Alpha‐synuclein oligomerization and aggregation: A model will always be a model

2021 | journal article; research paper. A publication with affiliation to the University of Göttingen.

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​Alpha‐synuclein oligomerization and aggregation: A model will always be a model​
Outeiro, T. F. ​ (2021) 
Journal of Neurochemistry157(4) pp. 889​-890​.​ DOI: https://doi.org/10.1111/jnc.15264 

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Title Variant(s)
This is a response to “Monitoring alpha‐synuclein oligomerization and aggregation using bimolecular fluorescence complementation assays: What you see is not always what you get”. Read the reply on “Alpha‐Synuclein oligomerization and aggregation: All models are useful but only if we know what they model”. The articles are accompanied by a Preface “How good are cellular models?”.
Authors
Outeiro, Tiago Fleming 
Abstract
Abstract image
The process of a‐syn aggregation is thought to be central in synucleinopathies, but has been difficult to study in the laboratory. Different models attempt to recapitulate specific aspects of the aggregation process. The BiFC assay uses engineered fusion proteins in order to enable the detection of a‐syn dimers and oligomers in living cells. As any model, it has strengths and limitations and, therefore, should only be regarded as a model for the study of basic molecular mechanisms involved in PD and other synucleinopathies. image
Issue Date
2021
Journal
Journal of Neurochemistry 
Project
EXC 2067: Multiscale Bioimaging 
Working Group
RG Outeiro (Experimental Neurodegeneration) 
ISSN
0022-3042
eISSN
1471-4159
Language
English
Sponsor
Deutsche Forschungsgemeinschaft http://dx.doi.org/10.13039/501100001659

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