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The New England Journal of Medicine, ISSN 0028-4793, 12/2011, Volume 365, Issue 25, pp. 2377 - 2388
The authors report that INF2 mutations are present in patients with focal segmental glomerulosclerosis (FSGS) associated with Charcot–Marie–Tooth neuropathy.... 
GLOMERULOSCLEROSIS | MEDICINE, GENERAL & INTERNAL | MYELIN | PROTEIN | NEUROPATHY | EPITHELIAL-CELLS | GENE | RHO | MEDIATED TRANSPORT | FORMIN | NEPHROPATHY | Humans | Middle Aged | Proteolipids - metabolism | Actins - metabolism | Male | Charcot-Marie-Tooth Disease - genetics | Young Adult | Kidney - metabolism | Glomerulosclerosis, Focal Segmental - etiology | Myelin and Lymphocyte-Associated Proteolipid Proteins | Adult | Female | Membrane Transport Proteins - metabolism | Microfilament Proteins - metabolism | Child | Microfilament Proteins - genetics | Charcot-Marie-Tooth Disease - complications | Schwann Cells - metabolism | Phenotype | Animals | Adolescent | Age of Onset | Heterozygote | Mice | Mutation | Myelin Proteins - metabolism | Glomerulonephritis | Gene mutations | Charcot-Marie-Tooth disease | Causes of | Genetic aspects | Research | Myelin proteins | Cdc42 protein | Disease | Exons | Genes | Amino acids | Nervous system | Neuropathy | Guanine nucleotide-binding protein | Proteins | Myelin P0 protein | Localization | Peripheral myelin protein 22 | Deoxyribonucleic acid--DNA | Kidneys | Schwann cells | Polymerization | Myelination | Genotyping | Biopsy | Glomerulus | Cytoskeleton | Genetic testing | Cytoplasm | Guanosinetriphosphatase | Schwann Cells | Genomics | Kidney | Charcot-Marie-Tooth Disease | Life Sciences | Proteolipids | Biochemistry, Molecular Biology | Actins | Microfilament Proteins | Membrane Transport Proteins | Myelin Proteins | Glomerulosclerosis, Focal Segmental
Journal Article
PLoS Pathogens, ISSN 1553-7366, 05/2015, Volume 11, Issue 5, p. e1004896
Clostridium perfringens epsilon-toxin (ETX) is a potent pore-forming toxin responsible for a central nervous system (CNS) disease in ruminant animals with... 
NERVOUS-SYSTEM | MDCK CELLS | MICROBIOLOGY | PLASMA-MEMBRANE | INTESTINAL INFECTIONS | DARBY CANINE KIDNEY | VIROLOGY | PORE-FORMING TOXIN | APICAL SORTING MACHINERY | RAFT-ASSOCIATED PROTEIN | HUMAN T-LYMPHOCYTES | PARASITOLOGY | INFLUENZA-VIRUS HEMAGGLUTININ | Injections, Intravenous | Cricetulus | Myelin and Lymphocyte-Associated Proteolipid Proteins - metabolism | Humans | Bacterial Toxins - toxicity | Recombinant Fusion Proteins - metabolism | Tissue Distribution | Protein Precursors - toxicity | Bacterial Toxins - genetics | Clostridium perfringens - metabolism | Protein Interaction Domains and Motifs | Cell Death - drug effects | Binding Sites | Clostridium perfringens - pathogenicity | Recombinant Fusion Proteins - administration & dosage | CHO Cells | Recombinant Proteins - metabolism | Protein Precursors - genetics | Protein Precursors - administration & dosage | Mice, Inbred C57BL | Rats | Recombinant Proteins - chemistry | Recombinant Fusion Proteins - toxicity | Recombinant Fusion Proteins - chemistry | Recombinant Proteins - administration & dosage | Mice, Knockout | Protein Precursors - metabolism | Toxicokinetics | Bacterial Toxins - metabolism | Animals | Myelin and Lymphocyte-Associated Proteolipid Proteins - chemistry | Recombinant Proteins - toxicity | Ligands | Mutagenesis, Insertional | Myelin and Lymphocyte-Associated Proteolipid Proteins - genetics
Journal Article
Nature Immunology, ISSN 1529-2908, 02/2006, Volume 7, Issue 2, pp. 148 - 155
Journal Article
Journal Article
Journal of Immunology, ISSN 0022-1767, 06/2011, Volume 186, Issue 11, pp. 6345 - 6356
T cell membrane receptors and signaling molecules assemble at the immunological synapse (IS) in a supramolecular activation cluster (SMAC), organized into two... 
MICROCLUSTERS | DYNAMIC POLARIZATION | APICAL TRANSPORT | RAFT LIPIDS | RECEPTOR | ANCHORED PROTEINS | TYROSINE KINASES | IMMUNOLOGY | IMMUNOLOGICAL SYNAPSE | PLASMA-MEMBRANE | CELL-ACTIVATION | Endosomes - immunology | Membrane Microdomains - metabolism | Humans | Proteolipids - metabolism | Lymphocyte Specific Protein Tyrosine Kinase p56(lck) - immunology | Green Fluorescent Proteins - genetics | Endosomes - metabolism | Membrane Microdomains - immunology | Microtubules - metabolism | Proteolipids - immunology | RNA Interference | T-Lymphocytes - metabolism | Membrane Transport Proteins - genetics | Myelin and Lymphocyte-Associated Proteolipid Proteins | Adaptor Proteins, Signal Transducing - immunology | Myelin Proteins - immunology | Membrane Transport Proteins - metabolism | Membrane Proteins - metabolism | Amino Acid Sequence | Green Fluorescent Proteins - metabolism | Proteolipids - genetics | Jurkat Cells | Membrane Proteins - genetics | Cells, Cultured | Microtubules - immunology | Membrane Proteins - immunology | Lymphocyte Specific Protein Tyrosine Kinase p56(lck) - metabolism | Myelin Proteins - genetics | Protein Transport | Microscopy, Confocal | Models, Immunological | Adaptor Proteins, Signal Transducing - genetics | Immunological Synapses - immunology | Cell Line, Tumor | Protein Binding | T-Lymphocytes - immunology | Lymphocyte Specific Protein Tyrosine Kinase p56(lck) - genetics | Adaptor Proteins, Signal Transducing - metabolism | Membrane Transport Proteins - immunology | Myelin Proteins - metabolism
Journal Article
The Journal of Cell Biology, ISSN 0021-9525, 4/2004, Volume 165, Issue 1, pp. 53 - 62
YidC of Echerichia coli, a member of the conserved Alb3/Oxa1/YidC family, is postulated to be important for biogenesis of membrane proteins. Here, we use as a... 
Membrane transport proteins | String theory | Plasmids | Escherichia coli | Fluorescence | Antibodies | Epitopes | Cells | P branes | Membrane proteins | Oxal/Alb3 protein family | Protein folding | SecYEG | Membrane insertion | LacY | RESPIRATORY-CHAIN | INSERTION | Oxa1/Alb3 protein family | ESCHERICHIA-COLI | MONOCLONAL-ANTIBODY | TRANSPORT PROTEINS | CELL BIOLOGY | SIGNAL-RECOGNITION PARTICLE | LACTOSE PERMEASE | NASCENT FTSQ | membrane insertion | protein folding | LAC PERMEASE | COLI INNER MEMBRANE | Protein Binding - genetics | Epitopes - metabolism | Molecular Chaperones - metabolism | Proteolipids - metabolism | Protein Transport - physiology | Epitopes - immunology | Membrane Transport Proteins - genetics | Escherichia coli - metabolism | Membrane Transport Proteins - metabolism | Membrane Proteins - metabolism | Protein Biosynthesis - genetics | Monosaccharide Transport Proteins - metabolism | Antibodies, Monoclonal - immunology | Monosaccharide Transport Proteins - genetics | Molecular Chaperones - genetics | Models, Molecular | Escherichia coli Proteins - metabolism | Protein Binding - immunology | Protein Folding | Symporters - metabolism | Carrier Proteins - metabolism | Symporters - genetics | Escherichia coli Proteins - genetics | Membrane Lipids - metabolism | Antibodies, Monoclonal - metabolism | Escherichia coli - ultrastructure | Intracellular Membranes - metabolism | Research | LacY; membrane insertion; protein folding; SecYEG; Oxa1 | Alb3 protein family
Journal Article
Neuron, ISSN 0896-6273, 2010, Volume 67, Issue 2, pp. 268 - 279
Acidification of synaptic vesicles by the vacuolar proton ATPase is essential for loading with neurotransmitter. Debated findings have suggested that V-ATPase... 
CELLBIO | MOLNEURO | SIGNALING | Signaling | Cellbio | Molneuro | A1 | PROTEIN-INTERACTION SITE | COMPLEX-FORMATION | FUSION | CALMODULIN | LIPID-BINDING | BINDING DOMAIN | CHANNELS | SYNAPTIC VESICLE EXOCYTOSIS | NEUROSCIENCES | SUBUNIT | Enzyme-Linked Immunosorbent Assay - methods | Synaptic Vesicles - metabolism | Rats, Wistar | Calcium - metabolism | Proteolipids - metabolism | Vesicle-Associated Membrane Protein 2 - genetics | Cerebral Cortex - cytology | Excitatory Postsynaptic Potentials - drug effects | Vacuolar Proton-Translocating ATPases - metabolism | Protein Subunits - metabolism | Neurons - ultrastructure | Peptides - metabolism | Neurotransmitter Agents - pharmacology | Protein Binding - drug effects | Macrolides - pharmacology | Cell Membrane - metabolism | Neurons - metabolism | Neurons - drug effects | Protein Subunits - genetics | Animals, Newborn | Synapses - physiology | Enzyme Inhibitors - pharmacology | Neurotransmitter Agents - metabolism | Rats | Mutation - genetics | Peptides - pharmacology | Sequence Alignment - methods | Two-Hybrid System Techniques | Animals | Vacuolar Proton-Translocating ATPases - chemistry | Liposomes - metabolism | In Vitro Techniques | Vesicle-Associated Membrane Protein 2 - metabolism | SNARE Proteins - metabolism | Protein Binding - physiology | Peptides | Neurons | Analysis | Adenosine triphosphatase | Proteins | Lipids | Binding sites | Protein Subunits | Cell Membrane | Enzyme Inhibitors | Calcium | Neurons and Cognition | Cerebral Cortex | Cellular Biology | Life Sciences | Proteolipids | Excitatory Postsynaptic Potentials | Subcellular Processes | SNARE Proteins | Vacuolar Proton-Translocating ATPases | Vesicle-Associated Membrane Protein 2 | Enzyme-Linked Immunosorbent Assay | Macrolides | Biochemistry, Molecular Biology | Neurotransmitter Agents | Sequence Alignment | Synaptic Vesicles | Protein Binding | Mutation | Liposomes | Synapses
Journal Article
Science, ISSN 0036-8075, 3/2012, Volume 335, Issue 6074, pp. 1355 - 1359
Journal Article
PLoS ONE, ISSN 1932-6203, 08/2011, Volume 6, Issue 8, p. e23989
Toll-like receptors (TLRs) activate a potent immunostimulatory response. There is clear evidence that overactivation of TLRs leads to infectious and... 
STRUCTURAL BASIS | CRYSTAL-STRUCTURE | PROTEIN-DOCKING | MULTIDISCIPLINARY SCIENCES | ENDOTOXIN TOLERANCE | TIR-DOMAIN | INTERLEUKIN-1 RECEPTOR | IL-1 RECEPTOR | MYD88 ADAPTER-LIKE | QUALITY ASSESSMENT | INNATE IMMUNITY | Interleukin-1 Receptor-Like 1 Protein | Humans | Protein Multimerization | Proteolipids - metabolism | Molecular Sequence Data | Myeloid Differentiation Factor 88 - chemistry | Myelin and Lymphocyte-Associated Proteolipid Proteins | Protein Structure, Quaternary | Membrane Transport Proteins - metabolism | Receptors, Cell Surface - chemistry | Protein Stability | Protein Structure, Tertiary | Toll-Like Receptor 6 - metabolism | Amino Acid Sequence | Toll-Like Receptor 6 - chemistry | Signal Transduction | Computational Biology | Receptors, Cell Surface - metabolism | Toll-Like Receptor 4 - chemistry | Toll-Like Receptor 2 - metabolism | Toll-Like Receptor 4 - metabolism | Molecular Dynamics Simulation | Membrane Transport Proteins - chemistry | Myelin Proteins - chemistry | Sequence Alignment | Myelin Proteins - metabolism | Myeloid Differentiation Factor 88 - metabolism | Toll-Like Receptor 2 - chemistry | Proteolipids - chemistry | Molecular dynamics | Medicine, Experimental | Medical research | Structure | Analysis | Crystals | Nuclear magnetic resonance--NMR | Genes | Science | Homology | Innate immunity | Interleukin 1 receptors | Kinases | Immunity | Inflammatory diseases | Molecular docking | Proteins | Signal transduction | Receptors | Pathways | Hydrogen bonds | Rodents | Interleukin 1 | Toll-like receptors | Trends | Inhibition | Crystal structure | Immune system | Immunostimulation | Cytokines | Computer simulation | Adapters | TLR4 protein | Signaling | Molecular modelling | TLR1 protein | TLR2 protein | MyD88 protein | Ligands | In vivo methods and tests | Regulation | Mutation | Three dimensional models | Nuclear magnetic resonance | NMR
Journal Article
Journal Article