|Amyloid pores from pathogenic mutations|
HA Lashuel, D Hartley, BM Petre, T Walz, PT Lansbury
Nature 418 (6895), 291-291, 2002
|The many faces of α-synuclein: from structure and toxicity to therapeutic target|
HA Lashuel, CR Overk, A Oueslati, E Masliah
Nature Reviews Neuroscience 14 (1), 38-48, 2013
|The UCH-L1 gene encodes two opposing enzymatic activities that affect α-synuclein degradation and Parkinson's disease susceptibility|
Y Liu, L Fallon, HA Lashuel, Z Liu, PT Lansbury Jr
Cell 111 (2), 209-218, 2002
|α-Synuclein, especially the Parkinson's disease-associated mutants, forms pore-like annular and tubular protofibrils|
HA Lashuel, BM Petre, J Wall, M Simon, RJ Nowak, T Walz, ...
Journal of molecular biology 322 (5), 1089-1102, 2002
|A century-old debate on protein aggregation and neurodegeneration enters the clinic|
PT Lansbury, HA Lashuel
Nature 443 (7113), 774-779, 2006
|Amyloidogenic protein–membrane interactions: mechanistic insight from model systems|
SM Butterfield, HA Lashuel
Angewandte Chemie International Edition 49 (33), 5628-5654, 2010
|α-Synuclein in central nervous system and from erythrocytes, mammalian cells, and Escherichia coli exists predominantly as disordered monomer|
B Fauvet, MK Mbefo, MB Fares, C Desobry, S Michael, MT Ardah, E Tsika, ...
Journal of Biological Chemistry 287 (19), 15345-15364, 2012
|Are amyloid diseases caused by protein aggregates that mimic bacterial pore-forming toxins?|
HA Lashuel, PT Lansbury
Quarterly reviews of biophysics 39 (ARTICLE), 167-201, 2006
|Inhibiting transthyretin amyloid fibril formation via protein stabilization|
GJ Miroy, Z Lai, HA Lashuel, SA Peterson, C Strang, JW Kelly
Proceedings of the National Academy of Sciences 93 (26), 15051-15056, 1996
|Protofilaments, filaments, ribbons, and fibrils from peptidomimetic self-assembly: implications for amyloid fibril formation and materials science|
HA Lashuel, SR LaBrenz, L Woo, LC Serpell, JW Kelly
Journal of the American Chemical Society 122 (22), 5262-5277, 2000
|Role of post-translational modifications in modulating the structure, function and toxicity of α-synuclein: implications for Parkinson’s disease pathogenesis and therapies|
A Oueslati, M Fournier, HA Lashuel
Progress in brain research 183, 115-145, 2010
|Phosphorylation at Ser-129 but not the phosphomimics S129E/D inhibits the fibrillation of α-synuclein|
KE Paleologou, AW Schmid, CC Rospigliosi, HY Kim, GR Lamberto, ...
Journal of Biological Chemistry 283 (24), 16895-16905, 2008
|Mixtures of wild-type and a pathogenic (E22G) form of Aβ40 in vitro accumulate protofibrils, including amyloid pores|
HA Lashuel, DM Hartley, BM Petre, JS Wall, MN Simon, T Walz, ...
Journal of molecular biology 332 (4), 795-808, 2003
|Quaternary structure, protein dynamics, and synaptic function of SAP97 controlled by L27 domain interactions|
T Nakagawa, K Futai, HA Lashuel, I Lo, K Okamoto, T Walz, Y Hayashi, ...
Neuron 44 (3), 453-467, 2004
|Phosphorylation at S87 is enhanced in synucleinopathies, inhibits α-synuclein oligomerization, and influences synuclein-membrane interactions|
KE Paleologou, A Oueslati, G Shakked, CC Rospigliosi, HY Kim, ...
Journal of Neuroscience 30 (9), 3184-3198, 2010
|Discovery of inhibitors that elucidate the role of UCH-L1 activity in the H1299 lung cancer cell line|
Y Liu, HA Lashuel, S Choi, X Xing, A Case, J Ni, LA Yeh, GD Cuny, ...
Chemistry & biology 10 (9), 837-846, 2003
|The ratio of monomeric to aggregated forms of Aβ40 and Aβ42 is an important determinant of amyloid-β aggregation, fibrillogenesis, and toxicity|
A Jan, O Gokce, R Luthi-Carter, HA Lashuel
Journal of Biological Chemistry 283 (42), 28176-28189, 2008
|Inhibiting transthyretin conformational changes that lead to amyloid fibril formation|
SA Peterson, T Klabunde, HA Lashuel, H Purkey, JC Sacchettini, JW Kelly
Proceedings of the National Academy of Sciences 95 (22), 12956-12960, 1998
|Amyloid-β aggregates cause alterations of astrocytic metabolic phenotype: impact on neuronal viability|
I Allaman, M Gavillet, M Bélanger, T Laroche, D Viertl, HA Lashuel, ...
Journal of Neuroscience 30 (9), 3326-3338, 2010
|Characterization of the transthyretin acid denaturation pathways by analytical ultracentrifugation: implications for wild-type, V30M, and L55P amyloid fibril formation|
HA Lashuel, Z Lai, JW Kelly
Biochemistry 37 (51), 17851-17864, 1998