Protein interaction studies of MAGP-1 with tropoelastin and fibrillin-1
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A disintegrin-like and metalloprotease domain containing thrombospondin type 1 motif-like 5 (ADAMTSL5) is a novel fibrillin-1-, fibrillin-2-, and heparin-binding member of the ADAMTS superfamily containing a netrin-like moduleHeparin/heparan sulfate controls fibrillin-1, -2 and -3 self-interactions in microfibril assemblyDifferential regulation of elastic fiber formation by fibulin-4 and -5Investigation of age-related decline of microfibril-associated glycoprotein-1 in human skin through immunohistochemistry studyStructure of the integrin binding fragment from fibrillin-1 gives new insights into microfibril organizationFunctional consequences of homocysteinylation of the elastic fiber proteins fibrillin-1 and tropoelastinThe molecular genetics of Marfan syndrome and related disordersAbsence of autoantibodies against correctly folded recombinant fibrillin-1 protein in systemic sclerosis patientsADAMTS proteins as modulators of microfibril formation and functionFibrillin-1 directly regulates osteoclast formation and function by a dual mechanismMAGP-2 has multiple binding regions on fibrillins and has covalent periodic association with fibrillin-containing microfibrilsDiagnostic Exome Sequencing Identifies a Novel Gene, EMILIN1, Associated with Autosomal-Dominant Hereditary Connective Tissue DiseaseMolecular interactions of biglycan and decorin with elastic fiber components: biglycan forms a ternary complex with tropoelastin and microfibril-associated glycoprotein 1Mutations of FBN1 and genotype-phenotype correlations in Marfan syndrome and related fibrillinopathiesIdentification of a major microfibril-associated glycoprotein-1-binding domain in fibrillin-2ADAMTSL-6 is a novel extracellular matrix protein that binds to fibrillin-1 and promotes fibrillin-1 fibril formationMicrofibril-associated MAGP-2 stimulates elastic fiber assemblyEnhanced expression of fibrillin-1, a constituent of the myocardial extracellular matrix in fibrosisAdamtsl2 deletion results in bronchial fibrillin microfibril accumulation and bronchial epithelial dysplasia--a novel mouse model providing insights into geleophysic dysplasiaTissue elasticity and the ageing elastic fibre.Microfibril-associated glycoprotein-2 interacts with fibrillin-1 and fibrillin-2 suggesting a role for MAGP-2 in elastic fiber assembly.Defining elastic fiber interactions by molecular fishing: an affinity purification and mass spectrometry approach.Biogenesis and function of fibrillin assemblies.Microfibril-associated glycoprotein-1, an extracellular matrix regulator of bone remodeling.Oxidative and nitrosative modifications of tropoelastin prevent elastic fiber assembly in vitro.Immobilized metal affinity chromatography co-purifies TGF-β1 with histidine-tagged recombinant extracellular proteinsFibrillin-1 interactions with fibulins depend on the first hybrid domain and provide an adaptor function to tropoelastin.Homocysteine modifies structural and functional properties of fibronectin and interferes with the fibronectin-fibrillin-1 interaction.Complex contributions of fibronectin to initiation and maturation of microfibrilsNotch signaling and Notch signaling modifiers.Fibrillins, fibulins, and matrix-associated glycoprotein modulate the kinetics and morphology of in vitro self-assembly of a recombinant elastin-like polypeptide.Biogenesis of extracellular microfibrils: Multimerization of the fibrillin-1 C terminus into bead-like structures enables self-assemblyApplying elastic fibre biology in vascular tissue engineering.Deficiency in microfibril-associated glycoprotein-1 leads to complex phenotypes in multiple organ systemsFibrillin assembly requires fibronectin.Fibrillin-3 expression in human development.The microfibril-associated glycoproteins (MAGPs) and the microfibrillar niche.Unusual life cycle and impact on microfibril assembly of ADAMTS17, a secreted metalloprotease mutated in genetic eye disease.TB domain proteins: evolutionary insights into the multifaceted roles of fibrillins and LTBPs.Fibrillin-1 interactions with heparin. Implications for microfibril and elastic fiber assembly.
P2860
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P2860
Protein interaction studies of MAGP-1 with tropoelastin and fibrillin-1
description
2001 nî lūn-bûn
@nan
2001 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
Protein interaction studies of MAGP-1 with tropoelastin and fibrillin-1
@ast
Protein interaction studies of MAGP-1 with tropoelastin and fibrillin-1
@en
Protein interaction studies of MAGP-1 with tropoelastin and fibrillin-1
@nl
type
label
Protein interaction studies of MAGP-1 with tropoelastin and fibrillin-1
@ast
Protein interaction studies of MAGP-1 with tropoelastin and fibrillin-1
@en
Protein interaction studies of MAGP-1 with tropoelastin and fibrillin-1
@nl
prefLabel
Protein interaction studies of MAGP-1 with tropoelastin and fibrillin-1
@ast
Protein interaction studies of MAGP-1 with tropoelastin and fibrillin-1
@en
Protein interaction studies of MAGP-1 with tropoelastin and fibrillin-1
@nl
P2860
P356
P1476
Protein interaction studies of MAGP-1 with tropoelastin and fibrillin-1
@en
P2093
D P Reinhardt
M A Gibson
P2860
P304
39661-39666
P356
10.1074/JBC.M104533200
P407
P577
2001-07-31T00:00:00Z