TY - JOUR
T1 - Getting in charge of β-synuclein fibrillation
AU - Landau, Meytal
N1 - Publisher Copyright:
© 2017 by The American Society for Biochemistry and Molecular Biology, Inc.
PY - 2017/9/29
Y1 - 2017/9/29
N2 - The synuclein family has long been associated with Parkinson’s disease and dementia. Although the self-assembly of α-synuclein (αS) into oligomers and amyloid fibrils is well established, the aggregation propensity of other members of the family and their role in disease is still under debate. Moriarty et al. now suggest that the pH switching that occurs between different cellular environments could control β-synuclein (βS) aggregation via altering its charge distribution, thus opening new possible roles for βS in Parkinson’s and other neurodegen-erative diseases.
AB - The synuclein family has long been associated with Parkinson’s disease and dementia. Although the self-assembly of α-synuclein (αS) into oligomers and amyloid fibrils is well established, the aggregation propensity of other members of the family and their role in disease is still under debate. Moriarty et al. now suggest that the pH switching that occurs between different cellular environments could control β-synuclein (βS) aggregation via altering its charge distribution, thus opening new possible roles for βS in Parkinson’s and other neurodegen-erative diseases.
UR - http://www.scopus.com/inward/record.url?scp=85030032352&partnerID=8YFLogxK
U2 - 10.1074/jbc.H117.780528
DO - 10.1074/jbc.H117.780528
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AN - SCOPUS:85030032352
SN - 0021-9258
VL - 292
SP - 16380
EP - 16381
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 39
ER -