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The BRICHOS domain = its proproteins...

Presto, Jenny.

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The BRICHOS domain = its proproteins and functions /

Record Type:	Electronic resources : Monograph/item
Title/Author:	The BRICHOS domain/ by Jenny Presto, Jan Johansson.
Reminder of title:	its proproteins and functions /
Author:	Presto, Jenny.
other author:	Johansson, Jan.
Published:	Cham :Springer International Publishing : : 2015.,
Description:	xv, 28 p. :ill., digital ;24 cm.
[NT 15003449]:	Introduction to BRICHOS Superfamily -- BRICHOS in proSP-C -- Proteins with a BRICHOS Domain -- A[beta] Amyloid Formation in Alzheimer's disease -- In vivo Effect of BRICHOS on A[beta] Aggregation and Toxicity.
Contained By:	Springer eBooks
Subject:	Protein folding. -
Online resource:	http://dx.doi.org/10.1007/978-3-319-16564-6
ISBN:	9783319165646 (electronic bk.)

The BRICHOS domain = its proproteins and functions /
Presto, Jenny.

The BRICHOS domainits proproteins and functions /[electronic resource] :by Jenny Presto, Jan Johansson. - Cham :Springer International Publishing :2015. - xv, 28 p. :ill., digital ;24 cm. - SpringerBriefs in molecular science. Protein folding and structure,2191-5407. - SpringerBriefs in molecular science.Protein folding and structure..

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

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 A[beta] aggregation and examine recent results from in vivo experiments where BRICHOS inhibits A[beta] 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.

ISBN: 9783319165646 (electronic bk.)

Standard No.: 10.1007/978-3-319-16564-6doiSubjects--Topical Terms:

661545
Protein folding.

LC Class. No.: QP551

Dewey Class. No.: 574.19245

The BRICHOS domain = its proproteins and functions /
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245 1 4 $a The BRICHOS domain $h [electronic resource] : $b its proproteins and functions / $c by Jenny Presto, Jan Johansson.
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300 $a xv, 28 p. : $b ill., digital ; $c 24 cm.
490 1 $a SpringerBriefs in molecular science. Protein folding and structure, $x 2191-5407
505 0 $a Introduction to BRICHOS Superfamily -- BRICHOS in proSP-C -- Proteins with a BRICHOS Domain -- A[beta] Amyloid Formation in Alzheimer's disease -- In vivo Effect of BRICHOS on A[beta] Aggregation and Toxicity.
520 $a 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 A[beta] aggregation and examine recent results from in vivo experiments where BRICHOS inhibits A[beta] 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.
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