Search


Current filters:

Start a new search
Add filters:

Use filters to refine the search results.


Results 1-10 of 10 (Search time: 0.002 seconds).
  • previous
  • 1
  • next
Item hits:
PreviewIssue DateTitleAuthor(s)
2014Amyloid fibril formation by β-Casein and its influence factorLiu, J.; Carver, J.; Thorn, D.
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.
2012The chaperone activity of α-synuclein: Utilizing deletion mutants to map its interaction with target proteinsRekas, A.; Ahn, K.; Kim, J.; 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.
2015The membrane-active amphibian peptide caerin 1.8 inhibits fibril formation of amyloid β1-42Liu, Y.; Wang, T.; Calabrese, A.; Carver, J.; Cummins, S.; Bowie, J.
2011Binding of the molecular chaperone alpha B-crystallin to A beta amyloid fibrils Inhibits fibril elongationShammas, S.; Waudby, C.; Wang, S.; Buell, A.; Knowles, T.; Ecroyd, H.; Welland, M.; Carver, J.; Dobson, C.; Meehan, S.
2010The quaternary organization and dynamics of the molecular chaperone HSP26 are thermally regulatedBenesch, J.; Aquilina, J.; Baldwin, A.; Rekas, A.; Stengel, F.; Lindner, R.; Basha, E.; Devlin, G.; Horwitz, J.; Vierling, E.; Carver, J.; Robinson, C.
2010The interaction of αB-crystallin with mature α-synuclein amyloid fibrils inhibits their elongationWaudby, C.; Knowles, T.; Devlin, G.; Skepper, J.; Ecroyd, H.; Carver, J.; Welland, M.; Christodoulou, J.; Dobson, C.; Meehan, S.
2012Amyloid-β oligomers are sequestered by both intracellular and extracellular chaperonesNarayan, P.; Meehan, S.; Carver, J.; Wilson, M.; Dobson, C.; Klenerman, D.