Synchrotron-based infrared spectroscopy brings to light the structure of protein aggregates in neurodegenerative diseases
The accumulation of misfolded proteins in the form of aggregates characterizes a number of diseases of the central nervous system such as Alzheimer’s disease, Parkinson’s disease, prion diseases, and the diseases of polyglutamine expansion. Recent evidence obtained in vitro and in mice has suggested...
Main Authors: | Hoffner Guylaine, André William, Sandt Christophe, Djian Philippe |
---|---|
Format: | Article |
Language: | English |
Published: |
De Gruyter
2014-12-01
|
Series: | Reviews in Analytical Chemistry |
Subjects: | |
Online Access: | https://doi.org/10.1515/revac-2014-0016 |
Similar Items
-
Identification of brain substrates of transglutaminase by functional proteomics supports its role in neurodegenerative diseases
by: William André, et al.
Published: (2017-05-01) -
The Evidence for the Spread and Seeding Capacities of the Mutant Huntingtin Protein in in Vitro Systems and Their Therapeutic Implications
by: Maria Masnata, et al.
Published: (2017-11-01) -
Prions and Prion-Like Pathogens in Neurodegenerative Disorders
by: Caterina Peggion, et al.
Published: (2014-02-01) -
Monomeric, Oligomeric and Polymeric Proteins in Huntington Disease and Other Diseases of Polyglutamine Expansion
by: Guylaine Hoffner, et al.
Published: (2014-03-01) -
The Quest for Cellular Prion Protein Functions in the Aged and Neurodegenerating Brain
by: Rosalina Gavín, et al.
Published: (2020-03-01)