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Cancer research (Chicago, Ill.), ISSN 1538-7445, 2017, Volume 77, Issue 21, pp. 5963 - 5976
Journal Article
FEBS Letters, ISSN 0014-5793, 2010, Volume 584, Issue 9, pp. 1887 - 1894
The plasma membrane (PM) is a major resource for production of bioactive lipids and contains a large proportion of the cellular sphingomyelin (SM) content.... 
Sphingolipid | Sphingomyelin synthase | Sphingomyelinase | Cell signaling | Plasma membrane | L-SMase | low density lipoprotein | bSMase | PLC | sphingosine kinase | bacterial sphingomyelinase | LDL | phosphatidylcholine | phospholipase C | plasma membrane | SMase | lysosomal acid sphingomyelinase | neutral sphingomyelinase | sphingomyelinase synthase 1 | sphingomyelin synthase 2 | sphingomyelinase | sphingomyelin | S-SMase | secretory sphingomyelinase | N-SMase | SMS1 | SMS2 | BETA-TOXIN | OXIDATIVE STRESS | BIOCHEMISTRY & MOLECULAR BIOLOGY | NECROSIS-FACTOR-ALPHA | ELEVATED SPHINGOMYELINASE | SECRETORY SPHINGOMYELINASE | CELL-DEATH | CELL BIOLOGY | LYSOSOMAL SPHINGOMYELINASE | BIOPHYSICS | NEUTRAL SPHINGOMYELINASE-2 | STAPHYLOCOCCUS-AUREUS | ACID SPHINGOMYELINASE | Hemolysis - drug effects | Bacteria - metabolism | Sphingomyelins - metabolism | Sphingolipids - pharmacology | Humans | Sphingolipids - metabolism | Sphingolipids - physiology | Inflammation - metabolism | Animals | Cell Death - physiology | Models, Biological | Sphingomyelin Phosphodiesterase - metabolism | Bacteria - enzymology | Biological Transport - drug effects | Biological Transport - physiology | Cell Membrane - metabolism | Cell Death - drug effects | Sphingomyelin Phosphodiesterase - secretion | Hemolysis - physiology | sphingomyelin synthase | sphingolipids
Journal Article
International journal of molecular sciences, ISSN 1422-0067, 2019, Volume 20, Issue 18, p. 4375
Journal Article
Journal Article
Journal Article
Journal of Lipid Research, ISSN 0022-2275, 04/2015, Volume 56, Issue 4, pp. 821 - 835
Besides bulk amounts of SM, mammalian cells produce small quantities of the SM analog ceramide phosphoethanolamine (CPE). Little is known about the biological... 
Enzyme inactivation | Sphingomyelin synthase-related protein | Sterile α motif domain-containing protein 8 | Brain lipids | Transgenic mice | Genetics | Sphingomyelin synthase | Sphingolipids | Mass spectrometry | RAT-LIVER | brain lipids | CELLS | APOPTOSIS | HOMEOSTASIS | sphingolipids | BIOCHEMISTRY & MOLECULAR BIOLOGY | sterile alpha motif domain-containing protein 8 | PROTEIN SMSR | sphingomyelin synthase | genetics | SMS2 DEFICIENCY | PLASMA | sphingomyelin synthase-related protein | transgenic mice | mass spectrometry | enzyme inactivation | MEMBRANE SPHINGOMYELIN | EXPRESSION | SPHINGOMYELIN SYNTHASE 2 | Liver - enzymology | Phosphatidylethanolamine N-Methyltransferase - metabolism | Transferases (Other Substituted Phosphate Groups) - genetics | Brain - enzymology | Male | Brain - metabolism | Transferases (Other Substituted Phosphate Groups) - metabolism | Gene Deletion | Transferases (Other Substituted Phosphate Groups) - deficiency | Brain - cytology | Catalytic Domain | Biocatalysis | Sphingomyelins - metabolism | Cell Survival | Liver - metabolism | Mice, Inbred C57BL | Exons - genetics | Organ Specificity | Protein Transport | Gene Expression Regulation, Enzymologic | Point Mutation | Animals | Liver - cytology | Mice | Sphingomyelins - biosynthesis | Enzyme Activation | Transferases (Other Substituted Phosphate Groups) - chemistry | sterile α motif domain-containing protein 8
Journal Article
PLoS ONE, ISSN 1932-6203, 09/2013, Volume 8, Issue 9, p. e74244
The cellular form of the prion protein (PrPC) is a normal constituent of neuronal cell membranes. The protein misfolding causes rare neurodegenerative... 
CHOLESTEROL | MULTIDISCIPLINARY SCIENCES | NEURONS | SURFACE | DEPLETION | MICE | ACID SPHINGOMYELINASE | EXPRESSION | CONTRIBUTES | Neurons - pathology | Sphingomyelin Phosphodiesterase - genetics | Synaptosomes - drug effects | Membrane Microdomains - metabolism | Male | Synaptosomes - metabolism | PrPSc Proteins - chemistry | Cholesterol - chemistry | PrPSc Proteins - metabolism | Neurons - metabolism | Neurons - drug effects | Fumonisins - pharmacology | Sphingomyelins - metabolism | Mice, Inbred C57BL | Membrane Microdomains - chemistry | Hippocampus - pathology | Scrapie - metabolism | Cholesterol - metabolism | Synaptosomes - chemistry | Protein Folding | Aging - pathology | Mice, Knockout | Sphingomyelin Phosphodiesterase - deficiency | Hippocampus - metabolism | Animals | Membrane Microdomains - drug effects | Scrapie - pathology | Sphingomyelins - chemistry | Mice | Octoxynol - pharmacology | Primary Cell Culture | Aging - metabolism | Brain | Medical research | Nervous system diseases | Proteases | Neurons | Prions | Medicine, Experimental | Bovine spongiform encephalopathy | Membranes | Neurosciences | Scrapie | Disease | Laboratories | Rafts | Homeostasis | Lipids | Lipid rafts | Biology | Experiments | Accumulation | Proteins | Neurodegeneration | Protein folding | Aging | Genetics | Physiology | Synaptosomes | Prion protein | Translocation | Neurodegenerative diseases | Attention | Transmissible spongiform encephalopathy | Cell membranes | Cholesterol | Sphingomyelin phosphodiesterase | Diseases | Neurological diseases | Fumonisin B1 | Sphingomyelin | Hippocampus
Journal Article
Molecular Therapy, ISSN 1525-0016, 07/2017, Volume 25, Issue 7, pp. 1686 - 1696
Acid sphingomyelinase deficiency in type B Niemann-Pick disease leads to lysosomal sphingomyelin storage, principally affecting lungs, liver, and spleen.... 
acid sphingomyelinase deficiency | enzyme replacement therapy | type B Niemann-Pick disease | ICAM-1 targeting | polymer nanocarriers | pulmonary effects | MEDICINE, RESEARCH & EXPERIMENTAL | INTERCELLULAR-ADHESION MOLECULE-1 | LYSOSOMAL STORAGE DISORDERS | CARRIERS | DEFICIENCY | THERAPEUTIC ENZYMES | BIOTECHNOLOGY & APPLIED MICROBIOLOGY | MEDIATED ENDOCYTOSIS | IN-VIVO | GENETICS & HEREDITY | INTRACELLULAR DELIVERY | POLYMER NANOCARRIERS | OLIPUDASE ALPHA | Liver - pathology | Liver - enzymology | Nanoparticles - chemistry | Humans | Niemann-Pick Disease, Type B - pathology | Spleen - drug effects | Niemann-Pick Disease, Type B - genetics | Molecular Targeted Therapy | Polystyrenes - chemistry | Drug Carriers | Lung - enzymology | Endocytosis | Biological Transport | Liver - drug effects | Spleen - enzymology | Drug Compounding | Polyglycolic Acid - metabolism | Spleen - pathology | Antibodies, Monoclonal - chemistry | Lung - pathology | Lactic Acid - chemistry | Sphingomyelin Phosphodiesterase - chemistry | Sphingomyelins - metabolism | Niemann-Pick Disease, Type B - enzymology | Polystyrenes - metabolism | Lactic Acid - metabolism | Mice, Inbred C57BL | Sphingomyelin Phosphodiesterase - pharmacology | Sphingomyelin Phosphodiesterase - deficiency | Intercellular Adhesion Molecule-1 - metabolism | Animals | Intercellular Adhesion Molecule-1 - genetics | Lung - drug effects | Polyglycolic Acid - chemistry | Mice | Nanoparticles - administration & dosage | Antibodies, Monoclonal - metabolism | Niemann-Pick Disease, Type B - therapy | Spleen | Niemann-Pick disease | Enzymes | Intercellular adhesion molecule 1 | Liver | Lung diseases | Clinical trials | Inflammation | Polystyrene | Macrophages | Experiments | Cell adhesion & migration | Endothelium | Sphingomyelin phosphodiesterase | Enzymatic activity | Lungs | Autopsy | Glycolic acid | Sphingomyelin | Original
Journal Article
Journal Article