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The New England journal of medicine, ISSN 1533-4406, 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 | Peripheral myelin protein 22 | Localization | Deoxyribonucleic acid--DNA | Kidneys | Schwann cells | Polymerization | Guanosine triphosphatases | Myelination | Genotyping | Biopsy | Glomerulus | Cytoskeleton | Genetic testing | Cytoplasm | 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
Journal Article
Neuron (Cambridge, Mass.), ISSN 0896-6273, 2010, Volume 66, Issue 5, pp. 663 - 670
Journal Article
Journal Article
The Journal of immunology (1950), ISSN 1550-6606, 2009, Volume 183, Issue 6, pp. 4067 - 4076
Journal Article
The Journal of cell biology, ISSN 0021-9525, 1/2006, Volume 172, Issue 3, pp. 469 - 478
The central nervous system (CNS) of terrestrial vertebrates underwent a prominent molecular change when a tetraspan membrane protein, myelin proteo-lipid... 
Axons | Proteolipids | Myelin | Neurons | Central nervous system | Nerves | Periodicity | Schwann cells | Optics | Mice | LOCALIZATION | PROTEOLIPID PROTEIN GENE | MULTIPLE-SCLEROSIS | CNS MYELIN | MAJOR STRUCTURAL PROTEIN | AXONAL-TRANSPORT | SCHWANN-CELLS | RAT-BRAIN | MESSENGER-RNA LEVELS | DEGENERATION | CELL BIOLOGY | Oligodendroglia - metabolism | Central Nervous System - metabolism | Spinal Cord - metabolism | Gene Expression - genetics | Central Nervous System - pathology | Promoter Regions, Genetic - genetics | Myelin Sheath - metabolism | Myelin Basic Protein - genetics | Exercise Test | Spinal Cord - pathology | X-Ray Diffraction | Amyloid beta-Protein Precursor - metabolism | Myelin Proteolipid Protein - metabolism | Sodium Channels - metabolism | Cell Adhesion Molecules, Neuronal - metabolism | Optic Nerve - chemistry | Phosphoric Diester Hydrolases - metabolism | Myelin Basic Protein - metabolism | Myelin Sheath - pathology | Axons - metabolism | Receptors, Cell Surface - metabolism | Mice, Transgenic | Longevity - genetics | Microscopy, Electron | Mice, Knockout | Motor Activity - genetics | 2',3'-Cyclic Nucleotide 3'-Phosphodiesterase | Animals | Myelin Proteolipid Protein - genetics | Myelin-Associated Glycoprotein | Axons - pathology | Survival Analysis | Myelin P0 Protein - genetics | Myelin Sheath - ultrastructure | Central Nervous System - physiopathology | Myelin P0 Protein - metabolism | Evolution, Molecular | Vertebrates | Genetic aspects | Research | Myelin proteins
Journal Article
Brain Research, ISSN 0006-8993, 2015, Volume 1641, Issue Pt A, pp. 43 - 63
Journal Article
The Journal of cell biology, ISSN 1540-8140, 2004, Volume 166, Issue 5, pp. 731 - 742
The myelin and lymphocyte protein (MAL) is a tetraspan raft-associated proteolipid predominantly expressed by oligodendrocytes and Schwann cells. We show that... 
Axons | Myelin | Rafts | Nerves | Central nervous system | Lipids | Mice | Cell membranes | Myelin sheath | P branes | Node of Ranvier | Glycolipid-enriched microdomains | Axon-glia interaction | Myelin proteolipids | CELL-ADHESION MOLECULE | OPTIC-NERVE | MICE DEFICIENT | UNMYELINATED AXONS | myelin proteolipids | node of Ranvier | MYELIN-ASSOCIATED GLYCOPROTEIN | OLIGODENDROCYTES | CELL BIOLOGY | glycolipid-enriched microdomains | DARBY CANINE KIDNEY | APICAL TRANSPORT | CONTACTIN | axon-glia interaction | DOMAINS | Oligodendroglia - metabolism | Optic Nerve - pathology | Potassium Channels, Voltage-Gated | Central Nervous System - ultrastructure | Central Nervous System - metabolism | Membrane Microdomains - metabolism | Proteolipids - metabolism | Myelin-Associated Glycoprotein - metabolism | Sciatic Nerve - ultrastructure | Nerve Growth Factors - metabolism | Ranvier's Nodes - metabolism | Membrane Microdomains - ultrastructure | Oligodendroglia - ultrastructure | Ranvier's Nodes - ultrastructure | Myelin Sheath - metabolism | Potassium Channels - metabolism | Sciatic Nerve - metabolism | Membrane Transport Proteins - genetics | Myelin and Lymphocyte-Associated Proteolipid Proteins | Axons - ultrastructure | Membrane Transport Proteins - metabolism | Proteolipids - genetics | Myelin Basic Protein - metabolism | Myelin Sheath - pathology | Neural Conduction - genetics | Sciatic Nerve - pathology | Axons - metabolism | Cell Communication - genetics | Kv1.2 Potassium Channel | Optic Nerve - ultrastructure | Microscopy, Electron | Cell Adhesion Molecules - metabolism | Myelin Proteins - genetics | Down-Regulation - genetics | Protein Transport - genetics | Mice, Knockout | Potassium Channels - genetics | Animals | Axons - pathology | Myelin Sheath - ultrastructure | Ranvier's Nodes - pathology | Myelin Proteins - metabolism | Optic Nerve - metabolism | Physiological aspects | Research | Myelin proteins | Cytology | axon–glia interaction; myelin proteolipids; glycolipid-enriched microdomains; node of Ranvier
Journal Article