Personne
Adrian Schmid
Cette personne n’est plus à l’EPFL
Publications associées (21)
Alpha-synuclein Post-translational Modifications as Potential Biomarkers for Parkinson Disease and Other Synucleinopathies
Hilal Lashuel, Marc Moniatte, Bruno Claude Daniel Fauvet, Adrian Schmid
The development of novel therapies against neurodegenerative disorders requires the ability to detect their early, presymptomatic manifestations in order to enable treatment before irreversible cellular damage occurs. Precocious signs indicative of neurode ...
Amer Soc Biochemistry Molecular Biology Inc2013Deamidation and Transamidation of Substance P by Tissue Transglutaminase Revealed by Electron-Capture Dissociation Fourier Transform Mass Spectrometry (Chem. Eur. J. 2/2011)
Horst Vogel, Yury Tsybin, Luigino Grasso, Adrian Schmid, Luca Fornelli
Tissue transglutaminase (tTGase) catalyzes both deamidation and transamidation of peptides and proteins by using a peptidyl glutamine as primary substrate. A precise consensus sequence for the enzyme is unknown and the ratio between deamidated and transami ...
Wiley-Blackwell2011Tissue Transglutaminase-mediated Glutamine Deamidation of beta-Amyloid Peptide Increases Peptide Solubility, Whereas Enzymatic Cross-linking and Peptide Fragmentation May Serve as Molecular Triggers for Rapid Peptide Aggregation
Horst Vogel, Yury Tsybin, Diego Chiappe, Marc Moniatte, Adrian Schmid, Enrico Condemi
Tissue transglutaminase (TGase) has been implicated in a number of cellular processes and disease states, where the enzymatic actions of TGase may serve in both, cell survival and apoptosis. To date, the precise functional properties of TGase in cell survi ...
American Society for Biochemistry and Molecular Biology2011Phosphorylation at S87 is enhanced in synucleinopathies, inhibits alpha-synuclein oligomerization, and influences synuclein-membrane interactions
Hilal Lashuel, Patrick Aebischer, Bernard Schneider, Diego Chiappe, Marc Moniatte, Adrian Schmid, Magdalena Zweckstetter, Abid Oueslati
Increasing evidence suggests that phosphorylation may play an important role in the oligomerization, fibrillogenesis, Lewy body (LB) formation, and neurotoxicity of alpha-synuclein (alpha-syn) in Parkinson disease. Herein we demonstrate that alpha-syn is p ...
2010Dissecting the mechanisms of tissue transglutaminase-induced cross-linking of alpha-synuclein: implications for the pathogenesis of Parkinson disease
Hilal Lashuel, Diego Chiappe, Marc Moniatte, Adrian Schmid, Ivan Hang
Tissue transglutaminase (tTG) has been implicated in the pathogenesis of Parkinson disease (PD). However, exactly how tTG modulates the structural and functional properties of alpha-synuclein (alpha-syn) and contributes to the pathogenesis of PD remains un ...
American Society for Biochemistry and Molecular Biology2009E46K Parkinson's-linked mutation enhances C-terminal-to-N-terminal contacts in alpha-synuclein
Parkinson's disease (PD) is associated with the deposition of fibrillar aggregates of the protein alpha-synuclein (alphaS) in neurons. Intramolecular contacts between the acidic C-terminal tail of alphaS and its N-terminal region have been proposed to regu ...
Elsevier2009Inhibition of alpha-synuclein fibrillization by dopamine is mediated by interactions with five C-terminal residues and with E83 in the NAC region
Hilal Lashuel, Adrian Schmid, Paolo Carloni, Alessandra Chesi
The interplay between dopamine and alpha-synuclein (AS) plays a central role in Parkinson's disease (PD). PD results primarily from a severe and selective devastation of dopaminergic neurons in substantia nigra pars compacta. The neuropathological hallmark ...
Public Library of Science2008Phosphorylation at Ser-129 but not the phosphomimics S129E/D inhibits the fibrillation of alpha-synuclein
Hilal Lashuel, Adrian Schmid, Magdalena Zweckstetter
alpha-Synuclein (alpha-syn) phosphorylation at serine 129 is characteristic of Parkinson disease (PD) and related alpha-synulceinopathies. However, whether phosphorylation promotes or inhibits alpha-syn aggregation and neurotoxicity in vivo remains unknown ...
American Society for Biochemistry and Molecular Biology2008Switch-peptides: design and characterization of controllable super-amyloid-forming host-guest peptides as tools for identifying anti-amyloid agents
Hilal Lashuel, Adrian Schmid, Sonia Dos Santos, Marie-Stéphanie Camus
Several amyloid-forming proteins are characterized by the presence of hydrophobic and highly amyloidogenic core sequences that play critical roles in the initiation and progression of amyloid fibril formation. Therefore targeting these sequences represents ...
Wiley-Blackwell2008Switch-peptides as folding precursors in self-assembling peptides and amyloid fibrillogenesis
Hilal Lashuel, Adrian Schmid, Richard Alan Mimna, Karine Murat, Marie-Stéphanie Camus, Jérémy Bérard
The study of conformational transitions of peptides has obtained considerable attention recently because of their importance as a mol. key event in a variety of degenerative diseases. However, the study of peptide self-assembly into beta-sheets and amyloid ...
2007