Journal article icon

Journal article

A specific nanobody prevents amyloidogenesis of D76N β2-microglobulin in vitro and modifies its tissue distribution in vivo.

Abstract:

Systemic amyloidosis is caused by misfolding and aggregation of globular proteins in vivo for which effective treatments are urgently needed. Inhibition of protein self-aggregation represents an attractive therapeutic strategy. Studies on the amyloidogenic variant of β2-microglobulin, D76N, causing hereditary systemic amyloidosis, have become particularly relevant since fibrils are formed in vitro in physiologically relevant conditions. Here we compare the potency of two previously described ...

Expand abstract
Publication status:
Published
Peer review status:
Peer reviewed

Actions


Access Document


Publisher copy:
10.1038/srep46711

Authors


More from this funder
Name:
Cariplo Foundation
Grant:
2014-0700
More from this funder
Name:
Telethon Foundation
Grant:
GG14127
More from this funder
Name:
Italian Ministry of Health
Grant:
RF-2013-02355259
More from this funder
Name:
Rosetrees Trust
Grant:
M427
More from this funder
Name:
Royal Free Charity
Grant:
M427
Publisher:
Nature Publishing Group
Journal:
Scientific Reports More from this journal
Volume:
7
Pages:
46711
Publication date:
2017-04-01
Acceptance date:
2017-03-23
DOI:
ISSN:
2045-2322
Language:
English
Keywords:
Pubs id:
pubs:690871
UUID:
uuid:8ffe25cc-47c3-498d-90d7-3990cbe0df8c
Local pid:
pubs:690871
Source identifiers:
690871
Deposit date:
2017-06-06

Terms of use


Views and Downloads






If you are the owner of this record, you can report an update to it here: Report update to this record

TO TOP