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1. Full Text MicroRNA‐140‐5p suppresses tumor growth and metastasis by targeting transforming growth factor β receptor 1 and fibroblast growth factor 9 in hepatocellular carcinoma
by Yang, Hao and Fang, Feng and Chang, Ruimin and Yang, Lianyue
Hepatology, ISSN 0270-9139, 07/2013, Volume 58, Issue 1, pp. 205 - 217
By comparing the expression profiles of microRNAs (miRNAs) in different hepatocellular carcinoma (HCC) subtypes, we identified miR‐140‐5p as an HCC‐related... 
LIVER-CANCER | PROTEIN | THERAPY | PATHWAY | MARKER | POOR-PROGNOSIS | CELL-PROLIFERATION | GASTROENTEROLOGY & HEPATOLOGY | HEPATIC RESECTION | DECREASED EXPRESSION | Prognosis | Fibroblast Growth Factor 9 - drug effects | Biomarkers, Tumor - analysis | Down-Regulation | Humans | Middle Aged | Liver Neoplasms - drug therapy | Male | Carcinoma, Hepatocellular - secondary | Disease-Free Survival | Animals | Carcinoma, Hepatocellular - drug therapy | Receptors, Transforming Growth Factor beta - drug effects | Neoplasm Metastasis - prevention & control | Carcinoma, Hepatocellular - pathology | Liver Neoplasms - metabolism | Protein-Serine-Threonine Kinases - drug effects | Cell Line, Tumor | Female | Liver Neoplasms - pathology | Mice | MicroRNAs - physiology | Carcinoma, Hepatocellular - metabolism | Index Medicus
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2. Full Text A novel, potent, and selective insulin-like growth factor-I receptor kinase inhibitor blocks insulin-like growth factor-I receptor signaling in vitro and inhibits insulin-like growth factor-I receptor–dependent tumor growth in vivo
by Qun-sheng Ji and Mark J. Mulvihill and Maryland Rosenfeld-Franklin and Andrew Cooke and Lixin Feng and Gilda Mak and Matthew O'Connor and Yan Yao and Caroline Pirritt and Elizabeth Buck and Alexandra Eyzaguirre and Lee D. Arnold and Neil W. Gibson and Jonathan A. Pachter
Molecular Cancer Therapeutics, ISSN 1535-7163, 08/2007, Volume 6, Issue 8, pp. 2158 - 2167
Insulin-like growth factor-I receptor (IGF-IR) and its ligands, IGF-I and IGF-II, are up-regulated in a variety of human cancers. In tumors, such as... 
Protein tyrosine kinases | Small Molecules and Other Therapeutics Agents | Autocrine-paracrine signaling | COLORECTAL-CANCER RISK | BREAST-CANCER | SARCOMA-CELLS | ONCOLOGY | PLASMA-LEVELS | IGF-BINDING PROTEIN-3 | FACTOR SYSTEM | ANTIBODY | ANTITUMOR-ACTIVITY | EXPRESSION | TUMORIGENESIS | Receptor, IGF Type 1 - metabolism | Receptor, IGF Type 1 - antagonists & inhibitors | Humans | Pyrazines - administration & dosage | Imidazoles - chemistry | Imidazoles - administration & dosage | Autocrine Communication - drug effects | Antineoplastic Agents - administration & dosage | Imidazoles - pharmacokinetics | Protein Kinase Inhibitors - chemistry | Female | Antineoplastic Agents - pharmacokinetics | Antineoplastic Agents - pharmacology | Phosphorylation - drug effects | Protein Kinase Inhibitors - pharmacokinetics | Tumor Stem Cell Assay | Imidazoles - pharmacology | Antineoplastic Agents - chemistry | Enzyme Activation - drug effects | Insulin-Like Growth Factor II - metabolism | Blood Glucose - drug effects | Xenograft Model Antitumor Assays | Protein Kinase Inhibitors - administration & dosage | Pyrazines - chemistry | Animals | Signal Transduction - drug effects | Mice, Nude | Pyrazines - pharmacokinetics | Cell Line, Tumor | Cell Proliferation - drug effects | Mice | Protein Kinase Inhibitors - pharmacology | Colorectal Neoplasms - pathology | Pyrazines - pharmacology | Index Medicus
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3. Full Text Hypoxia Inducible Factor Activates the Transforming Growth Factor-α/Epidermal Growth Factor Receptor Growth Stimulatory Pathway in VHL-/- Renal Cell Carcinoma Cells
by Gunaratnam, Lakshman and Morley, Melissa and Franovic, Aleksandra and De Paulsen, Natalie and Mekhail, Karim and Parolin, Doris A. E and Nakamura, Eijiro and Lorimer, Ian A. J and Lee, Stephen
Journal of Biological Chemistry, ISSN 0021-9258, 11/2003, Volume 278, Issue 45, pp. 44966 - 44974
Bi-allelic-inactivating mutations of the VHL tumor suppressor gene are found in the majority of clear cell renal cell carcinomas (VHL-/- RCC). VHL-/- RCC cells... 
CANCER-CELLS | UBIQUITIN LIGASE COMPLEX | PROLYL HYDROXYLATION | TYROSINE KINASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | GERMLINE MUTATIONS | GENE-EXPRESSION | LINDAU TUMOR-SUPPRESSOR | FACTOR-ALPHA | FAMILIAL PHEOCHROMOCYTOMA | REGULATE HIF | Phosphorylation | Humans | Kidney Neoplasms - metabolism | Recombinant Proteins | Ubiquitin-Protein Ligases - physiology | Blood | Hypoxia-Inducible Factor 1, alpha Subunit | Trans-Activators - physiology | Transfection | Culture Media | Tumor Suppressor Proteins - deficiency | Cell Division | Tumor Suppressor Proteins - genetics | Trans-Activators - genetics | Tumor Cells, Cultured | Receptor, Epidermal Growth Factor - physiology | Basic Helix-Loop-Helix Transcription Factors | Gene Expression | Transcription Factors - physiology | Carcinoma, Renal Cell - pathology | Transcription Factors - genetics | Reverse Transcriptase Polymerase Chain Reaction | Transforming Growth Factor alpha - genetics | Carcinoma, Renal Cell - metabolism | Tumor Suppressor Proteins - physiology | Ubiquitin-Protein Ligases - deficiency | Kidney Neoplasms - pathology | Von Hippel-Lindau Tumor Suppressor Protein | Mutation | Ubiquitin-Protein Ligases - genetics | Index Medicus
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4. 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 | Index Medicus | Medical and Health Sciences | Medicin och hälsovetenskap
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5. 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 | Index Medicus | TGF-β
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6. Full Text The JAK2/STAT3 signaling pathway is required for growth of CD44 +CD24- stem cell-like breast cancer cells in human tumors
by Marotta, Lauren L. C and Almendro, Vanessa and Marusyk, Andriy and Shipitsin, Michail and Schemme, Janina and Walker, Sarah R and Bloushtain-Qimron, Noga and Kim, Jessica J and Choudhury, Sibgat A and Maruyama, Reo and Wu, Zhenhua and Gönen, Mithat and Mulvey, Laura A and Bessarabova, Marina O and Huh, Sung Jin and Silver, Serena J and Kim, So Young and Park, So Yeon and Lee, Hee Eun and Anderson, Karen S and Richardson, Andrea L and Nikolskaya, Tatiana and Nikolsky, Yuri and Liu, X. Shirley and Root, David E and Hahn, William C and Frank, David A and Polyak, Kornelia
Journal of Clinical Investigation, ISSN 0021-9738, 07/2011, Volume 121, Issue 7, pp. 2723 - 2735
Intratumor heterogeneity is a major clinical problem because tumor cell subtypes display variable sensitivity to therapeutics and may play different roles in... 
SURVIVAL | HETEROGENEITY | MEDICINE, RESEARCH & EXPERIMENTAL | GENE-EXPRESSION SIGNATURE | STAT3 ACTIVATION | METASTASIS | THERAPY | IDENTIFICATION | CARCINOMA | IN-SITU | IL-6 | RNA, Small Interfering - genetics | CD24 Antigen - metabolism | Humans | Transplantation, Heterologous | Gene Expression Profiling | Stem Cells - cytology | Breast Neoplasms - metabolism | Janus Kinase 2 - metabolism | Hyaluronan Receptors - metabolism | CD24 Antigen - genetics | Female | Interleukin-6 - metabolism | Janus Kinase 2 - antagonists & inhibitors | STAT3 Transcription Factor - genetics | STAT3 Transcription Factor - metabolism | Interleukin-6 - genetics | Janus Kinase 2 - genetics | Hyaluronan Receptors - genetics | Animals | Breast Neoplasms - genetics | Breast Neoplasms - pathology | Cell Line, Tumor | Signal Transduction - physiology | Stem Cells - physiology | Mice | RNA, Small Interfering - metabolism | Growth | Cancer cells | Physiological aspects | Breast cancer | Research | Protein kinases | Risk factors | Index Medicus | Abridged Index Medicus
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7. Full Text Vascular endothelial growth factor-mediated decrease in plasma soluble vascular endothelial growth factor receptor-2 levels as a surrogate biomarker for tumor growth
by Ebos, John M. L and Lee, Christina R and Bogdanovic, Elena and Alami, Jennifer and Van Slyke, Paul and Francia, Giulio and Xu, Ping and Mutsaers, Anthony J and Dumont, Daniel J and Kerbel, Robert S
Cancer Research, ISSN 0008-5472, 01/2008, Volume 68, Issue 2, pp. 521 - 529
Vascular endothelial growth factor (VEGF) is a potent proangiogenic protein that activates VEGF receptor (VEGFR) tyrosine kinases expressed by,vascular... 
ONCOLOGY | METASTATIC BREAST-CANCER | IN-VIVO | VEGF RECEPTOR-1 | SERUM | LEUKEMIA | EXPRESSION | RENAL-CELL CARCINOMA | ANGIOGENIC FACTORS | MYELODYSPLASTIC SYNDROMES | ANTITUMOR EFFICACY | Neoplasm Transplantation | Prostatic Neoplasms - metabolism | Adenocarcinoma - pathology | Adenoviridae | Cell Proliferation | Humans | Male | Transplantation, Heterologous | Mammary Neoplasms, Experimental - metabolism | Vascular Endothelial Growth Factor A - genetics | Mammary Neoplasms, Experimental - genetics | Adenocarcinoma - metabolism | Prostatic Neoplasms - genetics | Mammary Neoplasms, Experimental - pathology | Female | Tumor Burden - genetics | Adenocarcinoma - genetics | Tumor Cells, Cultured | Prostatic Neoplasms - pathology | Transduction, Genetic | Mice, Inbred C57BL | Solubility | Vascular Endothelial Growth Factor Receptor-2 - blood | Vascular Endothelial Growth Factor Receptor-2 - metabolism | Mice, Transgenic | Biomarkers, Tumor - blood | HT29 Cells | Animals | Mice | Mice, Inbred BALB C | Vascular Endothelial Growth Factor A - physiology | Index Medicus
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8. Vascular growth factors and angiogenesis
by Claesson-Welsh, Lena
1999, Current topics in microbiology and immunology, ISBN 3540647317, Volume 237, 189
Vascular endothelium | Growth factors | Neovascularization
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9. Full Text Inhibition of brain tumor growth by intravenous poly (β-L-malic acid) nanobioconjugate with pH-dependent drug release
by Hui Ding and Satoshi Inoue and Alexander V. Ljubimov and Rameshwar Patil and Jose Portilla-Arias and Jinwei Hu and Bindu Konda and Kolja A. Wawrowsky and Manabu Fujita and Natalya Karabalin and Takako Sasaki and Keith L. Black and Eggehard Holler and Julia Y. Ljubimova and Alexander M. Klibanov
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 10/2010, Volume 107, Issue 42, pp. 18143 - 18148
Effective treatment of brain neurological disorders such as Alzheimer’s disease, multiple sclerosis, or tumors should be possible with drug delivery through... 
Glioma | Antineoplastics | Brain neoplasms | Cell membranes | Drug design | Liposomes | Polymers | Blood brain barrier | Tumors | Endosomes | Glioma treatment | Blood-brain barrier | Laminin-411 | Endosomal escape | Polymalic acid | blood-brain barrier | laminin-411 | GENE DELIVERY | ANGIOGENESIS | PERMEABILITY | MULTIDISCIPLINARY SCIENCES | BARRIER | endosomal escape | glioma treatment | PEPTIDE | CHEMOTHERAPY | LAMININ-8 | polymalic acid | IN-VIVO | MALIGNANT GLIOMAS | HPMA COPOLYMER | Polymers - administration & dosage | Brain Neoplasms - pathology | Brain Neoplasms - drug therapy | Endosomes - metabolism | Nanoparticles | Polymers - therapeutic use | Animals | Mice, Nude | Malates - pharmacokinetics | Polymers - pharmacokinetics | Mice | Infusions, Intravenous | Malates - administration & dosage | Malates - therapeutic use | Blood-Brain Barrier | Hydrogen-Ion Concentration | Drugs | Care and treatment | Drug delivery systems | Brain tumors | Malic acid | Dosage and administration | Research | Vehicles | Proteins | Brain | Cell growth | Membranes | Monoclonal antibodies | Alzheimers disease | Cells | Cytoplasm | Index Medicus | Multiple sclerosis | Intravenous administration | Neurodegenerative diseases | Biodegradability | Tumor cells | Antisense oligonucleotides | Esters | endosomes | Drug delivery | Leucine | Drug development | pH effects | Neurological diseases | Angiogenesis | Glioma cells | nanotechnology | Alzheimer's disease | Biological Sciences | Physical Sciences | blood–brain barrier
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10. Full Text Heparin-II Domain of Fibronectin Is a Vascular Endothelial Growth Factor-Binding Domain: Enhancement of VEGF Biological Activity by a Singular Growth Factor/Matrix Protein Synergism
by Wijelath, Errol S and Rahman, Salman and Namekata, Mayumi and Murray, Jacqueline and Nishimura, Tomoaki and Mostafavi-Pour, Zohreh and Patel, Yatin and Suda, Yasuo and Humphries, Martin J and Sobel, Michael
Circulation Research, ISSN 0009-7330, 10/2006, Volume 99, Issue 8, pp. 853 - 860
We describe extracellular interactions between fibronectin (Fn) and vascular endothelial growth factor (VEGF) that influence integrin-growth factor receptor... 
Signal transduction | Endothelial cell differentiation | Endothelial cell growth | Vascular endothelial growth factor | Endothelial cells | Fibronectin | Integrins | Vascular endothelial growth factor receptors | MIGRATION | endothelial cell growth | endothelial cells | ACTIVATION | CARDIAC & CARDIOVASCULAR SYSTEMS | ANGIOGENESIS | signal transduction | FACTOR RECEPTORS | endothelial cell differentiation | PEPTIDE | ADHESION | integrins | vascular endothelial growth factor receptors | fibronectin | vascular endothelial growth factor | PERIPHERAL VASCULAR DISEASE | HEMATOLOGY | TUMOR-GROWTH | SMOOTH-MUSCLE CELLS | BETA INTEGRIN | EMBRYOID BODIES | Binding, Competitive | Recombinant Proteins - metabolism | Heparin - metabolism | Cell Proliferation | Humans | Cells, Cultured | Extracellular Matrix Proteins - physiology | Vascular Endothelial Growth Factor A - metabolism | Protein Isoforms - isolation & purification | Cell Movement - physiology | Fibronectins - metabolism | Drug Synergism | Peptides - metabolism | Protein Isoforms - metabolism | Endothelial Cells - cytology | Fibronectins - physiology | Signal Transduction - physiology | Fibronectins - genetics | Binding Sites | Fibronectins - isolation & purification | Vascular Endothelial Growth Factor A - physiology | Endothelial Cells - physiology | Protein Isoforms - genetics | Protein Structure, Tertiary - physiology | Index Medicus
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11. Full Text Development of covalent inhibitors that can overcome resistance to first-generation FGFR kinase inhibitors
by Li Tan and Jun Wang and Junko Tanizaki and Zhifeng Huang and Amir R. Aref and Maria Rusan and Su-Jie Zhu and Yiyun Zhang and Dalia Ercan and Rachel G. Liao and Marzia Capelletti and Wenjun Zhou and Wooyoung Hur and NamDoo Kim and Taebo Sim and Suzanne Gaudet and David A. Barbie and Jing-Ruey Joanna Yeh and Cai-Hong Yun and Peter S. Hammerman and Moosa Mohammadi and Pasi A. Jänne and Nathanael S. Gray
Proceedings of the National Academy of Sciences, ISSN 0027-8424, 11/2014, Volume 111, Issue 45, pp. E4869 - E4877
The human FGF receptors (FGFRs) play critical roles in various human cancers, and several FGFR inhibitors are currently under clinical investigation.... 
Structure-based drug design | Drug discovery | Cancer drug resistance | Kinase inhibitor | structure-based drug design | WILD-TYPE | MULTIDISCIPLINARY SCIENCES | BCR-ABL | GROWTH-FACTOR RECEPTORS | DRUG-RESISTANCE | kinase inhibitor | LUNG-CANCER | GENE FUSIONS | cancer drug resistance | SELECTIVE INHIBITOR | drug discovery | THERAPEUTIC TARGET | FACTOR RECEPTOR 4 | REGULATES PROLIFERATION | Receptor, Fibroblast Growth Factor, Type 4 - chemistry | Receptor, Epidermal Growth Factor - genetics | Receptor, Fibroblast Growth Factor, Type 4 - metabolism | Receptor, Fibroblast Growth Factor, Type 2 - chemistry | Receptor, Fibroblast Growth Factor, Type 2 - metabolism | Humans | Receptor, Fibroblast Growth Factor, Type 1 - metabolism | Crystallography, X-Ray | Structure-Activity Relationship | Mutation, Missense | Receptor, Fibroblast Growth Factor, Type 1 - genetics | Protein Kinase Inhibitors - chemistry | Receptor, Epidermal Growth Factor - metabolism | Neoplasms - genetics | Receptor, Fibroblast Growth Factor, Type 2 - antagonists & inhibitors | Antineoplastic Agents - pharmacology | Receptor, Fibroblast Growth Factor, Type 4 - genetics | Binding Sites | Neoplasms - enzymology | Antineoplastic Agents - chemistry | Receptor, Fibroblast Growth Factor, Type 1 - antagonists & inhibitors | Receptor, Epidermal Growth Factor - chemistry | Neoplasms - drug therapy | Drug Resistance, Neoplasm - genetics | Cell Line, Tumor | Receptor, Epidermal Growth Factor - antagonists & inhibitors | Protein Kinase Inhibitors - pharmacology | Receptor, Fibroblast Growth Factor, Type 1 - chemistry | Neoplasms - pathology | Receptor, Fibroblast Growth Factor, Type 4 - antagonists & inhibitors | Receptor, Fibroblast Growth Factor, Type 2 - genetics | Amino Acid Substitution | Drug Resistance, Neoplasm - drug effects | Amino acids | T cell receptors | Mutation | Kinases | Binding sites | Adenosine triphosphatase | Index Medicus | Biological Sciences | PNAS Plus
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