Mutations linked to interstitial lung disease can abrogate anti-amyloid function of prosurfactant protein C.
about
The Brichos domain of prosurfactant protein C can hold and fold a transmembrane segmentSurfactant phospholipid metabolismHigh-resolution structure of a BRICHOS domain and its implications for anti-amyloid chaperone activity on lung surfactant protein C.Genetic disorders of surfactant dysfunctionAlveolar surfactant homeostasis and the pathogenesis of pulmonary diseaseMalfolded protein structure and proteostasis in lung diseases.Mediterranean versus Red sea corals facing climate change, a transcriptome analysis.Genetic risk factors associated with respiratory distress syndromeNedd4-2-mediated ubiquitination facilitates processing of surfactant protein-CThe chaperone domain BRICHOS prevents CNS toxicity of amyloid-β peptide in Drosophila melanogasterA non-BRICHOS surfactant protein c mutation disrupts epithelial cell function and intercellular signalingThe surfactant protein C mutation A116D alters cellular processing, stress tolerance, surfactant lipid composition, and immune cell activation.A non-BRICHOS SFTPC mutant (SP-CI73T) linked to interstitial lung disease promotes a late block in macroautophagy disrupting cellular proteostasis and mitophagyGenetic Basis of Children's Interstitial Lung Disease.Lessons from a Rare Familial Dementia: Amyloid and Beyond.4-Phenylbutyric acid treatment rescues trafficking and processing of a mutant surfactant protein-C.BRICHOS domain associated with lung fibrosis, dementia and cancer--a chaperone that prevents amyloid fibril formation?Control of amyloid assembly by autoregulation.A novel surfactant protein C L55F mutation associated with interstitial lung disease alters subcellular localization of proSP-C in A549 cells.Transthyretin and BRICHOS: The Paradox of Amyloidogenic Proteins with Anti-Amyloidogenic Activity for Aβ in the Central Nervous System.Folding and Intramembraneous BRICHOS Binding of the Prosurfactant Protein C Transmembrane SegmentBRICHOS domains efficiently delay fibrillation of amyloid β-peptide.SFTPC mutations cause SP-C degradation and aggregate formation without increasing ER stress.
P2860
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P2860
Mutations linked to interstitial lung disease can abrogate anti-amyloid function of prosurfactant protein C.
description
2008 nî lūn-bûn
@nan
2008 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2008 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
name
Mutations linked to interstiti ...... on of prosurfactant protein C.
@ast
Mutations linked to interstiti ...... on of prosurfactant protein C.
@en
type
label
Mutations linked to interstiti ...... on of prosurfactant protein C.
@ast
Mutations linked to interstiti ...... on of prosurfactant protein C.
@en
prefLabel
Mutations linked to interstiti ...... on of prosurfactant protein C.
@ast
Mutations linked to interstiti ...... on of prosurfactant protein C.
@en
P2093
P356
P1433
P1476
Mutations linked to interstiti ...... on of prosurfactant protein C.
@en
P2093
Charlotte Nerelius
Emily Martin
Kerstin Nordling
Magnus Gustafsson
Siwei Peng
Timothy Weaver
P304
P356
10.1042/BJ20080981
P407
P577
2008-12-01T00:00:00Z