Receptor Domain Kinase Kdr
Mostrando 1-12 de 16 artigos, teses e dissertações.
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1. The role of KDR in intrauterine adhesions may involve the TGF-β1/Smads signaling pathway
The aim of this study was to investigate the role of kinase-insert domain-containing receptor (KDR) in intrauterine adhesions (IUA) and its mechanism. The Case group consisted of 92 patients diagnosed with IUA, and the Control group included 86 patients with uterine septum who had normal endometrium verified with an uteroscope. In addition, 50 rats were rand
Braz J Med Biol Res. Publicado em: 07/10/2019
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2. Polimorfismos nos genes VEGF e KDR no desenvolvimento da endometriose: revisão sistemática
Resumo Objetivos: revisar os trabalhos que utilizaram o delineamento caso-controle para verificar a associação de polimorfismos nos genes VEGF e KDR no desenvolvimento da endometriose. Métodos: revisão sistemática que pesquisou nas bases de dados PubMed, MEDLINE, BVS, SciELO os artigos publicados até o dia 1 de setembro de 2015, considerando os descr
Rev. Bras. Saude Mater. Infant.. Publicado em: 2016-09
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3. Clonagem e expressão dos domínios 2 e 3 do receptor KDR (VEGFR-2) humano / Cloning and Expression of the 2 and 3 Domains KDR Receptor (VEGFR-2) Human
Em condições patológicas como o câncer, a angiogênese, ou seja, o crescimento de novos vasos a partir de uma rede vascular pré-existente, resulta numa maior oxigenação e nutrição das células e, consequentemente, num rápido crescimento do tumor [1]. Uma variedade de fatores estimulam a angiogênese, entre eles o Fator de Crescimento Endotelial Vas
Publicado em: 2009
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4. The second immunoglobulin-like domain of the VEGF tyrosine kinase receptor Flt-1 determines ligand binding and may initiate a signal transduction cascade.
Vascular endothelial growth factor (VEGF) is an angiogenic inducer that mediates its effects through two high affinity receptor tyrosine kinases, Flt-1 and KDR. Flt-1 is required for endothelial cell morphogenesis whereas KDR is involved primarily in mitogenesis. Flt-1 has an alternative ligand, placenta growth factor (PlGF). Both Flt-1 and KDR have seven im
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5. Fetal liver kinase 1 is a receptor for vascular endothelial growth factor and is selectively expressed in vascular endothelium.
Vascular endothelial growth factor (VEGF), also known as vascular permeability factor, induces endothelial proliferation in vitro and vascular permeability in vivo. The human transmembrane c-fms-like tyrosine kinase Flt-1 has recently been identified as a VEGF receptor. Flt-1 kinase has seven immunoglobulin-like extracellular domains and a kinase insert sequ
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6. Flt-1 lacking the tyrosine kinase domain is sufficient for normal development and angiogenesis in mice
Receptor tyrosine kinases Flt-1 and Flk-1/KDR, and their ligand, the vascular endothelial growth factor (VEGF), were shown to be essential for angiogenesis in the mouse embryo by gene targeting. Flk-1/KDR null mutant mice exhibited impaired endothelial and hematopoietic cell development. On the other hand, Flt-1 null mutation resulted in early embryonic deat
The National Academy of Sciences.
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7. Vascular endothelial growth factor: Crystal structure and functional mapping of the kinase domain receptor binding site
Vascular endothelial growth factor (VEGF) is a homodimeric member of the cystine knot family of growth factors, with limited sequence homology to platelet-derived growth factor (PDGF) and transforming growth factor β2 (TGF-β). We have determined its crystal structure at a resolution of 2.5 Å, and identified its kinase domain receptor (KDR) binding site u
The National Academy of Sciences of the USA.
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8. A repressor sequence in the juxtamembrane domain of Flt-1 (VEGFR-1) constitutively inhibits vascular endothelial growth factor-dependent phosphatidylinositol 3′-kinase activation and endothelial cell migration
Vascular endothelial growth factor (VEGF) has two highly homologous tyrosine kinase receptors: Flt-1 (VEGFR-1) and KDR (VEGFR-2). KDR is strongly phosphorylated on tyrosines and can transmit mitogenic and motogenic signals following VEGF binding, while Flt-1 is markedly less effective in mediating such functions. To dissect the regions that account for the d
Oxford University Press.
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9. Human Immunodeficiency Virus Tat Modulates the Flk-1/KDR Receptor, Mitogen-Activated Protein Kinases, and Components of Focal Adhesion in Kaposi’s Sarcoma Cells†
Kaposi’s sarcoma (KS) spindle cell growth and spread have been reported to be modulated by various cytokines as well as the human immunodeficiency virus (HIV) gene product Tat. Recently, HIV-1 Tat has been shown to act like a cytokine and bind to the Flk-1/KDR receptor for the vascular endothelial growth factor A (VEGF-A), which is expressed by KS cells. W
American Society for Microbiology.
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10. Identification of a peptide blocking vascular endothelial growth factor (VEGF)-mediated angiogenesis
Vascular endothelial growth factor (VEGF) binding to the kinase domain receptor (KDR/FLK1 or VEGFR–2) mediates vascularization and tumor-induced angiogenesis. Since there is evidence that KDR plays an important role in tumor angiogenesis, we sought to identify peptides able to block the VEGF–KDR interaction. A phage epitope library was screened by affini
Oxford University Press.
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11. Activation of hypoxia-inducible factors in hyperoxia through prolyl 4-hydroxylase blockade in cells and explants of primate lung
Preterm neonates with respiratory distress syndrome (RDS) often develop a chronic form of lung disease called bronchopulmonary dysplasia (BPD), characterized by decreased alveolar and vascular development. Ventilator treatment with supraphysiological O2 concentrations (hyperoxia) contribute to the development of BPD. Hyperoxia down-regulates and hypoxia up-r
National Academy of Sciences.
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12. In vitro and in vivo studies of a VEGF121/rGelonin chimeric fusion toxin targeting the neovasculature of solid tumors
Vascular endothelial growth factor (VEGF) plays a key role in the growth and metastasis of solid tumors. We generated a fusion protein containing VEGF121 linked by a flexible G4S tether to the toxin gelonin (rGel) and expressed this as a soluble protein in bacteria. Purified VEGF121/rGel migrated as an 84-kDa homodimer under nonreducing conditions. VEGF121/r
The National Academy of Sciences.