Publications
Molecular mechanisms used by chaperones to reduce the toxicity of aberrant protein oligomers.
Proceedings of the National Academy of Sciences
(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 nonâtoxic 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
J Mol Biol
(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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