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1. Full Text Puerarin Ameliorates Experimental Alcoholic Liver Injury by Inhibition of Endotoxin Gut Leakage, Kupffer Cell Activation, and Endotoxin Receptors Expression
by Peng, JH and Cui, T and Huang, F and Chen, L and Zhao, Y and Xu, L and Xu, LL and Feng, Q and Hu, YY
JOURNAL OF PHARMACOLOGY AND EXPERIMENTAL THERAPEUTICS, ISSN 0022-3565, 03/2013, Volume 344, Issue 3, pp. 646 - 654
Puerarin, an isoflavone component extracted from Kudzu (Pueraria lobata), has been demonstrated to alleviate alcohol-related disorders. Our study examined... 
HEPATITIS | LIPOPOLYSACCHARIDE-BINDING PROTEIN | DISEASE | BARRIER | FATTY LIVER | RATS | ETHANOL | PHARMACOLOGY & PHARMACY | MICE | KAPPA-B | INTESTINAL PERMEABILITY | Toll-Like Receptor 2 - genetics | Membrane Glycoproteins - metabolism | Tight Junctions - genetics | Isoflavones - pharmacology | Male | Alanine Transaminase - blood | Alcohol-Related Disorders - genetics | Antigens, CD - genetics | Receptors, Immunologic - antagonists & inhibitors | Antigens, CD - metabolism | Liver Diseases, Alcoholic - drug therapy | Zonula Occludens-1 Protein - metabolism | Neutrophil Infiltration - drug effects | Disease Models, Animal | Tight Junctions - drug effects | Tight Junctions - metabolism | Zonula Occludens-1 Protein - genetics | Fatty Liver - metabolism | Portal Vein - metabolism | Liver - metabolism | Rats | Toll-Like Receptor 4 - genetics | Toll-Like Receptor 2 - metabolism | Neutrophil Infiltration - genetics | Rats, Sprague-Dawley | Toll-Like Receptor 4 - metabolism | Fatty Liver - drug therapy | Triglycerides - metabolism | Microvilli - genetics | Aspartate Aminotransferases - blood | Diet | Microvilli - metabolism | Receptors, Immunologic - genetics | Intestines - drug effects | Tumor Necrosis Factor-alpha - metabolism | Liver - enzymology | Intestines - metabolism | Acute-Phase Proteins - genetics | Alcohol-Related Disorders - drug therapy | Lipopolysaccharide Receptors - metabolism | Alcohol-Related Disorders - metabolism | Liver Diseases, Alcoholic - genetics | Receptors, Immunologic - biosynthesis | Kupffer Cells - metabolism | Endotoxins - metabolism | Fatty Liver - genetics | Portal Vein - drug effects | Acute-Phase Proteins - metabolism | Endotoxins - genetics | gamma-Glutamyltransferase - metabolism | Antigens, Differentiation, Myelomonocytic - genetics | Liver Diseases, Alcoholic - metabolism | Kupffer Cells - drug effects | Membrane Glycoproteins - genetics | Carrier Proteins - genetics | Microvilli - drug effects | Endotoxins - antagonists & inhibitors | Animals | Carrier Proteins - metabolism | Antigens, Differentiation, Myelomonocytic - metabolism | Lipopolysaccharide Receptors - genetics | Receptors, Immunologic - metabolism | Index Medicus
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2. Full Text Cargo-selective apical exocytosis in epithelial cells is conducted by Myo5B, Slp4a, Vamp7, and Syntaxin 3
by Vogel, Georg F and Klee, Katharina M.C and Janecke, Andreas R and Müller, Thomas and Hess, Michael W and Huber, Lukas A
Journal of Cell Biology, ISSN 0021-9525, 11/2015, Volume 211, Issue 3, pp. 587 - 604
Mutations in the motor protein Myosin Vb (Myo5B) or the soluble NSF attachment protein receptor Syntaxin 3 (Stx3) disturb epithelial polarity and cause... 
SYSTEM | MYOSIN-VB | LOCALIZATION | SECRETORY VESICLES | REGULATED EXOCYTOSIS | TRAFFICKING | MEMBRANE-PROTEIN | MICROVILLUS INCLUSION DISEASE | ZINC-FINGER NUCLEASES | PLASMA-MEMBRANE | CELL BIOLOGY | Glucose Transporter Type 5 - metabolism | Epithelial Cells - metabolism | Vesicular Transport Proteins - metabolism | Humans | R-SNARE Proteins - metabolism | Munc18 Proteins - metabolism | Malabsorption Syndromes - metabolism | Exocytosis - physiology | Myosin Heavy Chains - metabolism | Sodium-Hydrogen Exchangers - metabolism | Epithelial Cells - physiology | Mutation - physiology | Mucolipidoses - metabolism | HEK293 Cells | Cell Membrane - metabolism | Caco-2 Cells | Microvilli - pathology | rab GTP-Binding Proteins - metabolism | Cell Line | Myosin Type V - metabolism | Cystic Fibrosis Transmembrane Conductance Regulator - metabolism | Microvilli - metabolism | Qa-SNARE Proteins - metabolism | Cell Line, Tumor | Cell Polarity - physiology | Signal Transduction - physiology | Sodium-Hydrogen Exchanger 3 | Gene mutations | Cellular control mechanisms | Genetic aspects | Exocytosis | Properties | Observations | Molecular motors (Biochemistry) | Genomes | Mutation | Newborn babies | Cellular biology | Index Medicus
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3. Full Text Sweet taste receptors in rat small intestine stimulate glucose absorption through apical GLUT2
by Oliver J. Mace and Julie Affleck and Nick Patel and George L. Kellett
The Journal of Physiology, ISSN 0022-3751, 07/2007, Volume 582, Issue 1, pp. 379 - 392
Natural sugars and artificial sweeteners are sensed by receptors in taste buds. T2R bitter and T1R sweet taste receptors are coupled through G-proteins,... 
CALCIUM-ABSORPTION | ENTEROENDOCRINE STC-1 CELLS | PROTEIN-KINASE-C | PHYSIOLOGY | FRUCTOSE TRANSPORT | SUGAR ABSORPTION | GASTROINTESTINAL-TRACT | BRUSH-BORDER MEMBRANE | EXPRESSION | CA(V)1.3 | FAMILY | Glucose Transporter Type 2 - agonists | Intestinal Mucosa - metabolism | Rats, Wistar | Receptors, G-Protein-Coupled - metabolism | Calcium - metabolism | Enterocytes - metabolism | Sucrose - analogs & derivatives | Intestinal Absorption - drug effects | Sucrose - pharmacology | Type C Phospholipases - metabolism | Male | Glucose Transporter Type 2 - metabolism | Intestinal Mucosa - drug effects | Jejunum - metabolism | Dose-Response Relationship, Drug | Intestinal Mucosa - cytology | Jejunum - drug effects | Phospholipase C beta | Time Factors | Isoenzymes - metabolism | Thiazines - pharmacology | Transducin - metabolism | Jejunum - cytology | Receptors, G-Protein-Coupled - drug effects | Paneth Cells - metabolism | Sweetening Agents - pharmacology | Rats | Microvilli - drug effects | Animals | Enterocytes - drug effects | Microvilli - metabolism | Signal Transduction - drug effects | Paneth Cells - drug effects | Perfusion | Glucose - metabolism | Saccharin - pharmacology | Index Medicus | Alimentary
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4. Full Text LRRK2 regulates autophagic activity and localizes to specific membrane microdomains in a novel human genomic reporter cellular model
by Alegre-Abarrategui, Javier and Christian, Helen and Lufino, Michele M.P and Mutihac, Ruxandra and Venda, Lara Lourenço and Ansorge, Olaf and Wade-Martins, Richard
Human Molecular Genetics, ISSN 0964-6906, 11/2009, Volume 18, Issue 21, pp. 4022 - 4034
Leucine rich repeat kinase 2 (LRRK2) mutations are the most common genetic cause of Parkinson's disease (PD) although LRRK2 function remains unclear. We report... 
KINASE-ACTIVITY | CELLS | CAG REPEATS | ALZHEIMERS-DISEASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | GENETICS & HEREDITY | NEURONS | MUTATIONS | PATHOLOGY | FLUORESCENT PROTEINS | MATURATION | PARKINSONS-DISEASE | RNA, Small Interfering - genetics | Immunoprecipitation | Caveolae - ultrastructure | Membrane Microdomains - metabolism | Microtubule-Associated Proteins - metabolism | Sequestosome-1 Protein | Humans | Immunoblotting | Green Fluorescent Proteins - genetics | Autophagy | Membrane Microdomains - ultrastructure | Recombinant Fusion Proteins - metabolism | Endosomes - metabolism | Microscopy, Immunoelectron | Brain - metabolism | Transfection | Endosomes - ultrastructure | Protein-Serine-Threonine Kinases - metabolism | Cell Line | Green Fluorescent Proteins - metabolism | Caveolae - metabolism | Protein-Serine-Threonine Kinases - genetics | Parkinson Disease - genetics | Leucine-Rich Repeat Serine-Threonine Protein Kinase-2 | Microvilli - metabolism | Microvilli - ultrastructure | Protein Binding | Recombinant Fusion Proteins - genetics | Mutation | Adaptor Proteins, Signal Transducing - metabolism | Index Medicus
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5. Full Text Evidence for a causal link between adaptor protein PDZK1 downregulation and Na+/H+ exchanger NHE3 dysfunction in human and murine colitis
by Yeruva, Sunil and Chodisetti, Giriprakash and Luo, Min and Chen, Mingmin and Cinar, Ayhan and Ludolph, Lisa and Lünnemann, Maria and Goldstein, Julia and Singh, Anurag Kumar and Riederer, Brigitte and Bachmann, Oliver and Bleich, Andre and Gereke, Markus and Bruder, Dunja and Hagen, Susan and He, Peijian and Yun, Chris and Seidler, Ursula
Pflügers Archiv - European Journal of Physiology, ISSN 0031-6768, 8/2015, Volume 467, Issue 8, pp. 1795 - 1807
A dysfunction of the Na+/H+ exchanger isoform 3 (NHE3) significantly contributes to the reduced salt absorptive capacity of the inflamed intestine. We... 
Inflammatory bowel disease | Biomedicine | Sodium absorption | Human Physiology | Intestinal inflammation | pH regulation | Electrolyte transport | ACTIVATION | PHYSIOLOGY | DIARRHEA | PERMEABILITY | TRANSPORTERS | MODEL | INFLAMMATORY-BOWEL-DISEASE | INHIBITION | ABSORPTION | EXPRESSION | CAMP | Tumor Necrosis Factor-alpha - metabolism | Dextran Sulfate | Ileum - pathology | Enterocytes - metabolism | Colitis - genetics | Humans | Ileitis - chemically induced | Tumor Necrosis Factor-alpha - genetics | Ileum - metabolism | Colitis - pathology | Intracellular Signaling Peptides and Proteins - metabolism | Mice, 129 Strain | RNA, Messenger - metabolism | Ileitis - pathology | Sodium-Hydrogen Exchangers - metabolism | DNA-Binding Proteins - metabolism | Intracellular Signaling Peptides and Proteins - deficiency | Transfection | RNA Interference | Colitis - chemically induced | Inflammation Mediators - metabolism | Interleukin-10 - metabolism | Sodium-Hydrogen Exchangers - genetics | Enterocytes - pathology | Ileitis - metabolism | Retrospective Studies | Intracellular Signaling Peptides and Proteins - genetics | Disease Models, Animal | Caco-2 Cells | Colon - pathology | Down-Regulation | DNA-Binding Proteins - genetics | Colon - metabolism | Mice, Knockout | Carrier Proteins - genetics | Animals | Carrier Proteins - metabolism | Microvilli - metabolism | Biopsy | Interleukin-10 - genetics | Colitis - metabolism | Ileitis - genetics | Sodium-Hydrogen Exchanger 3 | Index Medicus | Molecular and Cellular Mechanisms of Disease
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6. Full Text Identification of Intestinal Ion Transport Defects in Microvillus Inclusion Disease
by Kravtsov, Dmitri V and Ahsan, Kaimul and Kumari, Vandana and van Ijzendoorn, Sven C D and Reyes-Mugica, Miguel and Kumar, Anoop and Gujral, Tarunmeet and Dudeja, Pradeep K and Ameen, Nadia A
American Journal of Physiology-Gastrointestinal and Liver Physiology, ISSN 0193-1857, 07/2016, Volume 311, Issue 1, pp. 142 - 155
Loss of function mutations in the actin motor Myosin Vb (Myo5b) lead to Microvillus Inclusion Disease (MVID) and death in newborns and children. MVID results... 
MVID | MVI | Brush border | NHE3 | Myo5b | CFTR | CONGENITAL CHLORIDE DIARRHEA | MYOSIN VB | PHYSIOLOGY | EPITHELIAL-CELL POLARITY | brush border | PROTRACTED DIARRHEA | MEMBRANE TRAFFICKING | TRANSMEMBRANE CONDUCTANCE REGULATOR | RECYCLING ENDOSOMES | MYO5B MUTATIONS | GASTROENTEROLOGY & HEPATOLOGY | BRUSH-BORDER CYTOSKELETON | SYNTAXIN 3 | Jejunum - pathology | Enterocytes - metabolism | Humans | Myosin Heavy Chains - genetics | Malabsorption Syndromes - metabolism | Phosphoproteins - metabolism | Myosin Heavy Chains - metabolism | Jejunum - metabolism | Sodium-Hydrogen Exchangers - metabolism | Jejunum - ultrastructure | Transfection | RNA Interference | Membrane Transport Proteins - genetics | Mucolipidoses - metabolism | Membrane Transport Proteins - metabolism | Ion Transport | Caco-2 Cells | Microvilli - pathology | Myosin Type V - metabolism | Signal Transduction | Gene Expression Regulation | Mucolipidoses - genetics | Cystic Fibrosis Transmembrane Conductance Regulator - metabolism | Malabsorption Syndromes - genetics | Microvilli - genetics | Chloride-Bicarbonate Antiporters - metabolism | Mucolipidoses - pathology | Phenotype | Myosin Type V - genetics | Microvilli - metabolism | Microvilli - ultrastructure | Adaptor Proteins, Signal Transducing - metabolism | Enterocytes - ultrastructure | Malabsorption Syndromes - pathology | Sodium-Hydrogen Exchanger 3 | Ion transport | Genetic aspects | Health aspects | Gastrointestinal diseases | Mutation (Biology) | Index Medicus | Epithelial Biology and Secretion
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7. Full Text FGF23 decreases renal NaPi-2a and NaPi-2c expression and induces hypophosphatemia in vivo predominantly via FGF receptor 1
by Jyothsna Gattineni and Carlton Bates and Katherine Twombley and Vangipuram Dwarakanath and Michael L. Robinson and Regina Goetz and Moosa Mohammadi and Michel Baum
American Journal of Physiology - Renal Physiology, ISSN 1931-857X, 08/2009, Volume 297, Issue 2, pp. 282 - 291
Fibroblast growth factor-23 (FGF23) is a phosphaturic hormone that contributes to several hypophosphatemic disorders by reducing the expression of the type II... 
Phosphaturia | Proximal tubule | Phosphorus | OSTEOMALACIA | PHYSIOLOGY | VITAMIN-D METABOLISM | FIBROBLAST-GROWTH-FACTOR-23 | ENDOCRINE | FIBROBLAST-GROWTH-FACTOR | STIMULATORY G-PROTEIN | UROLOGY & NEPHROLOGY | PARATHYROID-HORMONE GENE | proximal tubule | KIDNEY | phosphaturia | ACTIVATING MUTATIONS | phosphorus | PHOSPHATE-TRANSPORT | Recombinant Proteins - metabolism | Receptor, Fibroblast Growth Factor, Type 4 - metabolism | Hypophosphatemia - blood | Down-Regulation | Humans | Mice, Inbred C57BL | Injections, Intraperitoneal | Receptor, Fibroblast Growth Factor, Type 1 - metabolism | Parathyroid Hormone - blood | RNA, Messenger - metabolism | Receptor, Fibroblast Growth Factor, Type 1 - genetics | Calcitriol - blood | Receptor, Fibroblast Growth Factor, Type 3 - metabolism | Mice, Knockout | Sodium-Phosphate Cotransporter Proteins, Type IIa - metabolism | Fibroblast Growth Factors - metabolism | Receptor, Fibroblast Growth Factor, Type 1 - deficiency | Animals | Microvilli - metabolism | Fibroblast Growth Factors - administration & dosage | Phosphorus - blood | Sodium-Phosphate Cotransporter Proteins, Type IIc - metabolism | Kidney Tubules, Proximal - metabolism | Mice | Proteins | Kidneys | Rodents | Physiology | Hormones | Gene expression | Ribonucleic acid--RNA | Index Medicus
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8. Full Text MYO5B and bile salt export pump contribute to cholestatic liver disorder in microvillous inclusion disease
by Girard, Muriel and Lacaille, Florence and Verkarre, Virginie and Mategot, Raphael and Feldmann, Gerard and Grodet, Alain and Sauvat, Frédérique and Irtan, Sabine and Davit‐Spraul, Anne and Jacquemin, Emmanuel and Ruemmele, Frank and Rainteau, Dominique and Goulet, Olivier and Colomb, Virginie and Chardot, Christophe and Henrion‐Caude, Alexandra and Debray, Dominique
Hepatology, ISSN 0270-9139, 07/2014, Volume 60, Issue 1, pp. 301 - 310
Microvillous inclusion disease (MVID) is a congenital disorder of the enterocyte related to mutations in the MYO5B gene, leading to intractable diarrhea often... 
CELLS | MYOSIN VB | HOMEOSTASIS | TRAFFICKING | PARENTERAL-NUTRITION | MUTATIONS | GASTROENTEROLOGY & HEPATOLOGY | APICAL MEMBRANE | FAMILIAL INTRAHEPATIC CHOLESTASIS | EXTERNAL BILIARY DIVERSION | CHILDREN | Cholestasis - genetics | Cholestasis - metabolism | Enterocytes - metabolism | Humans | Child, Preschool | Myosin Heavy Chains - genetics | Hepatocytes - pathology | Infant | Male | rab GTP-Binding Proteins - genetics | Hepatocytes - metabolism | Malabsorption Syndromes - metabolism | Myosin Heavy Chains - metabolism | Endosomes - metabolism | Mucolipidoses - metabolism | Diarrhea, Infantile - metabolism | Female | Enterocytes - pathology | Microvilli - pathology | rab GTP-Binding Proteins - metabolism | Myosin Type V - metabolism | Diarrhea, Infantile - pathology | Bile Acids and Salts - metabolism | Mucolipidoses - genetics | Endosomes - pathology | Malabsorption Syndromes - genetics | Cholestasis - pathology | Homozygote | Microvilli - genetics | Mucolipidoses - pathology | Myosin Type V - genetics | Microvilli - metabolism | Biopsy | Heterozygote | Diarrhea, Infantile - genetics | Malabsorption Syndromes - pathology | Mutation | Liver | Rodents | Bile | Index Medicus
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9. Full Text Cholinergic chemosensory cells in the trachea regulate breathing
by Gabriela Krasteva and Brendan J. Canning and Petra Hartmann and Tibor Z. Veres and Tamara Papadakis and Christian Mühlfeld and Kirstin Schliecker and Yvonne N. Tallini and Armin Braun and Holger Hackstein and Nelli Baal and Eberhard Weihe and Burkhard Schütz and Michael Kotlikoff and Ines Ibanez-Tallon and Wolfgang Kummer
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 6/2011, Volume 108, Issue 23, pp. 9478 - 9483
In the epithelium of the lower airways, a cell type of unknown function has been termed "brush cell" because of a distinctive ultrastructural feature, an... 
Cholinergics | Nerve fibers | Receptors | Neurons | Epithelial cells | Respiratory reflexes | Cellular immunity | Epithelium | Trachea | Taste cells | Jugular-nodose ganglion | Respiratory epithelium | Airway sensory innervation | Bitter-tasting substances | SYSTEM | BITTER TASTE RECEPTORS | RAT TRACHEA | ACETYLCHOLINE | SUBTYPES | jugular-nodose ganglion | MULTIDISCIPLINARY SCIENCES | TRANSDUCTION | RELEASE | respiratory epithelium | TRANSPORT | airway sensory innervation | bitter-tasting substances | TRPM5 | EXPRESSION | Immunohistochemistry | Chemoreceptor Cells - metabolism | Receptors, G-Protein-Coupled - metabolism | Heterotrimeric GTP-Binding Proteins - metabolism | Male | Green Fluorescent Proteins - genetics | Trachea - metabolism | Heterotrimeric GTP-Binding Proteins - genetics | Choline O-Acetyltransferase - metabolism | Vesicular Acetylcholine Transport Proteins - metabolism | Flow Cytometry | Trachea - physiology | Female | Microfilament Proteins - metabolism | Choline O-Acetyltransferase - genetics | Phospholipase C beta - metabolism | Green Fluorescent Proteins - metabolism | Receptors, Nicotinic - metabolism | Trachea - cytology | Mice, Inbred C57BL | Microscopy, Electron | Reverse Transcriptase Polymerase Chain Reaction | Phospholipase C beta - genetics | Microscopy, Confocal | Animals | Microvilli - metabolism | Microvilli - ultrastructure | Mice | Receptors, G-Protein-Coupled - genetics | Taste | Respiration | Signal transduction | Molecules | Throat | Rodents | Cells | Index Medicus | Biological Sciences | jugular--nodose ganglion
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10. Full Text Functional regulation of sugar assimilation by N-glycan-specific interaction of pancreatic α-amylase with glycoproteins of duodenal brush border membrane
by Asanuma-Date, Kimie and Hirano, Yuki and Le, Na and Sano, Kotone and Kawasaki, Nana and Hashii, Noritaka and Hiruta, Yoko and Nakayama, Ken-Ichi and Umemura, Mariko and Ishikawa, Kazuhiko and Sakagami, Hiromi and Ogawa, Haruko
Journal of Biological Chemistry, ISSN 0021-9258, 06/2012, Volume 287, Issue 27, pp. 23104 - 23118
Porcine pancreatic alpha-amylase (PPA) binds to N-linked glycans of glycoproteins (Matsushita, H., Takenaka, M., and Ogawa, H. (2002) J. Biol Chem., 277,... 
PROTEIN | ENZYME-ACTIVITY | RAT | GLUCOSE | BIOCHEMISTRY & MOLECULAR BIOLOGY | NA+ | SUCRASE-ISOMALTASE | AMINOPEPTIDASE-N | BINDING-ACTIVITY | GLYCOSYLATION | DIPEPTIDYL PEPTIDASE-IV | Humans | Glycoproteins - metabolism | Starch - metabolism | Lectins - metabolism | Pancreatic alpha-Amylases - metabolism | Duodenum - cytology | Swine | Duodenum - metabolism | Glycoproteins - isolation & purification | Sodium-Glucose Transporter 1 - metabolism | Enterocytes - enzymology | Recombinant Proteins - metabolism | Galactans - metabolism | Glycomics - methods | Glycosylation | Recombinant Proteins - pharmacology | Polysaccharides - metabolism | Animals | Oligo-1,6-Glucosidase - metabolism | Microvilli - metabolism | Homeostasis - physiology | Mannans - metabolism | Ligands | Glycoside Hydrolases - metabolism | Sucrase - metabolism | Blood Glucose - metabolism | Pancreatic alpha-Amylases - pharmacology | Index Medicus | Carbohydrate-binding Protein | Pancreatic α-Amylase | Glycobiology | Glucose Homeostasis | Glycoside Hydrolases | Glucose Metabolism | Glycoprotein | Brush Border Membrane | Na+ | Glycobiology and Extracellular Matrices | Glc Cotransporter 1 (SGLT1)
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11. Full Text Establishment of Intestinal Identity and Epithelial-Mesenchymal Signaling by Cdx2
by Gao, Nan and White, Peter and Kaestner, Klaus H
Developmental Cell, ISSN 1534-5807, 2009, Volume 16, Issue 4, pp. 588 - 599
We demonstrate that conditional ablation of the homeobox transcription factor Cdx2 from early endoderm results in the replacement of the posterior intestinal... 
DEVBIO | TRANSCRIPTION FACTORS | CELLS | MUTANT MICE | GASTROINTESTINAL-TRACT | ENDODERM DEVELOPMENT | MOUSE | GENE-EXPRESSION | DEVELOPMENTAL BIOLOGY | HOX GENES | TRANSGENIC MICE | GUT DEVELOPMENT | CELL BIOLOGY | Cell Proliferation | Homeodomain Proteins - metabolism | Endoderm - embryology | Intestines - embryology | Epithelium - ultrastructure | Intestines - metabolism | Mesoderm - cytology | Endoderm - cytology | Gene Expression Regulation, Developmental | Mice, Mutant Strains | Gene Deletion | Body Patterning | Cell Differentiation | Esophagus - cytology | Mesoderm - ultrastructure | Epithelium - metabolism | Signal Transduction | Esophagus - metabolism | Keratinocytes - cytology | Organ Specificity | Homeodomain Proteins - genetics | Endoderm - metabolism | Endoderm - ultrastructure | Intestines - ultrastructure | Transcription Factors - metabolism | Animals | Microvilli - metabolism | Microvilli - ultrastructure | Keratinocytes - metabolism | Trans-Activators - metabolism | Mesoderm - metabolism | Mice | CDX2 Transcription Factor | Intestines - cytology | Index Medicus | intestine | endoderm | Cdx2 | Cdx1 | keratinocyte | HNF4α | conditional gene ablation | HNF1α | Wnt | esophagus | Foxa3
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12. Full Text Cleavage and Oligomerization of Gliomedin, a Transmembrane Collagen Required for Node of Ranvier Formation
by Barbara Maertens and Delana Hopkins and Claus-Werner Franzke and Douglas R. Keene and Leena Bruckner-Tuderman and Daniel S. Greenspan and Manuel Koch
Journal of Biological Chemistry, ISSN 0021-9258, 04/2007, Volume 282, Issue 14, pp. 10647 - 10659
Gliomedin, which has been implicated as a major player in genesis of the nodes of Ranvier, contains two collagenous domains and an olfactomedin-like domain and... 
OPEN-ANGLE GLAUCOMA | OLFACTOMEDIN-DOMAIN | ADHESION PROTEIN | BONE MORPHOGENETIC PROTEIN-1 | BIOCHEMISTRY & MOLECULAR BIOLOGY | MOLECULAR-CLONING | FURIN | XIII COLLAGEN | GLYCOPROTEIN | HUMAN MYOCILIN | EXPRESSION | Autoantigens - metabolism | Humans | Ectodysplasins - metabolism | Cercopithecus aethiops | Metalloendopeptidases - metabolism | Nerve Growth Factors - metabolism | Ranvier's Nodes - metabolism | Collagen Type XIII - metabolism | Metalloproteases - metabolism | Bone Morphogenetic Proteins - metabolism | Sodium Channels - metabolism | Cell Adhesion Molecules, Neuronal - metabolism | Furin - metabolism | Protein Structure, Tertiary | Bone Morphogenetic Protein 1 | Axons - metabolism | Tolloid-Like Metalloproteinases | Schwann Cells - metabolism | Cell Adhesion Molecules - metabolism | Non-Fibrillar Collagens - metabolism | Animals | Microvilli - metabolism | Cell Adhesion Molecules, Neuronal - biosynthesis | Protein Binding | Mice | COS Cells | Index Medicus
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13.