Identification of amino acid sequences in fibrinogen gamma -chain and tenascin C C-terminal domains critical for binding to integrin alpha vbeta 3.
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The integrin alphavbeta3 is a receptor for the latency-associated peptides of transforming growth factors beta1 and beta3Fibrinogen-Related Proteins in Tissue Repair: How a Unique Domain with a Common Structure Controls Diverse Aspects of Wound HealingTenascin-C and integrins in cancerClinical impact and functional aspects of tenascin-C expression during glioma progressionTenfibgen ligand nanoencapsulation delivers bi-functional anti-CK2 RNAi oligomer to key sites for prostate cancer targeting using human xenograft tumors in miceCALEB binds via its acidic stretch to the fibrinogen-like domain of tenascin-C or tenascin-R and its expression is dynamically regulated after optic nerve lesionFibrinogen-gamma C-terminal fragments induce endothelial barrier dysfunction and microvascular leak via integrin-mediated and RhoA-dependent mechanismMicroparticle surface protein are associated with experimental venous thrombosis: a preliminary studyA T cell-binding fragment of fibrinogen can prevent autoimmunity.Mechanism and efficacy of sub-50-nm tenfibgen nanocapsules for cancer cell-directed delivery of anti-CK2 RNAi to primary and metastatic squamous cell carcinoma.Tenascin-C deficiency attenuates TGF-ß-mediated fibrosis following murine lung injuryProinflammatory secreted phospholipase A2 type IIA (sPLA-IIA) induces integrin activation through direct binding to a newly identified binding site (site 2) in integrins αvβ3, α4β1, and α5β1.Extra-cellular matrix proteins induce matrix metalloproteinase-1 (MMP-1) activity and increase airway smooth muscle contraction in asthma.Advances in tenascin-C biology.Revisiting the matricellular concept.Tenfibgen-DMAT Nanocapsule Delivers CK2 Inhibitor DMAT to Prostate Cancer Xenograft Tumors Causing Inhibition of Cell Proliferation.Nanoencapsulated anti-CK2 small molecule drug or siRNA specifically targets malignant cancer but not benign cellsInteraction of fibrin(ogen) with the endothelial cell receptor VE-cadherin: localization of the fibrin-binding site within the third extracellular VE-cadherin domain.Fibrin serves as a divalent ligand that regulates neutrophil-mediated melanoma cells adhesion to endothelium under shear conditionsCK2 Molecular Targeting-Tumor Cell-Specific Delivery of RNAi in Various Models of Cancer.Tenascin-C aptamers are generated using tumor cells and purified protein.Molecular recognition force spectroscopy study of the dynamic interaction between aptamer GBI-10 and extracellular matrix protein tenascin-C on human glioblastoma cell.Differential expression of long non-coding RNAs in hyperoxia-induced bronchopulmonary dysplasia.Thrombin-unique coagulation system protein with multifaceted impacts on cancer and metastasis.Fibrin binds to collagen and provides a bridge for αVβ3 integrin-dependent contraction of collagen gelsThe role of tenascin-C in tissue injury and tumorigenesis.Sequential binding of αVβ3 and ICAM-1 determines fibrin-mediated melanoma capture and stable adhesion to CD11b/CD18 on neutrophils.Non-cytotoxic cobra cardiotoxin A5 binds to alpha(v)beta3 integrin and inhibits bone resorption. Identification of cardiotoxins as non-RGD integrin-binding proteins of the Ly-6 family.Angiopoietin 2 induces glioma cell invasion by stimulating matrix metalloprotease 2 expression through the alphavbeta1 integrin and focal adhesion kinase signaling pathway.The cell adhesion domain of type XVII collagen promotes integrin-mediated cell spreading by a novel mechanism.Transglutaminase-mediated oligomerization of the fibrin(ogen) alphaC domains promotes integrin-dependent cell adhesion and signaling.Specific interaction of angiostatin with integrin alpha(v)beta(3) in endothelial cells.Hedgehog signaling stimulates Tenascin C to promote invasion of pancreatic ductal adenocarcinoma cells through Annexin A2.Internal Affairs: Tenascin-C as a Clinically Relevant, Endogenous Driver of Innate Immunity.Secreted Phospholipase A2 Type IIA (sPLA2-IIA) Activates Integrins in an Allosteric Manner.
P2860
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P2860
Identification of amino acid sequences in fibrinogen gamma -chain and tenascin C C-terminal domains critical for binding to integrin alpha vbeta 3.
description
2000 nî lūn-bûn
@nan
2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
2000年论文
@zh
2000年论文
@zh-cn
name
Identification of amino acid s ...... ing to integrin alpha vbeta 3.
@en
type
label
Identification of amino acid s ...... ing to integrin alpha vbeta 3.
@en
prefLabel
Identification of amino acid s ...... ing to integrin alpha vbeta 3.
@en
P2093
P2860
P356
P1476
Identification of amino acid s ...... ing to integrin alpha vbeta 3.
@en
P2093
P2860
P304
16891-16898
P356
10.1074/JBC.M000610200
P407
P577
2000-06-01T00:00:00Z