The role of coiled-coil alpha-helices and disulfide bonds in the assembly and stabilization of cartilage matrix protein subunits. A mutational analysis.
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Primary structure and expression of matrilin-2, the closest relative of cartilage matrix protein within the von Willebrand factor type A-like module superfamilyMatrilin-3 from chicken cartilageNMR structure of a parallel homotrimeric coiled coilWARP is a novel multimeric component of the chondrocyte pericellular matrix that interacts with perlecanWARP is a new member of the von Willebrand factor A-domain superfamily of extracellular matrix proteinsInteraction of cartilage matrix protein with aggrecan. Increased covalent cross-linking with tissue maturationThe C-terminal domain of matrilin-2 assembles into a three-stranded alpha-helical coiled coil.Primary structure of matrilin-3, a new member of a family of extracellular matrix proteins related to cartilage matrix protein (matrilin-1) and von Willebrand factor.Cartilage matrix protein forms a type II collagen-independent filamentous network: analysis in primary cell cultures with a retrovirus expression systemDoxorubicin-triggered self-assembly of native amphiphilic peptides into spherical nanoparticles.A Designed Angiopoietin-1 Variant, Dimeric CMP-Ang1 Activates Tie2 and Stimulates Angiogenesis and Vascular Stabilization in N-glycan Dependent Manner.Native chick laminin-4 containing the beta 2 chain (s-laminin) promotes motor axon growth.Heteronuclear NMR assignments and secondary structure of the coiled coil trimerization domain from cartilage matrix protein in oxidized and reduced forms.Assembly of a novel cartilage matrix protein filamentous network: molecular basis of differential requirement of von Willebrand factor A domainsMultiple functions of the von Willebrand Factor A domain in matrilins: secretion, assembly, and proteolysis.The role of disulfide bonds and alpha-helical coiled-coils in the biosynthesis of type XIII collagen and other collagenous transmembrane proteins.A single amino acid can switch the oligomerization state of the alpha-helical coiled-coil domain of cartilage matrix proteinOligomeric forms of the 148 kDa cartilage matrix proteinThe cartilage-specific lectin C-type lectin domain family 3 member A (CLEC3A) enhances tissue plasminogen activator-mediated plasminogen activation.Matrilin-3 forms disulfide-linked oligomers with matrilin-1 in bovine epiphyseal cartilage.Matrilin-4, a new member of the matrilin family of extracellular matrix proteins.The Oligomerization Domain of the Asialoglycoprotein Receptor Preferentially Forms 2:2 Heterotetramersin Vitro
P2860
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P2860
The role of coiled-coil alpha-helices and disulfide bonds in the assembly and stabilization of cartilage matrix protein subunits. A mutational analysis.
description
1995 nî lūn-bûn
@nan
1995年の論文
@ja
1995年学术文章
@wuu
1995年学术文章
@zh-cn
1995年学术文章
@zh-hans
1995年学术文章
@zh-my
1995年学术文章
@zh-sg
1995年學術文章
@yue
1995年學術文章
@zh
1995年學術文章
@zh-hant
name
The role of coiled-coil alpha- ...... bunits. A mutational analysis.
@en
type
label
The role of coiled-coil alpha- ...... bunits. A mutational analysis.
@en
prefLabel
The role of coiled-coil alpha- ...... bunits. A mutational analysis.
@en
P2093
P2860
P356
P1476
The role of coiled-coil alpha- ...... bunits. A mutational analysis.
@en
P2093
D R Haudenschild
M M Tondravi
P F Goetinck
P2860
P304
23150-23154
P356
10.1074/JBC.270.39.23150
P407
P577
1995-09-01T00:00:00Z