about
sameAs
Gremlin is a novel agonist of the major proangiogenic receptor VEGFR2Role of PlGF in the intra- and intermolecular cross talk between the VEGF receptors Flt1 and Flk1Targeting extracellular domains D4 and D7 of vascular endothelial growth factor receptor 2 reveals allosteric receptor regulatory sitesHighly efficient baculovirus-mediated multigene delivery in primary cells.Vascular Endothelial Growth Factor-A165b Is Protective and Restores Endothelial Glycocalyx in Diabetic NephropathyStructural determinants of growth factor binding and specificity by VEGF receptor 2Structural determinants of vascular endothelial growth factor-D receptor binding and specificityThermodynamic and structural description of allosterically regulated VEGFR-2 dimerizationStructural and mechanistic insights into VEGF receptor 3 ligand binding and activationStructure and function of VEGF receptorsFunctional and structural characterization of the kinase insert and the carboxy terminal domain in VEGF receptor 2 activation.Structure of the Full-length VEGFR-1 Extracellular Domain in Complex with VEGF-A.VEGFR2 pY949 signalling regulates adherens junction integrity and metastatic spread.VEGFR-2 conformational switch in response to ligand binding.Recombinant human VEGF165b protein is an effective anti-cancer agent in mice.Neuropilin-1 in regulation of VEGF-induced activation of p38MAPK and endothelial cell organizationThe CMT4B disease-causing proteins MTMR2 and MTMR13/SBF2 regulate AKT signallingMonomeric gremlin is a novel vascular endothelial growth factor receptor-2 antagonist.Structure-function analysis of VEGF receptor activation and the role of coreceptors in angiogenic signaling.The reception and the party after: how vascular endothelial growth factor receptor 2 explores cytoplasmic space.Signalling properties of an HIV-encoded angiogenic peptide mimicking vascular endothelial growth factor activity.Cell lines expressing recombinant transmembrane domain-activated receptor kinases as tools for drug discovery.A CD44v6 peptide reveals a role of CD44 in VEGFR-2 signaling and angiogenesis.Subcellular object quantification with Squassh3C and SquasshAnalyst.Polyomavirus middle-T antigen lacking a membrane anchor sequence accumulates in the nucleus.Structure of a VEGF-VEGF receptor complex determined by electron microscopy.Regulation of alternative VEGF-A mRNA splicing is a therapeutic target for analgesia.Herpesvirus saimiri protein StpB associates with cellular Src.Activation and nuclear translocation of mitogen-activated protein kinases by polyomavirus middle-T or serum depend on phosphatidylinositol 3-kinase.Domains in middle-T antigen that cooperate in polyomavirus-mediated oncogenic transformation.Stimulation of c-Src by prolactin is independent of Jak2.Enhanced heparan sulfate proteoglycan-mediated uptake of cell-penetrating peptide-modified liposomes.A proangiogenic peptide derived from vascular endothelial growth factor receptor-1 acts through alpha5beta1 integrin.Antennapedia and HIV transactivator of transcription (TAT) "protein transduction domains" promote endocytosis of high molecular weight cargo upon binding to cell surface glycosaminoglycans.Reconstitution of two recombinant LSm protein complexes reveals aspects of their architecture, assembly, and function.Characterization of a drug-targetable allosteric site regulating vascular endothelial growth factor signaling.ScFvs as Allosteric Inhibitors of VEGFR-2: Novel Tools to Harness VEGF Signaling.High-level secretion of recombinant full-length streptavidin in Pichia pastoris and its application to enantioselective catalysis.Structural and functional characterization of alternative transmembrane domain conformations in VEGF receptor 2 activation.Structural analysis of vascular endothelial growth factor receptor-2/ligand complexes by small-angle X-ray solution scattering.
P50
Q24293152-481D18B5-DD62-4993-A09D-5975B6597CE4Q24304277-2DFBCE0A-4007-420B-BFAB-C5B76344CB81Q26822568-8B96484E-F4F0-4F14-8E8B-712AEC783F3DQ27317062-6D810686-EF2A-4D3C-A893-21FD8E412CEFQ27342809-D775C99F-B1E0-43B6-A457-717757B6C0E9Q27659686-C9470CB5-5CE2-49DC-96B1-E02277141CD4Q27666332-8F3CFD7F-1444-4491-BC5A-7BBD316FAECCQ27676493-203B922F-3FAA-4BEA-A482-8EA38A121840Q27679183-8C4972D4-8F97-4E7C-A2D2-D066F91BF55BQ28253932-B8C73A51-595C-43C1-B428-104413B9F210Q35223222-84B81428-09A5-4F0B-BE0B-039780683AC4Q36256784-2DDFAE55-DB20-4460-B6DE-2C867CCED608Q36747249-9DCF2E38-F461-47E4-9B89-EAF5827BF11DQ36791927-977967AF-7CA1-4A19-92C8-5BD4F4E773CAQ36932464-6A9521AD-D751-46E8-893C-A5B9FC67BE6AQ36948568-DCBDC527-66F0-4669-BC9A-60327F3E0AE0Q37294507-C6CD95E5-5C0E-441B-8C27-B670DE37E6F4Q37376551-DEDBAFEA-636B-4B3C-B857-E1CAFB093BA1Q37599022-4C7DC69D-2D00-49D0-8F94-68CAA4975467Q37969702-04C4610A-3032-4CA4-939B-C96D84D8C427Q38304360-65EB89B3-E68A-43CE-A2C2-3B05484E3991Q38952976-90752EBC-C899-47F0-A1C8-A4B796194BDCQ39796335-136FE6A1-C552-4179-9FBD-A94CD05F3F4AQ40337846-6ED7B8FB-F16C-404B-B245-D7A8E9FD4D79Q41255245-86200BC5-065D-4662-98E3-7EA1637B11BCQ41792412-CCE70C17-7CE8-40A7-B0EC-10FF06679FF9Q41953953-C0DC62E2-8FFD-4CAD-B119-886D4495067BQ42641364-A5ECE5DA-A24A-44D4-BDDE-1ABB795573DDQ42819325-539DF769-37AD-4C03-8F38-924D84C696DEQ42828677-0C68EAD3-3B04-402E-AA2C-1D45345344CDQ42928957-BB2BC1A8-2665-4CC3-8074-F610C7C44B5AQ44969312-C2ACB37F-8011-4408-8875-5D76BEEB2B50Q46815664-D597FEDF-55C7-4EE2-AAED-CAB5B33A5A8EQ47448961-23ED7F00-0BA5-41A2-8573-01C6EA0253CAQ50336106-DCA2C334-8CCE-4E37-8F67-61DBAF6A74A2Q52368230-58BA8D6C-79D5-40B9-A76F-2A9CB907BC3DQ54112592-C88DDBC1-8965-414D-91AD-1B13BBCA4FD5Q54301221-C63EFD92-D99E-41E9-895D-3F6DD2FA8890Q54341152-6197C4D0-A24F-4EA2-AEE7-BBF15F097177Q54587420-B5E28859-C445-414F-A133-61926F9A6593
P50
description
hulumtues
@sq
onderzoeker
@nl
researcher
@en
հետազոտող
@hy
name
Kurt Ballmer-Hofer
@ast
Kurt Ballmer-Hofer
@en
Kurt Ballmer-Hofer
@es
Kurt Ballmer-Hofer
@nl
Kurt Ballmer-Hofer
@sl
type
label
Kurt Ballmer-Hofer
@ast
Kurt Ballmer-Hofer
@en
Kurt Ballmer-Hofer
@es
Kurt Ballmer-Hofer
@nl
Kurt Ballmer-Hofer
@sl
altLabel
K Ballmer-Hofer
@en
prefLabel
Kurt Ballmer-Hofer
@ast
Kurt Ballmer-Hofer
@en
Kurt Ballmer-Hofer
@es
Kurt Ballmer-Hofer
@nl
Kurt Ballmer-Hofer
@sl
P21
P31
P496
0000-0002-3800-9129