Quantification of quaternary structure stability in aggregation-prone proteins under physiological conditions: the transthyretin case.
about
Amyloidogenic and non-amyloidogenic transthyretin variants interact differently with human cardiomyocytes: insights into early events of non-fibrillar tissue damage.Repositioning tolcapone as a potent inhibitor of transthyretin amyloidogenesis and associated cellular toxicity.Autoimmune response to transthyretin in juvenile idiopathic arthritis.
P2860
Quantification of quaternary structure stability in aggregation-prone proteins under physiological conditions: the transthyretin case.
description
2014 nî lūn-bûn
@nan
2014 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2014 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
2014年の論文
@ja
2014年論文
@yue
2014年論文
@zh-hant
2014年論文
@zh-hk
2014年論文
@zh-mo
2014年論文
@zh-tw
2014年论文
@wuu
name
Quantification of quaternary s ...... tions: the transthyretin case.
@ast
Quantification of quaternary s ...... tions: the transthyretin case.
@en
Quantification of quaternary s ...... tions: the transthyretin case.
@nl
type
label
Quantification of quaternary s ...... tions: the transthyretin case.
@ast
Quantification of quaternary s ...... tions: the transthyretin case.
@en
Quantification of quaternary s ...... tions: the transthyretin case.
@nl
prefLabel
Quantification of quaternary s ...... tions: the transthyretin case.
@ast
Quantification of quaternary s ...... tions: the transthyretin case.
@en
Quantification of quaternary s ...... tions: the transthyretin case.
@nl
P2860
P356
P1433
P1476
Quantification of quaternary s ...... itions: the transthyretin case
@en
P2093
Lei Z Robinson
P2860
P304
P356
10.1021/BI500739Q
P407
P50
P577
2014-10-07T00:00:00Z