about
Plasminogen activator inhibitor-1 protects endothelial cells from FasL-mediated apoptosisPlasminogen Activator Inhibitor-1 in Cancer: Rationale and Insight for Future Therapeutic TestingTissue inhibitor of metalloproteinase-2 (TIMP-2) binds to the catalytic domain of the cell surface receptor, membrane type 1-matrix metalloproteinase 1 (MT1-MMP)Tumor microenvironment complexity: emerging roles in cancer therapy.Tissue inhibitors of matrix metalloproteinases in cancer.Paternal Risk Factors for Oral Clefts in Northern Africans, Southeast Asians, and Central Americans.Interactions between tumour cells and stromal cells and proteolytic modification of the extracellular matrix by metalloproteinases in cancer.Interleukin-6 in bone metastasis and cancer progression.MYCN-dependent expression of sulfatase-2 regulates neuroblastoma cell survival.Stromelysin-1 (MMP-3) is a target and a regulator of Wnt1-induced epithelial-mesenchymal transition (EMT)Proteases, extracellular matrix, and cancer: a workshop of the path B study sectionSmall Molecule Inhibitors of Plasminogen Activator Inhibitor-1 Elicit Anti-Tumorigenic and Anti-Angiogenic Activity.Oncogene MYCN regulates localization of NKT cells to the site of disease in neuroblastomaMechanisms of bone invasion and metastasis in human neuroblastoma.Mechanisms of pericyte recruitment in tumour angiogenesis: a new role for metalloproteinases.Modifying the soil to affect the seed: role of stromal-derived matrix metalloproteinases in cancer progression.Protumorigenic activity of plasminogen activator inhibitor-1 through an antiapoptotic functionValpha24-invariant NKT cells mediate antitumor activity via killing of tumor-associated macrophagesBone marrow-derived mesenchymal stromal cells promote survival and drug resistance in tumor cells.Runx2 promotes both osteoblastogenesis and novel osteoclastogenic signals in ST2 mesenchymal progenitor cells.More than the genes, the tumor microenvironment in neuroblastoma.Cancer-Associated Fibroblasts Share Characteristics and Protumorigenic Activity with Mesenchymal Stromal Cells.Interaction between bone marrow stromal cells and neuroblastoma cells leads to a VEGFA-mediated osteoblastogenesis.Identification of galectin-3-binding protein as a factor secreted by tumor cells that stimulates interleukin-6 expression in the bone marrow stroma.The contribution of bone marrow-derived cells to the tumor vasculature in neuroblastoma is matrix metalloproteinase-9 dependent.The matrix metalloproteinase inhibitor prinomastat enhances photodynamic therapy responsiveness in a mouse tumor model.TIMP-2 is released as an intact molecule following binding to MT1-MMP on the cell surface.Tissue inhibitor of metalloproteinase (TIMP)-2 acts synergistically with synthetic matrix metalloproteinase (MMP) inhibitors but not with TIMP-4 to enhance the (Membrane type 1)-MMP-dependent activation of pro-MMP-2.Contribution of neuroblastoma-derived exosomes to the production of pro-tumorigenic signals by bone marrow mesenchymal stromal cellsUrokinase induces receptor mediated brain tumor cell migration and invasion.Bone marrow microenvironment and tumor progression.The Tumor Microenvironment at a Turning Point Knowledge Gained Over the Last Decade, and Challenges and Opportunities Ahead: A White Paper from the NCI TME Network.The activity of zoledronic Acid on neuroblastoma bone metastasis involves inhibition of osteoclasts and tumor cell survival and proliferation.Sphingosine-1-Phosphate Receptor-1 Promotes Environment-Mediated and Acquired Chemoresistance.Tumor-associated macrophages promote neuroblastoma via STAT3 phosphorylation and up-regulation of c-MYC.Tumor progression and metastasis from genetic to microenvironmental determinants: a workshop of the tumor progression and metastasis NIH study section in honor of Dr. Martin L. Padarathsingh, May 31, 2006, Georgetown, Washington, DC.Conditional Knockdown of Gene Expression in Cancer Cell Lines to Study the Recruitment of Monocytes/Macrophages to the Tumor Microenvironment.Differential inhibition of membrane type 3 (MT3)-matrix metalloproteinase (MMP) and MT1-MMP by tissue inhibitor of metalloproteinase (TIMP)-2 and TIMP-3 rgulates pro-MMP-2 activation.Identification of the TIMP-2 binding site on the gelatinase A hemopexin C-domain by site-directed mutagenesis and the yeast two-hybrid systemComputerized quantification of tissue vascularization using high-resolution slide scanning of whole tumor sections
P50
Q24319106-D7850092-820C-498C-A26D-45BEF8C94452Q26801060-26FCEF5D-D431-4C3B-956A-C98E6FC48C71Q28258413-6F4E0743-3BA5-49A5-8E4D-137659AB4FC2Q30419311-F1AFEA66-3DAF-4817-85A6-9C3B888DB76EQ33692913-F393433C-75D4-4186-A3F3-6E6731CA96EFQ33840008-7E84D1A5-CD23-4C5F-BB2A-CFC16B6DD08BQ33959697-C3B659C6-A2FC-4844-B738-37E313A2A2D7Q34051820-4661831E-EC59-46EA-992D-68DAC884C8ACQ34438510-E8DF1F64-FDCD-4D71-9B06-C30E8069BB87Q34581929-E33E9BF1-F597-43CE-9B4B-C87863CB73B9Q35097428-FD9616B8-9E38-46D2-8884-8067CAD3A4B9Q35711136-00C60130-EFD3-4058-827E-A8531D3A9D8AQ35925629-1323210E-CB65-456F-8EA4-47DAD09573A2Q36173488-92C6A101-292A-4763-8E93-BDD1BE8964E3Q36365791-29D62177-A0DA-4612-8F7B-EF6CA247B1A0Q36471107-04B31BC4-D37F-4808-9712-3622445995ABQ36486880-918F1B66-CC9B-4DD7-B7FD-0C6FC9383881Q37209184-8E4417D5-F7B6-4703-9804-159E05FDFC1AQ37724189-7A4EA8FF-E6E2-408A-89E9-50E05F6D3598Q38332288-85EC336F-94C7-496C-9FF6-D2FC09DE689DQ38644731-CB3D1277-14C0-4EFA-8B53-F16EFC13E993Q38688878-5ED12CFD-C2DA-47BA-BCAA-448B9EF6FA1DQ38913336-94DA1B29-6F6E-4EA0-B3BA-C867EF7A856BQ39986427-8E5C67C2-4248-4B01-8829-FDBDE3CC0FBCQ40434427-5A8006ED-166F-4AFD-957E-CC2EC12CD0AAQ40571046-DEEFC413-E7A5-4AB6-A0E3-0F1D5CA07F3DQ40598577-406BB247-BF00-4041-B2C7-47C2D6D27ED6Q40853467-88A01658-8FBE-496B-9DF5-B227B154ED9FQ40980101-41134E21-74AF-41CB-BEC3-6F42DEEC8394Q41611040-3195A795-54A4-4255-9842-291907E516BAQ43164811-9915A551-BA8F-43E3-80FB-B7AEF818025FQ46026099-C8553C5B-3439-40DD-AAA0-1215979792BAQ46262276-F1053066-D64E-4066-BA14-8140F404EFECQ46444617-590F759D-FB17-4ED1-96FB-D8818F920625Q46745795-282747A8-CC85-427A-A6C7-8F28E9D9AB45Q46771686-E1E4307F-9E27-4C46-804E-4B710434997FQ47245967-C18D03D0-32B7-437A-8D44-EC9903DF7B2CQ47846803-6DD9083A-72DD-4536-A151-EA0DD0CD88C0Q78027558-E59DED36-46AA-45F9-8C8D-57D2C47CDD27Q78812059-C10CE000-F56E-43E2-A487-3F323D338B21
P50
description
researcher
@en
wetenschapper
@nl
name
Y A DeClerck
@en
Y A DeClerck
@nl
type
label
Y A DeClerck
@en
Y A DeClerck
@nl
prefLabel
Y A DeClerck
@en
Y A DeClerck
@nl
P106
P31
P496
0000-0002-3688-0113