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American Journal of Physiology - Cell Physiology, ISSN 0363-6143, 06/2009, Volume 296, Issue 6, pp. 1258 - 1270
Myostatin is a negative regulator of skeletal muscle size, previously shown to inhibit muscle cell differentiation. Myostatin requires both Smad2 and Smad3... 
MAFbx | Mammalian target of rapamycin complex signaling | MuRF1 | S6 kinase | Smad signaling | Human skeletal muscle cells | Transducer of regulated Ca | responsive element-binding protein activity | MuRF-1 | Atrogin | Transforming growth factor-β-like molecules | IGF-I | PHYSIOLOGY | ATROPHY | RAPID DISUSE | human skeletal muscle cells | transforming growth factor-beta-like molecules | SKELETAL-MUSCLE HYPERTROPHY | FOXO TRANSCRIPTION FACTORS | UBIQUITIN LIGASES | transducer of regulated Ca2+-responsive element-binding protein activity | CELL BIOLOGY | atrogin | PATHWAY | GROWTH | GENE-EXPRESSION | mammalian target of rapamycin complex signaling | CONDITIONAL ACTIVATION | Activin Receptors, Type I - antagonists & inhibitors | Protein Kinases - metabolism | Phosphorylation | Protein Kinases - genetics | Humans | Smad3 Protein - metabolism | Muscle Fibers, Skeletal - drug effects | Tripartite Motif Proteins | Smad3 Protein - genetics | Transfection | RNA Interference | Myoblasts, Skeletal - pathology | Smad2 Protein - genetics | Muscle Proteins - metabolism | Dioxoles - pharmacology | Regulatory-Associated Protein of mTOR | Benzamides - pharmacology | Myostatin - metabolism | Proto-Oncogene Proteins c-akt - metabolism | Rapamycin-Insensitive Companion of mTOR Protein | Ribosomal Protein S6 Kinases, 70-kDa - metabolism | Signal Transduction | Cell Size - drug effects | Cells, Cultured | Smad2 Protein - metabolism | Ubiquitin-Protein Ligases - metabolism | Organ Size | Activin Receptors, Type I - metabolism | Myoblasts, Skeletal - enzymology | SKP Cullin F-Box Protein Ligases - metabolism | Mice, SCID | Myostatin - antagonists & inhibitors | Adaptor Proteins, Signal Transducing | Animals | Carrier Proteins - metabolism | Proteins - metabolism | Cell Differentiation - drug effects | Follistatin - pharmacology | Muscle Fibers, Skeletal - pathology | Creatine Kinase - metabolism | Mice | Protein Kinase Inhibitors - pharmacology | TOR Serine-Threonine Kinases | Myoblasts, Skeletal - drug effects | Insulin-Like Growth Factor I - metabolism | Muscle Fibers, Skeletal - enzymology | RNA, Small Interfering - metabolism | Abdominal surgery | Musculoskeletal system | Signal transduction | Cell growth | Kinases | Gene expression | Cells | Index Medicus
Journal Article
Blood, ISSN 0006-4971, 08/2008, Volume 112, Issue 4, pp. 1503 - 1509
Journal Article
Developmental Cell, ISSN 1534-5807, 03/2012, Volume 22, Issue 3, pp. 501 - 514
Gradients of vascular endothelial growth factor (VEGF) induce single endothelial cells to become leading tip cells of emerging angiogenic sprouts. Tip cells... 
DEFECTS | TIP CELLS | ANGIOGENESIS | VEGF | ENDOTHELIAL-CELLS | ID PROTEINS | HES1 | DEVELOPMENTAL BIOLOGY | DIFFERENTIATION | EXPRESSION | INHIBITS TUMOR-GROWTH | CELL BIOLOGY | Transcription Factor HES-1 | Humans | Intercellular Signaling Peptides and Proteins - biosynthesis | Intracellular Signaling Peptides and Proteins - metabolism | Inhibitor of Differentiation Proteins - biosynthesis | Inhibitor of Differentiation Protein 1 - biosynthesis | Serrate-Jagged Proteins | Smad5 Protein - metabolism | Basic Helix-Loop-Helix Transcription Factors - biosynthesis | Smad1 Protein - genetics | Membrane Proteins - metabolism | Smad5 Protein - genetics | Intracellular Signaling Peptides and Proteins - genetics | Jagged-1 Protein | Calcium-Binding Proteins - biosynthesis | Homeodomain Proteins - biosynthesis | Signal Transduction | Inhibitor of Differentiation Protein 2 - biosynthesis | Membrane Proteins - genetics | Down-Regulation | Cells, Cultured | Mice, Transgenic | Cell Cycle Proteins - biosynthesis | Vascular Endothelial Growth Factor Receptor-1 - biosynthesis | Mice, Knockout | Membrane Proteins - biosynthesis | Phenotype | Animals | Smad1 Protein - metabolism | Mice | Neovascularization, Physiologic | Proteins | Endothelial growth factors | Genes | Genetic aspects | Transforming growth factors | Vascular endothelial growth factor | Endothelium | Index Medicus | Dll4 | tip cell | lateral inhibition | sprouting angiogenesis | BMP | directed migration | Notch | stalk cell | mouse embryo | Smad | polarity
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 02/2011, Volume 286, Issue 7, pp. 5157 - 5165
Bone morphogenetic proteins (BMPs) regulate many mammalian physiologic and pathophysiologic processes. These proteins bind with the kinase receptors BMPR-I and... 
SURVIVAL | FOREBRAIN | REPULSIVE GUIDANCE MOLECULE | DCC | BIOCHEMISTRY & MOLECULAR BIOLOGY | NEURONAL DIFFERENTIATION | SPINAL-CORD | EXPRESSION | RGMA | Phosphorylation - physiology | Bone Morphogenetic Protein Receptors, Type II - genetics | Membrane Proteins - genetics | Humans | Bone Morphogenetic Protein Receptors, Type I - genetics | Smad Proteins - genetics | rhoA GTP-Binding Protein - metabolism | rhoA GTP-Binding Protein - genetics | Bone Morphogenetic Protein Receptors, Type I - metabolism | Bone Morphogenetic Protein Receptors, Type II - metabolism | Bone Morphogenetic Proteins - metabolism | HEK293 Cells | Membrane Proteins - metabolism | Osteoblasts - cytology | Osteoblasts - metabolism | Bone Morphogenetic Proteins - genetics | Cell Differentiation - physiology | Enzyme Activation - physiology | Smad Proteins - metabolism | Protein Binding - physiology | Index Medicus | Bone morphogenetic protein 6 | Smad5 protein | Bone morphogenetic protein 4 | Phosphorylation | Smad protein | Transcription factors | Bone morphogenetic protein 2 | Bone morphogenetic protein receptor type II | RhoA protein | Osteoblasts | Bone morphogenetic protein receptor type I | Signal transduction | Osteoblastogenesis | Protein kinase | Bone morphogenetic proteins | Differentiation | Bone morphogenetic protein 7 | Rho | Bone Morphogenetic Protein (BMP) | SMAD Transcription Factor | Signal Transduction | Cell Biology
Journal Article
Molecular and Cellular Biology, ISSN 0270-7306, 07/2012, Volume 32, Issue 14, pp. 2904 - 2916
Journal Article
Biochemical Journal, ISSN 0264-6021, 03/2005, Volume 386, Issue 3, pp. 461 - 470
Inhibitory Smad, Smad7, is a potent inhibitor of TGF-beta (transforming growth factor-beta) superfamily signalling. By binding to activated type I receptors,... 
Developmentally down-regulated 4-2 (NEDD4-2) | Bone morphogenetic protein (BMP) | Smad | Neural precursor cell expressed | Homologous to the E6-accessory protein C-terminus (HECT) | Transforming growth factor-β (TGF-β) | Humans | Protein-Serine-Threonine Kinases | Ubiquitin - metabolism | Cytoplasm - metabolism | RNA, Messenger - metabolism | DNA-Binding Proteins - metabolism | Bone Morphogenetic Proteins - metabolism | Cell Nucleus - metabolism | Trans-Activators - genetics | Nedd4 Ubiquitin Protein Ligases | Transcription, Genetic | Proto-Oncogene Proteins - metabolism | Smad7 Protein | Cell Line | Signal Transduction | Smad6 Protein | Endosomal Sorting Complexes Required for Transport | RNA, Messenger - genetics | Ubiquitin-Protein Ligases - metabolism | Intracellular Signaling Peptides and Proteins | Activin Receptors, Type I - metabolism | DNA-Binding Proteins - genetics | Protein Transport | Two-Hybrid System Techniques | Smad3 Protein | Animals | Receptors, Transforming Growth Factor beta - metabolism | Cell Line, Tumor | Protein Binding | Ligands | Trans-Activators - metabolism | Mice | Ubiquitin-Protein Ligases - genetics | Transforming Growth Factor beta - metabolism | Smad2 Protein | Index Medicus | BMPR-IB, BMP type IB receptor | TβR-I, transforming growth factor-β type I receptor | developmentally down-regulated 4-2 (NEDD4-2) | Ski-related novel protein N (SnoN) | I-Smad, inhibitory Smad | transforming growth factor-β (TGF-β) | homologous to the E6-accessory protein C-terminus (HECT) | R-Smad, receptor-regulated Smad | SnoN, Ski-related novel protein N | RING, really interesting new gene | F-box protein | bone morphogenetic protein (BMP) | ROC1, regulator of Cullins 1 | HECT, homologous to the E6-accessory protein C-terminus | siRNA, small interfering RNA | NEDD4-2, neural precursor cell expressed, developmentally down-regulated 4-2 | SCF, Skp1 | neural precursor cell expressed | Smurf, Smad ubiquitin regulatory factor | TGF-β, transforming growth factor-β | Cullin1 | BMP, bone morphogenetic protein | Co-Smad, common-partner Smad
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 11/2010, Volume 107, Issue 44, pp. 18886 - 18891
The proper function of the bone morphogenic protein (BMP) pathway during embryonic development and organ maintenance requires its communication with other... 
Receptors | Phosphorylation | Plasmids | Neurons | Ubiquitins | Antibodies | Gene expression regulation | Embryos | Progenitor cells | Cells | PATHWAYS | NERVOUS-SYSTEM | TRANSCRIPTIONAL ACTIVATION | TGF-BETA | BMP | MULTIDISCIPLINARY SCIENCES | E3 UBIQUITIN LIGASES | RECEPTORS | CELL-TYPES | DORSAL SPINAL-CORD | FAMILY | Phosphorylation - physiology | Mitogen-Activated Protein Kinase Kinases - genetics | Cell Proliferation | Stem Cells - metabolism | Wnt Proteins - metabolism | Embryo, Mammalian - metabolism | Receptors, Retinoic Acid - genetics | Mitogen-Activated Protein Kinase Kinases - metabolism | Bone Morphogenetic Proteins - metabolism | Wnt Proteins - genetics | Tretinoin - metabolism | Smad1 Protein - genetics | Cell Cycle Proteins - genetics | Ubiquitination - physiology | Nuclear Proteins - genetics | Bone Morphogenetic Proteins - genetics | Cell Differentiation - physiology | Epidermal Growth Factor - genetics | Cell Cycle Proteins - metabolism | Ubiquitin-Protein Ligases - metabolism | Embryonic Development - physiology | Epidermal Growth Factor - metabolism | Nuclear Proteins - metabolism | Receptors, Retinoic Acid - metabolism | Glycogen Synthase Kinase 3 - metabolism | Chick Embryo | Proteasome Endopeptidase Complex - genetics | Animals | Glycogen Synthase Kinase 3 - genetics | Embryo, Mammalian - cytology | Cell Line, Tumor | Smad1 Protein - metabolism | Signal Transduction - physiology | Mice | Proteasome Endopeptidase Complex - metabolism | Neural Tube - embryology | Ubiquitin-Protein Ligases - genetics | Physiological aspects | Bone morphogenetic proteins | Research | Properties | Proteolysis | Tretinoin | Proteins | Signal transduction | Birds | T cell receptors | Gene expression | Index Medicus | Cell proliferation | Fibroblast growth factor | Pattern formation | Smad protein | Transcription | Wnt protein | Retinoic acid receptors | proteasomes | MAP kinase | Embryogenesis | Neural tube | ubiquitination | GADD45 protein | Neural stem cells | Differentiation | Retinoic acid | Ubiquitin-protein ligase | Communication | Biological Sciences
Journal Article
PLoS ONE, ISSN 1932-6203, 05/2012, Volume 7, Issue 5, pp. e36964 - e36964
Articular cartilage is physiologically exposed to repeated loads. The mechanical properties of cartilage are due to its extracellular matrix, and homeostasis... 
DISTURBED FLOW | GROWTH-FACTOR-BETA | IN-VITRO | TGF-BETA | BOVINE ARTICULAR CHONDROCYTES | MULTIDISCIPLINARY SCIENCES | ENDOTHELIAL-CELLS | SHEAR-STRESS | MECHANICAL STIMULATION | CARTILAGE TISSUE | PRIMARY CILIA | Chondrocytes - cytology | Phosphorylation | Transcription Factor AP-1 - genetics | Stress, Mechanical | Transcription Factor AP-1 - metabolism | Cartilage, Articular - physiology | MAP Kinase Signaling System - genetics | Chondrocytes - physiology | Cartilage, Articular - metabolism | Early Growth Response Protein 1 - genetics | p38 Mitogen-Activated Protein Kinases - metabolism | Mechanotransduction, Cellular - genetics | Chondrocytes - metabolism | Extracellular Matrix Proteins - metabolism | Hydrogel, Polyethylene Glycol Dimethacrylate - metabolism | Signal Transduction | Cartilage, Articular - cytology | Down-Regulation | Extracellular Matrix Proteins - genetics | p38 Mitogen-Activated Protein Kinases - genetics | Smad Proteins - genetics | Sepharose - metabolism | Animals | Transforming Growth Factor beta - genetics | Mitogen-Activated Protein Kinases - genetics | Mice | Smad Proteins - metabolism | Transforming Growth Factor beta - metabolism | Early Growth Response Protein 1 - metabolism | Mitogen-Activated Protein Kinases - metabolism | DNA microarrays | Analysis | Genes | Physiological aspects | Mechanical properties | Bone morphogenetic proteins | Transforming growth factors | Gene expression | Mitogens | Protein kinases | Compression | Transcription factors | Hydrogels | Genomics | Transforming growth factor-a | Homeostasis | Genomes | Shear stresses | Kinases | Western blotting | Proteins | Cartilage | Signal transduction | Pathways | Smad2 protein | Atherosclerosis | Extracellular matrix | Data analysis | Extracellular signal-regulated kinase | MAP kinase | Cartilage (articular) | Metabolism | Signaling | Embedded systems | Protein kinase | Collagen | Chondrocytes | Index Medicus | Mitogen-Activated Protein Kinases | Sepharose | Biochemistry, Molecular Biology | Cartilage, Articular/physiology | Cartilage, Articular/cytology | Transcription Factor AP-1 | MAP Kinase Signaling System | Life Sciences | Mechanotransduction, Cellular | Hydrogel, Polyethylene Glycol Dimethacrylate | Extracellular Matrix Proteins | Smad Proteins | Early Growth Response Protein 1 | p38 Mitogen-Activated Protein Kinases | Transforming Growth Factor beta | Cartilage, Articular/metabolism
Journal Article
Cell Death and Differentiation, ISSN 1350-9047, 02/2011, Volume 18, Issue 2, pp. 222 - 234
Journal Article
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 10/2010, Volume 107, Issue 43, pp. 18404 - 18409
Journal Article
PLoS ONE, ISSN 1932-6203, 09/2012, Volume 7, Issue 9, pp. e46307 - e46307
Bone morphogenetic proteins (BMPs) are members of the transforming growth factor beta superfamily that exert their effects via type I and type II serine... 
Bone Morphogenetic Protein 5 - chemistry | Bone Morphogenetic Protein 6 - chemistry | Bone Morphogenetic Protein 7 - chemistry | Hemochromatosis Protein | Bone Morphogenetic Protein 7 - genetics | Humans | Nerve Tissue Proteins - chemistry | Transfection | Bone Morphogenetic Protein 6 - genetics | Solutions | Growth Differentiation Factors - genetics | Genes, Reporter | Cell Line | Cell Adhesion Molecules, Neuronal - chemistry | Signal Transduction | Membrane Proteins - genetics | Bone Morphogenetic Protein 5 - genetics | Recombinant Proteins - chemistry | Histocompatibility Antigens Class I - genetics | Recombinant Proteins - genetics | Histocompatibility Antigens Class I - chemistry | Nerve Tissue Proteins - genetics | Cell Adhesion Molecules, Neuronal - genetics | GPI-Linked Proteins - chemistry | Membrane Proteins - chemistry | Protein Binding | Ligands | Kinetics | GPI-Linked Proteins - genetics | Growth Differentiation Factors - chemistry | Physiological aspects | Bone morphogenetic proteins | Genetic aspects | Research | Protein binding | Smad protein | Phosphorylation | Nephrology | Transforming growth factor-b | Homeostasis | Intracellular signalling | Iron | Biology | Kinases | Medical schools | Proteins | Signal transduction | Receptors | Rodents | Growth factors | Binding | Bone morphogenetic protein 6 | Bone morphogenetic protein 5 | Bone morphogenetic protein 4 | Bone morphogenetic protein 2 | Threonine | Research & development--R&D | Anemia | Affinity | Protein-serine/threonine kinase | Surface plasmon resonance | Mutation | Bone | Receptor mechanisms | Bone morphogenetic protein 9 | Bone morphogenetic protein 7 | Index Medicus | Research & development | R&D
Journal Article
Cancer Research, ISSN 0008-5472, 12/2009, Volume 69, Issue 23, pp. 8844 - 8852
Transforming growth factor-beta (TGF-beta) is a multifunctional cytokine that regulates cell growth, differentiation, and apoptosis of various types of cells.... 
SURVIVAL | THERAPY | BECLIN-1 | ONCOLOGY | INDUCED APOPTOSIS | MESANGIAL CELLS | PAI-1 GENE-EXPRESSION | INDUCTION | TUMORIGENESIS | CANCER | LC3 | Microtubule-Associated Proteins - genetics | Humans | Ubiquitin-Activating Enzymes - biosynthesis | Cell Growth Processes - physiology | JNK Mitogen-Activated Protein Kinases - metabolism | Autophagy - physiology | Proto-Oncogene Proteins - biosynthesis | Transforming Growth Factor beta - biosynthesis | Breast Neoplasms - metabolism | Transfection | Bcl-2-Like Protein 11 | Carcinoma, Hepatocellular - genetics | Apoptosis Regulatory Proteins - genetics | Liver Neoplasms - pathology | Apoptosis Regulatory Proteins - biosynthesis | Beclin-1 | Ubiquitin-Activating Enzymes - genetics | Liver Neoplasms - genetics | Membrane Proteins - genetics | Transforming Growth Factor beta - physiology | Proto-Oncogene Proteins - genetics | Microtubule-Associated Proteins - antagonists & inhibitors | Microtubule-Associated Proteins - biosynthesis | Autophagy-Related Protein 7 | Membrane Proteins - biosynthesis | Breast Neoplasms - genetics | Transforming Growth Factor beta - genetics | Autophagy-Related Protein 5 | Membrane Proteins - antagonists & inhibitors | Receptors, Transforming Growth Factor beta - metabolism | Breast Neoplasms - pathology | Ubiquitin-Activating Enzymes - antagonists & inhibitors | Adaptor Proteins, Signal Transducing - genetics | Apoptosis Regulatory Proteins - antagonists & inhibitors | Carcinoma, Hepatocellular - pathology | Liver Neoplasms - metabolism | Cell Line, Tumor | Adaptor Proteins, Signal Transducing - biosynthesis | Smad Proteins - metabolism | Carcinoma, Hepatocellular - metabolism | Index Medicus
Journal Article