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| Preview | Issue Date | Title | Author(s) |
| 2008 | Amyloid fibril formation by bovine milk αs₂-casein occurs under physiological conditions yet is prevented by its natural counterpart, αs₁-casein | Thorn, D.; Ecroyd, H.; Sunde, M.; Poon, S.; Carver, J. |
| 2014 | Amyloid fibril formation by β-Casein and its influence factor | Liu, J.; Carver, J.; Thorn, D. |
| 2012 | Amyloid-β oligomers are sequestered by both intracellular and extracellular chaperones | Narayan, P.; Meehan, S.; Carver, J.; Wilson, M.; Dobson, C.; Klenerman, D. |
| 2011 | Binding of the molecular chaperone alpha B-crystallin to A beta amyloid fibrils Inhibits fibril elongation | Shammas, S.; Waudby, C.; Wang, S.; Buell, A.; Knowles, T.; Ecroyd, H.; Welland, M.; Carver, J.; Dobson, C.; Meehan, S. |
| 2000 | Caerin 4.1, an antibiotic peptide from the Australian Tree Frog, Litoria caerulea. The N.M.R.-derived solution structure | Chia, C.; Carver, J.; Lindner, R.; Bowie, J.; Wong, H.; Lie, W. |
| 2005 | Casein proteins as molecular chaperones | Morgan, P.; Treweek, T.; Lindner, R.; Price, W.; Carver, J. |
| 2000 | Clusterin is an ATP-independent chaperone with broad specificity that stabilizes stressed proteins in a folding-competent state | Poon, S.; Easterbrook-Smith, S.; Rybchyn, M.; Carver, J.; Wilson, M. |
| 2002 | Clusterin is an extracellular chaperone that specifically interacts with slowly aggregating proteins on their off-folding pathway | Poon, S.; Treweek, T.; Wilson, M.; Easterbrook-Smith, S.; Carver, J. |
| 2004 | Host-defence peptides of Australian anurans: structure, mechanism of action and evolutionary significance | Sorrell, M.; Pukala, T.; Brinkworth, C.; Maselli, V.; Bowie, J.; Tyler, M.; Booker, G.; Wallace, J.; Carver, J.; Separovic, F.; Doyle, J.; Llewellyn, L. |
| 2003 | Intracellular protein unfolding and aggregation: the role of small heat-shock chaperone proteins | Treweek, T.; Morris, A.; Carver, J. |
| 2004 | Investigating the importance of the flexible hinge in caerin 1.1: Solution structures and activity of two synthetically modified caerin peptides | Pukala, T.; Brinkworth, C.; Carver, J.; Bowie, J. |
| 2013 | Invited review: Caseins and the casein micelle: their biological functions, structures, and behavior in foods | Holt, C.; Carver, J.; Ecroyd, H.; Thorn, D. |
| 2000 | Maculatin 1.1, an anti-microbial peptide from the Australian tree frog, Litoria genimaculata: Solution structure and biological activity | Chia, C.; Carver, J.; Mulhern, T.; Bowie, J. |
| 2002 | Mildly acidic pH activates the extracellular molecular chaperone clusterin | Poon, S.; Rybchyn, M.; Eastbrook-Smith, S.; Carver, J.; Pankhurst, G.; Wilson, M. |
| 2007 | Monitoring the prevention of amyloid fibril formation by a-crystallin: Temperature dependence and the nature of the aggregating species | Rekas, A.; Jankova, L.; Thorn, D.; Cappai, R.; Carver, J. |
| 2000 | Mouse Hsp25, a small heat-shock protein. The role of its C-terminal extension in oligomerization and chaperone action | Lindner, R.; Carver, J.; Ehrnsperger, M.; Buchner, J.; Esposito, G.; Behlke, J.; Lutsch, G.; Kotlyarov, A.; Gaestel, M. |
| 2003 | nNOS inhibition, antimicrobial and anticancer activity of the amphibian skin peptide, citropin 1.1 and synthetic modifications | Doyle, J.; Brinkworth, C.; Wegener, K.; Carver, J.; Llewellyn, L.; Olver, I.; Bowie, J.; Wabnitz, P.; Tyler, M. |
| 2000 | Non-oxidative modification of lens crystallins by kynurenine. A novel post-translational protein modification with possible relevance to ageing and cataract | Garner, B.; Shaw, D.; Lindner, J.; Carver, J.; Truscott, R. |
| 2000 | Polypeptide modification and cross-linking by oxidized 3-hydroxykynurenine | Aquilina, J.; Carver, J.; Truscott, R. |
| 2018 | Role of salt bridges in the dimer interface of 14-3-3ζ in dimer dynamics, N-terminal α-helical order, and molecular chaperone activity | Woodcock, J.; Goodwin, K.; Sandow, J.; Coolen, C.; Perugini, M.; Webb, A.; Pitson, S.; Lopez, A.; Carver, J. |
