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1. Full Text Expression of hypoxia-inducible factor 1 α , hypoxia-inducible factor 2 α , and von Hippel–Lindau protein in epithelial ovarian neoplasms and allelic loss of von Hippel-Lindau gene: nuclear expression of hypoxia-inducible factor 1 α is an independent prognostic factor in ovarian carcinoma
by Osada, Ryosuke, MD and Horiuchi, Akiko, MD, PhD and Kikuchi, Norihiko, MD and Yoshida, Junko, MD and Hayashi, Akiko, MD and Ota, Masao, PhD and Katsuyama, Yoshihiko, PhD and Mellilo, Giovanni, MD, PhD and Konishi, Ikuo, MD, PhD
Human Pathology, ISSN 0046-8177, 2007, Volume 38, Issue 9, pp. 1310 - 1320
Summary The hypoxia-inducible factor (HIF) is a transcriptional factor with important roles in tumor biology. To clarify the possible involvement of the HIF- α... 
Pathology | HIF-1 α | HIF-2 α | Prognosis | VHL | Ovarian carcinoma | HIF-1α | HIF-2α | CANCER PATIENTS | HIF-1 alpha | HIF-2 alpha | HYDROXYPROLINE | ovarian carcinoma | TUMOR ANGIOGENESIS | PATHOLOGY | prognosis | NECK-CANCER | HIF-2-ALPHA | FACTOR-1-ALPHA | FACTORS HIF-1-ALPHA | FACTOR (HIF)-1-ALPHA | HYPOXIA-INDUCIBLE FACTOR-2-ALPHA | ENDOTHELIAL GROWTH-FACTOR
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2. Full Text Trim13 potentiates toll-like receptor 2-mediated nuclear factor κb activation via K29-linked polyubiquitination of tumor necrosis factor receptor-associated factor 6
by Huang, Bin and Baek, Suk-Hwan
Molecular Pharmacology, ISSN 0026-895X, 04/2017, Volume 91, Issue 4, pp. 307 - 316
Ubiquitination is a versatile post-translational modification involved in nuclear factor-kappa B (NF-kappa B) activation of Toll-like receptor (TLR) signaling.... 
REGULATOR | SIGNALING PATHWAYS | RECOGNITION | UBIQUITIN | DOWN-REGULATION | DEGRADATION | PHARMACOLOGY & PHARMACY | CELL-GROWTH | AUTOPHAGY | PROTEINS | FAMILY | Polyubiquitin - metabolism | Chemokines - biosynthesis | Toll-Like Receptor 2 - agonists | Oligonucleotide Array Sequence Analysis | Humans | Mice, Inbred C57BL | Ubiquitin-Protein Ligases - metabolism | Male | NF-kappa B - metabolism | Up-Regulation - genetics | Toll-Like Receptor 2 - metabolism | Macrophage Activation | DNA-Binding Proteins - metabolism | Ubiquitination | Animals | HEK293 Cells | TNF Receptor-Associated Factor 6 - metabolism | Protein Binding | RAW 264.7 Cells | Lysine - metabolism | Mice | Tripartite Motif Proteins - metabolism
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3. Full Text Transforming growth factor-β and nuclear factor E2-related factor 2 regulate antioxidant responses in airway smooth muscle cells role in asthma
by Michaeloudes, Charalambos and Chang, Po-Jui and Petrou, Mario and Kian, Fan Chung
American Journal of Respiratory and Critical Care Medicine, ISSN 1073-449X, 10/2011, Volume 184, Issue 8, pp. 894 - 903
Rationale: Aberrant airway smooth muscle cell (ASMC) function and overexpression of transforming growth factor (TGF)-beta, which modulates ASMC proliferative... 
Antioxidant | Airway smooth muscle | Transforming growth factor-β | Nuclear factor E2-related factor 2 | Asthma | antioxidant | NRF2 ENHANCES SUSCEPTIBILITY | OXIDATIVE STRESS | DNA-BINDING | TGF-BETA | nuclear factor E2-related factor 2 | airway smooth muscle | asthma | INDUCTION | transforming growth factor-beta | IN-VITRO | REACTIVE OXYGEN | RESPIRATORY SYSTEM | NEGATIVE REGULATION | GENE-EXPRESSION | HEME OXYGENASE-1 | CRITICAL CARE MEDICINE | Asthma - metabolism | Gene Expression - drug effects | Antioxidants - metabolism | Humans | Gene Expression Regulation | Muscle, Smooth - metabolism | NF-E2 Transcription Factor - metabolism | NF-E2 Transcription Factor - antagonists & inhibitors | Transforming Growth Factor beta - pharmacology | Transfection | Adenoviridae - genetics | Thiocyanates - pharmacology | Cell Proliferation - drug effects | RNA, Small Interfering | Muscle, Smooth - cytology | Genetic Vectors | Isothiocyanates | Transforming Growth Factor beta - metabolism | transforming growth factor-β
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4. Full Text Angiotensin II Induces Connective Tissue Growth Factor and Collagen I Expression via Transforming Growth Factor–β–Dependent and –Independent Smad Pathways: The Role of Smad3
by Yang, Fuye and Chung, Arthur C.K and Ru Huang, Xiao and Lan, Hui Yao
Hypertension, ISSN 0194-911X, 10/2009, Volume 54, Issue 4, pp. 877 - 884
Connective tissue growth factor (CTGF) plays a critical role in angiotensin II (Ang II)–mediated hypertensive nephropathy. The present study investigated the... 
TGF-β | Smads | Angiotensin II | Renal fibrosis | MAP kinases | CTGF | SIGNAL | DIABETIC-NEPHROPATHY | renal fibrosis | FIBROBLASTS | MH1 DOMAIN | TGF-beta | SCLERODERMA | TUBULE EPITHELIAL-CELLS | GENE | angiotensin II | PERIPHERAL VASCULAR DISEASE | TRANSDIFFERENTIATION | Up-Regulation | Phosphorylation | Epithelial Cells - metabolism | Epithelial Cells - drug effects | Male | Smad3 Protein - metabolism | p38 Mitogen-Activated Protein Kinases - metabolism | Epithelial Cells - cytology | Kidney Tubules - metabolism | Disease Models, Animal | Kidney Diseases - metabolism | Smad7 Protein - metabolism | Cell Line | Collagen Type I - metabolism | Kidney Tubules - drug effects | Kidney Diseases - pathology | Smad2 Protein - metabolism | Rats | Rats, Sprague-Dawley | Hypertension - pathology | Hypertension - metabolism | Kidney Tubules - cytology | Animals | Mitogen-Activated Protein Kinase 3 - metabolism | Hypertension - complications | Signal Transduction - physiology | Kidney Diseases - etiology | Transforming Growth Factor beta - metabolism | Angiotensin II - physiology | Connective Tissue Growth Factor - metabolism | Mitogen-Activated Protein Kinase 1 - metabolism
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5. Full Text Transforming growth factor β-1 induces Snail transcription factor in epithelial cell lines. Mechanisms for epithelial mesenchymal transitions
by Peinado, Hector and Quintanilla, Miguel and Cano, Amparo
Journal of Biological Chemistry, ISSN 0021-9258, 06/2003, Volume 278, Issue 23, pp. 21113 - 21123
The Snail transcription factor has been described recently as a strong repressor of E-cadherin in epithelial cell lines, where its stable expression leads to... 
INVASION | TGF-BETA | SMAD PROTEINS | SIGNALING PATHWAY | HA-RAS | BIOCHEMISTRY & MOLECULAR BIOLOGY | E-CADHERIN EXPRESSION | KINASE | TUMOR-SUPPRESSOR GENE | CARCINOMA | CANCER | MAP Kinase Signaling System - physiology | Gene Expression - drug effects | Protein-Tyrosine Kinases - metabolism | Epithelial Cells - drug effects | Fibroblast Growth Factor 2 - pharmacology | Phosphatidylinositol 3-Kinases - metabolism | Mesoderm - cytology | MAP Kinase Kinase 2 | MAP Kinase Kinase 1 | Epithelial Cells - physiology | Genes, ras - physiology | Mitogen-Activated Protein Kinase Kinases - metabolism | Cadherins - genetics | Epithelial Cells - cytology | Snail Family Transcription Factors | Protein-Serine-Threonine Kinases - metabolism | Cell Line | Transforming Growth Factor beta1 | Kidney - cytology | Transcription Factors - genetics | DNA-Binding Proteins - genetics | Cell Movement - drug effects | Transforming Growth Factor beta - pharmacology | Phenotype | Animals | MAP Kinase Signaling System - drug effects | Promoter Regions, Genetic - physiology | Dogs | Snail protein | Smad4 protein | H-Ras protein
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6. Full Text VEGFR-3 controls tip to stalk conversion at vessel fusion sites by reinforcing Notch signalling
by Tammela, Tuomas and Zarkada, Georgia and Nurmi, Harri and Jakobsson, Lars and Heinolainen, Krista and Tvorogov, Denis and Zheng, Wei and Franco, Claudio A and Murtomäki, Aino and Aranda, Evelyn and Miura, Naoyuki and Ylä-Herttuala, Seppo and Fruttiger, Marcus and Mäkinen, Taija and Eichmann, Anne and Pollard, Jeffrey W and Gerhardt, Holger and Alitalo, Kari
Nature Cell Biology, ISSN 1465-7392, 10/2011, Volume 13, Issue 10, pp. 1202 - 1213
Angiogenesis, the growth of new blood vessels, involves specification of endothelial cells to tip cells and stalk cells, which is controlled by Notch... 
LYMPHATIC ENDOTHELIUM | KINASE-ACTIVITY | VASCULAR NETWORK FORMATION | ENDOTHELIAL-GROWTH-FACTOR | FACTOR-C | MOUSE EMBRYOS | EXTRACELLULAR-MATRIX | MONOCLONAL-ANTIBODY | TUMOR ANGIOGENESIS | FACTOR RECEPTOR-3 | CELL BIOLOGY | Neovascularization, Physiologic - drug effects | Human Umbilical Vein Endothelial Cells - metabolism | Receptors, Notch - metabolism | Humans | Vascular Endothelial Growth Factor A - metabolism | Vascular Endothelial Growth Factor A - genetics | Receptors, Notch - antagonists & inhibitors | Transfection | RNA Interference | Time Factors | Forkhead Transcription Factors - metabolism | Vascular Endothelial Growth Factor D - genetics | Phosphatidylinositol 3-Kinase - metabolism | Vascular Endothelial Growth Factor Receptor-3 - deficiency | Transduction, Genetic | Retinal Vessels - metabolism | Endothelial Cells - metabolism | Rhombencephalon - blood supply | Gene Expression Regulation | Vascular Endothelial Growth Factor Receptor-3 - metabolism | Forkhead Transcription Factors - genetics | Vascular Endothelial Growth Factor C - genetics | Mice, Knockout | Antibodies - pharmacology | Macrophages - metabolism | Vascular Endothelial Growth Factor D - metabolism | Animals | Signal Transduction - drug effects | Vascular Endothelial Growth Factor B - metabolism | Vascular Endothelial Growth Factor C - metabolism | Cell Line, Tumor | Neovascularization, Pathologic - genetics | Vascular Endothelial Growth Factor B - genetics | Mice | Neovascularization, Pathologic - metabolism | Protein Kinase Inhibitors - pharmacology | Vascular Endothelial Growth Factor Receptor-3 - genetics | Endothelial Cells - drug effects | Physiological aspects | Blood vessels | Cellular signal transduction | Growth factor receptors | Research | Vascular endothelial growth factor | Medical and Health Sciences | Medicin och hälsovetenskap
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7. Full Text Induction of latency‐associated peptide (transforming growth factor‐β1) expression on CD4+ T cells reduces Toll‐like receptor 4 ligand‐induced tumour necrosis factor‐α production in a transforming growth factor‐β‐dependent manner
by Boswell, Sandra and Sharif, Shayan and Alisa, Akeel and Pereira, Stephen P and Williams, Roger and Behboudi, Shahriar
Immunology, ISSN 0019-2805, 07/2011, Volume 133, Issue 3, pp. 278 - 287
CD4 + T cells expressing the latent form of transforming growth factor‐β [latency‐associated peptide (LAP) (TGF‐β 1 )] play an important role in the modulation... 
CD4 | T cells | glypican‐3 derived peptide | tumour necrosis factor‐α | latency‐associated peptide (transforming growth factor‐β | Tumour necrosis factor-α | Glypican-3 derived peptide | Latency-associated peptide (transforming growth factor-β | TGF-BETA | VASOACTIVE-INTESTINAL-PEPTIDE | MARKER | IMMUNOLOGY | TNF | ONCOFETAL PROTEIN GLYPICAN-3 | AUTOIMMUNE ENCEPHALOMYELITIS | CD4+T cells | glypican-3 derived peptide | latency-associated peptide (transforming growth factor-beta) | HEPATOCELLULAR-CARCINOMA | REGULATORY T-CELLS | CD3-SPECIFIC ANTIBODY | CORTICOSTEROIDS | tumour necrosis factor-alpha | Tumor Necrosis Factor-alpha - metabolism | Cell Line | Up-Regulation | Protein Precursors - genetics | Humans | Peptides - genetics | Glypicans - genetics | Toll-Like Receptor 4 - metabolism | Protein Precursors - metabolism | CD4-Positive T-Lymphocytes - immunology | Flow Cytometry | Peptides - metabolism | Transforming Growth Factor beta - genetics | Ligands | Transforming Growth Factor beta - metabolism | Indexing in process | tumour necrosis factor-α | CD4+ T cells | latency-associated peptide (transforming growth factor-β1) | Original
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8. Full Text Epidermal Growth Factor Receptor Tyrosine Kinase Inhibitors vs Conventional Chemotherapy in Non–Small Cell Lung Cancer Harboring Wild-Type Epidermal Growth Factor Receptor: A Meta-analysis
by Lee, June-Koo and Hahn, Seokyung and Kim, Dong-Wan and Suh, Koung Jin and Keam, Bhumsuk and Kim, Tae Min and Lee, Se-Hoon and Heo, Dae Seog
JAMA, ISSN 0098-7484, 04/2014, Volume 311, Issue 14, pp. 1430 - 1437
IMPORTANCE Current guidelines recommend both epidermal growth factor receptor (EGFR) tyrosine kinase inhibitors (TKIs) and cytotoxic chemotherapy drugs as... 
1ST-LINE ERLOTINIB | TRIAL | MEDICINE, GENERAL & INTERNAL | GEFITINIB | MULTICENTER | RANDOMIZED PHASE-3 | ADENOCARCINOMA | 2ND-LINE TREATMENT | OPEN-LABEL | MUTATIONS | EGFR | Disease-Free Survival | Lung Neoplasms - drug therapy | Receptor, Epidermal Growth Factor - genetics | Protein Kinase Inhibitors - therapeutic use | Humans | Receptor, Epidermal Growth Factor - antagonists & inhibitors | Antineoplastic Agents - therapeutic use | Carcinoma, Non-Small-Cell Lung - drug therapy | Mutation | Protein-Tyrosine Kinases - antagonists & inhibitors | Randomized Controlled Trials as Topic | Chemotherapy | Care and treatment | Research | Lung cancer, Non-small cell | Health aspects | Tyrosine metabolism | Cancer | Inhibitor drugs | Kinases | Lung cancer | Meta-analysis
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9. Full Text Transforming growth factor-β-induced epithelial-mesenchymal transition facilitates epidermal growth factor-dependent breast cancer progression
by Wendt, M.K and Smith, J.A and Schiemann, W.P
Oncogene, ISSN 0950-9232, 12/2010, Volume 29, Issue 49, pp. 6485 - 6498
Transforming growth factor-beta (TGF-beta) and epidermal growth factor (EGF) have critical roles in regulating the metastasis of aggressive breast cancers, yet... 
FAK | breast cancer | TGF-b | invasion | metastasis | EGFR | ACTIVATION | MAMMARY-CARCINOMA CELLS | BIOCHEMISTRY & MOLECULAR BIOLOGY | TUMOR | FACTOR RECEPTOR INHIBITION | PROLIFERATION | LINES | CELL BIOLOGY | TGF-beta | ONCOLOGY | GENETICS & HEREDITY | GENE-EXPRESSION | FOCAL ADHESION KINASE | Cadherins - metabolism | Humans | Mammary Neoplasms, Experimental - metabolism | Breast Neoplasms - metabolism | Receptor, Epidermal Growth Factor - metabolism | Epithelial-Mesenchymal Transition | Mammary Neoplasms, Experimental - pathology | Female | Indoles - pharmacology | p38 Mitogen-Activated Protein Kinases - metabolism | Carcinoma - secondary | Mammary Neoplasms, Experimental - drug therapy | Carcinoma - drug therapy | Focal Adhesion Protein-Tyrosine Kinases - metabolism | Epidermal Growth Factor - metabolism | Sulfonamides - pharmacology | Breast Neoplasms - drug therapy | Transforming Growth Factor beta - pharmacology | Animals | Receptors, Transforming Growth Factor beta - metabolism | Breast Neoplasms - pathology | Cell Line, Tumor | Mice | Carcinoma - metabolism | Epidermal Growth Factor - pharmacology | Transforming Growth Factor beta - metabolism | RNA, Small Interfering - metabolism | TGF-β
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10. Full Text Tumor necrosis factor receptor‐ associated factor 6 (TRAF6) regulation of development, function, and homeostasis of the immune system
by Walsh, Matthew C and Lee, JangEun and Choi, Yongwon
Immunological Reviews, ISSN 0105-2896, 07/2015, Volume 266, Issue 1, pp. 72 - 92
Tumor necrosis factor receptor ( TNFR )‐associated factor 6 ( TRAF 6) is an adapter protein that mediates a wide array of protein–protein interactions via its... 
K63‐linked | TRAF | signal transduction | mir‐146a | TAK | K63-linked | Signal transduction | TAK1 | TRAF-6 | TRAFs | Mir-146a | TGF-BETA | ACTIVATION-INDUCED CYTOKINE | CYTOSKELETAL ORGANIZATION | T-CELL | IMMUNOLOGY | mir-146a | TOLL-LIKE-RECEPTOR | THYMIC EPITHELIAL-CELLS | TNF FAMILY-MEMBER | NF-KAPPA-B | OSTEOCLAST DIFFERENTIATION | EPSTEIN-BARR-VIRUS | Animals | Signal Transduction | Immune System - metabolism | Lymphocyte Activation | Humans | TNF Receptor-Associated Factor 6 - metabolism | Homeostasis | Immune Tolerance | Immune System - growth & development | Toll-Like Receptors - metabolism | Tumor necrosis factor | Cellular signal transduction | B cells | Protein-protein interactions | Immune system | Tumors | Necrosis
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