Premium
Issue Cover (February 2017)
Publication year - 2017
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/jnc.13787
Subject(s) - internalization , context (archaeology) , fibril , inclusion bodies , glial fibrillary acidic protein , chemistry , microbiology and biotechnology , biology , neuroscience , biophysics , biochemistry , immunology , cell , immunohistochemistry , recombinant dna , paleontology , gene
Front cover: Robust binding of exogenous α‐synuclein fibrils to cells in primary neuronal‐glial cultures shown with an antibody to α‐synuclein (red) and an antibody to glial fibrillary acidic protein (green). Cells were counterstained with DAPI (blue). This process can lead to the internalization of α‐synuclein fibrils resulting in their degradation or conversely in the induction of endogenous α‐synuclein aggregation depending upon the physiological context. The balance between these pathways can play a pivotal role in the cellular transmission and spread of α‐synuclein inclusion pathology associated with neurodegenerative diseases.Read the full article ‘ Proteolysis of α‐synuclein fibrils in the lysosomal pathway limits induction of inclusion pathology ’ by A. N. Sacino, M. M. Brooks, P. Chakrabarty, K. Saha, H. Khoshbouei, T. E. Golde and B. I. Giasson ( J. Neurochem. 2017, vol. 140 (4), pp. 662–678) on doi: 10.1111/jnc.13743