Academic literature on the topic 'Saccharomyces cerevisiae, cell cycle, Snf1'

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Journal articles on the topic "Saccharomyces cerevisiae, cell cycle, Snf1"

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Soontorngun, Nitnipa, Marc Larochelle, Simon Drouin, François Robert, and Bernard Turcotte. "Regulation of Gluconeogenesis in Saccharomyces cerevisiae Is Mediated by Activator and Repressor Functions of Rds2." Molecular and Cellular Biology 27, no. 22 (2007): 7895–905. http://dx.doi.org/10.1128/mcb.01055-07.

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ABSTRACT In Saccharomyces cerevisiae, RDS2 encodes a zinc cluster transcription factor with unknown function. Here, we unravel a key function of Rds2 in gluconeogenesis using chromatin immunoprecipitation-chip technology. While we observed that Rds2 binds to only a few promoters in glucose-containing medium, it binds many additional genes when the medium is shifted to ethanol, a nonfermentable carbon source. Interestingly, many of these genes are involved in gluconeogenesis, the tricarboxylic acid cycle, and the glyoxylate cycle. Importantly, we show that Rds2 has a dual function: it directly
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Newcomb, Laura L., Jasper A. Diderich, Matthew G. Slattery, and Warren Heideman. "Glucose Regulation of Saccharomyces cerevisiae Cell Cycle Genes." Eukaryotic Cell 2, no. 1 (2003): 143–49. http://dx.doi.org/10.1128/ec.2.1.143-149.2003.

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ABSTRACT Nutrient-limited Saccharomyces cerevisiae cells rapidly resume proliferative growth when transferred into glucose medium. This is preceded by a rapid increase in CLN3, BCK2, and CDC28 mRNAs encoding cell cycle regulatory proteins that promote progress through Start. We have tested the ability of mutations in known glucose signaling pathways to block glucose induction of CLN3, BCK2, and CDC28. We find that loss of the Snf3 and Rgt2 glucose sensors does not block glucose induction, nor does deletion of HXK2, encoding the hexokinase isoenzyme involved in glucose repression signaling. Rap
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Timblin, Barbara K., Kelly Tatchell, and Lawrence W. Bergman. "Deletion of the Gene Encoding the Cyclin-Dependent Protein Kinase Pho85 Alters Glycogen Metabolism in Saccharomyces cerevisiae." Genetics 143, no. 1 (1996): 57–66. http://dx.doi.org/10.1093/genetics/143.1.57.

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Abstract Pho85, a protein kinase with significant homology to the cyclin-dependent kinase, Cdc28, has been shown to function in repression of transcription of acid phosphatase (APase, encoded by PHO5) in high phosphate (Pi) medium, as well as in regulation of the cell cycle at G1/S. We describe several unique phenotypes associated with the deletion of the PHO85 gene including growth defects on a variety of carbon sources and hyperaccumulation of glycogen in rich medium high in Pi. Hyperaccumulation of glycogen in the pho85 strains is independent of other APase regulatory molecules and is not s
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Gray, Joseph V., Gregory A. Petsko, Gerald C. Johnston, Dagmar Ringe, Richard A. Singer, and Margaret Werner-Washburne. "“Sleeping Beauty”: Quiescence in Saccharomyces cerevisiae." Microbiology and Molecular Biology Reviews 68, no. 2 (2004): 187–206. http://dx.doi.org/10.1128/mmbr.68.2.187-206.2004.

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SUMMARY The cells of organisms as diverse as bacteria and humans can enter stable, nonproliferating quiescent states. Quiescent cells of eukaryotic and prokaryotic microorganisms can survive for long periods without nutrients. This alternative state of cells is still poorly understood, yet much benefit is to be gained by understanding it both scientifically and with reference to human health. Here, we review our knowledge of one “model” quiescent cell population, in cultures of yeast grown to stationary phase in rich media. We outline the importance of understanding quiescence, summarize the p
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Miura, Natsuko, Masahiro Shinohara, Yohei Tatsukami, et al. "Spatial Reorganization of Saccharomyces cerevisiae Enolase To Alter Carbon Metabolism under Hypoxia." Eukaryotic Cell 12, no. 8 (2013): 1106–19. http://dx.doi.org/10.1128/ec.00093-13.

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ABSTRACTHypoxia has critical effects on the physiology of organisms. In the yeastSaccharomyces cerevisiae, glycolytic enzymes, including enolase (Eno2p), formed cellular foci under hypoxia. Here, we investigated the regulation and biological functions of these foci. Focus formation by Eno2p was inhibited temperature independently by the addition of cycloheximide or rapamycin or by the single substitution of alanine for the Val22 residue. Using mitochondrial inhibitors and an antioxidant, mitochondrial reactive oxygen species (ROS) production was shown to participate in focus formation. Focus f
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Dombek, Kenneth M., Valentina Voronkova, Alexa Raney, and Elton T. Young. "Functional Analysis of the Yeast Glc7-Binding Protein Reg1 Identifies a Protein Phosphatase Type 1-Binding Motif as Essential for Repression of ADH2 Expression." Molecular and Cellular Biology 19, no. 9 (1999): 6029–40. http://dx.doi.org/10.1128/mcb.19.9.6029.

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ABSTRACT In Saccharomyces cerevisiae, the protein phosphatase type 1 (PP1)-binding protein Reg1 is required to maintain complete repression of ADH2 expression during growth on glucose. Surprisingly, however, mutant forms of the yeast PP1 homologue Glc7, which are unable to repress expression of another glucose-regulated gene, SUC2, fully repressed ADH2. ConstitutiveADH2 expression in reg1 mutant cells did require Snf1 protein kinase activity like constitutive SUC2expression and was inhibited by unregulated cyclic AMP-dependent protein kinase activity like ADH2 expression in derepressed cells.
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Huang, Dongqing, Jason Moffat, Wayne A. Wilson, et al. "Cyclin Partners Determine Pho85 Protein Kinase Substrate Specificity In Vitro and In Vivo: Control of Glycogen Biosynthesis by Pcl8 and Pcl10." Molecular and Cellular Biology 18, no. 6 (1998): 3289–99. http://dx.doi.org/10.1128/mcb.18.6.3289.

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ABSTRACT In Saccharomyces cerevisiae, PHO85 encodes a cyclin-dependent protein kinase (Cdk) with multiple roles in cell cycle and metabolic controls. In association with the cyclin Pho80, Pho85 controls acid phosphatase gene expression through phosphorylation of the transcription factor Pho4. Pho85 has also been implicated as a kinase that phosphorylates and negatively regulates glycogen synthase (Gsy2), and deletion of PHO85 causes glycogen overaccumulation. We report that the Pcl8/Pcl10 subgroup of cyclins directs Pho85 to phosphorylate glycogen synthase both in vivo and in vitro. Disruption
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Miller, M. E., B. R. Cairns, R. S. Levinson, K. R. Yamamoto, D. A. Engel, and M. M. Smith. "Adenovirus E1A specifically blocks SWI/SNF-dependent transcriptional activation." Molecular and Cellular Biology 16, no. 10 (1996): 5737–43. http://dx.doi.org/10.1128/mcb.16.10.5737.

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Expression of the adenovirus E1A243 oncoprotein in Saccharomyces cerevisiae produces a slow-growth phenotype with accumulation of cells in the G1 phase of the cell cycle. This effect is due to the N-terminal and CR1 domains of E1A243, which in rodent cells are involved in triggering cellular transformation and also in binding to the cellular transcriptional coactivator p300. A genetic screen was undertaken to identify genes required for the function of E1A243 in S. cerevisiae. This screen identified SNF12, a gene encoding the 73-kDa subunit of the SWI/SNF transcriptional regulatory complex. Mu
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Neef, Daniel W., and Michael P. Kladde. "Polyphosphate Loss Promotes SNF/SWI- and Gcn5-Dependent Mitotic Induction of PHO5." Molecular and Cellular Biology 23, no. 11 (2003): 3788–97. http://dx.doi.org/10.1128/mcb.23.11.3788-3797.2003.

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ABSTRACT Approximately 800 transcripts in Saccharomyces cerevisiae are cell cycle regulated. The oscillation of ∼40% of these genes, including a prominent subclass involved in nutrient acquisition, is not understood. To address this problem, we focus on the mitosis-specific activation of the phosphate-responsive promoter, PHO5. We show that the unexpected mitotic induction of the PHO5 acid phosphatase in rich medium requires the transcriptional activators Pho4 and Pho2, the cyclin-dependent kinase inhibitor Pho81, and the chromatin-associated enzymes Gcn5 and Snf2/Swi2. PHO5 mitotic activation
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Barber, Louise J., Thomas A. Ward, John A. Hartley, and Peter J. McHugh. "DNA Interstrand Cross-Link Repair in the Saccharomyces cerevisiae Cell Cycle: Overlapping Roles for PSO2 (SNM1) with MutS Factors and EXO1 during S Phase." Molecular and Cellular Biology 25, no. 6 (2005): 2297–309. http://dx.doi.org/10.1128/mcb.25.6.2297-2309.2005.

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ABSTRACT Pso2/Snm1 is a member of the β-CASP metallo-β-lactamase family of proteins that include the V(D)J recombination factor Artemis. Saccharomyces cerevisiae pso2 mutants are specifically sensitive to agents that induce DNA interstrand cross-links (ICLs). Here we establish a novel overlapping function for PSO2 with MutS mismatch repair factors and the 5′-3′ exonuclease Exo1 in the repair of DNA ICLs, which is confined to S phase. Our data demonstrate a requirement for NER and Pso2, or Exo1 and MutS factors, in the processing of ICLs, and this is required prior to the repair of ICL-induced
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Dissertations / Theses on the topic "Saccharomyces cerevisiae, cell cycle, Snf1"

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BUSNELLI, SARA. "Protein Kinase Snf1/AMPK: a new regulator of G1/S transition in Saccharomyces cerevisiae." Doctoral thesis, Università degli Studi di Milano-Bicocca, 2013. http://hdl.handle.net/10281/40994.

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The AMP-activated protein kinase (AMPK) family is a group of Serine/Threonine kinases highly conserved in eukaryotes, from yeast and insects to plants and mammals. Their primary role is the integration of signals regarding nutrient availability and environmental stresses, ensuring the adaptation to those conditions and cell survival (Hardie G., 2007; Ghillebert R. et al., 2011). As its homologue AMPK, in Saccharomyces cerevisiae Snf1 exists as a heterotrimeric complex. Core of this enzyme is the catalytic α subunit (Snf1), made up of a canonical catalytic domain in its N-terminus and of an aut
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NICASTRO, RAFFAELE. "Role of Snf1/AMPK as regulator of cell cycle, signal transduction and metabolism in Saccharomyces cerevisiae." Doctoral thesis, Università degli Studi di Milano-Bicocca, 2015. http://hdl.handle.net/10281/68465.

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Snf1 è una serina/treonina chinasi necessaria per il lievito S. cerevisiae per la crescita in condizioni di limitazione di nutrienti e per l’utilizzo di fonti di carbonio alternative al glucosio. Nel nostro laboratorio è stato precedentemente dimostrato che la mancanza di Snf1 causa un difetto nella transizione G1/S del ciclo cellulare e un difetto nell’espressione dei geni di fase G1 anche in condizioni di sufficienza nutrizionale (2% glucosio). È stato quindi approfondito il coinvolgimento di Snf1 in tre importanti processi cellulari: ciclo, trasduzione del segnale e metabolismo. Per dimos
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Kiser, Gretchen Louise. "Cell cycle checkpoint control in budding yeast Saccharomyces cerevisiae." Diss., The University of Arizona, 1995. http://hdl.handle.net/10150/187074.

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Multiple checkpoint controls ensure that later cellular events are not initiated until previous cellular events have been successfully completed. Our laboratory studies the checkpoint at the G2/M boundary that ensures the integrity of chromosome transmission by blocking mitosis until DNA synthesis and repair is completed. The checkpoint-dependent cell division arrest is one of several prominent responses to DNA damage, which also includes transcriptional induction of damage-inducible genes and DNA repair. I undertook three projects that explore several aspects of the damage response: (1) I fur
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Gooding, Christopher Michael. "Mitochondrial DNA replication and transmission in Saccharomyces cerevisiae." Thesis, University of Hertfordshire, 1991. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.303447.

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Chotai, Dipti. "Cell cycle regulated expression of the DBF2 gene in Saccharomyces cerevisiae." Thesis, University of Hertfordshire, 1994. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.359005.

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Bahman, A. M. "Studies on the CDC7 gene product of Saccharomyces cerevisiae." Thesis, University of Manchester, 1988. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.233154.

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Mapa, Claudine E. "Identification of Deubiquitinating Enzymes that Control the Cell Cycle in Saccharomyces cerevisiae." eScholarship@UMMS, 2018. https://escholarship.umassmed.edu/gsbs_diss/1004.

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A large fraction of the proteome displays cell cycle-dependent expression, which is important for cells to accurately grow and divide. Cyclical protein expression requires protein degradation via the ubiquitin proteasome system (UPS), and several ubiquitin ligases (E3) have established roles in this regulation. Less is understood about the roles of deubiquitinating enzymes (DUB), which antagonize E3 activity. A few DUBs have been shown to interact with and deubiquitinate cell cycle-regulatory E3s and their protein substrates, suggesting DUBs play key roles in cell cycle control. However, in vi
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Mitteau, Romain. "Régulation par la phosphorylation d’un module Rho GTPase dans la levure Saccharomyces cerevisiae." Thesis, Bordeaux 2, 2013. http://www.theses.fr/2013BOR22084/document.

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Le cycle cellulaire eucaryote est caractérisé par des changements abrupts et dynamiques de la polarité cellulaire lorsque les chromosomes sont dupliqués et ségrégés. Ces évènements nécessitent une coordination entre la machinerie du cycle cellulaire et les régulateurs de la polarité. Les mécanismes qui contrôlent cette coordination ne sont pas totalement compris. Dans la levure S. cerevisiae, comme dans d’autres organismes eucaryotes, la GTPase Cdc42 joue un rôle important dans la régulation de la polarité cellulaire. En effet ses régulateurs constituent un module GTPase qui subit une phosphor
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Schaefer, Jonathan Brook. "Regulation of G1 exit by the Swi6p transcription factor /." Thesis, Connect to this title online; UW restricted, 2007. http://hdl.handle.net/1773/5080.

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Dieckhoff, Patrick. "Protein modification and degradation in the cell cycle of the yeast Saccharomyces cerevisiae." Doctoral thesis, [S.l. : s.n.], 2004. http://deposit.ddb.de/cgi-bin/dokserv?idn=972638644.

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Books on the topic "Saccharomyces cerevisiae, cell cycle, Snf1"

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Crider, David Garry. Mitochondrial inheritance and cell cycle regulation in Saccharomyces cerevisiae. [publisher not identified], 2012.

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Hamilton, John Michael Uwe. Search for a plant homologue of the Saccharomyces cerevisiae cell cycle control gene CDC7. University of Manchester, 1994.

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From a to Alpha: Yeast As a Model for Cellular Differentiation. Cold Spring Harbor Laboratory Press, 2006.

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Book chapters on the topic "Saccharomyces cerevisiae, cell cycle, Snf1"

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Tatchell, K., J. F. Cannon, L. C. Robinson, and R. B. Wilson. "Suppressors of RAS Function in Saccharomyces cerevisiae." In Cell Cycle and Oncogenes. Springer Berlin Heidelberg, 1986. http://dx.doi.org/10.1007/978-3-642-71686-7_13.

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Jenness, D. D., A. C. Burkholder, and L. H. Hartwell. "Hormonal Control of Cell Division in Saccharomyces cerevisiae." In Cell Cycle and Oncogenes. Springer Berlin Heidelberg, 1986. http://dx.doi.org/10.1007/978-3-642-71686-7_3.

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Greenwood, Brianna L., and David T. Stuart. "Synchronization of Saccharomyces cerevisiae Cells for Analysis of Progression Through the Cell Cycle." In Cell-Cycle Synchronization. Springer US, 2022. http://dx.doi.org/10.1007/978-1-0716-2736-5_12.

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Piatti, Simonetta. "Cell cycle regulation of S phase entry in Saccharomyces cerevisiae." In Progress in Cell Cycle Research. Springer US, 1997. http://dx.doi.org/10.1007/978-1-4615-5371-7_12.

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Brock, Jo-Ann, and Kerry Bloom. "Cell Cycle Regulation of Centromere Function in Saccharomyces Cerevisiae." In Chromosome Segregation and Aneuploidy. Springer Berlin Heidelberg, 1993. http://dx.doi.org/10.1007/978-3-642-84938-1_9.

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Thevelein, Johan M. "The RAS-adenylate cyclase pathway and cell cycle control in Saccharomyces cerevisiae." In Molecular Biology of Saccharomyces. Springer Netherlands, 1992. http://dx.doi.org/10.1007/978-94-011-2504-8_9.

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Wu, Xiaorong, Lili Liu, and Mingxia Huang. "Analysis of Changes in Protein Level and Subcellular Localization During Cell Cycle Progression Using the Budding Yeast Saccharomyces cerevisiae." In Cell Cycle Checkpoints. Humana Press, 2011. http://dx.doi.org/10.1007/978-1-61779-273-1_5.

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Schuster, T., C. Price, W. Rossoll, and B. Kovacech. "New Cell Cycle-Regulated Genes in the Yeast Saccharomyces cerevisiae." In Recent Results in Cancer Research. Springer Berlin Heidelberg, 1997. http://dx.doi.org/10.1007/978-3-642-60393-8_18.

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Schalbetter, Stephanie A., and Jonathan Baxter. "Preparation of Cell Cycle-Synchronized Saccharomyces cerevisiae Cells for Hi-C." In Methods in Molecular Biology. Springer New York, 2019. http://dx.doi.org/10.1007/978-1-4939-9520-2_12.

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Küntzel, H., J. Lisziewicz, A. Godány, et al. "Control of the Cell Cycle Start by Protein Kinase Genes in Saccharomyces Cerevisiae." In Metabolism and Enzymology of Nucleic Acids. Springer US, 1988. http://dx.doi.org/10.1007/978-1-4613-0749-5_18.

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Conference papers on the topic "Saccharomyces cerevisiae, cell cycle, Snf1"

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Caplain, Emmanuel, Jean-Marie Ringeard, Stephane Serfaty, Loic Martinez, Nicolas Wilkie-Chancellier, and Pascal Griesmar. "Microrheological monitoring of life cycle of yeast cell Saccharomyces Cerevisiae." In 2011 IEEE International Ultrasonics Symposium (IUS). IEEE, 2011. http://dx.doi.org/10.1109/ultsym.2011.0375.

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Mayhew, Michael B., and Alexander J. Hartemink. "Cell-cycle phenotyping with conditional random fields: A case study in Saccharomyces cerevisiae." In 2013 IEEE 10th International Symposium on Biomedical Imaging (ISBI 2013). IEEE, 2013. http://dx.doi.org/10.1109/isbi.2013.6556661.

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Peng Qiu, Z. J. Wang, and K. J. Ray Liu. "Tracking the Herd: Resynchronization Analysis of Cell-Cycle Gene Expression Data in Saccharomyces Cerevisiae." In 2005 27th Annual International Conference of the IEEE Engineering in Medicine and Biology Society. IEEE, 2005. http://dx.doi.org/10.1109/iembs.2005.1615552.

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Markdahl, Johan, Nicolo Colombo, Johan Thunberg, and Jorge Goncalves. "Experimental design trade-offs for gene regulatory network inference: An in silico study of the yeast Saccharomyces cerevisiae cell cycle." In 2017 IEEE 56th Annual Conference on Decision and Control (CDC). IEEE, 2017. http://dx.doi.org/10.1109/cdc.2017.8263701.

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Reports on the topic "Saccharomyces cerevisiae, cell cycle, Snf1"

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Yompakdee, Chulee, and Sittiruk Roytrakul. Molecular target of an anti-cancer compound from leaves of Clausena harmandiana (Pierre). Chulalongkorn University, 2016. https://doi.org/10.58837/chula.res.2016.32.

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Clausena harmandiana (Pierre) Guillaumin or Song faa dong (in Thai), is classified in Family Rutaceae. Previous study, a coumarin compound designated CHA-01 was isolated from leave extract of C. harmandiana with inhibitory activity against calcium signaling in a ZDS1 null mutant yeast Saccharomyces cerevisiae (delta zds1). However, not much has been known on biological activity of this coumarin. In the past, some other coumarins were reported to contain anti-cancer activity. The aim of this research was to study molecular mechanism on antiproliferation activity of CHA-01 in Jurkat T cells. The
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