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Reviews the molecular events initiated by unfolded or misfolded proteins leading to conformational human diseases, with special emphasis on the macromolecular homo- and heteroassociations of the malfolded proteins into characteristic ultrastructures found primarily in Parkinson's and Alzheimer's diseases.

Nervous system -- Degeneration -- Pathophysiology. --- Protein folding. --- Proteins -- Denaturation. --- Protein Folding --- Proteostasis Deficiencies --- Neurodegenerative Diseases --- Metabolic Diseases --- Biophysical Processes --- Biochemical Processes --- Nervous System Diseases --- Diseases --- Chemical Processes --- Nutritional and Metabolic Diseases --- Physical Processes --- Biophysical Phenomena --- Biochemical Phenomena --- Physical Phenomena --- Chemical Phenomena --- Phenomena and Processes --- Neurology --- Animal Biochemistry --- Medicine --- Human Anatomy & Physiology --- Health & Biological Sciences --- Nervous system --- Degeneration --- Pathophysiology. --- Folding of proteins --- Proteins --- Folding --- Medicine. --- Molecular biology. --- Neurosciences. --- Medical biochemistry. --- Cell biology. --- Neurobiology. --- Biomedicine. --- Biomedicine general. --- Molecular Medicine. --- Cell Biology. --- Medical Biochemistry. --- Organs (Anatomy) --- Neurosciences --- Conformation --- Cytology. --- Biochemistry. --- Biological chemistry --- Chemical composition of organisms --- Organisms --- Physiological chemistry --- Biology --- Chemistry --- Medical sciences --- Cell biology --- Cellular biology --- Cells --- Cytologists --- Neural sciences --- Neurological sciences --- Neuroscience --- Clinical sciences --- Medical profession --- Human biology --- Life sciences --- Pathology --- Physicians --- Composition --- Health Workforce --- Biomedicine, general. --- Medical biochemistry --- Pathobiochemistry --- Pathological biochemistry --- Biochemistry --- Molecular biochemistry --- Molecular biophysics --- Biophysics --- Biomolecules --- Systems biology

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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.

Histology. Cytology --- Molecular biology --- Human biochemistry --- Physiology of nerves and sense organs --- Pathological biochemistry --- Neuropathology --- medische biochemie --- neurologie --- biochemie --- cytologie --- histologie --- neurobiologie --- moleculaire biologie