Src kinase becomes preferentially associated with the VEGFR, KDR/Flk-1, following VEGF stimulation of vascular endothelial cells. - Wikidata - awgldk - TriplyDB

Src kinase becomes preferentially associated with the VEGFR, KDR/Flk-1, following VEGF stimulation of vascular endothelial cells.

Src kinase becomes preferentially associated with the VEGFR, KDR/Flk-1, following VEGF stimulation of vascular endothelial cells.

http://www.wikidata.org/entity/Q24796859

about

Phosphorylation of Tyr1214 within VEGFR-2 triggers the recruitment of Nck and activation of Fyn leading to SAPK2/p38 activation and endothelial cell migration in response to VEGF Src homology 2 (SH2) domain containing protein tyrosine phosphatase-1 (SHP-1) dephosphorylates VEGF Receptor-2 and attenuates endothelial DNA synthesis, but not migration Vascular endothelial growth factor A: just one of multiple mechanisms for sex-specific vascular development within the testis?The adaptor protein shb binds to tyrosine 1175 in vascular endothelial growth factor (VEGF) receptor-2 and regulates VEGF-dependent cellular migration Quercetin-4'-O-β-D-glucopyranoside (QODG) inhibits angiogenesis by suppressing VEGFR2-mediated signaling in zebrafish and endothelial cells Retinal vascular permeability suppression by topical application of a novel VEGFR2/Src kinase inhibitor in mice and rabbits.A link between SIN1 (MAPKAP1) and poly(rC) binding protein 2 (PCBP2) in counteracting environmental stress.Vascular endothelial-cadherin tyrosine phosphorylation in angiogenic and quiescent adult tissues Direct sensing of endothelial oxidants by vascular endothelial growth factor receptor-2 and c-Src.Regulation of endothelial permeability by Src kinase signaling: vascular leakage versus transcellular transport of drugs and macromolecules.1'-Acetoxychavicol acetate suppresses angiogenesis-mediated human prostate tumor growth by targeting VEGF-mediated Src-FAK-Rho GTPase-signaling pathway.Expression of vascular endothelial growth factor and basic fibroblast growth factor in extramammary Paget disease Inhibition of cytokine signaling in human retinal endothelial cells through modification of caveolae/lipid rafts by docosahexaenoic acid VEGF-induced Rac1 activation in endothelial cells is regulated by the guanine nucleotide exchange factor Vav2 Multifocal angiostatic therapy: an update.c-Yes response to growth factor activation.A systems biology approach to understanding the mechanisms of action of chinese herbs for treatment of cardiovascular disease.Advances in hemorrhagic stroke therapy: conventional and novel approaches.Tylophorine, a phenanthraindolizidine alkaloid isolated from Tylophora indica exerts antiangiogenic and antitumor activity by targeting vascular endothelial growth factor receptor 2-mediated angiogenesis.Ca2+ channels in retinal pigment epithelial cells regulate vascular endothelial growth factor secretion rates in health and disease.Targeting Src in breast cancer.Src family kinases as mediators of endothelial permeability: effects on inflammation and metastasis.Acetyl-11-keto-beta-boswellic acid inhibits prostate tumor growth by suppressing vascular endothelial growth factor receptor 2-mediated angiogenesis Compartmentalization of redox signaling through NADPH oxidase-derived ROS.Dasatinib: a potent SRC inhibitor in clinical development for the treatment of solid tumors.Regulation of caveolin-1 expression and phosphorylation by VEGF in ovine amnion cells.VEGF receptor signaling in vertebrate development.The potential for dasatinib in treating chronic lymphocytic leukemia, acute myeloid leukemia, and myeloproliferative neoplasms.Growth factor signaling in metastasis: current understanding and future opportunities.Regulation of pulmonary endothelial barrier function by kinases.Daphnetin inhibits TNF-α and VEGF-induced angiogenesis through inhibition of the IKKs/IκBα/NF-κB, Src/FAK/ERK1/2 and Akt signalling pathways.Neuropilin-1 mediates vascular permeability independently of vascular endothelial growth factor receptor-2 activation.Ligand-independent activation of vascular endothelial growth factor receptor 1 by low-density lipoprotein.Vascular endothelial growth factor receptor-1 mediates migration of human colorectal carcinoma cells by activation of Src family kinases.Vascular endothelial growth factor and nephrin interact and reduce apoptosis in human podocytes.Src blockade stabilizes a Flk/cadherin complex, reducing edema and tissue injury following myocardial infarction.Vascular Endothelial Growth Factor, Irradiation, and Axitinib Have Diverse Effects on Motility and Proliferation of Glioblastoma Multiforme Cells The von Hippel-Lindau Tumor Suppressor Protein Is Destabilized by Src: Implications for Tumor Angiogenesis and Progression Src kinases mediate VEGFR2 transactivation by the osteostatin domain of PTHrP to modulate osteoblastic function.VEGF and thrombin induce MKP-1 through distinct signaling pathways: role for MKP-1 in endothelial cell migration.

P2860

a97fba3dd546a122a60f60aac01fdc79a286a9f0 f6a88226c2f6e39abc4b965d298dffb19f2b622c

P248

Q24302435-1B80B3A5-1B7B-4D43-953E-C4F8CA6E9818 Q24315888-8FF64A96-4A7A-4A15-8F54-95C56E8345D4 Q26777347-21B3A384-6FB5-40AB-9389-5703EBB54940 Q28250994-78D2C4D9-3D1E-455E-9281-ED337E6BBA8F Q28480617-3E4FE143-EA76-4204-A2C7-EB81B81E6C20 Q33335166-56726A9B-E05D-4ABE-905C-5EE6818574BD Q33358627-6D347D8F-4AA8-481A-9DCB-4E987F257B8B Q33556970-1C09E7B5-35D6-471E-9D9C-C332C9E6B469 Q34092503-483BAE69-6B39-47AC-BCB6-5DCC65A3301D Q34401749-F6AAA851-E519-4997-A2CC-9ED500313537 Q35020469-C30A7020-2F40-4426-A3E3-3C5BE4764B58 Q35632284-8914B9B6-9F9C-470A-A16A-610FB820199C Q35989359-B12CC64A-6419-4055-8D25-823B2AFB5B19 Q36082465-CDB0E84F-8E5D-4A75-81F1-5F7237BE2380 Q36311166-01D31C65-886A-4328-B268-FF540829F1C5 Q36336583-C9DBFCD0-DAAF-4CBA-9E5C-82883BE17969 Q36396593-B7298858-B074-44B9-BAA6-F8FC4893CEDE Q36944012-C264722E-9D6B-4688-8060-316532E8BA7E Q37071525-DFF09FB6-E7E1-428B-882A-109F2DCC56DC Q37110107-D5BF00A8-AE12-4CA7-8823-33FD097D635F Q37167029-2A2396A1-72AC-4F78-8124-99FB1FEBC1F6 Q37278942-529E9C10-B383-4B8A-9710-661FFF616782 Q37299641-CC22C07F-644C-4EF0-9D00-992658FB8A26 Q37322476-CD831E67-9141-4A1B-B000-EEBC19028BD3 Q37613072-3B143047-A474-4EC4-8F0C-67A1A46EE847 Q37662176-A35D567E-FD46-41B3-997C-EB8367AEDA07 Q37795572-8493B733-5858-4320-A33E-97BA5568F209 Q37861186-D0024538-E4EC-43AA-BCBA-2B5EE834CEEE Q38019410-88F1087E-C82E-48B1-BAAB-781C0074D000 Q38963349-9DE74EDA-2862-4248-8C25-8A1243A295B2 Q39686369-F3B605B3-2945-4094-B097-E4D9C7FCAD33 Q39819854-6B69E705-E89A-4562-A6A8-5F5506584416 Q40061782-9EE6BB87-543D-4665-A75F-E77E71702C74 Q40281928-A53FF563-5ECA-4205-9EE5-30EDEE2FA5CE Q40520623-132A439D-B852-495D-B497-052E60E2FB48 Q40643967-1E3DE54E-FB7D-41B9-859D-3D7F337CAE4A Q41525538-D9FF59FF-0F8B-4556-97B1-3D958680DA7E Q41612038-2DF9DC8A-7F59-45E0-8DD8-ECC0E7D382D9 Q42825075-28C1DF04-BF6E-4117-885C-7325469F4462 Q46899889-B0112565-50A7-449F-8737-9D29E5A673F7

P2860

Src kinase becomes preferentially associated with the VEGFR, KDR/Flk-1, following VEGF stimulation of vascular endothelial cells.

http://www.wikidata.org/entity/Q24796859

description

2002 nî lūn-bûn

@nan

2002 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2002 թվականի դեկտեմբերին հրատարակված գիտական հոդված

@hy

2002年の論文

@ja

2002年論文

@yue

2002年論文

@zh-hant

2002年論文

@zh-hk

2002年論文

@zh-mo

2002年論文

@zh-tw

2002年论文

@wuu

name

Src kinase becomes preferentia ...... of vascular endothelial cells

@nl

Src kinase becomes preferentia ...... of vascular endothelial cells.

@ast

Src kinase becomes preferentia ...... of vascular endothelial cells.

@en

type

label

Src kinase becomes preferentia ...... of vascular endothelial cells

@nl

Src kinase becomes preferentia ...... of vascular endothelial cells.

@ast

Src kinase becomes preferentia ...... of vascular endothelial cells.

@en

prefLabel

Src kinase becomes preferentia ...... of vascular endothelial cells

@nl

Src kinase becomes preferentia ...... of vascular endothelial cells.

@ast

Src kinase becomes preferentia ...... of vascular endothelial cells.

@en

P1433

Q24796859-EDC02577-317B-4002-A886-F6714D5B1FD1

P1476

Q24796859-155D9450-E4A7-4DC7-BC3F-EC6268915F9E

P2093

Q24796859-3F2BD9A7-A169-48F4-BABE-674E7D881B53

Q24796859-944F6CF2-9098-40A8-9691-166A1224411C

Q24796859-A6E44F15-8BB6-4E6E-8421-F664C5FFDDB2

P2860

Q24796859-01448493-F865-477F-AFEB-BAADD2283626

Q24796859-06C972DA-A34B-48D2-8CAF-92C6CE033B78

Q24796859-0AA7C644-9D7B-4B47-8EDA-B4E6D43B580E

Q24796859-12C14EBD-BA8A-453A-93BC-054202624CB9

Q24796859-1363865C-E751-4359-AE6E-0AC575010D7E

Q24796859-19118B9F-74EA-45F0-896B-AB03192F8467

Q24796859-1F85EED7-B1D5-4D4C-88C4-89CE5A77C059

Q24796859-2002D539-0E18-4BA8-A0D7-AF46270EFAA0

Q24796859-21675D1E-BCCE-4129-9B57-98CD0EC66689

Q24796859-2437A59E-BAAA-4068-9DBF-54EF4DDEFE91

P2888

Q24796859-C8985EA1-A758-4A9B-BB3E-CB7C13D227AD

P304

Q24796859-2071D27F-A3FF-42D0-A882-E04460FD67AE

P31

Q24796859-39954AF0-123B-4059-84DA-52A87126266B

P356

Q24796859-058159B7-BB26-4E7B-A031-8F75AE8BD6DD

P407

Q24796859-8092BC14-0BD5-4A64-85F1-3A43B0DBF5E3

P433

Q24796859-26C16D0E-2A4E-45F4-ABBD-08E40D7CB254

P478

Q24796859-826777E0-C520-4252-8E71-78ABEB3BFD80

P577

Q24796859-6E47222E-E921-4A5D-8999-095764074956

P5875

Q24796859-C87398E3-72E0-4722-8F1F-D9189866B08A

P6179

Q24796859-8A2F07C5-EBAD-452D-A60C-4D7D0006CB16

P698

Q24796859-EFC29C5B-661F-4644-9EB3-A0C721915613

P921

Q24796859-84963AD9-9C4B-470C-8239-30C08FD53276

P932

Q24796859-C8AC67D1-AADE-4B8A-A60B-C3AF0C2D63DB

P356

P1433

BMC Biochemistry

P1476

Src kinase becomes preferentia ...... of vascular endothelial cells.

@en

P2093

Donald J Fujita

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

Jing Wang

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

Mary T Chou

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

P2860

Aids-related malignancies

c-Src-dependent Activation of the Epidermal Growth Factor Receptor and Mitogen-activated Protein Kinase Pathway by Arsenic

A single autophosphorylation site on KDR/Flk-1 is essential for VEGF-A-dependent activation of PLC-gamma and DNA synthesis in vascular endothelial cells

Myristoylation and differential palmitoylation of the HCK protein-tyrosine kinases govern their attachment to membranes and association with caveolae

Different signal transduction properties of KDR and Flt1, two receptors for vascular endothelial growth factor

Activation of the pp60c-src protein kinase is an early event in colonic carcinogenesis

Three-dimensional structure of the tyrosine kinase c-Src

The 2.35 A crystal structure of the inactivated form of chicken Src: a dynamic molecule with multiple regulatory interactions

SH2 domains recognize specific phosphopeptide sequences

Biological activity and phosphorylation sites of the bacterially expressed cytosolic domain of the KDR VEGF-receptor

P2888

P304

32

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

P31

scholarly article

P356

10.1186/1471-2091-3-32

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

P407

P433

1

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

P478

3

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

P577

2002-12-31T00:00:00Z

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

P5875

10967580

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

P6179

1006233289

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

P698

12509223

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

P921

P932

140315

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