
Royal Society Dororthy Hodgkin Research Fellow
Publications
Site-directed mutations in the C-terminal extension of human αB-crystallin affect chaperone function and block amyloid fibril formation
– PLoS ONE
(2007)
2,
e1046
(doi: 10.1371/journal.pone.0001046)
Characterisation of Amyloid Fibril Formation by Small Heat-shock Chaperone Proteins Human αA-, αB- and R120G αB-Crystallins
– Journal of Molecular Biology
(2007)
372,
470
(doi: 10.1016/j.jmb.2007.06.060)
Kinetics and thermodynamics of amyloid formation from direct measurements of fluctuations in fibril mass.
– Proceedings of the National Academy of Sciences of the United States of America
(2007)
104,
10016
(doi: 10.1073/pnas.0610659104)
The extracellular chaperone clusterin influences amyloid formation and toxicity by interacting with prefibrillar structures
– The FASEB Journal
(2007)
21,
2312
(doi: 10.1096/fj.06-7986com)
Mimicking phosphorylation of αB-crystallin affects its chaperone activity
– Biochem J
(2006)
401,
129
(doi: 10.1042/BJ20060981)
Amyloid Fibril Formation by Bovine Milk κ-Casein and Its Inhibition by the Molecular Chaperones αS- and β-Casein †
– Biochemistry
(2005)
44,
17027
(doi: 10.1021/bi051352r)
Amyloid fibril formation by lens crystallin proteins and its implications for cataract formation.
– J Biol Chem
(2003)
279,
3413
(doi: 10.1074/jbc.m308203200)
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