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A model system to elucidate the origin of protein-misfolding neurodegenerative diseases

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28.11.2008

Amyotropic lateral sclerosis (ALS) is a neurodegenerative disease linked to the misfolding and aggregation of the dimers of the enzyme superoxide dismutase (SOD1).

Other neurodegenerative disorders like Alzheimer’s disease, Creutzfeld-Jakob disease and Parkinson’s disease are also associated with protein misfolding and aggregation.

Anna Nordlung and Mikael Oliveberg from the Department of Biochemistry and Biophysics, in Stockholm University, in Sweden have been studying the folding and assembly pathway of the SOD1 dimer and how this is affected by ALS-provoking mutations.

In a Perspective published in the HFSP Journal, they argue that the relative ease with which such data can be obtained for SOD1 makes it a promising model for elucidating also the origin of other neurodegenerative diseases where the precursor proteins are structurally more
elusive.

This Perspective is part of a special issue on protein folding, which also features:

• a Perspective by Adriano Aguzzi from the University of Zurich that discusses the relevance of protein folding or misfolding to Creutzfeld-Jakob disease

• Perspective review articles by Peter Wolynes from the University of California at San Diego, Victor Munoz from the Spanish Research Council and Jane Clarke from Cambridge University and an article by Koby Levy from the Weizmann Institute in Israel that discuss the physics and biophysics of protein folding

• Perspectives by Martin Gruebele from the University of Illinois and Edward Engelman from the University of Virginia and Commentaries by Pal Ormos from the Hungarian Academy of Sciences and Thomas Schneider from the European Molecular Biology Laboratory in Germany and that present new experimental advances that have allowed for probing in details of protein structure, folding and dynamics

• Finally, articles by Sophie Jackson from Cambridge University and Lisa Lapidus from Michigan State University describe the folding of the model protein green fluorescent protein GFP and protein L respectively, and an article by Martin Mann from the University of Freiburg, Germany presents a computational model to predict protein folding and three-dimensional structures.

This special issue was Edited by Jose’ Onuchic from the Center for Theoretical Biological Physics and Department of Physics of the University of California at San Diego.

Valerie Ferrier | Source: alphagalileo
Further information: hfspj.aip.org

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