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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 ...

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Publication status:
Published
Peer review status:
Peer reviewed
Version:
Publisher's version

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Publisher copy:
10.1038/srep46711

Authors


Raimondi, S More by this author
Porcari, R More by this author
Mangione, PP More by this author
Marcoux, J More by this author
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University College London Amyloidosis Research Fund More from this funder
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Publisher:
Nature Publishing Group Publisher's website
Journal:
Scientific Reports Journal website
Volume:
7
Pages:
46711
Publication date:
2017-04-05
Acceptance date:
2017-03-23
DOI:
ISSN:
2045-2322
Pubs id:
pubs:690871
URN:
uri:8ffe25cc-47c3-498d-90d7-3990cbe0df8c
UUID:
uuid:8ffe25cc-47c3-498d-90d7-3990cbe0df8c
Local pid:
pubs:690871
Language:
English
Keywords:

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