1. Adelaide Research & Scholarship

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PreviewIssue DateTitleAuthor(s)
2003The solution structures and activity of caerin 1.1 and caerin 1.4 in aqueous trifluoroethanol and dodecylphosphocholine micellesWegener, K.; Carver, J.; Bowie, J.
2014Amyloid fibril formation by β-Casein and its influence factorLiu, J.; Carver, J.; Thorn, D.
2003The solution structure of frenatin 3, a neuronal nitric oxide synthase inhibitor from the giant tree frog, Litoria infrafrenataBrinkworth, C.; Carver, J.; Wegener, K.; Doyle, J.; Llewellyn, L.; Bowie, J.
2000Maculatin 1.1, an anti-microbial peptide from the Australian tree frog, Litoria genimaculata: Solution structure and biological activityChia, C.; Carver, J.; Mulhern, T.; Bowie, J.
2004Investigating the importance of the flexible hinge in caerin 1.1: Solution structures and activity of two synthetically modified caerin peptidesPukala, T.; Brinkworth, C.; Carver, J.; Bowie, J.
1997The Solution Structure Activity of Caetin 1.1Wong, H.; Bowie, J.; Carver, J.
2010The two-faced nature of small heat-shock proteins: Amyloid fibril assembly and the inhibition of fibril formation. Relevance to disease statesEcroyd, H.; Meehan, S.; Carver, J.; Simon, S.; Arrigo, A.
2001The molecular chaperone, α-crystallin, inhibits amyloid formation by apolipoprotein C-IIHatters, D.; Lindner, R.; Carver, J.; Howlett, G.
1998The peptide chemical arsenals of Australian tree frogs of the genus LitoriaBowie, J.; Chia, C.; Tyler, M.; Carver, J.; Wallace, J.
2000Caerin 4.1, an antibiotic peptide from the Australian Tree Frog, Litoria caerulea. The N.M.R.-derived solution structureChia, C.; Carver, J.; Lindner, R.; Bowie, J.; Wong, H.; Lie, W.

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