Academic literature on the topic 'Saccharomyces cerevisiae Saccharomyces cerevisiae Proteins Signal Transduction'

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Journal articles on the topic "Saccharomyces cerevisiae Saccharomyces cerevisiae Proteins Signal Transduction"

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Santangelo, George M. "Glucose Signaling in Saccharomyces cerevisiae." Microbiology and Molecular Biology Reviews 70, no. 1 (2006): 253–82. http://dx.doi.org/10.1128/mmbr.70.1.253-282.2006.

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SUMMARY Eukaryotic cells possess an exquisitely interwoven and fine-tuned series of signal transduction mechanisms with which to sense and respond to the ubiquitous fermentable carbon source glucose. The budding yeast Saccharomyces cerevisiae has proven to be a fertile model system with which to identify glucose signaling factors, determine the relevant functional and physical interrelationships, and characterize the corresponding metabolic, transcriptomic, and proteomic readouts. The early events in glucose signaling appear to require both extracellular sensing by transmembrane proteins and i
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Levin, David E. "Cell Wall Integrity Signaling in Saccharomyces cerevisiae." Microbiology and Molecular Biology Reviews 69, no. 2 (2005): 262–91. http://dx.doi.org/10.1128/mmbr.69.2.262-291.2005.

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SUMMARY The yeast cell wall is a highly dynamic structure that is responsible for protecting the cell from rapid changes in external osmotic potential. The wall is also critical for cell expansion during growth and morphogenesis. This review discusses recent advances in understanding the various signal transduction pathways that allow cells to monitor the state of the cell wall and respond to environmental challenges to this structure. The cell wall integrity signaling pathway controlled by the small G-protein Rho1 is principally responsible for orchestrating changes to the cell wall periodica
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Choi, You-Jeong, Sun-Hong Kim, Ki-Sook Park, and Kang-Yell Choi. "Differential transmission of G1 cell cycle arrest and mating signals by Saccharomyces cerevisiae Ste5 mutants in the pheromone pathway." Biochemistry and Cell Biology 77, no. 5 (1999): 459–68. http://dx.doi.org/10.1139/o99-054.

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Saccharomyces cerevisiae Ste5 is a scaffold protein that recruits many pheromone signaling molecules to sequester the pheromone pathway from other homologous mitogen-activated protein kinase pathways. G1 cell cycle arrest and mating are two different physiological consequences of pheromone signal transduction and Ste5 is required for both processes. However, the roles of Ste5 in G1 arrest and mating are not fully understood. To understand the roles of Ste5 better, we isolated 150 G1 cell cycle arrest defective STE5 mutants by chemical mutagenesis of the gene. Here, we found that two G1 cell cy
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Alepuz, Paula M., Dina Matheos, Kyle W. Cunningham, and Francisco Estruch. "The Saccharomyces cerevisiae RanGTP-Binding Protein Msn5p Is Involved in Different Signal Transduction Pathways." Genetics 153, no. 3 (1999): 1219–31. http://dx.doi.org/10.1093/genetics/153.3.1219.

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Abstract In eukaryotes, control of transcription by extracellular signals involves the translocation to the nucleus of at least one component of the signal transduction pathway. Transport through the nuclear envelope requires the activity of an import or export receptor that interacts with the small GTPase Ran. We have cloned the MSN5 gene of the yeast Saccharomyces cerevisiae that is postulated to encode one of these receptors. Msn5p belongs to a family of proteins with a conserved N-terminal sequence that acts as a RanGTP-binding domain. The results presented here provide genetic data suppor
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Moskow, John J., Amy S. Gladfelter, Rachel E. Lamson, Peter M. Pryciak, and Daniel J. Lew. "Role of Cdc42p in Pheromone-Stimulated Signal Transduction in Saccharomyces cerevisiae." Molecular and Cellular Biology 20, no. 20 (2000): 7559–71. http://dx.doi.org/10.1128/mcb.20.20.7559-7571.2000.

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ABSTRACT CDC42 encodes a highly conserved GTPase of the Rho family that is best known for its role in regulating cell polarity and actin organization. In addition, various studies of both yeast and mammalian cells have suggested that Cdc42p, through its interaction with p21-activated kinases (PAKs), plays a role in signaling pathways that regulate target gene transcription. However, recent studies of the yeast pheromone response pathway suggested that prior results with temperature-sensitive cdc42 mutants were misleading and that Cdc42p and the Cdc42p-PAK interaction are not involved in signal
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Kaniak, Aneta, Zhixiong Xue, Daniel Macool, Jeong-Ho Kim, and Mark Johnston. "Regulatory Network Connecting Two Glucose Signal Transduction Pathways in Saccharomyces cerevisiae." Eukaryotic Cell 3, no. 1 (2004): 221–31. http://dx.doi.org/10.1128/ec.3.1.221-231.2004.

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ABSTRACT The yeast Saccharomyces cerevisiae senses glucose, its preferred carbon source, through multiple signal transduction pathways. In one pathway, glucose represses the expression of many genes through the Mig1 transcriptional repressor, which is regulated by the Snf1 protein kinase. In another pathway, glucose induces the expression of HXT genes encoding glucose transporters through two glucose sensors on the cell surface that generate an intracellular signal that affects function of the Rgt1 transcription factor. We profiled the yeast transcriptome to determine the range of genes target
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Gerst, J. E., K. Ferguson, A. Vojtek, M. Wigler, and J. Field. "CAP is a bifunctional component of the Saccharomyces cerevisiae adenylyl cyclase complex." Molecular and Cellular Biology 11, no. 3 (1991): 1248–57. http://dx.doi.org/10.1128/mcb.11.3.1248.

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CAP, a protein from Saccharomyces cerevisiae that copurifies with adenylyl cyclase, appears to be required for yeast cells to be fully responsive to RAS proteins. CAP also appears to be required for normal cell morphology and responsiveness to nutrient deprivation and excess. We describe here a molecular and phenotypic analysis of the CAP protein. The N-terminal domain is necessary and sufficient for cellular response to activated RAS protein, while the C-terminal domain is necessary and sufficient for normal cellular morphology and responses to nutrient extremes. Thus, CAP is a novel example
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Gerst, J. E., K. Ferguson, A. Vojtek, M. Wigler, and J. Field. "CAP is a bifunctional component of the Saccharomyces cerevisiae adenylyl cyclase complex." Molecular and Cellular Biology 11, no. 3 (1991): 1248–57. http://dx.doi.org/10.1128/mcb.11.3.1248-1257.1991.

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CAP, a protein from Saccharomyces cerevisiae that copurifies with adenylyl cyclase, appears to be required for yeast cells to be fully responsive to RAS proteins. CAP also appears to be required for normal cell morphology and responsiveness to nutrient deprivation and excess. We describe here a molecular and phenotypic analysis of the CAP protein. The N-terminal domain is necessary and sufficient for cellular response to activated RAS protein, while the C-terminal domain is necessary and sufficient for normal cellular morphology and responses to nutrient extremes. Thus, CAP is a novel example
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Whiteway, Malcolm, Daniel Dignard та David Y. Thomas. "Mutagenesis of Ste18, a putative Gγ subunit in the Saccharomyces cerevisiae pheromone response pathway". Biochemistry and Cell Biology 70, № 10-11 (1992): 1230–37. http://dx.doi.org/10.1139/o92-169.

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The yeast STE18 gene product has sequence and functional similarity to the γ subunits of G proteins. The cloned STE18 gene was subjected to a saturation mutagenesis using doped oligonucleotides. The populations of mutant genes were screened for two classes of STE18 mutations, those that allowed for increased mating of a strain containing a defective STE4 gene (compensators) and those that inhibited mating even in the presence of a functional STE18 gene (dominant negatives). Three amino acid substitutions that enhanced mating in a specific STE4 (Gβ) point mutant background were identified. Thes
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Mösch, Hans-Ulrich, and Gerald R. Fink. "Dissection of Filamentous Growth by Transposon Mutagenesis in Saccharomyces cerevisiae." Genetics 145, no. 3 (1997): 671–84. http://dx.doi.org/10.1093/genetics/145.3.671.

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Diploid Saccharomyces cerevisiae strains starved for nitrogen undergo a developmental transition from growth as single yeast form (YF) cells to a multicellular form consisting of filaments of pseudohyphal (PH) cells. Filamentous growth is regulated by an evolutionarily conserved signaling pathway that includes the small GTP-binding proteins Ras2p and Cdc42p, the protein kinases Ste20p, Ste11p and Ste7p, and the transcription factor Ste12p. Here, we designed a genetic screen for mutant strains defective for filamentous growth (dfg) to identify novel targets of the filamentation signaling pathwa
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Dissertations / Theses on the topic "Saccharomyces cerevisiae Saccharomyces cerevisiae Proteins Signal Transduction"

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Powers, Ralph Wilson. "Genome-wide screens reveal that reduced TOR signaling extends chronological and replicative life span in S. cerevisiae /." Thesis, Connect to this title online; UW restricted, 2006. http://hdl.handle.net/1773/5044.

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Zeller, Corinne Eileen Dohlman Henrik G. "Regulation of signal transduction by G protein [beta] subunits in Saccharomyces cerevisiae." Chapel Hill, N.C. : University of North Carolina at Chapel Hill, 2007. http://dc.lib.unc.edu/u?/etd,1404.

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Thesis (Ph. D.)--University of North Carolina at Chapel Hill, 2007.<br>Title from electronic title page (viewed Apr. 25, 2008). "... in partial fulfillment of the requirements for the degree of Doctor of Philosophy in the Department of Biochemistry and Biophysics." Discipline: Biochemistry and Biophysics; Department/School: Medicine. On title page, [beta] appears as Greek character.
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Miller, Kristi E. "Negative Regulation of Polarity Establishment in Saccharomyces cerevisiae." The Ohio State University, 2019. http://rave.ohiolink.edu/etdc/view?acc_num=osu1555329407450767.

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Takahashi, Satoe. "Plasma Membrane Localization of Signaling Proteins in Yeast: a Dissertation." eScholarship@UMMS, 2008. https://escholarship.umassmed.edu/gsbs_diss/364.

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In response to external stimuli, many intracellular signaling proteins undergo dynamic changes in localization to the plasma membrane. Using the Saccharomyces cerevisiaemating pathway as a model, I investigated the molecular interactions that govern plasma membrane localization of signaling proteins, and how the plasma membrane compartmentalization of a signaling complex influences the overall signaling behavior of the pathway. Signaling proteins often consist of multiple interaction domains that collectively dictate their localization and function. Ste20 is a p21-activated kinase (PAK) that f
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Paulovich, Amanda G. "The regulation of S phase progression rate in yeast in response to DNA damage /." Thesis, Connect to this title online; UW restricted, 1996. http://hdl.handle.net/1773/10263.

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Robinson, Kevin Spencer. "The phosphatidylinositol signal transduction system in the yeast Saccharomyces cerevisiae." Thesis, University of Bath, 1992. https://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.316975.

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Van, Dyk Dewald 1975. "Genetic analysis of a signal transduction pathway : the regulation of invasive growth and starch degradation in Saccharomyces cerevisiae." Thesis, Stellenbosch : Stellenbosch University, 2004. http://hdl.handle.net/10019.1/49972.

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Dissertation (PhD)--University of Stellenbosch, 2004.<br>ENGLISH ABSTRACT: Cells of the yeast Saccharomyces cerevisiae are able to change their morphological appearance in response to a variety of extracellular and intracellular signals. The processes involved in morphogenesis are well characterised in this organism, but the exact mechanism by which information emanating from the environment is integrated into the regulation of the actin cytoskeleton and the yeast cell cycle, is still not clearly understood. Considerable progress has, however, been made. The processes are investigated o
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Roberts, Radclyffe L. (Radclyffe Lee) 1968. "Specificity determinants of a bifunctional signal transduction pathway in Saccharomyces cerevisiae." Thesis, Massachusetts Institute of Technology, 1997. http://hdl.handle.net/1721.1/43554.

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Kerwin, Christine. "Pho2 dependence in the phosphate signal transduction pathway of Saccharomyces cerevisiae and Candida glabrata." Click here for download, 2008. http://proquest.umi.com/pqdweb?did=1605126421&sid=1&Fmt=2&clientId=3260&RQT=309&VName=PQD.

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Nikolaou, Elissavet. "Phylogenetic diversity of fungal stress signaling pathways." Thesis, Available from the University of Aberdeen Library and Historic Collections Digital Resources, 2008. http://digitool.abdn.ac.uk:80/webclient/DeliveryManager?application=DIGITOOL-3&owner=resourcediscovery&custom_att_2=simple_viewer&pid=24849.

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Book chapters on the topic "Saccharomyces cerevisiae Saccharomyces cerevisiae Proteins Signal Transduction"

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Peeters, Ken, and Johan M. Thevelein. "Glucose Sensing and Signal Transduction in Saccharomyces cerevisiae." In Molecular Mechanisms in Yeast Carbon Metabolism. Springer Berlin Heidelberg, 2014. http://dx.doi.org/10.1007/978-3-662-45782-5_2.

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Levitzki, Alexander. "Regulation of Adenylate Cyclase in Mammalian Cells and Saccharomyces Cerevisiae." In Receptors, Membrane Transport and Signal Transduction. Springer Berlin Heidelberg, 1989. http://dx.doi.org/10.1007/978-3-642-74200-2_2.

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Thevelein, Johan M., Linda Van Aelst, Peter Durnez, and Stefan Hohmann. "The Signal Transduction Pathway Upstream of CDC25 — ras — Adenylate Cyclase in the Yeast Saccharomyces Cerevisiae and its Relationship to Nutrient Control of Cell Cycle Progression." In The Superfamily of ras-Related Genes. Springer US, 1991. http://dx.doi.org/10.1007/978-1-4684-6018-6_7.

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TATCHELL, KELLY. "RAS Genes in the Budding Yeast Saccharomyces cerevisiae." In Signal Transduction. Elsevier, 1993. http://dx.doi.org/10.1016/b978-0-12-429350-2.50011-5.

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WHITEWAY, MALCOLM, and BEVERLY ERREDE. "Signal Transduction Pathway for Pheromone Response in Saccharomyces cerevisiae." In Signal Transduction. Elsevier, 1993. http://dx.doi.org/10.1016/b978-0-12-429350-2.50012-7.

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Santos, Melina C., Carlos A. Breyer, Leonardo Schultz, et al. "Saccharomyces cerevisiae Peroxiredoxins in Biological Processes: Antioxidant Defense, Signal Transduction, Circadian Rhythm, and More." In Old Yeasts - New Questions. InTech, 2017. http://dx.doi.org/10.5772/intechopen.70401.

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