Journal article
Bifunctional crosslinking ligands for transthyretin.
- Abstract:
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Wild-type and variant forms of transthyretin (TTR), a normal plasma protein, are amyloidogenic and can be deposited in the tissues as amyloid fibrils causing acquired and hereditary systemic TTR amyloidosis, a debilitating and usually fatal disease. Reduction in the abundance of amyloid fibril precursor proteins arrests amyloid deposition and halts disease progression in all forms of amyloidosis including TTR type. Our previous demonstration that circulating serum amyloid P component (SAP) is...
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- Publication status:
- Published
- Peer review status:
- Peer reviewed
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(Version of record, pdf, 797.4KB)
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- Publisher copy:
- 10.1098/rsob.150105
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Authors
Funding
Bibliographic Details
- Publisher:
- Royal Society Publisher's website
- Journal:
- Open Biology Journal website
- Volume:
- 5
- Issue:
- 9
- Pages:
- 150105
- Publication date:
- 2015-09-01
- DOI:
- EISSN:
-
2046-2441
- ISSN:
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2046-2441
- Source identifiers:
-
569853
Item Description
- Language:
- English
- Keywords:
- Pubs id:
-
pubs:569853
- UUID:
-
uuid:b842d588-349f-4dc0-a413-be459cd248c1
- Local pid:
- pubs:569853
- Deposit date:
- 2016-02-03
Terms of use
- Copyright holder:
- Mangione et al
- Copyright date:
- 2015
- Notes:
- © 2015 The Authors. Published by the Royal Society under the terms of the Creative Commons Attribution License http://creativecommons.org/licenses/by/4.0/, which permits unrestricted use, provided the original author and source are credited.
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