1371_journal_pgen_1002332 |
| PublicationCentury | 2000 |
| PublicationDate | 2011-10-01 |
| PublicationDateYYYYMMDD | 2011-10-01 |
| PublicationDate_xml | – month: 10 year: 2011 text: 2011-10-01 day: 01 |
| PublicationDecade | 2010 |
| PublicationPlace | United States |
| PublicationPlace_xml | – name: United States – name: San Francisco, USA |
| PublicationTitle | PLoS genetics |
| PublicationTitleAlternate | PLoS Genet |
| PublicationYear | 2011 |
| Publisher | Public Library of Science Public Library of Science (PLoS) |
| Publisher_xml | – name: Public Library of Science – name: Public Library of Science (PLoS) |
| References | GS Wang (ref23) 1989; 26 NG Tsvetanova (ref16) 2010; 5 C Marcireau (ref57) 1990; 34 X Zhang (ref75) 2001; 40 XL Guan (ref85) 2010; 470 M Connerth (ref91) 2009; 579 G Giaever (ref8) 2004; 101 A Rahier (ref56) 1986; 25 LT Wu (ref33) 2001; 32 FJ Vizeacoumar (ref88) 2006; 281 W Lee (ref10) 2005; 1 AP Gasch (ref36) 2000; 11 D Ding (ref53) 2003; 47 RD Gietz (ref89) 2002; 350 X Zhang (ref76) 2004; 279 H Cai (ref19) 2001; 40 Y Li (ref30) 1992; 89 DE Levin (ref52) 2005; 69 TR Hughes (ref6) 2000; 102 DM Gelperin (ref81) 2005; 19 W Li (ref29) 2010 G Giaever (ref5) 2002; 418 T Efferth (ref28) 2005; 69 G Ren (ref51) 2006; 70 S Hoon (ref14) 2008; 4 LR Nunez (ref74) 2008; 283 AB Parsons (ref13) 2006; 126 L Moed (ref25) 2001; 137 M Liu (ref37) 2000; 182 VA Liepkalns (ref58) 1993; 34 KJ Sims (ref44) 2004; 82 WAM Loenen (ref4) 2006; 34 SE Pierce (ref41) 2007; 2 RT Lorenz (ref64) 1991; 35 M Costanzo (ref17) 2010; 327 L Gros (ref61) 2003; 63 PK Chiang (ref2) 1996; 10 T Czabany (ref47) 2008; 283 N Sengupta (ref54) 1981; 25 CC Wang (ref34) 2000; 147 P Jancova (ref59) 2010; 154 MA Collart (ref78) 1993 G Rigaut (ref82) 1999; 17 M Germann (ref71) 2005; 280 JE Katz (ref1) 2003; 2 JE Huh (ref27) 2004; 67 BD Bennett (ref83) 2009; 5 PY Lum (ref9) 2004; 116 XL Guan (ref43) 2006; 23 MV Mishra (ref62) 2008; 6 JE Katz (ref20) 2004; 43 TC Petrossian (ref22) 2009; 8 A Niewmierzycka (ref18) 1999; 274 RA Butcher (ref12) 2006; 2 ME Gardocki (ref48) 2005 SJ Kleene (ref38) 1977; 252 W Tsauer (ref32) 1997; 17 F Perocchi (ref80) 2007; 35 A Strunecka (ref55) 1985; 34 MA Grillo (ref66) 2008; 34 O Tehlivets (ref67) 2004; 577 E Ericson (ref77) 2010; 470 ED Murray Jr (ref84) 1986; 261 A Baryshnikova (ref87) 2010; 7 MC Gustin (ref73) 1998; 62 RE Honkanen (ref31) 1993; 330 A Balguerie (ref70) 2002; 1 PA Janmey (ref50) 2004; 5 K Juneau (ref79) 2007; 104 XL Guan (ref46) 2009; 20 P Kovacs (ref72) 2001; 19 A Hergovich (ref42) 2006; 7 DS Dumlao (ref21) 2007; 47 HL Yin (ref49) 2003; 65 R Weinshilboum (ref60) 1988; 21 R Banerjee (ref65) 2005; 43 G Giaever (ref7) 2003; 24 L Eberson (ref39) 1971; 93 N Malanovic (ref68) 2008; 283 CS Ejsing (ref45) 2009; 106 H Ishihara (ref35) 1989; 159 AHY Tong (ref40) 2001; 294 JA Sakoff (ref26) 2002; 20 C Kung (ref11) 2005; 102 HL Schubert (ref3) 2003; 28 MD Robinson (ref90) 2002; 3 CW Laidley (ref24) 1997; 280 L Desfarges (ref69) 1993; 9 AH Tong (ref86) 2006; 313 S Turro (ref63) 2006; 7 ME Hillenmeyer (ref15) 2008; 320 |
| References_xml | – volume: 102 start-page: 3587 year: 2005 ident: ref11 article-title: Chemical genomic profiling to identify intracellular targets of a multiplex kinase inhibitor. publication-title: Proc Natl Acad Sci USA doi: 10.1073/pnas.0407170102 – volume: 159 start-page: 871 year: 1989 ident: ref35 article-title: Calyculin A and okadaic acid: inhibitors of protein phosphatase activity. publication-title: Biochem Biophys Res Commun doi: 10.1016/0006-291X(89)92189-X – volume: 43 start-page: 5976 year: 2004 ident: ref20 article-title: 3-Isopropylmalate is the major endogenous substrate of the Saccharomyces cerevisiae trans-aconitate methyltransferase. publication-title: Biochemistry doi: 10.1021/bi049784+ – volume: 34 start-page: 543 year: 1985 ident: ref55 article-title: Lithium increases turnover of phospholipids in flight muscles of Periplaneta Americana. publication-title: L Physiol Bohemoslov – volume: 1 start-page: 1021 year: 2002 ident: ref70 article-title: Rvs161p and sphingolipids are required for actin repolarization following salt stress. publication-title: Eukaryot Cell doi: 10.1128/EC.1.6.1021-1031.2002 – volume: 9 start-page: 267 year: 1993 ident: ref69 article-title: Yeast mutants affected in viability upon starvation have a modified phospholipid composition. publication-title: Yeast doi: 10.1002/yea.320090306 – volume: 65 start-page: 761 year: 2003 ident: ref49 article-title: Phosphoinositide regulation of the actin cytoskeleton. publication-title: Annu Rev Physiol doi: 10.1146/annurev.physiol.65.092101.142517 – volume: 182 start-page: 6509 year: 2000 ident: ref37 article-title: Escherichia coli TehB requires S-Adenosylmethionine as a cofactor to mediate tellurite resistance. publication-title: J Bacteriol doi: 10.1128/JB.182.22.6509-6513.2000 – volume: 34 start-page: 989 year: 1990 ident: ref57 article-title: In vivo effects of fenpropimorph on the yeast Saccharomyces cerevisiae and determination of the molecular basis of the antifungal property. publication-title: Antimicrob Agents Chemother doi: 10.1128/AAC.34.6.989 – volume: 34 start-page: 187 year: 2008 ident: ref66 article-title: S-adenosylmethionine and its products. publication-title: Amino Acids doi: 10.1007/s00726-007-0500-9 – volume: 35 start-page: e128 year: 2007 ident: ref80 article-title: Antisense artifacts in transcriptome microarray experiments are resolved by actinomycin D. publication-title: Nuc Acids Research doi: 10.1093/nar/gkm683 – volume: 7 start-page: 253 year: 2006 ident: ref42 article-title: NDR kinases regulate essential cell processes from yeast to humans. publication-title: Nature Rev Mol Cell Biol doi: 10.1038/nrm1891 – volume: 116 start-page: 121 year: 2004 ident: ref9 article-title: Discovering modes of action for therapeutic compounds using a genome-wide screen of yeast heterozygotes. publication-title: Cell doi: 10.1016/S0092-8674(03)01035-3 – volume: 47 start-page: 698 year: 2007 ident: ref21 article-title: Secreted 3-isopropylmalate methyl ester signals invasive growth during amino acid starvation in Saccharomyces cerevisiae. publication-title: Biochemistry doi: 10.1021/bi7018157 – volume: 470 start-page: 369 year: 2010 ident: ref85 article-title: Yeast lipid analysis and quantification by mass spectrometry. publication-title: Meth Enzym doi: 10.1016/S0076-6879(10)70015-X – volume: 350 start-page: 87 year: 2002 ident: ref89 article-title: Transformation of yeast by lithium acetate/single-stranded carrier DNA/polyethylene glycol method. publication-title: Methods Enzymol doi: 10.1016/S0076-6879(02)50957-5 – volume: 470 start-page: 233 year: 2010 ident: ref77 article-title: Exploring gene function and drug action using chemogenomic dosage assays. publication-title: Methods Enzymol doi: 10.1016/S0076-6879(10)70010-0 – volume: 89 start-page: 11867 year: 1992 ident: ref30 article-title: Cantharidin-binding protein: identification as protein phosphatase 2A. publication-title: Proc Natl Acad Sci USA doi: 10.1073/pnas.89.24.11867 – volume: 106 start-page: 2136 year: 2009 ident: ref45 article-title: Global analysis of the yeast lipidome by quantitative shotgun mass spectrometry. publication-title: Proc Natl Acad Sci USA doi: 10.1073/pnas.0811700106 – volume: 579 start-page: 359 year: 2009 ident: ref91 article-title: Analysis of lipid particles from yeast. publication-title: Methods Mol Biol doi: 10.1007/978-1-60761-322-0_18 – volume: 320 start-page: 362 year: 2008 ident: ref15 article-title: The chemical genomic portrait of yeast: uncovering a phenotype for all genes. publication-title: Science doi: 10.1126/science.1150021 – volume: 7 start-page: 1017 year: 2010 ident: ref87 article-title: Quantitative analysis of fitness and genetic interactions in yeast on a genome scale. publication-title: Nat Methods doi: 10.1038/nmeth.1534 – volume: 93 start-page: 5821 year: 1971 ident: ref39 article-title: Cyclic anhydrides. III. Equilibrium constants for the acid-anhydride equilibrium in aqueous solutions of certain vicinal diacids. publication-title: J Am Chem Soc doi: 10.1021/ja00751a040 – volume: 261 start-page: 306 year: 1986 ident: ref84 article-title: Metabolism of a synthetic L-isoaspartyl-containing hexapeptide in erythrocyte extracts. Enzymatic methyl esterification is followed by nonenzymatic succinimide formation. publication-title: J Biol Chem doi: 10.1016/S0021-9258(17)42470-7 – volume: 2 start-page: 103 year: 2006 ident: ref12 article-title: Microarray-based method for monitoring yeast overexpression strains reveals small-molecule targets in TOR pathway. publication-title: Nat Chem Biol doi: 10.1038/nchembio762 – volume: 20 start-page: 1 year: 2002 ident: ref26 article-title: Anticancer activity and protein phosphatase 1 and 2A inhibition of a new generation of cantharidin analogues. publication-title: Invest New Drugs doi: 10.1023/A:1014460818734 – volume: 252 start-page: 3214 year: 1977 ident: ref38 article-title: Isolation of glutamic acid methyl ester from an Escherichia coli membrane protein involved in chemotaxis. publication-title: J Biol Chem doi: 10.1016/S0021-9258(17)40373-5 – volume: 35 start-page: 1532 year: 1991 ident: ref64 article-title: Physiological effects of fenpropimorph on wild-type Saccharomyces cerevisiae and fenpropimorph-resistant mutants. publication-title: Antimicrob Agents Chemother doi: 10.1128/AAC.35.8.1532 – volume: 17 start-page: 2095 year: 1997 ident: ref32 article-title: The effect of cantharidin analogues on xanthine oxidase. publication-title: Anticancer Res – volume: 104 start-page: 1522 year: 2007 ident: ref79 article-title: High-density yeast-tiling array reveals previously undiscovered introns and extensive regulation of meiotic splicing. publication-title: Proc Natl Acad Sci USA doi: 10.1073/pnas.0610354104 – volume: 34 start-page: 51 year: 1993 ident: ref58 article-title: Alterations in the metabolism of choline-containing phospholipids by lithium and carbachol in SH-SY5Y neuroblastoma cells. publication-title: Biol Psychiatry doi: 10.1016/0006-3223(93)90256-D – volume: 17 start-page: 1030 year: 1999 ident: ref82 article-title: A generic protein purification method for protein complex characterization and proteome exploration. publication-title: Nature – volume: 330 start-page: 283 year: 1993 ident: ref31 article-title: Cantharidin, another natural toxin that inhibits the activity of serine/threonine protein phosphatases types 1 and 2A. publication-title: FEBS Lett doi: 10.1016/0014-5793(93)80889-3 – volume: 11 start-page: 4241 year: 2000 ident: ref36 article-title: Genomic expression programs in the response of yeast cells to environmental changes. publication-title: Mol Biol Cell doi: 10.1091/mbc.11.12.4241 – volume: 67 start-page: 1811 year: 2004 ident: ref27 article-title: Roles of p38 and JNK mitogen-activated protein kinase pathways during cantharidin-induced apoptosis in U937 cells. publication-title: Biochem Pharmacol doi: 10.1016/j.bcp.2003.12.025 – volume: 25 start-page: 267 year: 1981 ident: ref54 article-title: Platelet and erythrocyte membrane lipid and phospholipid patterns in different types of mental patients. publication-title: Biochem Med doi: 10.1016/0006-2944(81)90084-3 – volume: 280 start-page: 4270 year: 2005 ident: ref71 article-title: Characterizing the sphingolipid signaling pathway that remediates defects associated with loss of the yeast amphiphysin-like orthologs, Rvs161p and Rvs167p. publication-title: J Biol Chem doi: 10.1074/jbc.M412454200 – volume: 28 start-page: 329 year: 2003 ident: ref3 article-title: Many paths to methyltransfer: a chronicle of convergence. publication-title: Trends Biochem Sci doi: 10.1016/S0968-0004(03)00090-2 – volume: 327 start-page: 425 year: 2010 ident: ref17 article-title: The genetic landscape of a cell. publication-title: Science doi: 10.1126/science.1180823 – volume: 40 start-page: 13699 year: 2001 ident: ref19 article-title: Identification of the gene and characterization of the activity of the trans-aconitate methyltransferase from Saccharomyces cerevisiae. publication-title: Biochemistry doi: 10.1021/bi011380j – volume: 26 start-page: 147 year: 1989 ident: ref23 article-title: Medical uses of mylabris in ancient China and recent studies. publication-title: J Ethnopharmacol doi: 10.1016/0378-8741(89)90062-7 – volume: 3 start-page: 35 year: 2002 ident: ref90 article-title: FunSpec: a web-based cluster interpreter for yeast. publication-title: BMC Bioinformatics doi: 10.1186/1471-2105-3-35 – volume: 8 start-page: 1516 year: 2009 ident: ref22 article-title: Multiple motif scanning to identify methyltransferases from the yeast proteome. publication-title: Mol Cel Proteomics doi: 10.1074/mcp.M900025-MCP200 – volume: 418 start-page: 387 year: 2002 ident: ref5 article-title: Functional profiling of the Saccharomyces cerevisiae genome. publication-title: Nature doi: 10.1038/nature00935 – volume: 24 start-page: 444 year: 2003 ident: ref7 article-title: A chemical genomics approach to understanding drug action. publication-title: Trends Pharmacol Sci doi: 10.1016/S0165-6147(03)00225-6 – volume: 5 start-page: 593 year: 2009 ident: ref83 article-title: Absolute metabolite concentrations and implied enzyme active site occupancy in Escherichia coli. publication-title: Nat Chem Biol doi: 10.1038/nchembio.186 – volume: 19 start-page: 197 year: 2001 ident: ref72 article-title: Effects of phosphoprotein phosphatase inhibitors (phenylarsine oxide and cantharidin) on Tetrahymena. publication-title: Cell Biochem Func doi: 10.1002/cbf.913 – volume: 283 start-page: 17065 year: 2008 ident: ref47 article-title: Structural and biochemical properties of lipid particles from the yeast Saccharomyces cerevisiae. publication-title: J Biol Chem doi: 10.1074/jbc.M800401200 – volume: 154 start-page: 103 year: 2010 ident: ref59 article-title: Phase II drug metabolizing enzymes. publication-title: Biomed Pap Med Fac Univ Palacky Olomouc Czech Repub doi: 10.5507/bp.2010.017 – volume: 25 start-page: 112 year: 1986 ident: ref56 article-title: Chemical structure activity relationships of the inhibition of sterol biosynthesis by N-substituted morpholines in higher plant cells. publication-title: Pestic Biochem Physiol doi: 10.1016/0048-3575(86)90038-6 – volume: 43 start-page: 144 year: 2005 ident: ref65 article-title: Redox regulation and reaction mechanism of human cystathionine-≤-synthase: a PLP-dependent hemesensor protein. publication-title: Arch Biochem Biophys doi: 10.1016/j.abb.2004.08.037 – volume: 40 start-page: 221 year: 2001 ident: ref75 article-title: Elevation of endogenous sphingolipid long-chain base phosphates kills Saccharomyces cerevisiae cells. publication-title: Curr Genet doi: 10.1007/s00294-001-0259-6 – volume: 126 start-page: 611 year: 2006 ident: ref13 article-title: Exploring the mode-of-action of bioactive compounds by chemical-genetic profiling in yeast. publication-title: Cell doi: 10.1016/j.cell.2006.06.040 – volume: 20 start-page: 2083 year: 2009 ident: ref46 article-title: Functional interactions between sphingolipids and sterols in biological membranes regulating cell physiology. publication-title: Mol Biol Cell doi: 10.1091/mbc.E08-11-1126 – volume: 274 start-page: 814 year: 1999 ident: ref18 article-title: S-Adenosylmethionine-dependent methylation in Saccharomyces cerevisiae. Identification of a novel protein arginine methyltransferase. publication-title: J Biol Chem doi: 10.1074/jbc.274.2.814 – volume: 2 start-page: 525 year: 2003 ident: ref1 article-title: Automated identification of putative methyltransferases from genomic open reading frames. publication-title: Mol Cell Proteomics doi: 10.1074/mcp.M300037-MCP200 – volume: 34 start-page: 330 year: 2006 ident: ref4 article-title: S-Adenosylmethionine: jack of all trades and master of everything? publication-title: Biochem Soc Trans doi: 10.1042/BST0340330 – volume: 19 start-page: 2816 year: 2005 ident: ref81 article-title: Biochemical and genetic analysis of the yeast proteome with a movable ORF collection. publication-title: Gen Dev doi: 10.1101/gad.1362105 – volume: 147 start-page: 77 year: 2000 ident: ref34 article-title: Cytotoxic effects of cantharidin on the growth of normal and carcinoma cells. publication-title: Toxicology doi: 10.1016/S0300-483X(00)00185-2 – volume: 69 start-page: 262 year: 2005 ident: ref52 article-title: Cell wall integrity signaling in Saccharomyces cerevisiae. publication-title: Microbiol Mol Biol Rev doi: 10.1128/MMBR.69.2.262-291.2005 – volume: 4 start-page: 498 year: 2008 ident: ref14 article-title: An integrated platform of genomic assays reveals small-molecule bioactivities. publication-title: Nat Chem Biol doi: 10.1038/nchembio.100 – volume: 280 start-page: 1152 year: 1997 ident: ref24 article-title: Protein phosphatase in neuroblastoma cells: [3H]cantharidin binding site in relation to cytotoxicity. publication-title: J Pharmacol Exp Ther doi: 10.1016/S0022-3565(24)36543-7 – volume: 10 start-page: 471 year: 1996 ident: ref2 article-title: S-Adenosylmethionine and methylation. publication-title: FASEB J doi: 10.1096/fasebj.10.4.8647346 – volume: 5 start-page: e12671 year: 2010 ident: ref16 article-title: Proteome-wide search reveals unexpected RNA-binding proteins in Saccharomyces cerevisiae. publication-title: PLoS ONE doi: 10.1371/journal.pone.0012671 – volume: 294 start-page: 2364 year: 2001 ident: ref40 article-title: Systematic genetic analysis with ordered arrays of yeast deletion mutants. publication-title: Science doi: 10.1126/science.1065810 – volume: 279 start-page: 22030 year: 2004 ident: ref76 article-title: Pil1p and Lsp1 negatively regulate the 3-phosphoinositide-dependent protein kinase-like kinase Pkh1p and downstream signaling pathways Pck1p and Ypk1p. publication-title: J Biol Chem doi: 10.1074/jbc.M400299200 – start-page: 89 year: 2005 ident: ref48 article-title: Phosphatidylinositol biosynthesis: biochemistry and regulation. publication-title: Bioch Biophyscia Acta doi: 10.1016/j.bbalip.2005.05.006 – volume: 283 start-page: 34204 year: 2008 ident: ref74 article-title: Cell Wall Integrity MAPK pathway is essential for lipid homeostasis. publication-title: J Biol Chem doi: 10.1074/jbc.M806391200 – volume: 102 start-page: 109 year: 2000 ident: ref6 article-title: Functional discovery via a compendium of expression profiles. publication-title: Cell doi: 10.1016/S0092-8674(00)00015-5 – volume: 62 start-page: 1264 year: 1998 ident: ref73 article-title: MAP kinase pathways in the yeast Saccharomyces cerevisiae. publication-title: Microbiol Mol Biol Rev doi: 10.1128/MMBR.62.4.1264-1300.1998 – start-page: 13.12.1 year: 1993 ident: ref78 article-title: Preparation of yeast RNA. publication-title: Current Protocols in Molecular Biology doi: 10.1002/0471142727.mb1312s23 – volume: 5 start-page: 658 year: 2004 ident: ref50 article-title: Cytoskeletal regulation: rich in lipids. publication-title: Nature Mol Cell Biol doi: 10.1038/nrm1434 – volume: 7 start-page: 1254 year: 2006 ident: ref63 article-title: Identification and characterization of associated with lipid droplet protein 1: a novel membrane-associated protein that resides on hepatic lipid droplets. publication-title: Traffic doi: 10.1111/j.1600-0854.2006.00465.x – start-page: 1 year: 2010 ident: ref29 article-title: Cantharidin, a potent and selective PP2A inhibitor, induces an oxidative stress-independent growth inhibition of pancreatic cancer cells through G2/M cell-cycle arrest and apoptosis. publication-title: Cancer Science – volume: 70 start-page: 37 year: 2006 ident: ref51 article-title: The BAR domain proteins: molding membranes in fission, fusion, and phagy. publication-title: Microbiol Mol Biol Rev doi: 10.1128/MMBR.70.1.37-120.2006 – volume: 577 start-page: 501 year: 2004 ident: ref67 article-title: S-Adenosyl-L-homocysteine hydrolase in yeast: key enzyme of methylation metabolism and coordinated regulation with phospholipid synthesis. publication-title: FEBS Lett doi: 10.1016/j.febslet.2004.10.057 – volume: 69 start-page: 811 year: 2005 ident: ref28 article-title: Molecular modes of action of cantharidin in tumor cells. publication-title: Biochem Pharmacol doi: 10.1016/j.bcp.2004.12.003 – volume: 6 start-page: 243 year: 2008 ident: ref62 article-title: DNMT1 as a molecular target in a multimodality-resistant phenotype in tumor cells. publication-title: Mol Cancer Res doi: 10.1158/1541-7786.MCR-07-0373 – volume: 101 start-page: 793 year: 2004 ident: ref8 article-title: Chemogenomic profiling: identifying the functional interactions of small molecules in yeast. publication-title: Proc Natl Acad Sci USA doi: 10.1073/pnas.0307490100 – volume: 47 start-page: 373 year: 2003 ident: ref53 article-title: Lithium and valproate decrease the membrane phosphatidylinositol/phosphatidylcholine ratio. publication-title: Mol Microbiol doi: 10.1046/j.1365-2958.2003.03284.x – volume: 23 start-page: 465 year: 2006 ident: ref43 article-title: Mass spectrometry-based profiling of phospholipids and sphingolipids in extracts from Saccharomyces cerevisiae. publication-title: Yeast doi: 10.1002/yea.1362 – volume: 313 start-page: 171 year: 2006 ident: ref86 article-title: Synthetic genetic array analysis in Saccharomyces cerevisiae. publication-title: Methods Mol Biol – volume: 2 start-page: 2958 year: 2007 ident: ref41 article-title: Genome-wide analysis of barcoded Saccharomyces cerevisiae gene-deletion mutants in pooled cultures. publication-title: Nat Protoc doi: 10.1038/nprot.2007.427 – volume: 63 start-page: 164 year: 2003 ident: ref61 article-title: Identification of new drug sensitivity genes using genetic suppressor elements: protein arginine N-methyltransferase mediates cell sensitivity to DNA-damaging agents. publication-title: Cancer Res – volume: 137 start-page: 1357 year: 2001 ident: ref25 article-title: Cantharidin revisited: a blistering defense of an ancient medicine. publication-title: Arch Dermatol doi: 10.1001/archderm.137.10.1357 – volume: 21 start-page: 201 year: 1988 ident: ref60 article-title: Pharmacogenetics of methylation: relationship to drug metabolism. publication-title: Clin Biochem doi: 10.1016/S0009-9120(88)80002-X – volume: 281 start-page: 12817 year: 2006 ident: ref88 article-title: The dynamin-like protein Vps1p of the yeast Saccharomyces cerevisiae associates with peroxisomes in a Pex19p-dependent manner. publication-title: J Biol Chem doi: 10.1074/jbc.M600365200 – volume: 32 start-page: 161 year: 2001 ident: ref33 article-title: Effect of norcantharidin on N-acetyltransferase activity in HepG2 cells. publication-title: American Journal of Chinese Medicine – volume: 82 start-page: 45 year: 2004 ident: ref44 article-title: Yeast sphingolipid metabolism: clues and connections. publication-title: Biochem Cell Biol doi: 10.1139/o03-086 – volume: 283 start-page: 23989 year: 2008 ident: ref68 article-title: S-Adenosyl-L-homocysteine hydrolase, key enzyme of methylation metabolism, regulates phosphatidylcholine synthesis and triacylglycerol homeostasis in yeast. publication-title: J Biol Chem doi: 10.1074/jbc.M800830200 – volume: 1 start-page: e24 year: 2005 ident: ref10 article-title: Genome-wide requirements for resistance to functionally distinct DNA-damaging agents. publication-title: PLoS Genet doi: 10.1371/journal.pgen.0010024 |
| SSID | ssj0035897 |
| Score | 2.1202817 |
| Snippet | Using small molecule probes to understand gene function is an attractive approach that allows functional characterization of genes that are dispensable in... Using small molecule probes to understand gene function is an attractive approach that allows functional characterization of genes that are dispensable in... |
| SourceID | plos doaj pubmedcentral proquest gale pubmed crossref |
| SourceType | Open Website Open Access Repository Aggregation Database Index Database Enrichment Source |
| StartPage | e1002332 |
| SubjectTerms | Actins - metabolism Animals Anticarcinogenic Agents - metabolism Anticarcinogenic Agents - pharmacology Biology Biomedical research Cantharidin - analogs & derivatives Cantharidin - metabolism Cantharidin - pharmacology Cell Wall - genetics Cell Wall - metabolism Coleoptera - chemistry Colleges & universities Cytoskeleton - metabolism Cytotoxicity Genes Genetic aspects Glycerophospholipids - metabolism Homeostasis Homeostasis - genetics Lipid Metabolism - genetics Lipids Metabolic Networks and Pathways Methods Methylation Methyltransferases Methyltransferases - genetics Methyltransferases - metabolism Mutagenesis, Site-Directed Phosphoprotein Phosphatases - antagonists & inhibitors Phosphoprotein Phosphatases - genetics Phosphoprotein Phosphatases - metabolism Physiological aspects Polymerase chain reaction Proteins Saccharomyces cerevisiae Saccharomyces cerevisiae - enzymology Saccharomyces cerevisiae - genetics Saccharomyces cerevisiae Proteins - genetics Saccharomyces cerevisiae Proteins - metabolism Sphingolipids - metabolism Stress, Physiological - genetics Systems Biology - methods Transferases |
| SummonAdditionalLinks | – databaseName: DOAJ Directory of Open Access Journals dbid: DOA link: http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwrV1Li9RAEG5kQPAivje6aiOCp7iZ7nQ6OY7isgquoK7sLfTTHRiTYTMj7MH_blV3Z9iIuHvwmv76kKpKPUjVV4S81FVjhYdK1RRzlZdGylxXmuOul8ZzVSgf2Pk_HldHJ-WHU3F6adUX9oRFeuAouAPHhTRFY7T2unQFa5SCkOS5qGXtuPPofSHmjcVU9MFwGteqCMFzCWV9Gprjcn6QdPR6DQoKBKScs0lQCtz9Ow89W6_64W_p559dlJfC0uEdcjvlk3QR3-MuueG6e-Rm3DB5cZ_8WtDI1TzQRLdERxZxiuRNYHwUUkCKTYa091TRrv_pVhQXS1-sNiGrdecQ6eiygwuhn9bRTU9NIhqgcdiEqs7S1XK9tPSs_-F6yDmH5fCAnBy--_r2KE8bF3IDSfYmn_tAR6NAuLzxykCsV1JWTjjLCisqnJv3thCaQUjTlrNCWsvqOiyhFJXhD8ms6zu3R6gVGmovXUL816UobW1tY-eVEKZhtfIiI3wUeWsSHTluxVi14R-bhLIkSrBFRbVJURnJd7fWkY7jCvwb1OYOi2Ta4QGYWJtMrL3KxDLyHG2hjZOpO5fQLphE-n1eNRl5ERBIqNFhx853tR2G9v2nb9cAfTm-DujzBPQqgXwPMjMqjVKA5JHNa4LcnyDBd5jJ8R6a9yi6AQSJdJUSyoSM0NHkW7yFvXid67dD2yAFFAPQPyBgGE0JxUdGHsWPZKcBxiCjrWSRETn5fCYqmp50y7PAew7RAqmHHv8PnT4ht9jYzTnfJ7PN-dY9hfRyo58FT_Ibxlh4-Q priority: 102 providerName: Directory of Open Access Journals |
| Title | A Systems Biology Approach Reveals the Role of a Novel Methyltransferase in Response to Chemical Stress and Lipid Homeostasis |
| URI | https://www.ncbi.nlm.nih.gov/pubmed/22028670 https://www.proquest.com/docview/900772971 https://www.proquest.com/docview/920794099 https://pubmed.ncbi.nlm.nih.gov/PMC3197675 https://doaj.org/article/e357c09cbbfb4e029aa124f35878e3ef http://dx.doi.org/10.1371/journal.pgen.1002332 |
| Volume | 7 |
| hasFullText | 1 |
| inHoldings | 1 |
| isFullTextHit | |
| isPrint | |
| link | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwjV1Lb9NAEF6VVEhcEO8aSlghJE6uHK_Xax8QSlGrgtSACkG5WftsLbl2iBNEDvx3ZtcPYVQg1_jbSJmZ3ZmJZ78PoVciThU10KnKYML9SDLmi1gQq_WSGsIDbhw7__ksPptHHxZ0sYc6zdbWgPWNrZ3Vk5qviqMf37ZvYcO_caoNbNItOlqCyR2lKCFwKO9DbmJWzOE86t8rEJo0ciuUEp9Bu99epvvbtwySleP070_u0bKo6pvK0j-nK39LV6f30N22zsTTJjDuoz1dPkC3G-XJ7UP0c4obDucatzRMuGMXx5bUCYyDoTTEdvgQVwZzXFbfdYGt4PS2WLtqV68gA-K8hAVuzlbjdYVlS0CAm0somJcKF_kyV_iqutYV1KJ1Xj9C89OTL-_O_FaJwZdQfK_9iXE0NZwmYDTDJdQAnLFYU63CQNHY3qc3KqAihFQnFAkDplSYJE6cksaSPEajsir1AcKKCujJRAR1gYhopBKlUjWJKZVpmHBDPUQ6k2eypSm3ahlF5t69MWhXGgtm1lFZ6ygP-f2qZUPT8R_8sfVmj7Uk2-6DanWZtXs204QyGaRSCCMiHYQp51ANGQgilmiijYde2FjImhur_VGRTUNmaflJnHropUNYoo3STvJc8k1dZ-8_ft0B9Hm2C-hiAHrdgkwFNpO8vWIBlrcsXwPk4QAJZ4ocPD6w4d2ZrgZDWhpLBu2Dh3AX8pldZWf0Sl1t6iy11FAhgP4BgcBII2hKPPSk2SS9B8IQKt2YBR5ig-0zcNHwSZlfOT50yCKWkujpzr_-GboTdqOck0M0Wq82-jnUlmsxRrfYgo3R_vHJ7NPF2P1DM3ZHyC9ZaXzy |
| linkProvider | Scholars Portal |
| openUrl | ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fsummon.serialssolutions.com&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.atitle=A+systems+biology+approach+reveals+the+role+of+a+novel+methyltransferase+in+response+to+chemical+stress+and+lipid+homeostasis&rft.jtitle=PLoS+genetics&rft.au=Lissina%2C+Elena&rft.au=Young%2C+Brian&rft.au=Urbanus%2C+Malene+L&rft.au=Guan%2C+Xue+Li&rft.date=2011-10-01&rft.pub=Public+Library+of+Science&rft.issn=1553-7390&rft.volume=7&rft.issue=10&rft_id=info:doi/10.1371%2Fjournal.pgen.1002332&rft.externalDocID=A272364369 |
| thumbnail_l | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=1553-7404&client=summon |
| thumbnail_m | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=1553-7404&client=summon |
| thumbnail_s | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=1553-7404&client=summon |