Elucidating the role of N-terminal phosphorylation in regulating the structure and the aggregation propensities of Huntingtin exon 1 using a semisynthetic strategy

• Lausanne: EPFL, 2014

Keywords: Huntington’s disease (HD) ; Huntingtin exon1 (Httex1) ; N-terminal 17 domain (Nt17) ; aggregation ; oligomers ; phosphorylation ; Post Translational Modifications (PTMs) ; protein semisynthesis ; Solid-Phase Peptide Synthesis (SPPS) ; Native Chemical Ligation (NCL) ; Expressed Protein Ligation (EPL) ; Transmission Electron Microscopy (TEM) ; Atomic Force Microscopy (AFM) ; Nuclear Magnetic Resonance (NMR) ; Circular Dichroism (CD)

Thèse École polytechnique fédérale de Lausanne EPFL, n° 6188 (2014)
Programme doctoral Neurosciences
Faculté des sciences de la vie
Institut des neurosciences
Laboratoire de neurobiologie moléculaire et neuroprotéomique
Jury: Prof. C. Sandi (présidente) ; Prof. H. Lashuel (directeur) ; Dr H. Hirling, Dr P. Paganetti, Prof. W. Yang (rapporteurs)

Public defense: 2014-5-2

Reference

• doi:10.5075/epfl-thesis-6188
• Print copy in library catalog

Record created on 2014-04-22, modified on 2017-05-12