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Journal Article
PLoS ONE, ISSN 1932-6203, 05/2017, Volume 12, Issue 5, p. e0177557
Highly coordinated regulation of cell proliferation and differentiation contributes to the formation of functionally shaped and sized teeth; however, the... 
DENTINOGENESIS IMPERFECTA | METABOLIC CHECKPOINT | MUTATIONS CAUSE | OSTEOBLAST DIFFERENTIATION | MULTIDISCIPLINARY SCIENCES | TEETH | PULP CELLS | AMPK | CELL-PROLIFERATION | GAP-JUNCTION PROTEINS | EXPRESSION | AMP-Activated Protein Kinases - metabolism | Sialoglycoproteins - metabolism | Phosphoproteins - metabolism | RNA, Messenger - metabolism | Aminoimidazole Carboxamide - pharmacology | Ribonucleotides - pharmacology | Cell Differentiation - genetics | Bone Morphogenetic Proteins - metabolism | Transfection | Adenosine Triphosphate - metabolism | Cyclin-Dependent Kinase Inhibitor p21 - metabolism | Phosphorylation - drug effects | Odontoblasts - cytology | Extracellular Matrix Proteins - metabolism | Odontoblasts - metabolism | Tooth Germ - metabolism | RNA, Messenger - genetics | Connexins - genetics | Enzyme Activation - drug effects | Mice, Inbred ICR | Connexins - metabolism | Gene Expression Regulation - drug effects | Dental Papilla - cytology | Animals | Aminoimidazole Carboxamide - analogs & derivatives | Signal Transduction - drug effects | Cell Differentiation - drug effects | Models, Biological | Intracellular Space - metabolism | Odontoblasts - drug effects | Cell Proliferation - drug effects | Smad Proteins - metabolism | RNA, Small Interfering - metabolism | Cellular signal transduction | Genetic aspects | Gene expression | Health aspects | Heart | Pediatrics | Regulations | Transcription factors | Differentiation (biology) | Central nervous system | Nervous system | AKT protein | Lethality | Glucose | Proteins | Cartilage | Bone growth | Cell growth | Cellular communication | Mineralization | Neurodegeneration | Biocompatibility | Tension | Hair | Deafness | AMP | Developmental biology | Teeth | Cell division | Ions | Anatomy | Metabolism | Epithelium | Root development | Embryonic growth stage | Osteoblastogenesis | Stem cells | Mice | Mutation | Endoplasmic reticulum | Hippocampus | Tracers | Dentin | Phosphorylation | Laboratories | Homology | Biology | Kinases | AMP-activated protein kinase | Tissues | Autophagy | Defects | Morphogenesis | Biomedical materials | Metabolites | Rodents | Cell cycle | Heart diseases | Communication | University graduates | Bone morphogenetic protein 2 | Dentistry | Cell differentiation | Ribonucleic acid--RNA | Dental enamel | Skull | Bone | ATP | Apoptosis | RNA | Ribonucleic acid
Journal Article
PLoS ONE, ISSN 1932-6203, 06/2013, Volume 8, Issue 6, p. e64946
Genome-wide association (GWA) studies have described a large number of new candidate genes that contribute to of Type 2 Diabetes (T2D). In some cases, small... 
INSULIN | INHIBITION | NUCLEAR | CDK5 | PHOSPHORYLATION | MULTIDISCIPLINARY SCIENCES | DEPENDENT PROTEIN-KINASE | PANCREATIC BETA-CELLS | CREB COACTIVATOR TORC2 | ENDOPLASMIC-RETICULUM STRESS | TETRASPANIN PROTEINS | RNA, Small Interfering - genetics | Calcium-Calmodulin-Dependent Protein Kinase Type 1 - genetics | Phosphorylation | Ribosomal Protein S6 Kinases - metabolism | Diabetes Mellitus, Type 2 - genetics | Humans | Phosphoenolpyruvate Carboxykinase (GTP) - metabolism | Homeostasis | Intracellular Signaling Peptides and Proteins - metabolism | Extracellular Signal-Regulated MAP Kinases - metabolism | Hepatocytes - metabolism | Phosphoenolpyruvate Carboxykinase (GTP) - genetics | Gene Knockdown Techniques | Cyclin-Dependent Kinase 5 - genetics | Glycogen - metabolism | RNA Interference | Pyruvic Acid - metabolism | Intracellular Signaling Peptides and Proteins - genetics | Cyclic AMP-Dependent Protein Kinases - metabolism | Genome-Wide Association Study | Signal Transduction | Glucagon - physiology | Cyclin-Dependent Kinase 5 - metabolism | Hep G2 Cells | Protein Transport | Transcription Factors - metabolism | tRNA Methyltransferases | Glucose - metabolism | Polymorphism, Single Nucleotide | Protein Processing, Post-Translational | Primary Cell Culture | Genome, Human | Type 2 diabetes | Glycogen | Genes | Genomics | Genomes | Glucose | Insulin | Cells | Dextrose | Protein kinase A | Cell culture | Regulations | Neurosciences | Glucagon | Liver | Pyruvic acid | Kinases | Nuclei | Cyclin-dependent kinase 5 | Proteins | Signal transduction | Rodents | Cell cycle | Pancreas | Localization | Gluconeogenesis | Fasting | RNA-mediated interference | Diabetes mellitus | Ribosomal protein S6 | Metabolism | Gene expression | Medical screening | Musculoskeletal system | Signaling | Storage | Cellular biology | Hepatocytes | Glycolysis | Diabetes | Mutation | Molecular biology | Pharmaceuticals
Journal Article
Neuroscience, ISSN 0306-4522, 2014, Volume 284, pp. 470 - 482
Highlights • Pre- and post-somatic segments of type I spiral ganglion neurons (SGNs) are unmyelinated in man. • Following hair cell loss and retrograde nerve... 
Neurology | spiral ganglion neurons | collagen IV | laminin-β2 | immunohistochemistry | human cochlea | non-myelinated Schwann cells | Immunohistochemistry | Laminin-β2 | Spiral ganglion neurons | Collagen IV | Non-myelinated Schwann cells | Human cochlea | SURVIVAL | NERVE | IMMUNOHISTOCHEMICAL LOCALIZATION | DORSAL-ROOT GANGLIA | ELECTRON-MICROSCOPY | laminin-beta 2 | NEUROSCIENCES | SATELLITE GLIAL-CELLS | HEARING-LOSS | BASAL LAMINA | CORTI LOSS | immuno-histochemistry | HUMAN INNER-EAR | Satellite Cells, Perineuronal - cytology | Neurons - pathology | Humans | Middle Aged | Male | Neurons - cytology | Satellite Cells, Perineuronal - metabolism | Basement Membrane - pathology | Spiral Ganglion - cytology | Schwann Cells - cytology | Spiral Ganglion - pathology | Adult | Female | Neurons - metabolism | Imaging, Three-Dimensional | Microscopy, Electron, Transmission | Microscopy, Electron, Scanning | Basement Membrane - cytology | Schwann Cells - pathology | Schwann Cells - metabolism | Spiral Ganglion - metabolism | Basement Membrane - metabolism | Collagen - metabolism | Microscopy, Confocal | Cochlear Implantation | Laminin - metabolism | Satellite Cells, Perineuronal - pathology | Deafness | Ganglion | Neurons | Analysis | Cx43, connexin 43 | ECM, extracellular matrix | CI, cochlear implants | SGN, spiral ganglion neuron | BM, basement membrane | NMSC, non-myelinated Schwann cell | NIHL, noise-induced hearing loss | PBS, phosphate-buffered saline | SEM, scanning electron microscopy | IHC, immunohistochemistry | SGC, satellite glial cell | EDTA, ethylene-diamine-tetra-acetic acid | SG, spiral ganglion | type I ganglion cells, large afferent neurons innervating inner hair cell | Nav1.6, Na+-channels | TEM, transmission electron microscopy | LM, light microscopy | MBP, myelin basic protein | AIS, axonal initial segment | type II ganglion cells, small afferent neurons innervating outer hair cells | Basic Medicine | Neurosciences | Medical and Health Sciences | Medicin och hälsovetenskap | Klinisk medicin | Kirurgi | Clinical Medicine | Surgery | Medicinska och farmaceutiska grundvetenskaper | Neurovetenskaper
Journal Article
Neuron, ISSN 0896-6273, 2004, Volume 43, Issue 1, pp. 5 - 17
One cause of amyotrophic lateral sclerosis (ALS) is mutation in ubiquitously expressed copper/zinc superoxide dismutase (SOD1), but the mechanism of toxicity... 
COPPER CHAPERONE | DEAFNESS DYSTONIA SYNDROME | PROPOSED MECHANISM | CU,ZN-SUPEROXIDE DISMUTASE | MOTONEURON DEGENERATION | CU/ZN SUPEROXIDE-DISMUTASE | AMYOTROPHIC-LATERAL-SCLEROSIS | MOTOR-NEURON DISEASE | TRANSGENIC MOUSE MODEL | NEUROSCIENCES | MOLECULAR-WEIGHT COMPLEXES | Mitochondria - enzymology | Protein Binding - genetics | Superoxide Dismutase - genetics | Intracellular Membranes - enzymology | Molecular Chaperones - metabolism | Humans | Nerve Degeneration - physiopathology | Nerve Degeneration - genetics | Cytoplasm - metabolism | Intracellular Membranes - ultrastructure | Superoxide Dismutase - toxicity | Spinal Cord - chemistry | Protein Isoforms - metabolism | Mitochondria - genetics | Motor Neuron Disease - genetics | Mitochondrial Proteins - metabolism | Spinal Cord - pathology | Motor Neuron Disease - enzymology | Intracellular Membranes - pathology | Superoxide Dismutase - metabolism | Disease Models, Animal | Nerve Degeneration - enzymology | Spinal Cord - enzymology | Mice, Transgenic | Mitochondria - pathology | Microscopy, Electron | Mutation - genetics | Protein Folding | Protein Transport - genetics | Macromolecular Substances | Motor Neuron Disease - pathology | Animals | Mice | Superoxide Dismutase-1 | Aging - metabolism | Protein Isoforms - genetics | Medical research | Amyotrophic lateral sclerosis | Spinal cord | Mutation | Toxicity | Rodents | Protein Binding/genetics | Aging/metabolism | Mice; Transgenic | Protein Isoforms/genetics/metabolism | Mutation/genetics | Cytoplasm/metabolism | Nerve Degeneration/enzymology/genetics/physiopathology | Microscopy; Electron | Mitochondrial Proteins/metabolism | Spinal Cord/chemistry/enzymology/pathology | Mitochondria/enzymology/genetics/pathology | Motor Neuron Disease/enzymology/genetics/pathology | Protein Transport/genetics | Intracellular Membranes/enzymology/pathology/ultrastructure | Molecular Chaperones/metabolism | Disease Models; Animal | Superoxide Dismutase/genetics/metabolism/toxicity
Journal Article
Journal Article
BBA - Biomembranes, ISSN 0005-2736, 12/2017, Volume 1859, Issue 12, pp. 2420 - 2434
The availability of the first crystal structure of a bacterial member (SLC26Dg) of the solute carrier SLC26 family of anion transporters has allowed us to... 
Pathogenic mutations | Anion transporters | Trafficking | Homology modeling | SLC26 | Solute carriers | Transport | Membrane proteins | NONSYNDROMIC HEARING-LOSS | SULFATE-TRANSPORTER | PROCESSING DEFECT | BIOCHEMISTRY & MOLECULAR BIOLOGY | FUNCTIONAL-CHARACTERIZATION | N-GLYCOSYLATION | BIOPHYSICS | GENE | MOTOR PROTEIN | HUMAN PENDRIN | CYSTIC-FIBROSIS | STAS DOMAIN | Goiter, Nodular - genetics | Chloride-Bicarbonate Antiporters - genetics | Osteochondrodysplasias - pathology | Humans | Bacterial Proteins - chemistry | Substrate Specificity | Anion Transport Proteins - chemistry | Deinococcus - metabolism | Diarrhea - pathology | Deinococcus - genetics | Goiter, Nodular - metabolism | Osteochondrodysplasias - genetics | Membrane Transport Proteins - genetics | Goiter, Nodular - pathology | Membrane Transport Proteins - metabolism | Ion Transport | Protein Interaction Domains and Motifs | Binding Sites | Amino Acid Sequence | Protein Conformation, alpha-Helical | Chloride-Bicarbonate Antiporters - chemistry | Gene Expression | Hearing Loss, Sensorineural - metabolism | Diarrhea - congenital | Bacterial Proteins - genetics | Computational Biology | Metabolism, Inborn Errors - metabolism | Hearing Loss, Sensorineural - pathology | Models, Molecular | Hearing Loss, Sensorineural - genetics | Anion Transport Proteins - metabolism | Metabolism, Inborn Errors - genetics | Membrane Transport Proteins - chemistry | Chloride-Bicarbonate Antiporters - metabolism | Protein Conformation, beta-Strand | Diarrhea - genetics | Protein Binding | Bacterial Proteins - metabolism | Diarrhea - metabolism | Structural Homology, Protein | Mutation | Metabolism, Inborn Errors - pathology | Anion Transport Proteins - genetics | Osteochondrodysplasias - metabolism | Deafness | Disease transmission | Gene mutations | Analysis | Crystals | Genetic aspects | Glycoproteins | Structure | Protein binding | Sulfates
Journal Article
Nature genetics, ISSN 1061-4036, 2012, Volume 44, Issue 7, pp. 797 - U231
Journal Article
Clinical Genetics, ISSN 0009-9163, 11/2015, Volume 88, Issue 5, pp. 405 - 415
The spliceosome is a large ribonucleoprotein complex that removes introns from pre‐mRNA transcripts. Mutations in EFTUD2, encoding a component of the major... 
mandibulofacial dysostosis | congenital malformations | spliceosome | craniofacial | Spliceosome | Craniofacial | Congenital malformations | Mandibulofacial dysostosis | ESOPHAGEAL ATRESIA | MENTAL-RETARDATION | DEVELOPMENTAL DISORDER | AUTOSOMAL RECESSIVE INHERITANCE | COSTO-MANDIBULAR SYNDROME | DOMINANT RETINITIS-PIGMENTOSA | MESSENGER-RNA | CHOANAL ATRESIA | GENETICS & HEREDITY | OTO-FACIAL SYNDROME | RNA-Binding Proteins - genetics | Clubfoot - metabolism | Deafness - genetics | Spliceosomes - genetics | Humans | Male | Ribonucleoprotein, U5 Small Nuclear - genetics | Intellectual Disability - genetics | Intellectual Disability - metabolism | Ribs - abnormalities | Clubfoot - genetics | Heart Defects, Congenital - genetics | Micrognathism - metabolism | Spliceosomes - metabolism | Mandibulofacial Dysostosis - genetics | Ribs - metabolism | Facies | Hand Deformities, Congenital - metabolism | Female | Peptide Elongation Factors - genetics | Eukaryotic Initiation Factor-4A - genetics | Choanal Atresia - genetics | Micrognathism - genetics | RNA Splicing Factors | Pierre Robin Syndrome - metabolism | DEAD-box RNA Helicases - genetics | Choanal Atresia - metabolism | Pierre Robin Syndrome - genetics | Hand Deformities, Congenital - genetics | Deafness - metabolism | Heart Defects, Congenital - metabolism | Mandibulofacial Dysostosis - metabolism | Mutation | Deafness - congenital | Genetic disorders | Defects
Journal Article