Publications
Chaperones suppress the toxicity of aberrant protein aggregates. Molecular insight into the mechanism of action
FEBS JOURNAL
(2012)
279
224
Molecular mechanisms used by chaperones to reduce the toxicity of aberrant protein oligomers
Proc Natl Acad Sci U S A
(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)
A comparison of the biochemical modifications caused by toxic and non-toxic protein oligomers in cells
J Cell Mol Med
(2011)
15
2106
Chaperones suppress protein oligomer toxicity: Insight into the molecular mechanism of action
FEBS JOURNAL
(2011)
278
117
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
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)
Role of aggregation conditions in structure, and toxicity of Yeast Hexokinase aggregates
FEBS JOURNAL
(2010)
277
254
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)
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