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"The editor of this volume, having research interests in the field of ROS production and the damage to cellular systems, has identified a number of enzymes showing ·OH scavenging activities details of which are anticipated to be published in the near future as confirmatory experiments are awaited. It is hoped that the information presented in this book on NDs will stimulate both expert and novice researchers in the field with excellent overviews of the current status of research and pointers to future research goals. Also the insights gained should be valuable for further understanding of the diseases at molecular levels and should lead to development of new biomarkers, novel diagnostic tools and more effective therapeutic drugs to treat the clinical problems raised by these devastating diseases."

"This book discusses the various methods to reprogram cells, the control and determination of cell identity, the epigenetic models that have emerged and the application of iPS cell therapy for brain diseases, in particular Parkinson’s disease and Vanishing White Matter (VWM).​"

"Amyloid-forming proteins are implicated in over 30 human diseases. The proteins involved in each disease have unrelated sequences and dissimilar native structures, but they all undergo conformational alterations to form fibrillar polymers. The fibrillar assemblies accumulate progressively into disease-specific lesions in vivo. Substantial evidence suggests these lesions are the end state of aberrant protein folding whereas the actual disease-causing culprits likely are soluble, non-fibrillar assemblies preceding the aggregates. The non-fibrillar protein assemblies range from small, low-order oligomers to spherical, annular, and protofibrillar species. Oligomeric species are believed to mediate various pathogenic mechanisms that lead to cellular dysfunction, cytotoxicity, and cell loss, eventuating in disease-specific degeneration and systemic morbidity. The particular pathologies thus are determined by the afflicted cell types, organs, systems, and the proteins involved. Evidence suggests that the oligomeric species may share structural features and possibly common mechanisms of action. In many cases, the structure–function interrelationships amongst the various protein assemblies described in vitro are still elusive. Deciphering these intricate structure–function correlations will help understanding a complex array of pathogenic mechanisms, some of which may be common across different diseases albeit affecting different cell types and systems."

"Metal ions in the brain are a necessity as well as a poison. The presence of metal ions in the active sites of biological catalysts or metalloproteins and in the biological functioning of nucleic acids is very well documented and they are required for brain activity. On the other hand, metals are very effective in generating oxidative stress. This effect does not only play a role in immunology but also is the root of practically all neurodegenerative disorders by inducing disease via the death of neurons. Managing metal ions in the brain could therefore be an important strategy in the search for therapeutic agents used in the treatment of neurodegenerative diseases. This new title gives an overview to key topics in the area of metal ions in the brain. It focuses on the role of metal ions in neurological systems by describing their advantageous functions as well as their poisonous features. It is therefore of interest for scientists in biochemistry and biophysics, physiology, toxicology as well as for physicians focused on this topic."