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

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  
2014
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Type
doctoral thesis
DOI
10.5075/epfl-thesis-6188
Author(s)
Ansaloni, Annalisa  
Advisors
Lashuel, Hilal  
Jury

Prof. C. Sandi (présidente) ; Prof. H. Lashuel (directeur) ; Dr H. Hirling, Dr P. Paganetti, Prof. W. Yang (rapporteurs)

Date Issued

2014

Publisher

EPFL

Publisher place

Lausanne

Public defense year

2014-05-02

Thesis number

6188

Subjects

Huntington’s disease (HD)

•

Huntingtin exon1 (Httex1)

•

N-terminal 17 domain (Nt17)

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aggregation

•

oligomers

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phosphorylation

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Post Translational Modifications (PTMs)

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protein semisynthesis

•

Solid-Phase Peptide Synthesis (SPPS)

•

Native Chemical Ligation (NCL)

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Expressed Protein Ligation (EPL)

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Transmission Electron Microscopy (TEM)

•

Atomic Force Microscopy (AFM)

•

Nuclear Magnetic Resonance (NMR)

•

Circular Dichroism (CD)

EPFL units
LMNN  
Faculty
SV  
School
BMI  
Doctoral School
EDNE  
Use this identifier to reference this record
https://infoscience.epfl.ch/handle/20.500.14299/102920
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