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Protein Misfolding and Disease (Paperback, Softcover reprint of hardcover 1st ed. 2003)
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Protein Misfolding and Disease (Paperback, Softcover reprint of hardcover 1st ed. 2003)
Series: Methods in Molecular Biology, 232
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For decades it has been known that structured conformations are
important for the proper functioning of most cellular proteins.
However, appreciation that protein folding to the functional
conformations as well as the structural maintenance of protein
molecules are very complex processes has only emerged during the
last ten years. The intimate interplay uncovered by this scientific
development led us to realize that perturbations of the protein
folding process and disturbances of conformational maintenance are
major disease mechanisms. This development has given rise to the
concept of conformational diseases and the broader signature of
protein folding diseases, comprising diseases in which mutations or
environmental stresses may result in a partial misfolding that
leads then to alternative conformations capable of disturbing
cellular processes. This may happen by self-association
(aggregation), as in prion and Alzheimer's diseases, or by
incorporation of alternatively folded subunits into structural
entities, as in collagen diseases. Another possibility is that
folding to the native structure is impaired or abolished, resulting
in decreased stea- state levels of the correctly folded protein, as
is observed in cystic fibrosis and 1-antitrypsin deficiency, as
well as in many enzyme deficiencies. In addition, deficiencies of
proteins that are engaged in assisting and supervising protein
folding (protein quality control) may impair the folding of many
other proteins, resulting in pathological phenotypes. Examples of
this are the spastic paraplegia attributable to mutations in
mitochondrial protease/chaperone complexes.
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