Beth McInnes
Monash University, Clayton campus
7 Papers
81 Citations
Beth McInnes is an academic researcher from Monash University, Clayton campus. The author has contributed to research in topics: Amino acid & Site-directed mutagenesis. The author has an hindex of 6, co-authored 7 publications.
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Papers
Functional significance of amino acid residues within conserved hydrophilic regions in human interferons-α
TL;DR: The abrogation of antiviral activity resulting from amino acid substitutions for the arginine residue at position 33 suggests that this arginin residue is required for binding to the IFN-alpha receptor on the cell surface.
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Structure–Function Studies of Interferons-α: Amino Acid Substitutions at the Conserved Residue Tyrosine 123 in Human Interferon-α1
TL;DR: Analogs of human interferon- α1 (IFN-α1) were created in vitro by site-directed mutagenesis to investigate the structural requirements at amino acid position 123 for binding to the IFN.
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Structure-function studies of human interferons-α: Enhanced activity on human and murine cells
Brian F. Cheetham,Beth McInnes,Theo Mantamadiotis,Peter J. Murray,Per Ålin,Peter Bourke,Anthony W. Linnane,Martin J. Tymms +7 more
TL;DR: The utility of the in vitro mutagenesis and rabbit reticulocyte lysate systems for the investigation of structure-function relationships is illustrated, and knowledge of the biologically active regions and species specificity of the human IFN-α molecule is extended.
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Efficient in vitro expression of interferon alpha analogs using SP6 polymerase and rabbit reticulocyte lysate.
Martin J. Tymms,Beth McInnes +1 more
TL;DR: The use of in vitro expression as a quick and convenient means of screening large numbers of interferon (IFN) analogs generated using in vitro mutagenesis is investigated, and all analogs tested were well expressed in RRL.
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Structure-function studies of interferon-α based on random mutagenesis and expression in vitro☆
TL;DR: An efficient procedure for random chemical mutagenesis was used to create analogs of human interferon (IFN)-alpha 4, suggesting that the integrity of the carboxy terminus is important for the antiproliferative activity of human IFN-alpha 4.
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