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Current medicinal chemistry, ISSN 0929-8673, 08/2017, Volume 24, Issue 26, pp. 2860 - 2886
Journal Article
Proceedings of the National Academy of Sciences - PNAS, ISSN 1091-6490, 2013, Volume 110, Issue 43, pp. 17380 - 17385
Journal Article
Matrix biology, ISSN 0945-053X, 2017, Volume 57-58, pp. 285 - 298
Perlecan, a large basement membrane heparan sulfate proteoglycan, is expressed in a wide array of tissues where it regulates diverse cellular processes... 
Heparan sulfate | Proteoglycan | Angiogenesis | Autophagy | Endorepellin | SCHWARTZ-JAMPEL-SYNDROME | PERICELLULAR MATRIX | BIOCHEMISTRY & MOLECULAR BIOLOGY | MUSCLE-CELL PROLIFERATION | SILVERMAN-HANDMAKER TYPE | PROTEIN CORE | BASEMENT-MEMBRANES | CELL BIOLOGY | DENSITY-LIPOPROTEIN-RECEPTOR | HEPARAN-SULFATE PROTEOGLYCAN | EXTRACELLULAR-MATRIX | PROTEOMIC ANALYSIS | AMP-Activated Protein Kinases - metabolism | Peptide Fragments - metabolism | Signal Transduction | TOR Serine-Threonine Kinases - metabolism | Neovascularization, Physiologic - genetics | Basement Membrane - cytology | Heart - growth & development | Humans | Gene Expression Regulation | Vascular Endothelial Growth Factor Receptor-2 - metabolism | Inflammation | Basement Membrane - metabolism | Vascular Endothelial Growth Factor Receptor-2 - genetics | Animals | TOR Serine-Threonine Kinases - genetics | Heparan Sulfate Proteoglycans - genetics | Heparan Sulfate Proteoglycans - metabolism | Organogenesis - genetics | Protein Domains | Peptide Fragments - genetics | AMP-Activated Protein Kinases - genetics | Osteogenesis - genetics | Endothelial growth factors | Physiological aspects | Analysis | Phosphatases | Sarcoma | Low density lipoproteins | T cells | Biological response modifiers | Sulfates | Cells | Endothelium | Laminin | Mitogens | Protein kinases | Growth factors | Interferon gamma
Journal Article
Journal Article
The Journal of biological chemistry, ISSN 0021-9258, 07/2011, Volume 286, Issue 29, pp. 25947 - 25962
Endorepellin, the C-terminal module of perlecan, negatively regulates angiogenesis counter to its proangiogenic parental molecule. Endorepellin (the C-terminal... 
Transcription, Genetic - drug effects | Vascular Endothelial Growth Factor A - biosynthesis | Vascular Endothelial Growth Factor Receptor-1 - antagonists & inhibitors | Humans | Angiostatic Proteins - pharmacology | Peptide Fragments - pharmacology | Vascular Endothelial Growth Factor A - genetics | Vascular Endothelial Growth Factor Receptor-2 - antagonists & inhibitors | Vascular Endothelial Growth Factor A - pharmacology | Heparan Sulfate Proteoglycans - chemistry | Protein Structure, Tertiary | Cell Line | Peptide Fragments - metabolism | Endothelial Cells - metabolism | Angiostatic Proteins - chemistry | Rats | Vascular Endothelial Growth Factor Receptor-2 - metabolism | Vascular Endothelial Growth Factor Receptor-1 - metabolism | Down-Regulation - drug effects | Vascular Endothelial Growth Factor Receptor-1 - chemistry | Protein Transport | Peptide Fragments - chemistry | Vascular Endothelial Growth Factor Receptor-2 - chemistry | Animals | Protein Tyrosine Phosphatase, Non-Receptor Type 6 - metabolism | Heparan Sulfate Proteoglycans - metabolism | Integrin alpha2beta1 - antagonists & inhibitors | Protein Binding | Integrin alpha2beta1 - metabolism | Angiostatic Proteins - metabolism | Endothelial Cells - drug effects | Heparan Sulfate Proteoglycans - pharmacology | Proteoglycan Structure | VEGFR2 | Basement Membrane | Perlecan | Heparan Sulfate | Glycobiology and Extracellular Matrices | Cell Surface Receptor | α2β1 Integrin | Protein-Protein Interactions | Endorepellin | Heparan Sulfate Proteoglycan
Journal Article
Journal of lipid research, ISSN 1539-7262, 2017, Volume 58, Issue 1, pp. 216 - 225
In mice lacking glycosylphosphatidylinositol-anchored high density lipoprotein binding protein 1 (GPIHBP1), the LPL secreted by adipocytes and myocytes remains... 
Chemistry | Glycosylphosphatidylinositolanchored high density lipoprotein binding protein | Lipolysis and fatty acid metabolism | Supplementary chylomicrons | Lipids | Lipoprotein lipase | Triglycerides | Endothelial cells | Heparan sulfate proteoglycan | endothelial cells | TERMINAL DOMAIN | CLEARING FACTOR | BIOCHEMISTRY & MOLECULAR BIOLOGY | RECEPTOR | triglycerides | CHYLOMICRONEMIA | IDENTIFICATION | HYPERTRIGLYCERIDEMIA | ACTIVATED LIPOPROTEIN LIPASE | lipids/chemistry | lipoprotein lipase | BINDING PROTEIN-1 GPIHBP1 | glycosylphosphatidylinositol-anchored high density lipoprotein binding protein 1 | HEPARAN-SULFATE PROTEOGLYCAN | MUTATIONS | lipolysis and fatty acid metabolism | heparan sulfate proteoglycan | chylomicrons | Cell Line | Lipoprotein Lipase - genetics | Humans | Receptors, Lipoprotein - genetics | Capillaries - enzymology | Hep G2 Cells | Lipolysis - genetics | Chylomicrons - metabolism | Animals | Heparan Sulfate Proteoglycans - metabolism | Adipocytes - metabolism | Mice | Culture Media - chemistry | Capillaries - metabolism | Lipoprotein Lipase - metabolism | Heparan sulfate | Cell culture | Proteoglycans | Adipose tissue | Mobility | Adipocytes | Myocytes | Missense mutation | Rodents | Heparan sulfate proteoglycans | Glycosylphosphatidylinositol | Sulfate | Capillaries | Adipose tissue (brown) | chemistry | lipids
Journal Article
Molecules and Cells, ISSN 1016-8478, 5/2009, Volume 27, Issue 5, pp. 503 - 513
Journal Article