School of Molecular and Biomedical Science

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https://hdl.handle.net/2440/300
Comprising the disciplines of biochemistry, genetics, physiology, microbiology and immunology.

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Browsing School of Molecular and Biomedical Science by Author "A.P.T. Patent and Trade Mark Attorneys"

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    Altered insulin-like growth factor binding proteins
    (2009) Forbes, B.; University of Adelaide; A.P.T. Patent and Trade Mark Attorneys
    Altered IGFBPs are able to bind IGF but the release is inhibited by resistance to protease cleavage and/or reduced binding to extracellular matrix (ECM). Alterations have been made in IGFBP-2 to the linker domain in particular and two amino acid motifs found to be important for ECM binding. IGF-1 mediated proliferation of cancer cells have been inhibited by the use of these altered IGFBPs.
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    Altered Insulin-Like Growth Factor binding Proteins
    (2010) Forbes, B.; University of Adelaide; A.P.T. Patent and Trade Mark Attorneys
    Altered IGFBPs are able to bind IGF but the release is inhibited by resistance to protease cleavage and/or reduced binding to extracellular matrix (ECM). Alterations have been made in IGFBP-2 to the linker domain in particular and two amino acid motifs found to be important for ECM binding. IGF-1 mediated proliferation of cancer cells have been inhibited by the use of these altered IGFBPs.
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    Altered Insulin-Like Growth Factor binding Proteins
    (2008) Forbes, B.; University of Adelaide; A.P.T. Patent and Trade Mark Attorneys
    Disclosed are altered Insulin-like Growth Factor Binding Protein molecules able to effect binding of IGF-I or IGF-II with high affinity characterised in having an inhibited release of IGF on contact with extracellular matrix and exposure to a protease. Also disclosed are nucleic acids encoding the altered IGFBP molecules, a host cell carrying that nucleic acid, and methods of reducing IGF mediated proliferation of a population of cancerous cells.
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    Asparagine Hydroxylation of the CAD Domain of a HIF Protein
    (2009) Whitelaw, M.; Peet, D.; Karttunen, S.; Lando, D.; Gorman, J.; ARI Pty Ltd; A.P.T. Patent and Trade Mark Attorneys
    A target asparagine residue of HIF 1 alpha and 2 alpha is hydroxylated at high oxygen tension to render HIF as a weak transcription factor. An asparagine hydroxylase hydroxylation motif and binding motif is proposed. A method of screening for agonists or antagonists of an asparagine hydroxylase is also proposed and involves mixing peptides or proteins having the hydroxylation and or the binding motif with asparagine hydroxylase and a candidate agonist or antagonist. The extent of inhibition or enhancement of binding; level of asparagine hydroxylation or transactivation may be measured depending on the nature of the protein or peptide. Additionally altered proteins resistant to hydroxylation are described as are nucleic acids encoding such proteins.
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    Cytotoxin with a Subtilase Domain
    (2010) Paton, J.; Morona, R.; Paton, A.; ARI Pty Ltd; A.P.T. Patent and Trade Mark Attorneys
    A member of a new class of bacterial toxin has been isolated and characterised. The bacterial toxin is of the AB₅ type and is characterised in that it has a subtilase domain. It is cytotoxic to Vero cells, and toxicity in vivo in mice occurs in a number of different sites. Mutation of the serine active residue results in greater than 99% reduction in activity. The protein has been purified and antibodies have been prepared for both the A subunit and B subunits, and ELISA detection methods have been developed. The nucleic acid sequence has been determined and primers specific for the toxin have been used for a preliminary screen of a range of patient samples to ascertain the extent to which the toxin is present.