Structure based aggregation studies reveal the presence of helix-rich intermediate during α-Synuclein aggregation-Reference-Cited by-同舟云学术

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Structure based aggregation studies reveal the presence of helix-rich intermediate during α-Synuclein aggregation

Published:2015-03-18 Issue:1 Volume:5 Page:
ISSN:2045-2322
Container-title:Scientific Reports
language:en
Short-container-title:Sci Rep

Author:

Ghosh Dhiman,Singh Pradeep K.,Sahay Shruti,Jha Narendra Nath,Jacob Reeba S.,Sen Shamik,Kumar Ashutosh,Riek Roland,Maji Samir K.

Publisher

Springer Science and Business Media LLC

Subject

Multidisciplinary

Link

http://www.nature.com/articles/srep09228.pdf

Reference91 articles.

1. Clayton, D. F. & George, J. M. The synucleins: a family of proteins involved in synaptic function, plasticity, neurodegeneration and disease. Trends Neurosci. 21, 249–254 (1998).

2. Iwai, A. et al. The precursor protein of non-Aβ component of Alzheimer's disease amyloid is a presynaptic protein of the central nervous system. Neuron 14, 467–475 (1995).

3. Zhang, L. et al. Semi-quantitative analysis of α-Syn in subcellular pools of rat brain neurons: an immunogold electron microscopic study using a C-terminal specific monoclonal antibody. Brain Res. 1244, 40–52 (2008).

4. Abeliovich, A. et al. Mice lacking α-Syn display functional deficits in the nigrostriatal dopamine system. Neuron 25, 239–252 (2000).

5. Cabin, D. E. et al. Synaptic vesicle depletion correlates with attenuated synaptic responses to prolonged repetitive stimulation in mice lacking α-Syn. J. Neurosci. 22, 8797–8807 (2002).

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