Non-fibrillar Amyloidogenic Protein Assemblies - Common Cytotoxins Underlying Degenerative Diseases

Nonfiction, Science & Nature, Science, Biological Sciences, Biochemistry, Health & Well Being, Medical, Specialties, Internal Medicine, Neuroscience
Cover of the book Non-fibrillar Amyloidogenic Protein Assemblies - Common Cytotoxins Underlying Degenerative Diseases by , Springer Netherlands
View on Amazon View on AbeBooks View on Kobo View on B.Depository View on eBay View on Walmart
Author: ISBN: 9789400727748
Publisher: Springer Netherlands Publication: January 11, 2012
Imprint: Springer Language: English
Author:
ISBN: 9789400727748
Publisher: Springer Netherlands
Publication: January 11, 2012
Imprint: Springer
Language: English

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.

View on Amazon View on AbeBooks View on Kobo View on B.Depository View on eBay View on Walmart

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.

More books from Springer Netherlands

Cover of the book Trace Gas Emissions and Plants by
Cover of the book The Legal Status, Privileges and Immunities of the Specialized Agencies of the United Nations and Certain Other International Organizations by
Cover of the book WiMAX Networks by
Cover of the book Nāgārjuna’s Twelve Gate Treatise by
Cover of the book On Genes, Gods and Tyrants by
Cover of the book Factor X by
Cover of the book Geography, History and Social Sciences by
Cover of the book Analysing China's Population by
Cover of the book Transitions Between Contexts of Mathematical Practices by
Cover of the book Diabetic Retinopathy by
Cover of the book Introduction to the Scientific Study of Atmospheric Pollution by
Cover of the book Anticipating and Assessing Health Care Technology by
Cover of the book The Ethics of Screening in Health Care and Medicine by
Cover of the book EPSA Philosophical Issues in the Sciences by
Cover of the book Transcendentalism Overturned by
We use our own "cookies" and third party cookies to improve services and to see statistical information. By using this website, you agree to our Privacy Policy