Electrochemistry of nonconjugated proteins and glycoproteins. Toward sensors for biomedicine and glycomics

E Paleček, J Tkáč, M Bartosik, T Bertók… - Chemical …, 2015 - ACS Publications
The present advances in biology are related to progress in genomics, proteomics, and other
“-omics”, including glycomics, working with a large amount of data regarding human and …

The interplay between alpha-synuclein clearance and spreading

T Lopes da Fonseca, A Villar-Piqué, TF Outeiro - Biomolecules, 2015 - mdpi.com
Parkinson's Disease (PD) is a complex neurodegenerative disorder classically
characterized by movement impairment. Pathologically, the most striking features of PD are …

Lipid vesicles trigger α-synuclein aggregation by stimulating primary nucleation

C Galvagnion, AK Buell, G Meisl, TCT Michaels… - Nature chemical …, 2015 - nature.com
Abstract α-Synuclein (α-syn) is a 140-residue intrinsically disordered protein that is involved
in neuronal and synaptic vesicle plasticity, but its aggregation to form amyloid fibrils is the …

Fast flow microfluidics and single-molecule fluorescence for the rapid characterization of α-synuclein oligomers

MH Horrocks, L Tosatto, AJ Dear, GA Garcia… - Analytical …, 2015 - ACS Publications
α-Synuclein oligomers can be toxic to cells and may be responsible for cell death in
Parkinson's disease. Their typically low abundance and highly heterogeneous nature …

Biophysical insight into the anti-amyloidogenic behavior of taurine

SK Chaturvedi, P Alam, JM Khan, MK Siddiqui… - International journal of …, 2015 - Elsevier
In this work, we investigated the inhibitory ability of taurine on the aggregation of Human
serum albumin (HSA) and also examined how it controls the kinetic parameters of the …

The H50Q mutation induces a 10-fold decrease in the solubility of α-synuclein

R Porcari, C Proukakis, CA Waudby… - Journal of Biological …, 2015 - ASBMB
The conversion of α-synuclein from its intrinsically disordered monomeric state into the
fibrillar cross-β aggregates characteristically present in Lewy bodies is largely unknown. The …

Parkinson disease mutant E46K enhances α-synuclein phosphorylation in mammalian cell lines, in yeast, and in vivo

MK Mbefo, MB Fares, K Paleologou, A Oueslati… - Journal of Biological …, 2015 - ASBMB
Background: Little is known about the effect of PD-linked mutations on α-synuclein (α-syn)
phosphorylation. Results: The E46K mutation increases α-syn phosphorylation at Ser-129 …

Single fibril growth kinetics of α-synuclein

MM Wördehoff, O Bannach, H Shaykhalishahi… - Journal of molecular …, 2015 - Elsevier
Neurodegenerative disorders associated with protein misfolding are fatal diseases that are
caused by fibrillation of endogenous proteins such as α-synuclein (α-syn) in Parkinson's …

Toxic oligomeric alpha-synuclein variants present in human Parkinson's disease brains are differentially generated in mammalian cell models

W Xin, S Emadi, S Williams, Q Liu, P Schulz, P He… - Biomolecules, 2015 - mdpi.com
Misfolding and aggregation of α-synuclein into toxic soluble oligomeric α-synuclein
aggregates has been strongly correlated with the pathogenesis of Parkinson's disease (PD) …

Hsp31 is a stress response chaperone that intervenes in the protein misfolding process

C Tsai, K Aslam, HM Drendel, JM Asiago… - Journal of Biological …, 2015 - ASBMB
The Saccharomyces cerevisiae heat shock protein Hsp31 is a stress-inducible homodimeric
protein that is involved in diauxic shift reprogramming and has glyoxalase activity. We show …