Activation of distinct alpha5beta1-mediated signaling pathways by fibronectin's cell adhesion and matrix assembly domains. - Wikidata - awgldk - TriplyDB

Activation of distinct alpha5beta1-mediated signaling pathways by fibronectin's cell adhesion and matrix assembly domains.

Activation of distinct alpha5beta1-mediated signaling pathways by fibronectin's cell adhesion and matrix assembly domains.

http://www.wikidata.org/entity/Q36255267

about

Prolactin-induced protein mediates cell invasion and regulates integrin signaling in estrogen receptor-negative breast cancer Tissue transglutaminase is an integrin-binding adhesion coreceptor for fibronectin Electrophoretic characterization of species of fibronectin bearing sequences from the N-terminal heparin-binding domain in synovial fluid samples from patients with osteoarthritis and rheumatoid arthritis The headpiece domain of dematin regulates cell shape, motility, and wound healing by modulating RhoA activation Fibronectin polymerization regulates the composition and stability of extracellular matrix fibrils and cell-matrix adhesions.The low density lipoprotein receptor-related protein mediates fibronectin catabolism and inhibits fibronectin accumulation on cell surfaces.Assembly of fibronectin extracellular matrix.iso-DGR sequences do not mediate binding of fibronectin N-terminal modules to adherent fibronectin-null fibroblasts.Force measurements of the alpha5beta1 integrin-fibronectin interaction Engineering of vascular ingrowth matrices: are protein domains an alternative to peptides?Chimeric fibronectin matrix mimetic as a functional growth- and migration-promoting adhesive substrate.The N-terminal 70-kDa fragment of fibronectin binds to cell surface fibronectin assembly sites in the absence of intact fibronectin Fibronectin aggregation and assembly: the unfolding of the second fibronectin type III domain.Comparison of the early stages of forced unfolding for fibronectin type III modules.Ail protein binds ninth type III fibronectin repeat (9FNIII) within central 120-kDa region of fibronectin to facilitate cell binding by Yersinia pestis Regulation of alpha5beta1 integrin conformation and function by urokinase receptor binding.Integrins and chondrocyte-matrix interactions in articular cartilage Recombinant fibronectin matrix mimetics specify integrin adhesion and extracellular matrix assembly.Deletion of inositol hexakisphosphate kinase 1 (IP6K1) reduces cell migration and invasion, conferring protection from aerodigestive tract carcinoma in mice Thrombin induces fibronectin-specific migration of pulmonary microvascular endothelial cells: requirement of calcium/calmodulin-dependent protein kinase II Endothelial progenitor cells and integrins: adhesive needs.Mapping the heparin-binding site on the 13-14F3 fragment of fibronectin.Optimizing a multifunctional microsphere scaffold to improve neural precursor cell transplantation for traumatic brain injury repair.Ail binding to fibronectin facilitates Yersinia pestis binding to host cells and Yop delivery.The receptor for urokinase-type plasminogen activator regulates fibronectin matrix assembly in human skin fibroblasts.Dynamic seeding of perfusing human umbilical vein endothelial cells (HUVECs) onto dual-function cell adhesion ligands: Arg-Gly-Asp (RGD)-streptavidin and biotinylated fibronectin.Integrin-mediated muscle cell spreading. The role of protein kinase c in outside-in and inside-out signaling and evidence of integrin cross-talk.Targeting Inflammatory Cytokines and Extracellular Matrix Composition to Promote Wound Regeneration.Fibronectin fragments and blocking antibodies to alpha2beta1 and alpha5beta1 integrins stimulate mitogen-activated protein kinase signaling and increase collagenase 3 (matrix metalloproteinase 13) production by human articular chondrocytes.A new model of dual interacting ligand binding sites on integrin alphaIIbbeta3.Impairment of gingival fibroblast adherence by IL-6/sIL-6R.Blood-brain barrier properties in vitro depend on composition and assembly of endogenous extracellular matrices.Cooperative Role for Activated α4β1 Integrin and Chondroitin Sulfate Proteoglycans in Cell Adhesion to the Heparin III Domain of Fibronectin

P2860

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P2860

Activation of distinct alpha5beta1-mediated signaling pathways by fibronectin's cell adhesion and matrix assembly domains.

http://www.wikidata.org/entity/Q36255267

description

1998 nî lūn-bûn

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1998年の論文

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1998年学术文章

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1998年学术文章

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1998年学术文章

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1998年学术文章

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1998年学术文章

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1998年學術文章

@yue

1998年學術文章

@zh

1998年學術文章

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name

Activation of distinct alpha5b ...... n and matrix assembly domains.

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Activation of distinct alpha5b ...... n and matrix assembly domains.

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type

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Activation of distinct alpha5b ...... n and matrix assembly domains.

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Activation of distinct alpha5b ...... n and matrix assembly domains.

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prefLabel

Activation of distinct alpha5b ...... n and matrix assembly domains.

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Activation of distinct alpha5b ...... n and matrix assembly domains.

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Journal of Cell Biology

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Activation of distinct alpha5b ...... n and matrix assembly domains.

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P2093

D C Hocking

http://www.w3.org/2001/XMLSchema#string

J Sottile

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P J McKeown-Longo

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P2860

pp125FAK a structurally distinctive protein-tyrosine kinase associated with focal adhesions.

Paxillin, a tyrosine phosphorylated focal adhesion-associated protein binds to the carboxyl terminal domain of focal adhesion kinase.

Tyrosine phosphorylation of paxillin and pp125FAK accompanies cell adhesion to extracellular matrix: a role in cytoskeletal assembly

Effects of cytochalasin and phalloidin on actin

Cleavage of structural proteins during the assembly of the head of bacteriophage T4

Integrins: versatility, modulation, and signaling in cell adhesion

Integrins: emerging paradigms of signal transduction

Primary sequence of paxillin contains putative SH2 and SH3 domain binding motifs and multiple LIM domains: identification of a vinculin and pp125Fak-binding region

Integrins: a family of cell surface receptors

Characterization of tyrosine phosphorylation of paxillin in vitro by focal adhesion kinase

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241-253

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10.1083/JCB.141.1.241

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141

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9531562

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