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1. Full Text TGFβ and BMP signaling in skeletal muscle: potential significance for muscle-related disease
by Sartori, Roberta and Gregorevic, Paul and Sandri, Marco
Trends in Endocrinology & Metabolism, ISSN 1043-2760, 2014, Volume 25, Issue 9, pp. 464 - 471
Highlights • The TFGβ superfamily is divided in two subfamilies with opposite function on muscle mass: myostatin/activin/TGFβ and BMP/GDF. • Myostatin is a... 
Endocrinology & Metabolism | HYPERTROPHY | ATROPHY | MYOSTATIN | MASS | GROWTH | TRANSCRIPTION | ENDOCRINOLOGY & METABOLISM | MICE | DIFFERENTIATION | PROTEIN-SYNTHESIS | EXPRESSION | Receptors, Transforming Growth Factor beta - agonists | Receptors, Transforming Growth Factor beta - genetics | Bone Morphogenetic Protein Receptors - genetics | Humans | Activins - metabolism | Muscle, Skeletal - metabolism | Autophagy | Activin Receptors - genetics | Bone Morphogenetic Proteins - metabolism | Protein Isoforms - metabolism | Protein Isoforms - agonists | Bone Morphogenetic Protein Receptors - agonists | Muscular Atrophy - metabolism | Signal Transduction | Muscular Diseases - metabolism | Muscular Atrophy - pathology | Bone Morphogenetic Protein Receptors - metabolism | Mice, Transgenic | Muscular Diseases - pathology | Mice, Knockout | Activin Receptors - chemistry | Activin Receptors - metabolism | Animals | Transforming Growth Factor beta - genetics | Receptors, Transforming Growth Factor beta - metabolism | Models, Biological | Activins - genetics | Muscle, Skeletal - pathology | Transforming Growth Factor beta - metabolism | Hypertrophy | Protein Isoforms - genetics
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2. Full Text Growth Differentiation Factor-9 Signaling Is Mediated by the Type I Receptor, Activin Receptor-Like Kinase 5
by Mazerbourg, Sabine and Klein, Cynthia and Roh, Jaesook and Kaivo-Oja, Noora and Mottershead, David G and Korchynskyi, Olexander and Ritvos, Olli and Hsueh, Aaron J. W
Molecular Endocrinology, ISSN 0888-8809, 03/2004, Volume 18, Issue 3, pp. 653 - 665
Growth differentiation factor-9 (GDF-9) is an oocyte-derived growth factor and a member of the TGF-β superfamily that includes TGF-β, activin, and bone... 
ALK7 SIGNALS | BONE MORPHOGENETIC PROTEIN | MAD-RELATED PROTEIN | ENDOCRINOLOGY & METABOLISM | OSTEOGENIC PROTEIN-1 | FOLLICULAR-GROWTH | TGF-BETA RECEPTOR | OVARIAN GRANULOSA-CELLS | IDENTIFICATION | HOMOLOG GDF-9B | LUTEAL CELLS | Phosphorylation | Receptors, Transforming Growth Factor beta - genetics | Trans-Activators - drug effects | Protein-Serine-Threonine Kinases | Activin Receptors - drug effects | Activins - metabolism | COS Cells - drug effects | Activin Receptors - genetics | Granulosa Cells - drug effects | Granulosa Cells - metabolism | COS Cells - metabolism | DNA-Binding Proteins - metabolism | Intercellular Signaling Peptides and Proteins - metabolism | Bone Morphogenetic Proteins - metabolism | Growth Differentiation Factor 9 | Trans-Activators - genetics | Female | Smad7 Protein | Promoter Regions, Genetic | Signal Transduction | Smad6 Protein | Cells, Cultured | DNA-Binding Proteins - drug effects | Rats | Activin Receptors, Type I - metabolism | DNA-Binding Proteins - genetics | Activin Receptors, Type I - genetics | Rats, Sprague-Dawley | Activin Receptors, Type I - drug effects | Transforming Growth Factor beta - pharmacology | Bone Morphogenetic Protein 15 | Smad3 Protein | Activin Receptors - metabolism | Animals | Activins - pharmacology | Receptors, Transforming Growth Factor beta - drug effects | Receptors, Transforming Growth Factor beta - metabolism | Intercellular Signaling Peptides and Proteins - pharmacology | Smad Proteins | Trans-Activators - metabolism | RNA, Small Interfering | Transforming Growth Factor beta - metabolism | Smad2 Protein
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3. Full Text Structural studies of the TGF-βs and their receptors – insights into evolution of the TGF-β superfamily
by Hinck, Andrew P
FEBS Letters, ISSN 0014-5793, 07/2012, Volume 586, Issue 14, pp. 1860 - 1870
TGF-βs are small secreted signaling proteins that function as vital regulators of cellular growth and differentiation. They signal through a single pair of... 
TGF-β | Evolution | Specificity | Receptor complex | Signaling protein | Structure | BINDING-SPECIFICITY | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | EXTRACELLULAR DOMAIN | MESENCHYMAL TRANSITION | CELL BIOLOGY | 3-DIMENSIONAL STRUCTURE | SIGNAL-TRANSDUCTION | TGF-beta | GROWTH-FACTOR-BETA | BIOPHYSICS | EPITHELIAL-CELLS | TRANSFORMING GROWTH-FACTOR-BETA-2 | II RECEPTOR | Signal Transduction | Humans | Molecular Conformation | Models, Molecular | Activins - metabolism | Phylogeny | Bone Morphogenetic Proteins - metabolism | Activin Receptors - metabolism | Animals | Receptors, Transforming Growth Factor beta - metabolism | Models, Biological | Protein Binding | Protein Conformation | Transforming Growth Factor beta - metabolism | Protein-Serine-Threonine Kinases - metabolism | Evolution, Molecular
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4. Full Text Midgut-Derived Activin Regulates Glucagon-like Action in the Fat Body and Glycemic Control
by Song, Wei and Cheng, Daojun and Hong, Shangyu and Sappe, Benoit and Hu, Yanhui and Wei, Neil and Zhu, Changqi and O’Connor, Michael B and Pissios, Pavlos and Perrimon, Norbert
Cell Metabolism, ISSN 1550-4131, 02/2017, Volume 25, Issue 2, pp. 386 - 399
While high-caloric diet impairs insulin response to cause hyperglycemia, whether and how counter-regulatory hormones are modulated by high-caloric diet is... 
INSULIN | LIFE-SPAN | STEM-CELLS | OBESITY | DIET | DROSOPHILA-MELANOGASTER | GLUCOSE-METABOLISM | KINASE | ENDOCRINOLOGY & METABOLISM | SUGAR HOMEOSTASIS | BETA | CELL BIOLOGY | Activins - metabolism | Hepatocytes - metabolism | Pyrrolidonecarboxylic Acid - analogs & derivatives | Drosophila Proteins - metabolism | RNA, Messenger - metabolism | Pyrrolidonecarboxylic Acid - metabolism | Drosophila melanogaster - metabolism | RNA Interference | Insect Hormones - metabolism | Hyperglycemia - pathology | Enteroendocrine Cells - metabolism | Fat Body - metabolism | Disease Models, Animal | Receptors, Glucagon - genetics | Signal Transduction | Larva - metabolism | RNA, Messenger - genetics | Carbohydrate Metabolism | Receptors, Glucagon - metabolism | Oligopeptides - metabolism | Gastrointestinal Tract - metabolism | Hyperglycemia - metabolism | Activin Receptors - metabolism | Animals | Carrier Proteins - metabolism | Glucagon - metabolism | Mice | Dietary Carbohydrates - adverse effects | Drosophila Proteins - genetics | Medical colleges | Hyperglycemia | Glucagon | Genomics | Physiological aspects | Glucose | Cells | Dextrose | Diabetes therapy
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5. Full Text Bone morphogenetic protein heterodimers assemble heteromeric type I receptor complexes to pattern the dorsoventral axis
by Little, Shawn C and Mullins, Mary C
Nature Cell Biology, ISSN 1465-7392, 05/2009, Volume 11, Issue 5, pp. 637 - 643
Patterning the embryonic dorsoventral axis of both vertebrates and invertebrates requires signalling through bone morphogenetic proteins (BMPs). Although a... 
SERINE/THREONINE KINASE RECEPTOR | BMP ACTIVITY | XENOPUS | SPEMANNS ORGANIZER | BMP2B/SWIRL | SIGNALS | CHORDIN | ZEBRAFISH EMBRYO | BMP7/SNAILHOUSE | DORSAL | CELL BIOLOGY | Phosphorylation | Bone Morphogenetic Protein 7 - genetics | Embryo, Nonmammalian - metabolism | Zebrafish - embryology | Bone Morphogenetic Proteins - metabolism | Cell Nucleus - metabolism | Smad5 Protein - metabolism | Bone Morphogenetic Protein 2 - metabolism | RNA, Messenger - antagonists & inhibitors | Bone Morphogenetic Proteins - genetics | Bone Morphogenetic Protein 2 - genetics | Zebrafish Proteins - metabolism | RNA, Messenger - genetics | Bone Morphogenetic Protein Receptors, Type I - genetics | Activin Receptors, Type I - metabolism | Bone Morphogenetic Protein Receptors, Type I - metabolism | Activin Receptors, Type I - genetics | Body Patterning - physiology | Embryo, Nonmammalian - abnormalities | Activin Receptors - metabolism | Animals | Oligonucleotides, Antisense - genetics | Models, Biological | Bone Morphogenetic Protein 7 - metabolism | Smad1 Protein - metabolism | Signal Transduction - physiology | Zebrafish Proteins - genetics | Protein Binding - physiology | Physiological aspects | Bone morphogenetic proteins | Cell receptors | Genetic aspects | Cellular signal transduction | Research
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6. Full Text Hemojuvelin regulates hepcidin expression via a selective subset of BMP ligands and receptors independently of neogenin
by Xia, Yin and Babitt, Jodie L and Sidis, Yisrael and Chung, Raymond T and Lin, Herbert Y
Blood, ISSN 0006-4971, 05/2008, Volume 111, Issue 10, pp. 5195 - 5204
Hemojuvelin (HJV) is a coreceptor for bone morphogenetic protein (BMP) signaling that regulates hepcidin expression and iron metabolism. However, the precise... 
ELEMENTS | SIGNALING PATHWAYS | IRON-METABOLISM | REPULSIVE GUIDANCE MOLECULE | GRANULOSA-CELLS | MORPHOGENETIC PROTEIN SYSTEM | BONE | IDENTIFICATION | PROMOTER | HEMATOLOGY | PEPTIDE | Activin Receptors, Type II - metabolism | Bone Morphogenetic Protein 6 | Bone Morphogenetic Protein 4 | Bone Morphogenetic Protein 2 | Humans | GPI-Linked Proteins | Gene Expression Regulation | Bone Morphogenetic Protein Receptors - metabolism | Activin Receptors, Type I - metabolism | Bone Morphogenetic Protein Receptors, Type I - metabolism | Bone Morphogenetic Protein Receptors, Type II - metabolism | Liver - chemistry | Bone Morphogenetic Proteins - metabolism | Membrane Proteins - antagonists & inhibitors | Hepcidins | Membrane Proteins - physiology | Carcinoma, Hepatocellular - pathology | Ligands | Carcinoma, Hepatocellular - chemistry | Antimicrobial Cationic Peptides - genetics | Transforming Growth Factor beta | Red Cells
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7. Full Text BMP signaling in vascular diseases
by Cai, Jie and Pardali, Evangelia and Sánchez-Duffhues, Gonzalo and ten Dijke, Peter
FEBS Letters, ISSN 0014-5793, 07/2012, Volume 586, Issue 14, pp. 1993 - 2002
Bone morphogenetic proteins (BMPs) are members of the transforming growth factor-β (TGF-β) family that signal via type I and type II serine/threonine kinase... 
Vascular calcification | Tumor angiogenesis | BMP signaling | Cardiovascular disease | Pulmonary arterial hypertension | Hereditary hemorrhagic telangiectasia | ALK | Apo | BMP Type II receptor | apolipoprotein | eNOS | BMPR2 | platelet-derived growth factor subunit BB | basic fibroblast growth factor | delta-like 4 | endothelial to mesenchymal transition | BMPER | ECs | Smad-binding elements | AMH | CV2 | aortic valve | BMP and activin membrane-bound inhibitor | BMP endothelial cell precursor derived regulator | activin receptor-like kinase | PRDC | AVMs | FOP | PKC | repulsive guidance molecule | GDFs | IPAH | bFGF | micro RNAs | smooth muscle cells | BMPs | latency associated peptide | fibrodysplasia ossificans progressiva | matrix GLA protein | transforming growth factor-β | BAECs | receptor-regulated Smads | miR | ROS | RGM | tyrosine-protein phosphatase non-receptor type 14 | induced pluripotent stem cells | pulmonary artery endothelial cells | HUVECs | uterine sensitization-associated gene-1 | arteriovenous malformation | EndoMT | endothelial cells | growth and differentiation factors | hereditary or familial PAH | I-Smads | SMCs | hereditary hemorrhagic telangiectasia | Dll4 | FPAH | iPSCs | USAG-1 | HHT | LDL | endothelial progenitor cells | reactive oxygen species | SBE | TGF-β | EPCs | protein kinase C | bone morphogenetic proteins | endothelial nitric-oxide synthase | sporadic or idiopathic PAH | VEGF | anti-müllerian hormone | inhibitory Smads | PAEC | PTPN14 | low-density lipoprotein | DAN | cross-veinless 2 | BAMBI | LTBP | R-Smads | vascular endothelial growth factor | human umbilical vein endothelial cells | MGP | bovine aortic endothelial cells | LAP | protein related to DAN and Cerberus | differential screening-selected gene aberrative in neuroblastoma | endoplasmic reticulum | latent TGF-β binding protein | PDGF-BB | MATRIX GLA PROTEIN | PULMONARY ARTERIAL-HYPERTENSION | BONE MORPHOGENETIC PROTEIN | BIOCHEMISTRY & MOLECULAR BIOLOGY | MICROVASCULAR ENDOTHELIAL-CELLS | HETEROZYGOUS BMPR2-MUTANT MICE | CELL BIOLOGY | PLURIPOTENT STEM-CELLS | RECEPTOR-LIKE KINASE-1 | GROWTH-FACTOR-BETA | BIOPHYSICS | SMOOTH-MUSCLE-CELLS | Neoplasms - metabolism | Signal Transduction | Humans | Neovascularization, Pathologic | Bone Morphogenetic Protein Receptors - metabolism | Familial Primary Pulmonary Hypertension | Hypertension, Pulmonary - metabolism | Atherosclerosis - metabolism | Mice, Knockout | Vascular Calcification - metabolism | Bone Morphogenetic Proteins - metabolism | Animals | Models, Biological | Mice | Models, Genetic | Vascular Diseases - metabolism | Smad Proteins - metabolism | Telangiectasia, Hereditary Hemorrhagic - metabolism | Platelet-derived growth factor | Phosphatases | Peptides | Endothelial growth factors | Genes | Low density lipoproteins | DNA binding proteins | Transforming growth factors | Cells | Pulmonary hypertension | Endothelium | Proteins | Telangiectasis | Blood circulation disorders | Analysis | Stem cells | Bone morphogenetic proteins | Fibroblast growth factors | Cardiovascular diseases | Vascular endothelial growth factor | Protein binding
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