4 results on '"Dianne Watt"'
Search Results
2. Australian Validation of the Hierarchical Personality Inventory for Children (HiPIC)
- Author
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Laura Hopkinson, Dianne Watt, and John Roodenburg
- Subjects
Flemish ,Extraversion and introversion ,Developmental and Educational Psychology ,language ,Alternative five model of personality ,16PF Questionnaire ,Big Five personality traits and culture ,Personality Assessment Inventory ,Big Five personality traits ,Psychology ,Exploratory factor analysis ,language.human_language ,Developmental psychology - Abstract
The Hierarchical Personality Inventory for Children (HiPIC) is a developmentally appropriate parent-report measure of the Five Factor Model (FFM) that has been validated in several European languages but only recently in English. The English translation of the HiPIC was evaluated in an Australian context. Parent-rated HiPIC scores were obtained for 202 children (aged 5–14 years) via an online survey. Exploratory factor analysis indicated five factors that appeared reasonably congruent with the original Flemish HiPIC structure, though with some apparent differences particularly in regard to the Extraversion and Benevolence facets. A Procrustes targeted rotation was used to evaluate the congruence with the original Flemish structure. This indicated encouragingly high congruences for the overall model (.97), as well as high facet and factor congruence (.92–.99). These findings can be taken to reflect the robust nature of the HiPIC model, validating the instrument and more specifically confirming its applicability for use in practice and research investigating children's development and wellbeing in Australia.
- Published
- 2014
- Full Text
- View/download PDF
3. [Untitled]
- Author
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Bruce A. Philip, Dianne Watt, William A. Laing, Michelle A. Wright, H.S. Gatehouse, Colleen Murray, Gáabor L. Lövei, L. N. Gatehouse, Lynn M. Watson, Louise A. Malone, Elisabeth P. J. Burgess, Ngaire P. Markwick, April L. Shannon, John T. Christeller, Margaret M. Phung, and Valentina Mett
- Subjects
chemistry.chemical_classification ,Chymotrypsin ,biology ,Trypsin inhibitor ,Nicotiana tabacum ,fungi ,Helicoverpa armigera ,Trypsin ,biology.organism_classification ,Aminopeptidase ,Enzyme ,chemistry ,Biochemistry ,Enzyme inhibitor ,Genetics ,medicine ,biology.protein ,Animal Science and Zoology ,Agronomy and Crop Science ,Biotechnology ,medicine.drug - Abstract
The cDNA for bovine spleen trypsin inhibitor (SI), a homologue of bovine pancreatic trypsin inhibitor (BPTI), including the natural mammalian presequence was expressed in tobacco using Agrobacterium tumefaciens-mediated transformation. Stable expression required the N-terminal targeting signal presequence although subcellular localization was not proven. SI was found to exist as two forms, one coinciding with authentic BPTI on western blots and the second marginally larger due to retention of the C-terminal peptide. Both were retained on a trypsin-agarose affinity gel and had inhibitory activity. Newly emergent leaves contained predominantly the large form whereas senescent leaves had little except the fully processed form present. Intermediate-aged leaves showed a gradual change indicating that a slow processing of the inhibitor peptide was occurring. The stability of SI was shown by the presence of protein at high levels in completely senescent leaves. Modifications to the cDNA (3' and 5' changes and minor codon changes) resulted in a 20-fold variation in expression. Expression of modified SI in transgenic tobacco leaves at 0.5% total soluble protein reduced both survival and growth of Helicoverpa armigera larvae feeding on leaves from the late first instar. In larvae surviving for 8 days, midgut trypsin activity was reduced in SI-tobacco fed larvae, while chymotrypsin activity was increased. Activities of leucine aminopeptidase and elastase-like chymotrypsin remained unaltered. The use of SI as an insect resistance factor is discussed.
- Published
- 2002
- Full Text
- View/download PDF
4. The expression of a mammalian proteinase inhibitor, bovine spleen trypsin inhibitor in tobacco and its effects on Helicoverpa armigera larvae
- Author
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John T, Christeller, Elisabeth P J, Burgess, Valentina, Mett, Heather S, Gatehouse, Ngaire P, Markwick, Colleen, Murray, Louise A, Malone, Michelle A, Wright, Bruce A, Philip, Dianne, Watt, Laurence N, Gatehouse, Gábor L, Lövei, April L, Shannon, Margaret M, Phung, Lynn M, Watson, and William A, Laing
- Subjects
Lepidoptera ,Agrobacterium tumefaciens ,Larva ,Genetic Vectors ,Tobacco ,Animals ,Cattle ,Trypsin ,Pest Control, Biological ,Plants, Genetically Modified ,Trypsin Inhibitors ,Spleen - Abstract
The cDNA for bovine spleen trypsin inhibitor (SI), a homologue of bovine pancreatic trypsin inhibitor (BPTI), including the natural mammalian presequence was expressed in tobacco using Agrobacterium tumefaciens-mediated transformation. Stable expression required the N-terminal targeting signal presequence although subcellular localization was not proven. SI was found to exist as two forms, one coinciding with authentic BPTI on western blots and the second marginally larger due to retention of the C-terminal peptide. Both were retained on a trypsin-agarose affinity gel and had inhibitory activity. Newly emergent leaves contained predominantly the large form whereas senescent leaves had little except the fully processed form present. Intermediate-aged leaves showed a gradual change indicating that a slow processing of the inhibitor peptide was occurring. The stability of SI was shown by the presence of protein at high levels in completely senescent leaves. Modifications to the cDNA (3' and 5' changes and minor codon changes) resulted in a 20-fold variation in expression. Expression of modified SI in transgenic tobacco leaves at 0.5% total soluble protein reduced both survival and growth of Helicoverpa armigera larvae feeding on leaves from the late first instar. In larvae surviving for 8 days, midgut trypsin activity was reduced in SI-tobacco fed larvae, while chymotrypsin activity was increased. Activities of leucine aminopeptidase and elastase-like chymotrypsin remained unaltered. The use of SI as an insect resistance factor is discussed.
- Published
- 2002
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