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Non-Fibrillar Amyloidogenic Protein Assemblies - Common Cytotoxins Underlying Degenerative Diseases
. Ed(S): Rahimi, Farid; Bitan, Gal
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Description for Non-Fibrillar Amyloidogenic Protein Assemblies - Common Cytotoxins Underlying Degenerative Diseases
Paperback. Editor(s): Rahimi, Farid; Bitan, Gal. Num Pages: 576 pages, 9 black & white tables, biography. BIC Classification: MBGR; MMF; PSAN; PSBC. Category: (P) Professional & Vocational. Dimension: 235 x 155 x 30. Weight in Grams: 872.
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 ... Read more
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 ... Read more
Product Details
Format
Paperback
Publication date
2014
Publisher
Springer Netherlands
Number of pages
576
Condition
New
Number of Pages
568
Place of Publication
Dordrecht, Netherlands
ISBN
9789400798953
SKU
V9789400798953
Shipping Time
Usually ships in 15 to 20 working days
Ref
99-15
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