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Amilial amyotrophic lateral sclerosis-associated proteins form aggregates via distinct pathways in cells

Journal Article


Abstract


  • Background: ALS pathology is characterised by intraneuronal

    protein deposits including ubiquitylated round, conglomerate

    or skein-like inclusions. The composition of ubiquitylated

    inclusions varies considerably depending on whether the disease

    is sporadic or familial and the genetics of the familial

    forms. Both FUS and SOD1 mutations cause ALS with FUS

    (1, 2) and SOD1 positive inclusions (3), respectively. However,

    most other cases have inclusions positive for TDP-43

    (3). Given that protein aggregation is linked to toxicity we

    sought to understand the types of aggregates formed by

    TDP-43, FUS and SOD1.

Publication Date


  • 2014

Citation


  • Yerbury, J., Farrawell, N. & Lambert-Smith, I. (2014). Amilial amyotrophic lateral sclerosis-associated proteins form aggregates via distinct pathways in cells. Amyotrophic Lateral Sclerosis and Frontotemporal Degeneration, 15 (S1), 170-170.

Ro Metadata Url


  • http://ro.uow.edu.au/smhpapers/2768

Number Of Pages


  • 0

Start Page


  • 170

End Page


  • 170

Volume


  • 15

Issue


  • S1

Abstract


  • Background: ALS pathology is characterised by intraneuronal

    protein deposits including ubiquitylated round, conglomerate

    or skein-like inclusions. The composition of ubiquitylated

    inclusions varies considerably depending on whether the disease

    is sporadic or familial and the genetics of the familial

    forms. Both FUS and SOD1 mutations cause ALS with FUS

    (1, 2) and SOD1 positive inclusions (3), respectively. However,

    most other cases have inclusions positive for TDP-43

    (3). Given that protein aggregation is linked to toxicity we

    sought to understand the types of aggregates formed by

    TDP-43, FUS and SOD1.

Publication Date


  • 2014

Citation


  • Yerbury, J., Farrawell, N. & Lambert-Smith, I. (2014). Amilial amyotrophic lateral sclerosis-associated proteins form aggregates via distinct pathways in cells. Amyotrophic Lateral Sclerosis and Frontotemporal Degeneration, 15 (S1), 170-170.

Ro Metadata Url


  • http://ro.uow.edu.au/smhpapers/2768

Number Of Pages


  • 0

Start Page


  • 170

End Page


  • 170

Volume


  • 15

Issue


  • S1