Endorepellin, the angiostatic module of perlecan, interacts with both the α2β1 integrin and vascular endothelial growth factor receptor 2 (VEGFR2): a dual receptor antagonism
about
Proteoglycan form and function: A comprehensive nomenclature of proteoglycansDecorin causes autophagy in endothelial cells via Peg3Endorepellin laminin-like globular 1/2 domains bind Ig3-5 of vascular endothelial growth factor (VEGF) receptor 2 and block pro-angiogenic signaling by VEGFA in endothelial cellsOncosuppressive functions of decorinMatricryptins Network with Matricellular Receptors at the Surface of Endothelial and Tumor CellsHeparan Sulfate Proteoglycans May Promote or Inhibit Cancer Progression by Interacting with Integrins and Affecting Cell MigrationThe role of perlecan and endorepellin in the control of tumor angiogenesis and endothelial cell autophagyDecoding the Matrix: Instructive Roles of Proteoglycan ReceptorsExtracellular Matrix, a Hard Player in AngiogenesisInsights into the key roles of proteoglycans in breast cancer biology and translational medicineHeparan sulfate signaling in cancerA current view of perlecan in physiology and pathology: A mosaic of functions.Endorepellin evokes autophagy in endothelial cellsRegulation of Tumor Angiogenesis and Choroidal Neovascularization by Endogenous Angioinhibitors.LG3 fragment of endorepellin is a possible biomarker of severity in IgA nephropathy.Perlecan maintains microvessel integrity in vivo and modulates their formation in vitroEndogenous angiogenesis inhibitor blocks tumor growth via direct and indirect effects on tumor microenvironment.Proteolytically Derived Endogenous Angioinhibitors Originating from the Extracellular MatrixDecorin antagonizes the angiogenic network: concurrent inhibition of Met, hypoxia inducible factor 1α, vascular endothelial growth factor A, and induction of thrombospondin-1 and TIMP3.Perlecan modulates VEGF signaling and is essential for vascularization in endochondral bone formation.Decorin is an autophagy-inducible proteoglycan and is required for proper in vivo autophagyMapping the differential distribution of proteoglycan core proteins in the adult human retina, choroid, and sclera.Endorepellin affects angiogenesis by antagonizing diverse vascular endothelial growth factor receptor 2 (VEGFR2)-evoked signaling pathways: transcriptional repression of hypoxia-inducible factor 1α and VEGFA and concurrent inhibition of nuclear factEndostatin and endorepellin: A common route of action for similar angiostatic cancer avengersDecorin induces rapid secretion of thrombospondin-1 in basal breast carcinoma cells via inhibition of Ras homolog gene family, member A/Rho-associated coiled-coil containing protein kinase 1.Border patrol: insights into the unique role of perlecan/heparan sulfate proteoglycan 2 at cell and tissue bordersDecorin-inducible Peg3 Evokes Beclin 1-mediated Autophagy and Thrombospondin 1-mediated AngiostasisMatricryptins and matrikines: biologically active fragments of the extracellular matrix.The potential role of perlecan domain V as novel therapy in vascular dementia.Perlecan domain V inhibits amyloid-β induced brain endothelial cell toxicity and restores angiogenic function.Proteoglycans: Potential Agents in Mammographic Density and the Associated Breast Cancer Risk.The nature and biology of basement membranes.Mast cells produce novel shorter forms of perlecan that contain functional endorepellin: a role in angiogenesis and wound healing.Perlecan deficiency causes endothelial dysfunction by reducing the expression of endothelial nitric oxide synthase.Targeted proteomics effectively quantifies differences between native lung and detergent-decellularized lung extracellular matrices.Endorepellin-evoked Autophagy Contributes to Angiostasis.Decorin-evoked paternally expressed gene 3 (PEG3) is an upstream regulator of the transcription factor EB (TFEB) in endothelial cell autophagy.Recombinant Domain V of Human Perlecan Is a Bioactive Vascular Proteoglycan.Perlecan Domain V Inhibits Amyloid-β Induced Activation of the α2β1 Integrin-Mediated Neurotoxic Signaling Cascade.Extracellular matrix: The driving force of mammalian diseases.
P2860
Q21710680-B01FD307-16BC-4644-9954-B24BAE2E8D0DQ24296756-B0B8452C-A6A3-4E1F-A9CD-247F2E13AFF6Q24312922-DD473E63-2CEC-468A-AEF2-51EC97622FC1Q26745697-6F322F4A-E5DD-4ACB-ABD4-FF9C1C25F2DBQ26766481-CED14E72-F55B-4966-A02A-88A6F580179AQ26777586-97742114-7FAB-4BED-AD65-5EDB4282D0D3Q26800258-4C05FE63-DB39-4335-ACC8-A5DF3636B8A0Q26801397-23EE9098-DAF5-4AC7-B55F-10C556F60510Q28072886-200507C5-B60F-444F-9954-9FCFD3546088Q28085548-183C047E-FAFF-4DCC-85CF-E77A05CFE3DFQ28657828-6F485D4F-C0BE-414F-BD39-4D2F7B7FD94BQ30392738-02BBCD3A-585B-4116-8123-4D6CE203FFA8Q33718473-9C3F8DD0-C21A-456C-83D0-EC2C1EC63D51Q34230899-299CEF29-1750-413A-B250-921371E4284AQ34480669-2F424994-F865-46F1-BE5A-ADAA0F8343E4Q34548326-5239FA29-9138-4B72-94C0-60C02C048574Q35475215-5ED0490E-AE5C-4920-87EA-4E9E146D1F9CQ35679807-5BF40AA5-AF23-4549-AB4C-C1865D9E1F43Q35773980-300DF47D-C0A0-4C29-AF59-4B9F81CF190BQ35923316-53F8A96B-42B1-463B-903E-42D240DDDC38Q36322642-CAB4FCB3-3DCC-4293-A59C-FC6A5023B617Q36383629-0FA9CBD5-BEC6-4721-AD42-2E10C95828E1Q36481790-4B10233B-9AD9-49C6-BBA9-29F13CB84503Q36578668-4E1C5CC3-20B8-4C92-BE70-A424EF263B94Q36828327-BACBA955-3A43-4507-8B58-8B1217008DC8Q37610826-C8B66915-0732-4000-8C2E-650F3D790527Q37735163-0A3C92AC-E765-450B-A5F5-4FF49ECC8B1FQ38210749-6D1D6541-9777-4215-94DF-5346ADAF1FD8Q38223223-F7E48259-0009-4F5B-882F-9894AD7F957EQ38313097-DE002D4A-F0EA-4F1A-8A89-25BF842FDFD5Q38616484-6D95C822-71EC-4D71-B2EF-B0CED9AB9C6BQ39063783-230293DD-8BC4-4420-B799-FE4FA45EBA11Q39227219-025FA90F-751D-4451-97E6-9028EE8EB5A3Q39321049-84292FD4-0E02-442E-91AA-BEDF57B22C1AQ39331635-0AAF7778-5513-4F4C-B4FF-C1FF34BA6480Q41049426-5F364F8E-80F4-44D0-9074-0A49A74E2B9AQ42095044-98B889EC-2161-4AA4-B8CE-271692DF3778Q47748239-E32724A1-CB55-45ED-8F65-46C36E9603D3Q48468895-EBF49F27-884C-463D-9BAB-900E950871D8Q52602287-CB119A51-10DC-4C26-BE18-E8D1510393DA
P2860
Endorepellin, the angiostatic module of perlecan, interacts with both the α2β1 integrin and vascular endothelial growth factor receptor 2 (VEGFR2): a dual receptor antagonism
description
2011 nî lūn-bûn
@nan
2011 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
name
Endorepellin, the angiostatic ...... 2): a dual receptor antagonism
@ast
Endorepellin, the angiostatic ...... 2): a dual receptor antagonism
@en
Endorepellin, the angiostatic ...... 2): a dual receptor antagonism
@en-gb
Endorepellin, the angiostatic ...... 2): a dual receptor antagonism
@nl
type
label
Endorepellin, the angiostatic ...... 2): a dual receptor antagonism
@ast
Endorepellin, the angiostatic ...... 2): a dual receptor antagonism
@en
Endorepellin, the angiostatic ...... 2): a dual receptor antagonism
@en-gb
Endorepellin, the angiostatic ...... 2): a dual receptor antagonism
@nl
prefLabel
Endorepellin, the angiostatic ...... 2): a dual receptor antagonism
@ast
Endorepellin, the angiostatic ...... 2): a dual receptor antagonism
@en
Endorepellin, the angiostatic ...... 2): a dual receptor antagonism
@en-gb
Endorepellin, the angiostatic ...... 2): a dual receptor antagonism
@nl
P2093
P2860
P50
P356
P1476
Endorepellin, the angiostatic ...... 2): a dual receptor antagonism
@en
P2093
Atul Goyal
Chiara Poluzzi
Kiyotoshi Sekiguchi
Matthew Concannon
Matthew Paul
Thomas Neill
P2860
P304
25947-25962
P356
10.1074/JBC.M111.243626
P407
P577
2011-05-19T00:00:00Z