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1. Full Text The Crumbs Complex Couples Cell Density Sensing to Hippo-Dependent Control of the TGF-β-SMAD Pathway
by Varelas, Xaralabos and Samavarchi-Tehrani, Payman and Narimatsu, Masahiro and Weiss, Alexander and Cockburn, Katie and Larsen, Brett G and Rossant, Janet and Wrana, Jeffrey L
Developmental Cell, ISSN 1534-5807, 2010, Volume 19, Issue 6, pp. 831 - 844
The Hippo pathway senses cell density information to control tissue growth by regulating the localization of the transcriptional regulators TAZ and YAP... 
TISSUE-GROWTH | GROWTH-CONTROL | PROTEIN | EPITHELIAL-CELLS | POLARITY | ORGAN SIZE CONTROL | SIGNALING PATHWAY | TRANSCRIPTION FACTOR SNAIL | TUMOR-SUPPRESSOR | DEVELOPMENTAL BIOLOGY | MESENCHYMAL TRANSITION | CELL BIOLOGY | RNA, Small Interfering - genetics | Cell Count | Nerve Tissue Proteins - deficiency | Phosphoproteins - antagonists & inhibitors | Gene Knockdown Techniques | Adaptor Proteins, Signal Transducing - antagonists & inhibitors | Base Sequence | Female | Phosphoproteins - physiology | Active Transport, Cell Nucleus | Nerve Tissue Proteins - physiology | Transcription Factors - physiology | Signal Transduction | Blastocyst - metabolism | Cells, Cultured | Transforming Growth Factor beta - physiology | Transcription Factors - antagonists & inhibitors | Phosphoproteins - genetics | Smad Proteins - physiology | Transcription Factors - genetics | Nerve Tissue Proteins - genetics | Pregnancy | Adaptor Proteins, Signal Transducing - physiology | Animals | Adaptor Proteins, Signal Transducing - genetics | Mice | In Vitro Techniques | Index Medicus
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2. Full Text Kindlin-2 mediates activation of TGF-β/Smad signaling and renal fibrosis
by Wei, Xiaofan and Xia, Yang and Li, Feng and Tang, Yan and Nie, Jing and Liu, Youhua and Zhou, Zhanmei and Zhang, Hongquan and Hou, Fan Fan
Journal of the American Society of Nephrology, ISSN 1046-6673, 09/2013, Volume 24, Issue 9, pp. 1387 - 1398
Activation of TGF-/Smad signaling plays a central role in the pathogenesis of tubulointerstitial fibrosis, but the mechanisms underlying the initial... 
GROWTH-FACTOR-BETA | FIBROTIC RESPONSE | TRANSFORMING GROWTH-FACTOR-BETA-1 | INTERSTITIAL FIBROSIS | TUBULOINTERSTITIAL FIBROSIS | UROLOGY & NEPHROLOGY | GENE-THERAPY | MECHANISMS | EPITHELIAL-MESENCHYMAL TRANSITIONS | CELL-MATRIX ADHESION | URETERAL OBSTRUCTION | Kidney - pathology | Cytoskeletal Proteins - genetics | Humans | Neoplasm Proteins - physiology | Receptors, Transforming Growth Factor beta - physiology | Integrin beta1 - physiology | Neoplasm Proteins - drug effects | Membrane Proteins - physiology | Cytoskeletal Proteins - drug effects | Cytoskeletal Proteins - physiology | Neoplasm Proteins - genetics | Muscle Proteins - physiology | Kidney - physiopathology | Disease Models, Animal | Membrane Proteins - genetics | Protein-Serine-Threonine Kinases - physiology | RNA, Small Interfering - pharmacology | Cells, Cultured | Transforming Growth Factor beta - physiology | Muscle Proteins - drug effects | Smad Proteins - physiology | Ureteral Obstruction - physiopathology | Gene Expression Regulation - drug effects | Muscle Proteins - genetics | Animals | Ureteral Obstruction - pathology | Fibrosis | Membrane Proteins - drug effects | Signal Transduction - physiology | Mice | Smad3 Protein - physiology | Index Medicus | Basic Research
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3. Full Text BMP canonical Smad signaling through Smad1 and Smad5 is required for endochondral bone formation
by Kelsey N. Retting and Buer Song and Byeong S. Yoon and Karen M. Lyons
Development, ISSN 0950-1991, 04/2009, Volume 136, Issue 7, pp. 1093 - 1104
Bone morphogenetic protein (BMP) signaling is required for endochondral bone formation. However, whether or not the effects of BMPs are mediated via canonical... 
Growth plate | Smad | BMP | Mouse | Chondrogenesis | TGF-BETA | PTH/PTHRP-RECEPTOR | CONDITIONAL KNOCKOUT | CHONDROGENIC DIFFERENTIATION | DEVELOPMENTAL BIOLOGY | EARLY MOUSE EMBRYO | GROWTH-FACTOR RECEPTOR-3 | INDIAN-HEDGEHOG | CHONDROCYTE PROLIFERATION | SKELETAL DEVELOPMENT | TRANSGENIC MICE | Smad8 Protein - genetics | Chondrocytes - cytology | Osteogenesis - physiology | Phosphorylation | Smad1 Protein - deficiency | Cell Proliferation | Smad5 Protein - physiology | Bone Morphogenetic Proteins - physiology | Chondrogenesis - genetics | Male | Hedgehog Proteins - physiology | Extremities - embryology | Chondrocytes - physiology | Smad4 Protein - genetics | Mice, Mutant Strains | Smad1 Protein - genetics | Female | Cell Differentiation | Smad5 Protein - genetics | Osteogenesis - genetics | Fibroblast Growth Factors - physiology | Smad5 Protein - deficiency | Signal Transduction | Cell Survival | Smad1 Protein - physiology | Smad4 Protein - physiology | Mice, Knockout | Chondrogenesis - physiology | Smad8 Protein - deficiency | Animals | Smad8 Protein - physiology | Parathyroid Hormone-Related Protein - physiology | Mice | Smad4 Protein - deficiency | Index Medicus
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4. Full Text Identification of TWSG1 as a second novel erythroid regulator of hepcidin expression in murine and human cells
by Tanno, Toshihiko and Porayette, Prashanth and Sripichai, Orapan and Noh, Seung-Jae and Byrnes, Colleen and Bhupatiraju, Ajoy and Lee, Y. Terry and Goodnough, Julia B and Harandi, Omid and Ganz, Tomas and Paulson, Robert F and Miller, Jeffery L
Blood, ISSN 0006-4971, 2009, Volume 114, Issue 1, pp. 181 - 186
In thalassemia and other iron loading anemias, ineffective erythropoiesis and erythroid signaling molecules are thought to cause inappropriate suppression of a... 
IRON HOMEOSTASIS | TWISTED-GASTRULATION | ERYTHROPOIESIS | BMP ANTAGONIST | MOUSE MODEL | GENES | LIVER | COOLEY-ANEMIA | BETA-THALASSEMIA | HEMATOLOGY | HEMOJUVELIN | Thalassemia - blood | Antimicrobial Cationic Peptides - physiology | Humans | Growth Differentiation Factor 15 - physiology | Homeostasis | Cytokines - physiology | Growth Differentiation Factor 15 - genetics | Hepatocytes - cytology | Hepcidins | Mice, Mutant Strains | Female | Antimicrobial Cationic Peptides - genetics | Thalassemia - genetics | Cytokines - genetics | Hepatocytes - physiology | Erythropoiesis - genetics | Proteins - physiology | Mice, Inbred C57BL | Bone Morphogenetic Protein 4 - physiology | Thalassemia - pathology | Smad Proteins - physiology | Bone Morphogenetic Protein 2 - physiology | Iron - metabolism | Erythropoiesis - physiology | Proteins - genetics | Animals | Mice | Thalassemia - physiopathology | Index Medicus | Abridged Index Medicus | Red Cells, Iron, and Erythropoiesis
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5. Full Text LIM-kinase 2 and cofilin phosphorylation mediate actin cytoskeleton reorganization induced by transforming growth factor-β
by Vardouli, Lina and Moustakas, Aristidis and Stournaras, Christos
Journal of Biological Chemistry, ISSN 0021-9258, 03/2005, Volume 280, Issue 12, pp. 11448 - 11457
Reorganization of the actin cytoskeleton in response to growth factor signaling, such as transforming growth factor beta (TGF-beta), controls cell adhesion,... 
SIGNAL-TRANSDUCTION | RHO-ASSOCIATED KINASE | ACTIVATION | TGF-BETA | SMAD PROTEINS | POLYMERIZATION DYNAMICS | CELL-MIGRATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | LIM-KINASE | RAS TRANSFORMATION | MESENCHYMAL TRANSDIFFERENTIATION | Smad7 Protein | DNA-Binding Proteins - physiology | Phosphorylation | Protein-Serine-Threonine Kinases - physiology | Humans | Microfilament Proteins - physiology | Intracellular Signaling Peptides and Proteins | Lim Kinases | rhoA GTP-Binding Protein - metabolism | Actin Depolymerizing Factors | rhoB GTP-Binding Protein - metabolism | Trans-Activators - physiology | Transforming Growth Factor beta - pharmacology | Animals | Protein Kinases - physiology | rho-Associated Kinases | Cytoskeleton - physiology | Mice | Actins - physiology | Index Medicus | rhoB GTP-Binding Protein/metabolism | Actins/physiology | Cytoskeleton/physiology | Protein Kinases/physiology | Microfilament Proteins/physiology | Trans-Activators/physiology | Transforming Growth Factor beta/pharmacology | rhoA GTP-Binding Protein/metabolism | DNA-Binding Proteins/physiology | Protein-Serine-Threonine Kinases/physiology | Research Support; Non-U.S. Gov't
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6. Full Text Tumor-Derived Jagged1 Promotes Osteolytic Bone Metastasis of Breast Cancer by Engaging Notch Signaling in Bone Cells
by Sethi, Nilay and Dai, Xudong and Winter, Christopher G and Kang, Yibin
Cancer Cell, ISSN 1535-6108, 2011, Volume 19, Issue 2, pp. 192 - 205
Despite evidence supporting an oncogenic role in breast cancer, the Notch pathway's contribution to metastasis remains unknown. Here, we report that the Notch... 
SURVIVAL | TO-MESENCHYMAL TRANSITION | ACTIVATION | HORMONE-RELATED PROTEIN | ONCOLOGY | GROWTH-FACTOR | KAPPA-B | DIFFERENTIATION | INTERLEUKIN-6 | OSTEOCLAST PRECURSORS | EXPRESSION | CELL BIOLOGY | Signal Transduction | Receptors, Notch - metabolism | Enzyme Inhibitors - pharmacology | Bone Neoplasms - secondary | Interleukin-6 - secretion | Intercellular Signaling Peptides and Proteins - physiology | Osteoblasts - pathology | Animals | Membrane Proteins - physiology | Serrate-Jagged Proteins | Calcium-Binding Proteins - physiology | Mammary Neoplasms, Experimental - pathology | Ligands | Cell Differentiation | Mice | Amyloid Precursor Protein Secretases - antagonists & inhibitors | Osteoblasts - metabolism | Smad Proteins - metabolism | Transforming Growth Factor beta - metabolism | 3T3 Cells | Jagged-1 Protein | Breast cancer | Research | Metastasis | Transforming growth factors | Oncology, Experimental | Cancer | Index Medicus
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7. Full Text ALK1 Signaling Inhibits Angiogenesis by Cooperating with the Notch Pathway
by Larrivée, Bruno and Prahst, Claudia and Gordon, Emma and del Toro, Raquel and Mathivet, Thomas and Duarte, Antonio and Simons, Michael and Eichmann, Anne
Developmental Cell, ISSN 1534-5807, 03/2012, Volume 22, Issue 3, pp. 489 - 500
Activin receptor-like kinase 1 (ALK1) is an endothelial-specific member of the TGF-β/BMP receptor family that is inactivated in patients with hereditary... 
TIP CELL-FORMATION | VASCULAR DEVELOPMENT | DLL4 | ARTERIOVENOUS-MALFORMATIONS | ACTIVATION | HEREDITARY HEMORRHAGIC TELANGIECTASIA | VEGF | RECEPTOR | DEVELOPMENTAL BIOLOGY | IDENTIFICATION | EXPRESSION | CELL BIOLOGY | Activin Receptors, Type I - antagonists & inhibitors | Telangiectasia, Hereditary Hemorrhagic - physiopathology | Neovascularization, Physiologic - drug effects | Basic Helix-Loop-Helix Transcription Factors - physiology | Retina - growth & development | Signal Transduction | Dipeptides - pharmacology | Humans | Mice, Inbred C57BL | Receptors, Notch - physiology | Telangiectasia, Hereditary Hemorrhagic - drug therapy | Smad Proteins - physiology | Vascular Endothelial Growth Factors - physiology | Arteriovenous Malformations - enzymology | Repressor Proteins - physiology | Neovascularization, Physiologic - physiology | Animals | Mice | Activin Receptors, Type I - physiology | Cell Cycle Proteins - physiology | Retina - pathology | Disease Models, Animal | Growth Differentiation Factors - physiology | Universities and colleges | Endothelial growth factors | Transforming growth factors | Vascular endothelial growth factor | Index Medicus
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8. Full Text EGFR-AKT-Smad signaling promotes formation of glioma stem-like cells and tumor angiogenesis by ID3-driven cytokine induction
by Jin, Xun and Yin, Jinlong and Kim, Sung-Hak and Sohn, Young-Woo and Beck, Samuel and Lim, Young Chang and Nam, Do-Hyun and Choi, Yun-Jaie and Kim, Hyunggee
Cancer Research, ISSN 0008-5472, 11/2011, Volume 71, Issue 22, pp. 7125 - 7134
Aberrant activation of receptor tyrosine kinases (RTK) is causally linked to the pathobiological traits of glioblastoma and genesis of glioma stem-like cells... 
GROWTH-FACTOR RECEPTOR | ACTIVATION | ONCOLOGY | HUMAN GLIOBLASTOMA | ID1 | GENES | IL-6 PRODUCTION | PROLIFERATION | DIFFERENTIATION | INHIBITORS | PROTEINS | Phosphorylation | Inhibitor of Differentiation Proteins - physiology | Humans | Neoplasm Proteins - physiology | Proto-Oncogene Proteins c-akt - physiology | Smad Proteins - physiology | Neovascularization, Pathologic - etiology | Cyclin-Dependent Kinase Inhibitor p16 - physiology | Animals | Glioma - pathology | Interleukin-6 - physiology | Cell Line, Tumor | Neoplastic Stem Cells - pathology | Signal Transduction - physiology | Mice | Mice, Inbred BALB C | Receptor, Epidermal Growth Factor - physiology | Cytokines - biosynthesis | Index Medicus
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9. Full Text BMP/SMAD pathway promotes neurogenesis of midbrain dopaminergic neurons in vivo and in human induced pluripotent and neural stem cells
by Jovanovic, Vukasin M and Salti, Ahmad and Tilleman, Hadas and Zega, Ksenija and Jukic, Marin M and Zou, Hongyan and Friedel, Roland H and Prakash, Nilima and Blaess, Sandra and Edenhofer, Frank and Brodski, Claude
Journal of Neuroscience, ISSN 0270-6474, 02/2018, Volume 38, Issue 7, pp. 1662 - 1676
The embryonic formation of midbrain dopaminergic (mDA) neurons in vivo provides critical guidelines for the in vitro differentiation of mDA neurons from stem... 
Neuronal differentiation | Embryonic development | IPSC | Neurogenesis | Stem cells | Midbrain dopaminergic neurons | stem cells | SMAD1 | HUMAN ES | BMP | embryonic development | iPSC | BONE MORPHOGENETIC PROTEINS | SPECIFICATION | BETA-CATENIN | FATE | NEUROSCIENCES | neuronal differentiation | MULTIPLE ROLES | GROWTH | neurogenesis | midbrain dopaminergic neurons | DIFFERENTIATION | Cell Proliferation | Mesencephalon - cytology | Bone Morphogenetic Proteins - physiology | Bone Morphogenetic Protein 7 - genetics | Homeodomain Proteins - metabolism | Humans | Hedgehog Proteins - metabolism | Bone Morphogenetic Protein 5 - metabolism | Pluripotent Stem Cells | Hedgehog Proteins - genetics | Gene Expression Regulation, Developmental | MSX1 Transcription Factor - genetics | Smad1 Protein - genetics | Dopaminergic Neurons - physiology | Mesencephalon - physiology | Bone Morphogenetic Protein 5 - genetics | Neural Stem Cells | Smad Proteins - physiology | Homeodomain Proteins - genetics | Mice, Knockout | Animals | Neurogenesis - physiology | Bone Morphogenetic Protein 7 - metabolism | Smad1 Protein - metabolism | Signal Transduction - physiology | Mice | MSX1 Transcription Factor - metabolism | Smad protein | Parkinson's disease | Mesencephalon | Substantia nigra | Embryo cells | Differentiation (biology) | Stem cell transplantation | Tyrosine 3-monooxygenase | Homeobox | Proteins | Allografts | Cell cycle | Bone morphogenetic proteins | Potassium channels (voltage-gated) | Inhibition | Movement disorders | Dopamine receptors | Tyrosine | Bone morphogenetic protein 5 | Dopamine | Neurodegenerative diseases | Potassium channels (inwardly-rectifying) | Neurons | Hydroxylase | Mammals | Cell differentiation | Gene expression | Progenitor cells | Mutants | Molecular modelling | Hedgehog protein | Cells (biology) | Neural stem cells | Potassium | Pluripotency | Bone morphogenetic protein 7 | Index Medicus
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10. Full Text Id2 and Id3 Define the Potency of Cell Proliferation and Differentiation Responses to Transforming Growth Factor β and Bone Morphogenetic Protein
by Marcin Kowanetz and Ulrich Valcourt and Rosita Bergström and Carl-Henrik Heldin and Aristidis Moustakas and Medicinska och farmaceutiska vetenskapsområdet and Medicinska och farmaceutiska vetenskapsområdet, centrumbildningar mm and Ludwiginstitutet för cancerforskning and Teknisk-naturvetenskapliga vetenskapsområdet and Biologiska sektionen and Uppsala universitet and Institutionen för fysiologi och utvecklingsbiologi
Molecular and Cellular Biology, ISSN 0270-7306, 05/2004, Volume 24, Issue 10, pp. 4241 - 4254
Article Usage Stats Services MCB Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley... 
I RECEPTORS | TGF-BETA | SMAD PROTEINS | EPITHELIAL-CELLS | GENE | REPRESSION | BIOCHEMISTRY & MOLECULAR BIOLOGY | ENDOTHELIAL-CELLS | UP-REGULATION | EXPRESSION | CANCER | CELL BIOLOGY | Multigene Family | Humans | Neoplasm Proteins - physiology | Repressor Proteins | DNA, Complementary - genetics | Mesoderm - drug effects | Inhibitor of Differentiation Proteins | Trans-Activators - physiology | Inhibitor of Differentiation Protein 2 | Cell Differentiation - genetics | Base Sequence | Trans-Activators - genetics | Neoplasm Proteins - genetics | Bone Morphogenetic Proteins - pharmacology | Cell Differentiation - physiology | Cell Division - genetics | Cell Line | Epithelium - drug effects | DNA-Binding Proteins - physiology | Transcription Factors - physiology | Signal Transduction | Smad4 Protein | Transcription Factors - genetics | DNA-Binding Proteins - genetics | Cell Division - drug effects | Cell Division - physiology | Transforming Growth Factor beta - pharmacology | Animals | Cell Differentiation - drug effects | Mesoderm - physiology | Epithelium - physiology | Mice | Bone Morphogenetic Protein 7 | Index Medicus | Cell Growth and Development | Medical and Health Sciences | MEDICINE | Medicin och hälsovetenskap | MEDICIN
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11. Full Text TGF-β induces miR-182 to sustain NF-κB activation in glioma subsets
by Song, Libing and Liu, Liping and Wu, Zhiqiang and Li, Yun and Ying, Zhe and Lin, Chuyong and Wu, Jueheng and Hu, Bo and Cheng, Shi-Yuan and Li, Mengfeng and Li, Jun
Journal of Clinical Investigation, ISSN 0021-9738, 10/2012, Volume 122, Issue 10, pp. 3563 - 3578
The strength and duration of NF-kappa B signaling are tightly controlled by multiple negative feedback mechanisms. However, in cancer cells, these feedback... 
UBIQUITINATION | MEDICINE, RESEARCH & EXPERIMENTAL | STEM-CELLS | KINASE | BREAST-CANCER PROGRESSION | PROGNOSTIC MARKER | ALPHA | CELL-PROLIFERATION | PATIENT SURVIVAL | EXPRESSION | A20 | Phosphorylation | MicroRNAs - antagonists & inhibitors | Deubiquitinating Enzyme CYLD | Humans | Brain Neoplasms - pathology | NF-kappa B - metabolism | Cell Line, Tumor - drug effects | Cell Line, Tumor - transplantation | Neoplasm Proteins - metabolism | Brain Neoplasms - metabolism | Glioma - metabolism | RNA - genetics | Glioma - genetics | Smad Proteins - biosynthesis | Ubiquitination - drug effects | I-kappa B Kinase - metabolism | Glioma - pathology | Tumor Suppressor Proteins - genetics | Neovascularization, Pathologic - physiopathology | Transcription, Genetic | Neoplasm Proteins - genetics | Cell Line, Tumor - metabolism | Genes, Reporter | NF-KappaB Inhibitor alpha | RNA, Neoplasm - physiology | Neoplasm Invasiveness | Neoplasm Proteins - biosynthesis | Transforming Growth Factor beta - physiology | Brain Neoplasms - genetics | MicroRNAs - biosynthesis | Smad Proteins - genetics | RNA - biosynthesis | Transforming Growth Factor beta - pharmacology | Tumor Suppressor Proteins - physiology | Animals | RNA, Neoplasm - biosynthesis | Signal Transduction - drug effects | Mice, Nude | RNA, Neoplasm - genetics | Mice | MicroRNAs - genetics | Protein Processing, Post-Translational | MicroRNAs - physiology | Tumor Suppressor Proteins - biosynthesis | I-kappa B Proteins - deficiency | Index Medicus | Abridged Index Medicus
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12. Full Text OAZ uses distinct DNA- and protein-binding zinc fingers in separate BMP-Smad and Olf signaling pathways
by Hata, A and Seoane, J and Lagna, G and Montalvo, E and Hemmati-Brivanlou, A and Massague, J
CELL, ISSN 0092-8674, 01/2000, Volume 100, Issue 2, pp. 229 - 240
We have identified the 30-zinc finger protein OAZ as a DNA-binding factor that associates with Smads in response to BMP2, forming a complex that... 
TGF-BETA | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | TRANSCRIPTION | BONE MORPHOGENETIC PROTEINS | GENE-EXPRESSION | TUMOR-SUPPRESSOR | FUNCTIONAL-CHARACTERIZATION | REGULATORS | HOMEOBOX GENE | XENOPUS MESODERM | CELL BIOLOGY | Xenopus | Xenopus Proteins - genetics | Homeodomain Proteins - metabolism | Humans | Molecular Sequence Data | DNA-Binding Proteins - analysis | Trans-Activators - physiology | DNA-Binding Proteins - metabolism | Bone Morphogenetic Proteins - metabolism | Base Sequence | Cloning, Molecular | Bone Morphogenetic Proteins - genetics | Genes, Reporter | Xenopus Proteins - analysis | Basic Helix-Loop-Helix Transcription Factors | Gene Expression Regulation, Developmental - physiology | Amino Acid Sequence | DNA-Binding Proteins - physiology | Transcription Factors - physiology | Rats | Transcription Factors - genetics | DNA-Binding Proteins - genetics | Homeodomain Proteins - genetics | Nerve Tissue Proteins - metabolism | Transcription Factors - metabolism | Yeasts - genetics | Smad3 Protein | Transcription, Genetic - physiology | Animals | Oocytes - physiology | Smad Proteins | Xenopus Proteins - physiology | Signal Transduction - physiology | Xenopus Proteins - metabolism | Zinc Fingers - genetics | Cell Nucleus - chemistry | Transcription Factors - analysis | COS Cells | Lac Operon | Protein Binding - physiology | Smad2 Protein | Homeobox genes | Neurons | Zinc in the body | Physiological aspects | Mesoderm | Bones | Cellular signal transduction | Regulation | Genetic aspects | Research | Genetic transcription | Cytochemistry | OA protein | Xvent-2 protein | EBF protein | Smad proteins | Olf-1/EBF protein | double prime OAZ protein | Olf-1 protein | Index Medicus
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13. Full Text ERBIN deficiency links STAT3 and TGF-β pathway defects with atopy in humans
by Lyons, J.J and Liu, Y and Ma, C.A and Yu, X and O'Connell, M.P and Lawrence, M.G and Zhang, Y and Karpe, K and Zhao, M and Siegel, A.M and Stone, K.D and Nelson, C and Jones, N and DiMaggio, T and Darnell, D.N and Mendoza-Caamal, E and Orozco, L and Hughes, J.D and McElwee, J and Hohman, R.J and Frischmeyer-Guerrerio, P.A and Rothenberg, M.E and Freeman, A.F and Holland, S.M and Milner, J.D
The Journal of experimental medicine, ISSN 0022-1007, 03/2017, Volume 214, Issue 3, pp. 669 - 680
Nonimmunological connective tissue phenotypes in humans are common among some congenital and acquired allergic diseases. Several of these congenital disorders... 
MEDICINE, RESEARCH & EXPERIMENTAL | GROWTH-FACTOR-BETA | COMPETITION | CD4(+) | MUTATIONS | INDUCTION | IMMUNOLOGY | NAIVE | EXPRESSION | T-CELLS | EOSINOPHILIC ESOPHAGITIS | GATA-3 | Humans | Transforming Growth Factor beta - physiology | Hypersensitivity - immunology | Adaptor Proteins, Signal Transducing - physiology | Receptors, Interleukin-4 - physiology | STAT3 Transcription Factor - physiology | Adaptor Proteins, Signal Transducing - deficiency | Signal Transduction - physiology | Smad3 Protein - analysis | Interleukin-4 - physiology | Smad2 Protein - analysis | Smad2 Protein - physiology | Smad3 Protein - physiology | Smad protein | Deregulation | Complex formation | Immunoglobulin E | Activation | Allergic diseases | Lymphocytes T | Kinases | Atopy | Connective tissues | Signal transduction | Interleukin 4 | Cell activation | Lymphocytes | Smad2 protein | Foxp3 protein | Immunoregulation | Stat3 protein | ErbB-2 protein | Anchors | Signaling | GATA-3 protein | Mutation | Receptor mechanisms | Auditory defects | Index Medicus | 316
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14. Full Text Neogenin Regulation of BMP-Induced Canonical Smad Signaling and Endochondral Bone Formation
by Zhou, Zheng and Zhou, Lijuan and Xie, Jianxin and Lee, Daehoon and Liu, Yu and Jung, Jiung and Xiong, Wen-Cheng and Xiong, Shan and Mei, Lin
Developmental Cell, ISSN 1534-5807, 07/2010, Volume 19, Issue 1, pp. 90 - 102
Neogenin has been identified as a receptor for the neuronal axon guidance cues netrins and RGMs (repulsive guidance molecules). Here we provide evidence for... 
DEVIO | SIGNALING | Signaling | Devio | RECEPTOR COMPLEXES | REPULSIVE GUIDANCE MOLECULE | LIPID RAFTS | GROWTH-PLATE | DEVELOPMENTAL BIOLOGY | HEPCIDIN EXPRESSION | MORPHOGENETIC PROTEIN CORECEPTOR | PLASMA-MEMBRANE | SKELETAL DEVELOPMENT | MOUSE LIMB | CHONDROGENESIS | CELL BIOLOGY | Bone Morphogenetic Protein 2 - pharmacology | Chondrocytes - cytology | Chondrogenesis - drug effects | Phosphorylation | Cell Proliferation | Bone Morphogenetic Proteins - physiology | Chondrogenesis - genetics | Membrane Microdomains - metabolism | Bone Development - physiology | Growth Plate - embryology | Core Binding Factor Alpha 1 Subunit - metabolism | Chondrocytes - drug effects | Chondrocytes - physiology | Membrane Proteins - physiology | Mice, Mutant Strains | Female | Cell Differentiation | p38 Mitogen-Activated Protein Kinases - metabolism | Bone Morphogenetic Proteins - genetics | Membrane Proteins - genetics | Mice, Inbred C57BL | Bone Morphogenetic Protein Receptors - metabolism | Smad Proteins - genetics | Recombinant Proteins - pharmacology | Smad Proteins - physiology | Growth Plate - metabolism | Pregnancy | Chondrogenesis - physiology | Animals | Signal Transduction - drug effects | Mice | Bone Development - genetics | Developmental biology | Bone morphogenetic proteins | Index Medicus
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