Jong-Sup Bae mostly deals with Cell biology, Pharmacology, Immunology, Inflammation and Lipopolysaccharide. His work deals with themes such as Tumor microenvironment, Endothelial protein C receptor and Cell adhesion, which intersect with Cell biology. His work on Curcumin as part of general Pharmacology research is frequently linked to Baicalin, thereby connecting diverse disciplines of science.
His research investigates the connection between Immunology and topics such as Endothelium that intersect with issues in Endothelial dysfunction and Rutin. His studies in Inflammation integrate themes in fields like Umbilical vein and Cell adhesion molecule. His Lipopolysaccharide research is multidisciplinary, relying on both Biochemistry and Leukocyte migration.
Jong-Sup Bae focuses on Pharmacology, Lipopolysaccharide, Umbilical vein, Biochemistry and Inflammation. His studies deal with areas such as Tumor necrosis factor alpha, Immunology, Sepsis, HMGB1 and Thrombin as well as Pharmacology. His HMGB1 study combines topics from a wide range of disciplines, such as Proinflammatory cytokine, Endothelium and Leukocyte migration.
His Umbilical vein study integrates concerns from other disciplines, such as Phospholipase A2, Extracellular matrix and Signal transduction. His work carried out in the field of Inflammation brings together such families of science as Cell adhesion molecule and Vascular permeability. His Cell adhesion molecule study is focused on Cell biology in general.
Pharmacology, Lipopolysaccharide, Sepsis, HMGB1 and Umbilical vein are his primary areas of study. His biological study spans a wide range of topics, including Nitric oxide synthase, Vascular permeability, Leukocyte migration, Proinflammatory cytokine and Lung injury. His Lipopolysaccharide research integrates issues from Tumor necrosis factor alpha, Inflammation, NF-κB and Toll-like receptor.
His Inflammation study incorporates themes from Molecular biology, Ferritin and Cell biology. The various areas that Jong-Sup Bae examines in his HMGB1 study include Bioactive compound, Survival rate, High-mobility group, Endothelium and Cudratricusxanthone A. The Umbilical vein study combines topics in areas such as Cytotoxic T cell, Cell adhesion molecule and MAPK/ERK pathway.
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Tumor-Associated Macrophages and Neutrophils in Tumor Microenvironment
Jaehong Kim;Jong-Sup Bae.
Mediators of Inflammation (2016)
The ligand occupancy of endothelial protein C receptor switches the protease-activated receptor 1-dependent signaling specificity of thrombin from a permeability-enhancing to a barrier-protective response in endothelial cells
Jong-Sup Bae;Likui Yang;Chandrashekhara Manithody;Alireza R. Rezaie.
Structural Coupling of Smad and Runx2 for Execution of the BMP2 Osteogenic Signal
Amjad Javed;Jong-Sup Bae;Faiza Afzal;Soraya E. Gutierrez.
Journal of Biological Chemistry (2008)
Receptors of the protein C activation and activated protein C signaling pathways are colocalized in lipid rafts of endothelial cells
Jong-Sup Bae;Likui Yang;Alireza R. Rezaie.
Proceedings of the National Academy of Sciences of the United States of America (2007)
Protease activated receptor 1 (PAR-1) activation by thrombin is protective in human pulmonary artery endothelial cells if endothelial protein C receptor is occupied by its natural ligand.
Jong-Sup Bae;Alireza R. Rezaie.
Thrombosis and Haemostasis (2008)
βig-h3 supports keratinocyte adhesion, migration, and proliferation through α3β1 integrin
Jong Sup Bae;Suk Hee Lee;Jung Eun Kim;Je Yong Choi.
Biochemical and Biophysical Research Communications (2002)
Role of high mobility group box 1 in inflammatory disease: Focus on sepsis
Archives of Pharmacal Research (2012)
ROS homeostasis and metabolism: a critical liaison for cancer therapy.
Jongdoo Kim;Jaehong Kim;Jong-Sup Bae.
Experimental and Molecular Medicine (2016)
Activated protein C inhibits high mobility group box 1 signaling in endothelial cells
Jong-Sup Bae;Alireza R. Rezaie.
Anti-inflammatory Effects of Baicalin, Baicalein, and Wogonin In Vitro and In Vivo
Wonhwa Lee;Sae-Kwang Ku;Jong-Sup Bae.
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