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Journal Article
by Sim, MY and Huynh, H and Go, ML and Yuen, JSP
PLOS ONE, ISSN 1932-6203, 06/2017, Volume 12, Issue 6, p. e0178168
The dioxonapthoimidazolium YM155 is a survivin suppressant which has been investigated as an anticancer agent in clinical trials. Here, we investigated its... 
BREAST-CANCER | HEPATOCELLULAR-CARCINOMA | PLUS DOCETAXEL | APOPTOSIS PROTEINS IAPS | MULTIDISCIPLINARY SCIENCES | PROSTATE-CANCER | PHASE-II | ANTITUMOR-ACTIVITY | NF-KAPPA-B | TARGETING SURVIVIN | SMALL-MOLECULE SUPPRESSOR | Niacinamide - analogs & derivatives | Kidney Neoplasms - genetics | Deubiquitinating Enzyme CYLD | Inhibitor of Apoptosis Proteins - genetics | Humans | Gene Expression Regulation, Neoplastic | Carcinoma, Renal Cell - genetics | Male | Kidney Neoplasms - metabolism | Dose-Response Relationship, Drug | Inhibitor of Apoptosis Proteins - antagonists & inhibitors | Tumor Suppressor Proteins - genetics | Antineoplastic Agents - pharmacology | Inhibitor of Apoptosis Proteins - metabolism | Von Hippel-Lindau Tumor Suppressor Protein - genetics | Von Hippel-Lindau Tumor Suppressor Protein - antagonists & inhibitors | Carcinoma, Renal Cell - drug therapy | Von Hippel-Lindau Tumor Suppressor Protein - metabolism | Cell Survival - drug effects | Forkhead Box Protein O1 - metabolism | Tumor Suppressor Proteins - metabolism | Signal Transduction | Carcinoma, Renal Cell - pathology | Naphthoquinones - pharmacology | Imidazoles - pharmacology | Survivin | Inhibitor of Differentiation Protein 1 - metabolism | Mice, SCID | Xenograft Model Antitumor Assays | Carcinoma, Renal Cell - metabolism | Animals | Sorafenib | Cell Line, Tumor | Inhibitor of Differentiation Protein 1 - genetics | Kidney Neoplasms - pathology | Mice | Phenylurea Compounds - pharmacology | Niacinamide - pharmacology | Primary Cell Culture | Kidney Neoplasms - drug therapy | Forkhead Box Protein O1 - genetics | Drug Combinations | Antimitotic agents | Usage | RNA | Clinical trials | Genetic aspects | Carcinoma, Renal cell | Research | Antineoplastic agents | Drugs | Therapy | Biotechnology | Schedules | Id1 protein | Target recognition | Transcription | Syngeneic grafts | Genes | Immunoblotting | Cancer therapies | Anticancer properties | Proteins | Functional anatomy | FOXO1 protein | Xenografts | Inhibition | Medical research | Dosing | Enzymes | Effectiveness | Tumor cell lines | Real time | Patients | Mode of action | Polymerase chain reaction | Pathology | DNA microarrays | Ribonucleic acids | Kidney cancer | Protein expression | VHL protein | Neoplasia | Clear cell-type renal cell carcinoma | Tumors | Kidney transplantation
Journal Article
Arteriosclerosis, Thrombosis, and Vascular Biology, ISSN 1079-5642, 11/2013, Volume 33, Issue 11, pp. 2577 - 2584
OBJECTIVE—To investigate the role of bone morphogenetic proteins (BMPs) on α-B-crystallin (CRYAB) expression and its physiological consequences on endothelial... 
ACVRL1 protein, human | Smad proteins | BMPR2 protein, human | RNA, small interfering | anoxia | Id1 protein, human | SURVIVAL | TRANSLOCATION | ACTIVATION | Id1 protein | BMPR2 protein | RNA | ANGIOGENESIS | ACVRL1 protein | HEAT-SHOCK-PROTEIN | PATHOGENESIS | INHIBITION | ARTERIAL-HYPERTENSION | PERIPHERAL VASCULAR DISEASE | small interfering | SMOOTH-MUSCLE-CELLS | HEMATOLOGY | human | EXPRESSION | Human Umbilical Vein Endothelial Cells | alpha-Crystallin B Chain - genetics | Activin Receptors, Type II - metabolism | Apoptosis - drug effects | Humans | alpha-Crystallin B Chain - metabolism | Bone Morphogenetic Protein 4 - metabolism | Bone Morphogenetic Proteins - metabolism | Growth Differentiation Factors - pharmacology | Up-Regulation - physiology | Bone Morphogenetic Proteins - pharmacology | Disease Models, Animal | Endothelial Cells - metabolism | RNA, Small Interfering - pharmacology | Familial Primary Pulmonary Hypertension | Hypertension, Pulmonary - metabolism | Bone Morphogenetic Protein 4 - pharmacology | Bone Morphogenetic Protein Receptors, Type II - metabolism | Up-Regulation - drug effects | Growth Differentiation Factors - metabolism | Animals | Signal Transduction - drug effects | Endothelial Cells - cytology | Bone Morphogenetic Protein 7 - metabolism | Signal Transduction - physiology | Mice | Apoptosis - physiology | Lung - blood supply | Hypertension, Pulmonary - pathology | Bone Morphogenetic Protein 7 - pharmacology | Endothelial Cells - drug effects
Journal Article
PLoS ONE, ISSN 1932-6203, 06/2016, Volume 11, Issue 6, p. e0156994
Background Fibulin-5 is an extracellular matrix glycoprotein that plays critical roles in vasculogenesis and embryonic development. Deletion of Fibulin-5 in... 
EXTRACELLULAR-MATRIX PROTEINS | ANGIOGENESIS | MECHANISM | TIE2 | PATHWAY | ROLES | MULTIDISCIPLINARY SCIENCES | IN-VIVO | ALPHA-5-BETA-1 | EXPRESSION | Cricetulus | Gene Expression - drug effects | Human Umbilical Vein Endothelial Cells - metabolism | Humans | Immunoblotting | Angiopoietin-1 - metabolism | Early Growth Response Protein 1 - genetics | HEK293 Cells | Receptor, TIE-2 - metabolism | Extracellular Matrix Proteins - metabolism | Angiopoietin-1 - pharmacology | CHO Cells | Recombinant Proteins - metabolism | Cell Survival - drug effects | Cricetinae | Human Umbilical Vein Endothelial Cells - drug effects | Signal Transduction | Extracellular Matrix Proteins - genetics | Cells, Cultured | Extracellular Matrix Proteins - pharmacology | Recombinant Proteins - pharmacology | Reverse Transcriptase Polymerase Chain Reaction | Receptor, TIE-2 - genetics | Angiopoietin-1 - genetics | Animals | Inhibitor of Differentiation Protein 1 - genetics | Protein Binding | Mutation | Kruppel-Like Transcription Factors - genetics | Transcription factors | Phosphorylation | Id1 protein | Laboratories | Toxicity | Angiopoietin | Cytotoxicity | AKT protein | Kinases | Caspase-3 | Cell surface | Cell adhesion & migration | Proteins | Angiogenesis | Signal transduction | Embryogenesis | Cell growth | Clonal deletion | Penicillin | Deletion | Extracellular matrix | Deoxyribonucleic acid--DNA | Kruppel protein | Recombinant | Binding | Deprivation | Proteoglycans | Cell survival | EGR-1 protein | Incubation | Research & development--R&D | Glycoprotein | Extracellular signal-regulated kinase | Caspase | Gene expression | Endothelial cells | Embryonic growth stage | Medicine | Signaling | Inhibitors | Respiratory diseases | Skin | Lung Kruppel-like factor | Heparin | Angiogenesis inhibitors | Viability | Integrins | Research & development | R&D | Deoxyribonucleic acid | DNA
Journal Article
Gastroenterology, ISSN 0016-5085, 2011, Volume 141, Issue 5, pp. 1907 - 1914
Journal Article
PLoS ONE, ISSN 1932-6203, 09/2012, Volume 7, Issue 9, p. e44622
Hepcidin is an antimicrobial peptide, which also negatively regulates iron in circulation by controlling iron absorption from dietary sources and iron release... 
OVERLOAD | ELEMENTS | IRON-METABOLISM | INHIBITION | MESSENGER-RNA EXPRESSION | INFLAMMATION | MULTIDISCIPLINARY SCIENCES | TRANSCRIPTION | BONE MORPHOGENETIC PROTEIN-6 | INTERLEUKIN-6 | PROMOTER | Cell Line | NF-kappa B - antagonists & inhibitors | Sulfoxides - pharmacology | Tetrazoles - pharmacology | Antimicrobial Cationic Peptides | Cells, Cultured | NF-kappa B - metabolism | Bone Morphogenetic Protein 6 - pharmacology | Inhibitor of Differentiation Protein 1 - metabolism | Blotting, Western | Bone Morphogenetic Protein 4 - pharmacology | Macrophages - metabolism | Animals | Hepcidins | Smad5 Protein - metabolism | Lipopolysaccharides - pharmacology | Smad1 Protein - metabolism | Macrophages - drug effects | Mice | Phosphorylation - drug effects | Smad8 Protein - metabolism | Bone Morphogenetic Proteins - pharmacology | Bone morphogenetic proteins | Bacterial infections | Research | Macrophages | Mitogens | Health aspects | Nephrology | Phosphorylation | Smad protein | Id1 protein | Liver | Paracrine signalling | Homeostasis | Iron | Biology | Kinases | Medical schools | Lipopolysaccharides | Proteins | Immunology | Loading | Rodents | Autocrine signalling | Bone morphogenetic protein 6 | NF-κB protein | Bone morphogenetic protein 4 | Cytokines | Anemia | Inflammation | Hospitals | Diet | Hepatocytes | Womens health | Cell lines | Hypoxia | Ligands | Hepcidin | Peritoneum
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 05/2011, Volume 286, Issue 20, pp. 18104 - 18117
Increasing evidence supports a role forPKC alpha in growth arrest and tumor suppression in the intestinal epithelium. In contrast, the Id1 transcriptional... 
LOOP-HELIX PROTEINS | INCREASED EXPRESSION | DIFFERENTIATION ID1 | COLORECTAL-CANCER | BIOCHEMISTRY & MOLECULAR BIOLOGY | PKC-ALPHA | ID PROTEINS | COLON CARCINOGENESIS | CELL-CYCLE ARREST | GROWTH-FACTOR | SERTOLI-CELLS | Cyclin D1 - metabolism | Colonic Neoplasms - genetics | Intestinal Mucosa - metabolism | Protein Kinase C-alpha - metabolism | Protein Kinase C-alpha - genetics | Inhibitor of Differentiation Proteins - genetics | Extracellular Signal-Regulated MAP Kinases - metabolism | Neoplasm Proteins - metabolism | RNA, Messenger - metabolism | Extracellular Signal-Regulated MAP Kinases - genetics | Colonic Neoplasms - metabolism | Inhibitor of Differentiation Protein 2 - genetics | Neoplasm Proteins - genetics | Gene Expression Regulation, Neoplastic - genetics | Signal Transduction | RNA, Messenger - genetics | Inhibitor of Differentiation Proteins - metabolism | Inhibitor of Differentiation Protein 1 - metabolism | Inhibitor of Differentiation Protein 2 - metabolism | Down-Regulation - genetics | Mice, Knockout | Protein Kinase C-delta - metabolism | Animals | Cyclin D1 - genetics | Inhibitor of Differentiation Protein 1 - genetics | Mice | Protein Kinase C-delta - genetics | Homeostasis - genetics | Helix-Loop-Helix Transcription Factors | Intestine | Colon Cancer | Protein Kinase C (PKC) | PKCalpha | Phorbol Esters | Inhibitor of DNA Binding 1 (Id1) | Cyclins | ERK
Journal Article
ChemMedChem, ISSN 1860-7179, 09/2017, Volume 12, Issue 18, pp. 1497 - 1503
Journal Article
Journal Article
Oncogene, ISSN 0950-9232, 05/2012, Volume 31, Issue 19, pp. 2480 - 2490
Journal Article
Breast Cancer Research and Treatment, ISSN 0167-6806, 12/2010, Volume 124, Issue 3, pp. 623 - 633
Inhibitors of differentiation or DNA binding (Id) proteins have been shown to be involved in tumor growth, invasiveness, metastasis, and angiogenesis.... 
Medicine & Public Health | Cell cycle arrest | Oncology | Breast cancer | Peptide aptamer | Id1 and Id3 | Apoptosis | TRANSCRIPTION FACTORS | MAMMALIAN-CELLS | ID-1 PROTEIN | P21 | LOOP-HELIX PROTEINS | OVEREXPRESSION | ONCOLOGY | DNA | DIFFERENTIATION | INHIBITOR | EXPRESSION | Up-Regulation | Cell Proliferation | Apoptosis - drug effects | Humans | Inhibitor of Differentiation Proteins - genetics | Inhibitor of Differentiation Protein 1 - antagonists & inhibitors | Neoplasm Proteins - antagonists & inhibitors | Intracellular Signaling Peptides and Proteins - metabolism | Neoplasm Proteins - metabolism | Promoter Regions, Genetic - drug effects | Breast Neoplasms - metabolism | Dose-Response Relationship, Drug | Transfection | Transcription Factor 3 - metabolism | Cyclin-Dependent Kinase Inhibitor p21 - metabolism | Female | Antineoplastic Agents - pharmacology | Gene Expression Regulation, Neoplastic - drug effects | Neoplasm Proteins - genetics | E-Box Elements - drug effects | Inhibitor of Differentiation Proteins - metabolism | Inhibitor of Differentiation Protein 1 - metabolism | Cyclin-Dependent Kinase Inhibitor p27 | Inhibitor of Differentiation Proteins - antagonists & inhibitors | Two-Hybrid System Techniques | Poly(ADP-ribose) Polymerases - metabolism | Breast Neoplasms - genetics | Breast Neoplasms - pathology | Aptamers, Peptide - pharmacology | Inhibitor of Differentiation Protein 1 - genetics | Protein Binding | HeLa Cells | Cell Cycle - drug effects | Proteins | Cancer cells | Cell cycle | Protein binding
Journal Article