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Results 11-20 of 37 (Search time: 0.005 seconds).
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PreviewIssue DateTitleAuthor(s)
2000Mouse Hsp25, a small heat-shock protein. The role of its C-terminal extension in oligomerization and chaperone actionLindner, R.; Carver, J.; Ehrnsperger, M.; Buchner, J.; Esposito, G.; Behlke, J.; Lutsch, G.; Kotlyarov, A.; Gaestel, M.
2018Role of salt bridges in the dimer interface of 14-3-3ζ in dimer dynamics, N-terminal α-helical order, and molecular chaperone activityWoodcock, J.; Goodwin, K.; Sandow, J.; Coolen, C.; Perugini, M.; Webb, A.; Pitson, S.; Lopez, A.; Carver, J.
2020The molecular chaperone β-casein prevents amorphous and fibrillar aggregation of α-lactalbumin by stabilisation of dynamic disorderSanders, H.M.; Jovcevski, B.; Carver, J.; Pukala, T.L.
2007Monitoring the prevention of amyloid fibril formation by a-crystallin: Temperature dependence and the nature of the aggregating speciesRekas, A.; Jankova, L.; Thorn, D.; Cappai, R.; Carver, J.
2003nNOS inhibition, antimicrobial and anticancer activity of the amphibian skin peptide, citropin 1.1 and synthetic modificationsDoyle, J.; Brinkworth, C.; Wegener, K.; Carver, J.; Llewellyn, L.; Olver, I.; Bowie, J.; Wabnitz, P.; Tyler, M.
2002Clusterin is an extracellular chaperone that specifically interacts with slowly aggregating proteins on their off-folding pathwayPoon, S.; Treweek, T.; Wilson, M.; Easterbrook-Smith, S.; Carver, J.
2012The chaperone activity of α-synuclein: Utilizing deletion mutants to map its interaction with target proteinsRekas, A.; Ahn, K.; Kim, J.; Carver, J.
2008Unravelling the mysteries of protein folding and misfoldingEcroyd, H.; Carver, J.
2016The effect of milk constituents and crowding agents on amyloid fibril formation by κ-caseinLiu, J.; Dehle, F.; Liu, Y.; Bahraminejad, E.; Ecroyd, H.; Thorn, D.; Carver, J.
2013Invited review: Caseins and the casein micelle: their biological functions, structures, and behavior in foodsHolt, C.; Carver, J.; Ecroyd, H.; Thorn, D.