It is well established that the proteases that cleave APP and their proteolytic cut sites within APP are not exact, e. A large abundance of fragments are easily detectable due to a high copy number e. Even so, there is still a great deal that remains to be determined. The implementation and development of these techniques will help to answer questions about how metal ions shift in a diseased brain and how metal ions such as Fe or Cu contribute to the oxidative stress observed in AD.
The evidence covered by this review suggests that abnormal interactions with biological metals are upstream in the AD pathophysiology, and represent an attractive novel drug target.
However, specificity and selectivity are important factors that must be considered when testing new drug candidates. Volume , Issue s1. The full text of this article hosted at iucr. If you do not receive an email within 10 minutes, your email address may not be registered, and you may need to create a new Wiley Online Library account. If the address matches an existing account you will receive an email with instructions to retrieve your username. Journal of Neurochemistry.
Blaine R. Timothy M. Ashley I. Colin L. James A.
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Password Changed Successfully Your password has been changed. Returning user. Request Username Can't sign in? Forgot your username? ARA Arachidonic acid. CNS central nervous system. CP ceruloplasmin. DFC diferric peroxo complex. GIF growth inhibitory factor. GSH glutathione. IRE iron responsive elements. IRP iron-regulator protein. KNG kininogen.
Summary. This book describes the latest research on neurodegenerative disease and metal-binding proteins. It lays strong emphasis on biochemistry and cell. Brain Diseases and Metalloproteins: Medicine & Health Science Books @ ethtafibtapa.cf
MT metallothionein. PD Parkinson disease. PPD prion protein disease. ROS reactive oxygen species. SOD superoxide dismutase. TfR transferrin receptor. TGA thioglycolic acid. TSEs transmissible spongiform encephalopathies. ZEN zinc-enriched neurons.
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