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Title:          Biasing the native α-synuclein conformational ensemble towards compact states abolishes aggregation and neurotoxicity
Subject:        Redox Biology, 22 (2019) 101135. doi:10.1016/j.redox.2019.101135
Keywords:       α-synuclein; Disulfide bond; Amyloid; Protein aggregation; Parkinson's disease; 
Author:         Anita Carija
Creator:        Elsevier
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      Title: Biasing the native α-synuclein conformational ensemble towards compact states abolishes aggregation and neurotoxicity
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        Title: Introduction
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        Title: Materials and methods
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          Title: Design of α-syn disulfide bond
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          Title: Analysis of aggregation propensity, disorder, and hydrophobicity of α-syn sequences
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          Title: Expression and purification of wt α-syn and α-synCC
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          Title: Mass spectrometry
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          Title: Reverse-phase high performance liquid chromatography (RP-HPLC) analysis
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          Title: Electrospray ionization mass spectrometry (ESI-MS) analysis
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          Title: NMR spectroscopy
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         Item: 
          Title: Conformational properties of soluble wt α-syn and α-synCC in different buffers
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          Title: Aggregation assay
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         Item: 
          Title: Conformational properties of wt α-syn and α-synCC aggregated in different buffers
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          Title: Transmission electron microscopy (TEM)
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          Title: Limited proteolysis
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          Title: Secondary structure determination
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          Title: Internalization of wt α-syn and α-synCC aggregates in neuronal cells
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          Title: Aggregation in the presence of lipid vesicles
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          Title: Impact of α-synCC on the aggregation of wt α-syn
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          Title: Preparation and analysis of oligomer-rich samples of wt α-syn and α-synCC
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        Title: Results
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         Item: 
          Title: Design of a disulfide bond within α-syn Greek-key motif
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          Title: Cys mutations in the NAC domain do not alter the predicted aggregation propensity, hydrophobicity or disorder of α-syn
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         Item: 
          Title: Cross-linking the α-syn NAC region
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          Title: NAC cross-linking promotes α-syn compaction
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          Title: Conformational properties of wt α-syn and α-synCC under different solution conditions
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          Title: Kinetics of wt α-syn and α-synCC aggregation
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          Title: Conformational and morphological characterization of wt α-syn and α-synCC aggregation reactions
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          Title: Internalization of wt α-syn and α-synCC aggregates in human cells
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          Title: Impact of α-synCC on the aggregation of wt α-syn
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          Title: Aggregation of wt α-syn and α-synCC in the presence of lipids
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          Title: Conformational and toxic properties of wt α-syn and α-synCC oligomers
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        Title: Discussion
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        Title: Acknowledgements
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        Title: Conflict of interest
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        Title: Supporting information
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        Title: References
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   Info: 
    Title: Biasing the native α-synuclein conformational ensemble towards compact states abolishes aggregation and neurotoxicity
    Author: Anita Carija
    Subject: Redox Biology, 22 (2019) 101135. doi:10.1016/j.redox.2019.101135
    Keywords: α-synuclein; Disulfide bond; Amyloid; Protein aggregation; Parkinson's disease; 
    Creator: Elsevier
    CreationDate: Fri Mar 22 14:55:15 CET 2019
    ModDate: Fri Mar 22 14:55:15 CET 2019
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   Type: CRC32
  Checksum: 62dcb22815082d572e317920d726a60d
   Type: MD5
  Checksum: 721c37d5b4efa438bc8050fcf2ff6bf9898de305
   Type: SHA-1