By Icon Health Publications
It is a 3-in-1 reference booklet. It offers a whole scientific dictionary overlaying thousands of phrases and expressions in terms of amyloidosis. It additionally provides huge lists of bibliographic citations. eventually, it offers info to clients on how one can replace their wisdom utilizing a number of net assets. The e-book is designed for physicians, scientific scholars getting ready for Board examinations, scientific researchers, and sufferers who are looking to get to grips with examine devoted to amyloidosis. in case your time is efficacious, this ebook is for you. First, you won't waste time looking the net whereas lacking loads of proper info. moment, the publication additionally saves you time indexing and defining entries. eventually, you won't waste money and time printing enormous quantities of websites.
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Extra resources for Amyloidosis - A Medical Dictionary, Bibliography, and Annotated Research Guide to Internet References
In addition to biochemical measurements, they will perform time-resolved small angle x-ray scattering measurements on solutions of the amyloid forming proteins and their mutants in order to study the kinetics of selfassociation and the size and shape of oligomers formed on the pathway to their formation. The long term aim of this research will be to gain sufficient information about the molecular derails of fibril formation so that eventually it will be possible to design drugs for slowing down or possibly inhibiting the deposition process which is believed to be at the root of this class of disease.
Professor; Medicine; University of Tennessee Knoxville Knoxville, Tn 37996 Timing: Fiscal Year 2002; Project Start 01-SEP-2001; Project End 31-AUG-2006 Summary: (From the Applicant's Abstract): Amyloid fibrils are found associated with a growing number of human diseases, including several neurodegenerative diseases, the most prevalent of which is Alzheimer's Disease (AD). In each of these diseases, the protein that is the main component of the amyloid fibril is different. Thus, amyloid is a characteristic type of aggregate structure, rather than a particular protein molecule.
Hence, a LOX-L2/RP-associated pathomechanism of cerebrovascular amyloid-beta productipn could be targeted by specific therapeutic approach. We hypothesize that enzymatic crosslinking of matrix proteins by LOX-Lr/RP secreted by senescent vascular cells. reduces clearance of soluble amyloid-beta peptide (ABeta), crosslinks ABeta to matrix and causes aggregation of ABeta. Thus, amyloid would be deposited at sites of over-production of both ABeta and LOX-L2/RP. To test the hypothesis we created a cell culture model of vascular amyloidosis--established Iines of brain vascular smooth muscle cells which secrete and accumulate ABeta.