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Polyalanine expansions drive a shift into α-helical clusters without amyloid-fibril formation.
Polling, Saskia; Ormsby, Angelique R; Wood, Rebecca J; Lee, Kristie; Shoubridge, Cheryl; Hughes, James N; Thomas, Paul Q; Griffin, Michael D W; Hill, Andrew F; Bowden, Quill; Böcking, Till; Hatters, Danny M.
Afiliación
  • Polling S; Department of Biochemistry and Molecular Biology, University of Melbourne, Melbourne, Victoria, Australia.
  • Ormsby AR; Bio21 Molecular Science and Biotechnology Institute, University of Melbourne, Melbourne, Victoria, Australia.
  • Wood RJ; Department of Biochemistry and Molecular Biology, University of Melbourne, Melbourne, Victoria, Australia.
  • Lee K; Bio21 Molecular Science and Biotechnology Institute, University of Melbourne, Melbourne, Victoria, Australia.
  • Shoubridge C; Department of Biochemistry and Molecular Biology, University of Melbourne, Melbourne, Victoria, Australia.
  • Hughes JN; Bio21 Molecular Science and Biotechnology Institute, University of Melbourne, Melbourne, Victoria, Australia.
  • Thomas PQ; Robinson Research Institute, School of Paediatrics and Reproductive Health, University of Adelaide, Adelaide, South Australia, Australia.
  • Griffin MD; Robinson Research Institute, School of Paediatrics and Reproductive Health, University of Adelaide, Adelaide, South Australia, Australia.
  • Hill AF; School of Molecular and Biomedical Science, University of Adelaide, Adelaide, South Australia, Australia.
  • Bowden Q; School of Molecular and Biomedical Science, University of Adelaide, Adelaide, South Australia, Australia.
  • Böcking T; Department of Biochemistry and Molecular Biology, University of Melbourne, Melbourne, Victoria, Australia.
  • Hatters DM; Bio21 Molecular Science and Biotechnology Institute, University of Melbourne, Melbourne, Victoria, Australia.
Nat Struct Mol Biol ; 22(12): 1008-15, 2015 Dec.
Article en En | MEDLINE | ID: mdl-26571108
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Péptidos / Multimerización de Proteína / Agregación Patológica de Proteínas / Amiloide Límite: Humans Idioma: En Revista: Nat Struct Mol Biol Asunto de la revista: BIOLOGIA MOLECULAR Año: 2015 Tipo del documento: Article País de afiliación: Australia
Texto completo
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Péptidos / Multimerización de Proteína / Agregación Patológica de Proteínas / Amiloide Límite: Humans Idioma: En Revista: Nat Struct Mol Biol Asunto de la revista: BIOLOGIA MOLECULAR Año: 2015 Tipo del documento: Article País de afiliación: Australia