
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.
– European Journal of Medicinal Chemistry
(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
– Biol Chem
(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 chemical biology
(2014)
9,
2309
(DOI: 10.1021/cb500505m)
Transthyretin suppresses the toxicity of oligomers formed by misfolded proteins in vitro
– Biochim Biophys 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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