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Further characterisation of the rad18 gene of Schizosaccharomyces pombeMunday, Caroline Anne January 1998 (has links)
No description available.
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Environmental and medical studies on microbial growth under low nutrient (oligotrophic) conditionsAl-Talhi, Abdullah Dakheel D. January 2000 (has links)
No description available.
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Identification, quantification and assessment of oestrogenic chemicals in domestic sewage-treatment work effluentsRoutledge, Edwin John January 1997 (has links)
No description available.
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Investigations into the K1 killer toxin from Saccharomyces cerevisiaeSergeant, John A. January 2000 (has links)
No description available.
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Real-time on-line control of a fermentation processBelger, I. S. January 1991 (has links)
No description available.
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A novel optical fibre sensor based on inter-fibre distributed coupling for particle concentration measurementZhang, Feng Hong January 1997 (has links)
No description available.
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Development of a yeast-based colour assay for monitoring genetic and dietary influences on microsatellite instabilityLarkin, Kenneth John January 1999 (has links)
No description available.
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Chromatin modulation in Saccharomyces cerevisiae by Centromere and Promoter Factor 1Kent, Nicholas A. January 1994 (has links)
No description available.
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Characterisation of the murine homologue of the CIC-5 gene : a voltage-gated chloride channel implicated in human X-linked hereditary nephrolithiasisTanaka, Karo January 1999 (has links)
No description available.
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A functional analysis of mitotic tyrosine phosphatases by site-directed mutagenesisSTOBBE, STEPHANIE 12 September 2013 (has links)
In Schizosaccharomyces pombe mitosis is initiated when Cdc25 tyrosine phosphatase dephosphorylates Cdc2 (Cdk1) and in turn Cdc2 kinase phosphorylates mitotic targets. Cdc2 is thought to phosphorylate and further activate Cdc25, forming a positive feedback loop between the two for robust entry into mitosis. Pyp3 tyrosine phosphatase is essential in the absence of Cdc25. Its role is thought to be in directly dephosphorylating Cdc2 under these conditions. Pyp3 also presents a link between cell division and growth. It interacts physically and genetically with the mRNA cap-binding protein eIF4E and is thought to play the same role as mammalian 4E-binding proteins. Pyp3 has a consensus TOS motif potentially enabling nutritional input from the TOR pathway into translation regulation. Since known 4E-BPs are not phosphatases, Pyp3 may act as a 4E-binding protein independently of its phosphatase activity.
Evolutionarily conserved Cdc2 phosphorylation sites in Cdc25 were substituted to non-phosphorylatable Ala, or to Glu as a phosphomimic. The T89E phosphomimic mutation creates an activated allele of Cdc25, cdc25-89w. It has a dominant semi-wee phenotype due to accelerated entry into mitosis. Pyp3 was mutagenized to remove the function of the phosphatase active site and also the putative TOS motif. The Pyp3 active site is essential for its role in cell cycle initiation. It is also essential for the genetic interaction with eIF4E, tif1. Removal of a putative Pyp3 TOS motif affects the Pyp3 localization to cytoplasmic foci following co-overexpression of eIF4E. Similar localization occurs in response to heat stress. These results make important contributions to the understanding of mitotic initiation, and link between cell growth and division. / Thesis (Master, Biology) -- Queen's University, 2013-09-12 14:40:40.384
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