Normal development, wound healing, and adenovirus susceptibility in beta5-deficient mice - Wikidata - awgldk - TriplyDB

Normal development, wound healing, and adenovirus susceptibility in beta5-deficient mice

Normal development, wound healing, and adenovirus susceptibility in beta5-deficient mice

http://www.wikidata.org/entity/Q39450655

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Regulation of endodermal differentiation of human embryonic stem cells through integrin-ECM interactions Endothelial integrins and angiogenesis: not so simple anymore Angiopoietin-like 4 interacts with integrins beta1 and beta5 to modulate keratinocyte migration Src-mediated coupling of focal adhesion kinase to integrin alpha(v)beta5 in vascular endothelial growth factor signaling.Integrin-mediated regulation of epidermal wound functions Defective associations between blood vessels and brain parenchyma lead to cerebral hemorrhage in mice lacking alphav integrins Tetraspanin CD81 is required for the alpha v beta5-integrin-dependent particle-binding step of RPE phagocytosis Angiogenesis in differentiated placental multipotent mesenchymal stromal cells is dependent on integrin alpha5beta1.A novel signaling pathway of tissue kallikrein in promoting keratinocyte migration: activation of proteinase-activated receptor 1 and epidermal growth factor receptor.Integrins as Therapeutic Targets for Respiratory Diseases Endothelial alpha5 and alphav integrins cooperate in remodeling of the vasculature during development Integrin-α5β1 is not required for mural cell functions during development of blood vessels but is required for lymphatic-blood vessel separation and lymphovenous valve formation.Adenovirus receptors.Transcription of the transforming growth factor beta activating integrin beta8 subunit is regulated by SP3, AP-1, and the p38 pathway.Proteolytic events of wound-healing--coordinated interactions among matrix metalloproteinases (MMPs), integrins, and extracellular matrix molecules.Tiny dancers: the integrin-growth factor nexus in angiogenic signaling.Mfge8 promotes obesity by mediating the uptake of dietary fats and serum fatty acids.Role of integrins in regulating epidermal adhesion, growth and differentiation.A reevaluation of integrins as regulators of angiogenesis.Why integrin as a primary target for imaging and therapy.Macrophage migration inhibitory factor: a central regulator of wound healing.Neovascularization of ischemic tissues by gene delivery of the extracellular matrix protein Del-1.The diverse roles of integrins and their ligands in angiogenesis.Increased primary tumor growth in mice null for beta3- or beta3/beta5-integrins or selectins Novel role for alphavbeta5-integrin in retinal adhesion and its diurnal peak.Microglia use multiple mechanisms to mediate interactions with vitronectin; non-essential roles for the highly-expressed αvβ3 and αvβ5 integrins Integrin αvβ5-mediated TGF-β activation by airway smooth muscle cells in asthma Integrins: roles in cancer development and as treatment targets.Gene expression profiling of cutaneous wound healing.Dietary antioxidants prevent age-related retinal pigment epithelium actin damage and blindness in mice lacking αvβ5 integrin Essential diurnal Rac1 activation during retinal phagocytosis requires αvβ5 integrin but not tyrosine kinases focal adhesion kinase or Mer tyrosine kinase Essential role for MFG-E8 as ligand for alphavbeta5 integrin in diurnal retinal phagocytosis.Porphyromonas gingivalis promotes monocyte migration by activating MMP-9.Diurnal, localized exposure of phosphatidylserine by rod outer segment tips in wild-type but not Itgb5-/- or Mfge8-/- mouse retina.Ulcerative colitis and autoimmunity induced by loss of myeloid alphav integrins.Insulin-like growth factor binding protein-3 inhibits cell adhesion via suppression of integrin β4 expression.Focal-adhesion-independent integrin-αv regulation of FAK and c-Myc is necessary for 3D skin formation and tumor invasion Loss of synchronized retinal phagocytosis and age-related blindness in mice lacking alphavbeta5 integrin.αv Integrins combine with LC3 and atg5 to regulate Toll-like receptor signalling in B cells The integrins.

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P2860

Normal development, wound healing, and adenovirus susceptibility in beta5-deficient mice

http://www.wikidata.org/entity/Q39450655

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2000 nî lūn-bûn

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2000年の論文

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2000年学术文章

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2000年学术文章

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2000年学术文章

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2000年学术文章

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2000年学术文章

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2000年學術文章

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2000年學術文章

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2000年學術文章

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name

Normal development, wound healing, and adenovirus susceptibility in beta5-deficient mice

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Normal development, wound healing, and adenovirus susceptibility in beta5-deficient mice.

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type

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Normal development, wound healing, and adenovirus susceptibility in beta5-deficient mice

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Normal development, wound healing, and adenovirus susceptibility in beta5-deficient mice.

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Normal development, wound healing, and adenovirus susceptibility in beta5-deficient mice

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Normal development, wound healing, and adenovirus susceptibility in beta5-deficient mice.

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MCB.20.3.755-759.2000

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Molecular and Cellular Biology

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Normal development, wound healing, and adenovirus susceptibility in beta5-deficient mice

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D Sheppard

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

J Wu

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M Griffiths

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R V Farese

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P2860

Purification and functional characterization of integrin alpha v beta 5. An adhesion receptor for vitronectin

Integrin alpha v beta 8. Interaction with vitronectin and functional divergence of the beta 8 cytoplasmic domain

Cloning, primary structure and properties of a novel human integrin beta subunit

Multiple integrins mediate cell attachment to cytotactin/tenascin

Expression of beta 1, beta 3, beta 4, and beta 5 integrins by human epidermal keratinocytes and non-differentiating keratinocytes

Inactivation of the integrin beta 6 subunit gene reveals a role of epithelial integrins in regulating inflammation in the lung and skin

Role of the integrin alpha v beta 6 in cell attachment to fibronectin. Heterologous expression of intact and secreted forms of the receptor

Altering the genome by homologous recombination

Characterization of the integrin alpha v beta 6 as a fibronectin-binding protein

New perspectives in cell adhesion: RGD and integrins

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