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Unraveling the mysteries of protein folding and misfolding

Journal Article


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Abstract


  • This mini-review focuses on the processes and consequences of protein folding and misfolding. The latter process often leads to protein aggregation and precipitation with the aggregates adopting either highly ordered (amyloid fibril) or disordered (amorphous) forms. In particular, the amyloid fibril is discussed because this form has gained considerable notoriety due to its close links to a variety of debilitating diseases including Alzheimer's, Parkinson's, Huntington's, and Creutzfeldt-Jakob diseases, and type-II diabetes. In each of these diseases a different protein forms fibrils, yet the fibrils formed have a very similar structure. The mechanism by which fibrils form, fibril structure, and the cytotoxicity associated with fibril formation are discussed. The generic nature of amyloid fibril structure suggests that a common target may be accessible to treat amyloid fibril-associated diseases. As such, the ability of some molecules, for example, the small heat-shock family of molecular chaperone proteins, to inhibit fibril formation is of interest due to their therapeutic potential.

Publication Date


  • 2008

Citation


  • Ecroyd, H. & Carver, J. A. (2008). Unraveling the mysteries of protein folding and misfolding. IUBMB Life, 60 (12), 769-774.

Scopus Eid


  • 2-s2.0-59649108278

Ro Full-text Url


  • http://ro.uow.edu.au/cgi/viewcontent.cgi?article=1968&context=scipapers

Ro Metadata Url


  • http://ro.uow.edu.au/scipapers/929

Has Global Citation Frequency


Number Of Pages


  • 5

Start Page


  • 769

End Page


  • 774

Volume


  • 60

Issue


  • 12

Abstract


  • This mini-review focuses on the processes and consequences of protein folding and misfolding. The latter process often leads to protein aggregation and precipitation with the aggregates adopting either highly ordered (amyloid fibril) or disordered (amorphous) forms. In particular, the amyloid fibril is discussed because this form has gained considerable notoriety due to its close links to a variety of debilitating diseases including Alzheimer's, Parkinson's, Huntington's, and Creutzfeldt-Jakob diseases, and type-II diabetes. In each of these diseases a different protein forms fibrils, yet the fibrils formed have a very similar structure. The mechanism by which fibrils form, fibril structure, and the cytotoxicity associated with fibril formation are discussed. The generic nature of amyloid fibril structure suggests that a common target may be accessible to treat amyloid fibril-associated diseases. As such, the ability of some molecules, for example, the small heat-shock family of molecular chaperone proteins, to inhibit fibril formation is of interest due to their therapeutic potential.

Publication Date


  • 2008

Citation


  • Ecroyd, H. & Carver, J. A. (2008). Unraveling the mysteries of protein folding and misfolding. IUBMB Life, 60 (12), 769-774.

Scopus Eid


  • 2-s2.0-59649108278

Ro Full-text Url


  • http://ro.uow.edu.au/cgi/viewcontent.cgi?article=1968&context=scipapers

Ro Metadata Url


  • http://ro.uow.edu.au/scipapers/929

Has Global Citation Frequency


Number Of Pages


  • 5

Start Page


  • 769

End Page


  • 774

Volume


  • 60

Issue


  • 12