Publications
Chaperones as Suppressors of Protein Misfolded Oligomer Toxicity.
Frontiers in Molecular Neuroscience
(2017)
10
98
(doi: 10.3389/fnmol.2017.00098)
Attenuating the Toxicity of Amyloid-Beta Aggregation with Specific Species
Biophysical Journal
(2017)
112
494A
(doi: 10.1016/j.bpj.2016.11.2673)
Systematic development of small molecules to inhibit specific microscopic steps of Aβ42 aggregation in Alzheimer’s disease
Proceedings of the National Academy of Sciences
(2016)
114
E200
(doi: 10.1073/pnas.1615613114)
Bis(indolyl)phenylmethane derivatives are effective small molecules for inhibition of amyloid fibril formation by hen lysozyme.
Eur J Med Chem
(2016)
124
361
(doi: 10.1016/j.ejmech.2016.08.056)
Effect of molecular chaperones on aberrant protein oligomers in vitro: super-versus sub-stoichiometric chaperone concentrations
Biological Chemistry
(2016)
397
401
(doi: 10.1515/hsz-2015-0250)
SERS Detection of Amyloid Oligomers on Metallorganic-Decorated Plasmonic Beads
ACS applied materials & interfaces
(2015)
7
9420
(doi: 10.1021/acsami.5b01056)
Toxicity of protein oligomers is rationalized by a function combining size and surface hydrophobicity
ACS Chem Biol
(2014)
9
2309
(doi: 10.1021/cb500505m)
Transthyretin suppresses the toxicity of oligomers formed by misfolded proteins in vitro.
Biochimica et biophysica acta
(2013)
1832
2302
(doi: 10.1016/j.bbadis.2013.09.011)
Amyloid-β oligomer synaptotoxicity is mimicked by oligomers of the model protein HypF-N.
Neurobiol Aging
(2013)
34
2100
Salt anions promote the conversion of HypF-N into amyloid-like oligomers and modulate the structure of the oligomers and the monomeric precursor state.
Journal of molecular biology
(2012)
424
132
(doi: 10.1016/j.jmb.2012.09.023)
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