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International Journal of Pediatrics (1)
Nucleic Acids Research (1)
Botting, C H (1)
Hay, R T (1)
Jamieson, L. M. (1)
Mills, H. (1)
Misan, G. (1)
Parker, E J (1)
Parker, E. J. (1)
Richards, L. (1)
Russell, A. (1)
Shearer, M. (1)
Webster, A (1)
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Planning, Implementing, and Evaluating a Program to Address the Oral Health Needs of Aboriginal Children in Port Augusta, Australia
Jamieson, L. M.
International Journal of Pediatrics
Aboriginal Australian children experience profound oral health disparities relative to their non-Aboriginal counterparts. In response to community concerns regarding Aboriginal child oral health in the regional town of Port Augusta, South Australia, a child dental health service was established within a Community Controlled Aboriginal Health Service. A partnership approach was employed with the key aims of (1) quantifying rates of dental service utilisation, (2) identifying factors influencing participation, and (3) planning and establishing a program for delivery of Aboriginal children's dental services that would increase participation and adapt to community needs. In planning the program, levels of participation were quantified and key issues identified through semistructured interviews. After 3.5 years, the participation rate for dental care among the target population increased from 53 to 70 percent. Key areas were identified to encourage further improvements and ensure sustainability in Aboriginal child oral health in this regional location.
Adenovirus DNA polymerase: domain organisation and interaction with preterminal protein.
Botting, C H
Hay, R T
Nucleic Acids Research
Adenovirus DNA polymerase is one of three viral proteins and two cellular proteins required for replication of the adenovirus genome. During initiation of viral DNA synthesis the viral DNA polymerase transfers dCMP onto the adenovirus preterminal protein, to which it is tightly bound. The domain structure of the 140 kDa DNA polymerase has been probed by partial proteolysis and the sites of proteolytic cleavage determined by N-terminal sequencing. At least four domains can be recognised within the DNA polymerase. Adenovirus preterminal protein interacts with three of the four proteolytically derived domains. This was confirmed by cloning and expression of each of the individual domains. These data indicate that, like other members of the pol alpha family of DNA polymerases, the adenovirus DNA polymerase has a multidomain structure and that interaction with preterminal protein takes place with non-contiguous regions of the polypeptide chain over a large surface area of the viral DNA polymerase.
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