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A public health approach to reducing diarrhoea caused by infectious diseases in children less than 5 yers of ageMorse, Tracy Dawn January 2006 (has links)
No description available.
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Detection and characterisation by molecular methods of the protozoan parasite Cryptosporidium parvumThompson, Heather P. January 2005 (has links)
No description available.
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Epidemiology of cryptorchidism and hypospadias in the Northern Region of England 1985-2002Abdullah, Nor Aini January 2007 (has links)
No description available.
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Genetics of susceptibility to malaria and leishmaniasisCarpenter, Danielle January 2003 (has links)
No description available.
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Host specificity and molecular detection of Cryptosporidium hominis and Cryptosporidium parvumGiles, Michaela January 2006 (has links)
No description available.
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Cryptosporidiosis in Jeddah City, Saudi ArabiaAl-Braikan, Faten January 2004 (has links)
No description available.
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An integrated approach to unravelling malaria cell signalling pathwaysGraciotti, Michele January 2013 (has links)
In the current thesis we analyse protein phosphorylation pathways in P. falciparum, the protozoa responsible for the most virulent form of malaria in order to both understand the role and scope of this protein modification in the parasite, and to explore its feasibility as a new drug target. With the aim to map phosphorylation pathways controlled by P. falciparum Casein Kinase 2 (PfCK2), we developed a new chemical-biological approach based on γ-modified ATP analogues bearing reporting groups on the transferred phosphate in order to selectively tag CK2 substrates. Despite being able to efficiently synthesise a small set of analogues, the data presented here shows that the P-N linkage bond between the nucleotide and the tag is stable during the assay conditions but not during the product analysis due to its acidic liability (e.g. with HPLC, MALDI); suggesting that a different type of linkage should be chosen in the future. Detailed characterisation studies of the parasite PfCK2 presented here showed a number of important features differing from human CK2. Docking analyses with a CK2 inhibitor showed that the PfCK2 ATP binding pocket is smaller than human CK2 due to the presence of Val116 and Leu45 which in the human kinase are replaced by more bulky isoleucine residues: Ile120 and Ile49. The difference between the human and parasite CK2 orthologues extends further to mechanisms of activation and regulation. Shown here is the autophosphorylation of PfCK2 that, unlike the human orthologue, occurs within subdomain I at Thr63. This autophosphorylation is essential for full catalytic activity. In addition we also showed that Thr63 phosphorylation regulates the interaction between the calalytic α-subunit and the regulatory β2-subunit. Here, we also presented evidence for tyrosine phosphorylated proteins in parasite infected red blood cells. PfCK2 can act as a dual specificity kinase phosphorylating P. falciparum Minichromosome Maintenance protein 2 (PfMCM2) on Tyr16 in vitro. It is therefore possible that PfCK2 may contribute to tyrosine phosphorylation within the parasite. Finally, we also reported a study regarding MCM2-Ser13 phosphorylation which successfully identified PfCK1 as the kinase responsible for this event.
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