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  • 1
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    The transcriptional program of sporulation in budding yeast (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-10-23
    Description: Diploid cells of budding yeast produce haploid cells through the developmental program of sporulation, which consists of meiosis and spore morphogenesis. DNA microarrays containing nearly every yeast gene were used to assay changes in gene expression during sporulation. At least seven distinct temporal patterns of induction were observed. The transcription factor Ndt80 appeared to be important for induction of a large group of genes at the end of meiotic prophase. Consensus sequences known or proposed to be responsible for temporal regulation could be identified solely from analysis of sequences of coordinately expressed genes. The temporal expression pattern provided clues to potential functions of hundreds of previously uncharacterized genes, some of which have vertebrate homologs that may function during gametogenesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chu, S -- DeRisi, J -- Eisen, M -- Mulholland, J -- Botstein, D -- Brown, P O -- Herskowitz, I -- AI18738/AI/NIAID NIH HHS/ -- GH00450/GH/CGH CDC HHS/ -- GM46406/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1998 Oct 23;282(5389):699-705.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Biophysics, University of California, San Francisco, San Francisco, CA 94143-0448, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9784122" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Chromosomes, Fungal/physiology ; *DNA-Binding Proteins ; Fungal Proteins/genetics/metabolism ; *Gene Expression Regulation, Fungal ; Genes, Fungal ; Genome, Fungal ; Humans ; Meiosis/*genetics ; Morphogenesis ; Organelles/ultrastructure ; Saccharomyces cerevisiae/*genetics/physiology ; *Saccharomyces cerevisiae Proteins ; Spores, Fungal/*genetics/physiology/ultrastructure ; Transcription Factors/genetics/metabolism ; *Transcription, Genetic
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 2
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    Regulating natural health products (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-04-19
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Herskowitz, Ira -- New York, N.Y. -- Science. 2002 Apr 5;296(5565):46-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11962491" target="_blank"〉PubMed〈/a〉
    Keywords: Bicyclo Compounds ; Drug Interactions ; *Drug Labeling ; Humans ; Hypericum/*adverse effects ; Phloroglucinol/analogs & derivatives ; Phytotherapy/*adverse effects ; Plant Preparations/*adverse effects ; Terpenes/adverse effects/metabolism ; United States
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 3
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    The role of Far1p in linking the heterotrimeric G protein to polarity establishment proteins during yeast mating (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-11-20
    Description: Heterotrimeric guanosine triphosphate (GTP)-binding proteins (G proteins) determine tissue and cell polarity in a variety of organisms. In yeast, cells orient polarized growth toward the mating partner along a pheromone gradient by a mechanism that requires Far1p and Cdc24p. Far1p bound Gbetagamma and interacted with polarity establishment proteins, which organize the actin cytoskeleton. Cells containing mutated Far1p unable to bind Gbetagamma or polarity establishment proteins were defective for orienting growth toward their mating partner. In response to pheromones, Far1p moves from the nucleus to the cytoplasm. Thus, Far1p functions as an adaptor that recruits polarity establishment proteins to the site of extracellular signaling marked by Gbetagamma to polarize assembly of the cytoskeleton in a morphogenetic gradient.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Butty, A C -- Pryciak, P M -- Huang, L S -- Herskowitz, I -- Peter, M -- F32 GM017494/GM/NIGMS NIH HHS/ -- GM48052/GM/NIGMS NIH HHS/ -- GM57769/GM/NIGMS NIH HHS/ -- R01 GM057769/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1998 Nov 20;282(5393):1511-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Swiss Institute for Experimental Cancer Research (ISREC), Chemin des Boveresses 155, 1066 Epalinges/VD, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9822386" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptor Proteins, Signal Transducing ; Binding Sites ; Carrier Proteins/metabolism ; Cell Cycle Proteins/metabolism ; Cell Membrane/metabolism ; Cell Nucleus/metabolism ; *Cell Polarity ; Cyclin-Dependent Kinase Inhibitor Proteins ; Cytoskeleton/physiology ; Fungal Proteins/chemistry/genetics/*metabolism ; *GTP-Binding Protein beta Subunits ; GTP-Binding Proteins/*metabolism ; *Guanine Nucleotide Exchange Factors ; *Heterotrimeric GTP-Binding Proteins ; Models, Biological ; Mutation ; Peptides/metabolism/pharmacology ; Pheromones/metabolism/pharmacology ; Proto-Oncogene Proteins/metabolism ; *Repressor Proteins ; Saccharomyces cerevisiae/cytology/*physiology ; *Saccharomyces cerevisiae Proteins ; Signal Transduction ; cdc42 GTP-Binding Protein, Saccharomyces cerevisiae
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 4
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    Direct inhibition of the yeast cyclin-dependent kinase Cdc28-Cln by Far1 (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-08-26
    Description: Cell cycle arrest of Saccharomyces cerevisiae in G1 by the antimitogen alpha-factor is mediated by activation of a signal transduction pathway that results in inhibition of the cyclin-dependent kinase Cdc28-Cln. The Far1 protein is required for cell cycle arrest and associates with the Cdc28-Cln complex. The kinase activity of Cdc28-Cln was directly inhibited by Far1 both in vivo and in vitro, thus demonstrating that Far1 acts at the final step in the alpha-factor response pathway by inhibiting a G1 cyclin-dependent kinase.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Peter, M -- Herskowitz, I -- GM31286/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1994 Aug 26;265(5176):1228-31.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Biophysics, University of California at San Francisco 94143-0448.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8066461" target="_blank"〉PubMed〈/a〉
    Keywords: CDC28 Protein Kinase, S cerevisiae/*antagonists & inhibitors/metabolism ; *Cell Cycle Proteins ; Cyclin-Dependent Kinase Inhibitor Proteins ; Cyclins/genetics/*metabolism ; Fungal Proteins/metabolism/*pharmacology ; G1 Phase ; Peptides/pharmacology ; Phosphorylation ; Protamine Kinase/metabolism ; Recombinant Fusion Proteins/metabolism/pharmacology ; *Repressor Proteins ; Saccharomyces cerevisiae/cytology/*enzymology ; *Saccharomyces cerevisiae Proteins
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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