Homocysteine modifies structural and functional properties of fibronectin and interferes with the fibronectin-fibrillin-1 interaction.
about
The evolution of extracellular fibrillins and their functional domainsLow bone mineral density is a common finding in patients with homocystinuria.Epithelial-mesenchymal status influences how cells deposit fibrillin microfibrils.Tailoring protein nanomechanics with chemical reactivity.Early fibrillin-1 assembly monitored through a modifiable recombinant cell approach.Mutations in Fibronectin Cause a Subtype of Spondylometaphyseal Dysplasia with "Corner Fractures".Tuning the interactions between chiral plasmonic films and living cells.Moderately Elevated Homocysteine Does Not Contribute to Thoracic Aortic Aneurysm in Mice.
P2860
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P2860
Homocysteine modifies structural and functional properties of fibronectin and interferes with the fibronectin-fibrillin-1 interaction.
description
2011 nî lūn-bûn
@nan
2011 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
name
Homocysteine modifies structur ...... ectin-fibrillin-1 interaction.
@ast
Homocysteine modifies structur ...... ectin-fibrillin-1 interaction.
@en
type
label
Homocysteine modifies structur ...... ectin-fibrillin-1 interaction.
@ast
Homocysteine modifies structur ...... ectin-fibrillin-1 interaction.
@en
prefLabel
Homocysteine modifies structur ...... ectin-fibrillin-1 interaction.
@ast
Homocysteine modifies structur ...... ectin-fibrillin-1 interaction.
@en
P2093
P2860
P356
P1433
P1476
Homocysteine modifies structur ...... nectin-fibrillin-1 interaction
@en
P2093
Deane F Mosher
Douglas S Annis
Laetitia Sabatier
P2860
P304
P356
10.1021/BI200183Z
P407
P577
2011-05-19T00:00:00Z