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Protein folding and misfolding: neurodegenerative diseases (Paperback, Softcover reprint of hardcover 1st ed. 2009)
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Protein folding and misfolding: neurodegenerative diseases (Paperback, Softcover reprint of hardcover 1st ed. 2009)
Series: Focus on Structural Biology, 7
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It was twenty ?ve years ago this year that for the ?rst time a
protein under- ing a form of human cerebral amyloidosis, the
Icelandic-type hereditary cerebral haemorrhage was identi?ed. This,
together with the recognition that an amino acid substitution can
transform the wild type cystatin C into a disease-associated
amyloid-forming protein in this condition, was only a prelude to a
series of imp- tant discoveries that followed. As a result,
pathologically altered proteins have been brought into the centre
stage of research into the pathomechanism of a n- ber of
neurodegenerative diseases, which include epidemiologically such
important conditions as Alzheimer's disease or Parkinson's disease
and, among others, also the transmissible spongiform
encephalopathies, Huntington's chorea, spinocereb- lar ataxias,
frontotemporal lobar degenerations and amyotrophic lateral
sclerosis. Despite the diversity in the amino acid sequence of the
different proteins involved in these neurological diseases, one of
the common themes underlying the patho- chanisms of all these
conditions is protein misfolding, aggregation - hence the term
protein folding disorders -, which can trigger cascades of events
ultimately resulting in synapse loss and neuron death with
devastating clinical consequences in many of the most precious
spheres of human existence including personality, cognition,
memory, skilled movements and affection. It is always a challenging
task to unite the different topics of the individual ch- ters into
a common theme in a multi-author volume, but the current book
edited by Judit Ovadi and Ferenc Orosz ?ts this task admirably.
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