
Publications
Molecular mechanisms used by chaperones to reduce the toxicity of aberrant protein oligomers
Proceedings of the National Academy of Sciences of the United States of America
(2012)
109
12479
(doi: 10.1073/pnas.1117799109)
Glycosaminoglycans (GAGs) suppress the toxicity of HypF-N prefibrillar aggregates.
Journal of molecular biology
(2012)
421
616
(doi: 10.1016/j.jmb.2012.02.007)
Chaperones suppress the toxicity of aberrant protein aggregates. Molecular insight into the mechanism of action
FEBS JOURNAL
(2012)
279
224
A comparison of the biochemical modifications caused by toxic and non‐toxic protein oligomers in cells
Journal of Cellular and Molecular Medicine
(2011)
15
2106
Chaperones suppress protein oligomer toxicity: Insight into the molecular mechanism of action
FEBS JOURNAL
(2011)
278
117
The induction of α-helical structure in partially unfolded HypF-N does not affect its aggregation propensity.
Protein Eng Des Sel
(2011)
24
553
(doi: 10.1093/protein/gzr018)
Large Proteins Have a Great Tendency to Aggregate but a Low Propensity to Form Amyloid Fibrils
PloS one
(2011)
6
e16075
(doi: 10.1371/journal.pone.0016075)
Misfolded protein oligomers formed by a model protein mimic the effect of a-beta oligomers on synaptic plasticity involved in Alzheimer's disease
FEBS JOURNAL
(2011)
278
481
Low-Level Expression of a Folding-Incompetent Protein in Escherichia coli: Search for the Molecular Determinants of Protein Aggregation In Vivo
Journal of molecular biology
(2010)
398
600
(doi: 10.1016/j.jmb.2010.03.030)
A causative link between the structure of aberrant protein oligomers and their toxicity
Nature Chemical Biology
(2010)
6
140
(doi: 10.1038/nchembio.283)
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