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

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

Ansaloni, Annalisa ; Lashuel, Hilal

Advisor(s):
Lashuel, Hilal
Year:
2014
Publisher:
Lausanne, EPFL
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)
DOI:
10.5075/epfl-thesis-6188
Other identifiers:
urn: urn:nbn:ch:bel-epfl-thesis6188-1
Laboratories:
LMNN

Record appears in:
Scientific production and competences > SV - School of Life Sciences > BMI - Brain Mind Institute > LMNN - Laboratory of Molecular Neurobiology and Neuroproteomics
Scientific production and competences > Archives > PhD Thesis
Scientific production and competences > PhD Theses
Restricted access
Work produced at EPFL
Published
Theses

Note: The status of this file is: EPFL only


 Record created 2014-04-22, last modified 2018-05-01

n/a:
Download fulltext
PDF
Rate this document:

Rate this document:
1
2
3
4
5
 
(Not yet reviewed)