Superfibronectin is a functionally distinct form of fibronectin.
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The proteoglycan brevican binds to fibronectin after proteolytic cleavage and promotes glioma cell motilityCell adhesion and signaling on the fibronectin 1st type III repeat; requisite roles for cell surface proteoglycans and integrinsThe monoclonal antibody SM5-1 recognizes a fibronectin variant which is widely expressed in melanomaFibronectin Mechanobiology Regulates TumorigenesisUtilizing Fibronectin Integrin-Binding Specificity to Control Cellular ResponsesMolecular mechanisms involved in vascular interactions of the Lyme disease pathogen in a living hostDifferential effects of tissue culture coating substrates on prostate cancer cell adherence, morphology and behaviorForce-induced unfolding of fibronectin in the extracellular matrix of living cellsStructure and functional significance of mechanically unfolded fibronectin type III1 intermediatesInterdomain association in fibronectin: insight into cryptic sites and fibrillogenesisFibronectin is an important regulator of flow-induced vascular remodelingFibronectin polymerization regulates the composition and stability of extracellular matrix fibrils and cell-matrix adhesions.Structure and unfolding of the third type III domain from human fibronectinFibronectins, their fibrillogenesis, and in vivo functions.Matrix fibronectin binds gammaretrovirus and assists in entry: new light on viral infections.Dynamics and elasticity of the fibronectin matrix in living cell culture visualized by fibronectin-green fluorescent proteinAssembly of fibronectin extracellular matrix.Plasma fibronectin stabilizes Borrelia burgdorferi-endothelial interactions under vascular shear stress by a catch-bond mechanismTransient opening of fibronectin type III (FNIII) domains: the interaction of the third FNIII domain of FN with anastellin.Display of cell surface sites for fibronectin assembly is modulated by cell adherence to (1)F3 and C-terminal modules of fibronectinOpposing effects of collagen I and vitronectin on fibronectin fibril structure and functionFibronectin matrix turnover occurs through a caveolin-1-dependent process.Angiostatic peptides use plasma fibronectin to home to angiogenic vasculaturePlasma fibronectin promotes lung metastasis by contributions to fibrin clots and tumor cell invasionRegulation of tissue injury responses by the exposure of matricryptic sites within extracellular matrix moleculesProtein crosslinking in assembly and remodelling of extracellular matrices: the role of transglutaminases.Direct-contact co-culture between smooth muscle and endothelial cells inhibits TNF-alpha-mediated endothelial cell activation.Conformational remodeling of the fibronectin matrix selectively regulates VEGF signaling.Eukaryotic translation elongation factor 1A induces anoikis by triggering cell detachmentThe first type III repeat in fibronectin activates an inflammatory pathway in dermal fibroblasts.Extracellular matrix fibronectin stimulates the self-assembly of microtissues on native collagen gels.Chimeric fibronectin matrix mimetic as a functional growth- and migration-promoting adhesive substrate.A novel Treponema pallidum antigen, TP0136, is an outer membrane protein that binds human fibronectinImmunohistochemical staining, laser capture microdissection, and filter-aided sample preparation-assisted proteomic analysis of target cell populations within tissue samples.A fibronectin fragment inhibits tumor growth, angiogenesis, and metastasis.Fibronectin mRNA splice variant in articular cartilage lacks bases encoding the V, III-15, and I-10 protein segments.Dermatopontin interacts with fibronectin, promotes fibronectin fibril formation, and enhances cell adhesion.Broad coverage identification of multiple proteolytic cleavage site sequences in complex high molecular weight proteins using quantitative proteomics as a complement to edman sequencingFibronectin matrix polymerization regulates smooth muscle cell phenotype through a Rac1 dependent mechanism.Treponema pallidum subsp. pallidum TP0136 protein is heterogeneous among isolates and binds cellular and plasma fibronectin via its NH2-terminal end.
P2860
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P2860
Superfibronectin is a functionally distinct form of fibronectin.
description
1994 nî lūn-bûn
@nan
1994年の論文
@ja
1994年論文
@yue
1994年論文
@zh-hant
1994年論文
@zh-hk
1994年論文
@zh-mo
1994年論文
@zh-tw
1994年论文
@wuu
1994年论文
@zh
1994年论文
@zh-cn
name
Superfibronectin is a functionally distinct form of fibronectin.
@en
type
label
Superfibronectin is a functionally distinct form of fibronectin.
@en
prefLabel
Superfibronectin is a functionally distinct form of fibronectin.
@en
P2093
P356
P1433
P1476
Superfibronectin is a functionally distinct form of fibronectin.
@en
P2093
P2888
P304
P356
10.1038/367193A0
P407
P577
1994-01-01T00:00:00Z
P6179
1029630298