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The BRICHOS domain = its proproteins...

Presto, Jenny.

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The BRICHOS domain = its proproteins and functions /

紀錄類型:	書目-電子資源 : Monograph/item
正題名/作者:	The BRICHOS domain/ by Jenny Presto, Jan Johansson.
其他題名:	its proproteins and functions /
作者:	Presto, Jenny.
其他作者:	Johansson, Jan.
出版者:	Cham :Springer International Publishing : : 2015.,
面頁冊數:	xv, 28 p. :ill., digital ;24 cm.
內容註:	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
標題:	Protein folding. -
電子資源:	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

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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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