The BRICHOS Domain: Its Proproteins and Functions by Jenny PrestoThe BRICHOS Domain: Its Proproteins and Functions by Jenny Presto

The BRICHOS Domain: Its Proproteins and Functions

byJenny Presto, Jan Johansson

Paperback | April 17, 2015

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This Brief summarizes the current research on the novel BRICHOS domain, which is a chaperone domain found in a variety of proteins and is shown to exhibit anti-amyloidogenic chaperone-like functions. The BRICHOS domain is defined from sequence similarities, lacks established physiological function(s) and is found about 10 distantly related pro-protein families, several of which are associated with human disease. In this work, the authors review the mechanism by which BRICHOS inhibits Aβ aggregation and examine recent results from in vivo experiments where BRICHOS inhibits Aβ aggregation and toxicity in Drosophila melanogaster. BRICHOS is one of nature´s (more specific) ways to protect against fibril formation, and exploring the potential of using the BRICHOS domain in the fight against Alzeimer's Disease and other amyloid diseases seems highly relevant. This brief is useful for newcomers to this field or researchers in related fields wishing to gain a quick overview of the latest findings.
Jenny Presto obtained her PhD in Medical Biochemistry from Uppsala University in 2006, where she studied the biosynthesis of heparan sulfate. She did a postdoc at the Swedish University of Agricultural Sciences (SLU) in Uppsala, Sweden, studying the function of the BRICHOS domain as a chaperone for surfactant protein C.In 2011, Jenny m...
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Title:The BRICHOS Domain: Its Proproteins and FunctionsFormat:PaperbackDimensions:28 pagesPublished:April 17, 2015Publisher:Springer-Verlag/Sci-Tech/TradeLanguage:English

The following ISBNs are associated with this title:

ISBN - 10:3319165631

ISBN - 13:9783319165639

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Table of Contents

Introduction to BRICHOS Superfamily.- BRICHOS in proSP-C.- Proteins with a BRICHOS Domain.- Aβ Amyloid Formation in Alzheimer's disease.- In vivo Effect of BRICHOS on Aβ Aggregation and Toxicity.