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The application of representational difference analysis and plant differentiationVorster, Barend Juan 19 May 2005 (has links)
Please read the abstract in the section 00front of this document / Dissertation (MSc (Botany))--University of Pretoria, 2005. / Plant Science / unrestricted
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Chloroplast control of nuclear gene expressionSornarajah, Renuka January 1995 (has links)
No description available.
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Physical and transcript map 6p21.2-p21.3Tripodis, Nicholas January 1998 (has links)
No description available.
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A study of the population genetics of nucleopolyhedrovirus infections within infected insectsBull, James Christopher January 2001 (has links)
No description available.
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Towards versatile vectors based on cauliflower mosaic virusNoad, Robert James January 1997 (has links)
No description available.
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Molecular characterization of the mouse cytoglobinChow, Kwok-fai, Joseph, January 2006 (has links)
Thesis (Ph. D.)--University of Hong Kong, 2007. / Title proper from title frame. Also available in printed format.
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Transcriptional regulation of the shaker homolog Kv3Draper, Moon 28 August 2008 (has links)
Not available / text
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Characterisation of a phage encoded protein that switches the directionality of ψC31 integraseKhaleel, Thanafez January 2012 (has links)
Integrases (Int) are enzymes that mediate the integration and excision of viral DNA into or out of their hosts‟ chromosomes and can therefore be exploited to integrate or delete genes in a precise way. In order to establish lysogeny, integrase mediates recombination between the bacterial and phage attachment sites, attB and attP respectively to generate an integrated prophage flanked by attL and attR. This reaction occurs in vitro without any need for accessory proteins prompting the question, how does the prophage excise? Phages use accessory proteins, Recombination Directionality Factors, RDFs to control the directionality of integrase. For the serine integrase family, RDFs have been identified for three phages, TP901-1, φRv1 and Bxb1, and there is no detectable sequence conservation between them. This work has identified the φC31 early protein gp3 as the RDF. Gp3 acts stoichiometrically to activate excision and binds to Int in solution and in complex with DNA. Insight into the mechanism of gp3 action has revealed that it is at the synapse level that gp3 switches the directionality of Int. The properties of the gp3+Int driven reaction was found to be similar to that mediated by a previously characterised mutated Int, IntE449K that triggers gp3 independent excision (Rowley et al., 2008). Despite φC31 and φBT1 Ints being only 21% identical in sequence, the gp3 homologues from these phages cross-react. Both the gp3s bind to the last 200 amino acids of C-terminal domain of φC31 Int to activate excision and inhibit integration. Evidence is presented that gp3, on binding to Int, overcomes an innate mechanism that normally prevents synapsis of the excision substrates. These observations could lead to further exploitation of φC31 system as a tool for genome engineering.
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Genome-scale strategies controlling the impact of deleterious mutationsMartincorena, Iñigo January 2012 (has links)
No description available.
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Improving gene annotation of complete viral genomesMills, Ryan E. 08 1900 (has links)
No description available.
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