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1. Full Text Sphingomyelin phosphodiesterase acid-like 3A (SMPDL3A) is a novel nucleotide phosphodiesterase regulated by cholesterol in human macrophages
by Traini, Mathew and Quinn, Carmel M and Sandoval, Cecilia and Johansson, Erik and Schroder, Kate and Kockx, Maaike and Meikle, Peter J and Jessup, Wendy and Kritharides, Leonard
The Journal of biological chemistry, ISSN 0021-9258, 11/2014, Volume 289, Issue 47, pp. 32895 - 32913
Life Sciences & Biomedicine | Biochemistry & Molecular Biology | Science & Technology | Sphingomyelin Phosphodiesterase - genetics | Cricetulus | Oligonucleotide Array Sequence Analysis | Humans | Orphan Nuclear Receptors - metabolism | Foam Cells - drug effects | RNA Interference | Liver X Receptors | Sphingomyelin Phosphodiesterase - metabolism | HEK293 Cells | Nucleotides - pharmacology | Foam Cells - metabolism | CHO Cells | Cricetinae | Phosphoric Diester Hydrolases - metabolism | Cells, Cultured | Phosphoric Diester Hydrolases - genetics | Transcriptome - drug effects | Transcriptome - genetics | Cholesterol - metabolism | Nucleotides - metabolism | Reverse Transcriptase Polymerase Chain Reaction | Blotting, Western | Cyclic AMP - pharmacology | Microscopy, Confocal | Macrophages - metabolism | Animals | Cell Line, Tumor | Cholesterol - pharmacology | Golgi Apparatus - metabolism | Macrophages - drug effects | Sphingomyelin Phosphodiesterase - blood | Index Medicus | Enzymology | Metalloenzyme | Phosphodiesterases | Cholesterol | Atherosclerosis | Macrophage
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2. Full Text The structure and catalytic mechanism of human sphingomyelin phosphodiesterase like 3a – an acid sphingomyelinase homologue with a novel nucleotide hydrolase activity
by Lim, Sing Mei and Yeung, Kit and Trésaugues, Lionel and Ling, Teo Hsiang and Nordlund, Pär
The FEBS journal, ISSN 1742-464X, 03/2016, Volume 283, Issue 6, pp. 1107 - 1123
calcineurin‐like phosphodiesterase | binuclear metallophosphodiesterase | acid sphingomyelinase like | Niemann–Pick disease | nucleotide hydrolase | Niemann-Pick disease | Nucleotide hydrolase | Binuclear metallophosphodiesterase | Acid sphingomyelinase like | Calcineurin-like phosphodiesterase | calcineurin-like phosphodiesterase | Life Sciences & Biomedicine | Biochemistry & Molecular Biology | Science & Technology | Cytidine Monophosphate - metabolism | Sphingomyelin Phosphodiesterase - genetics | Zinc - metabolism | Humans | Molecular Sequence Data | Substrate Specificity | Crystallography, X-Ray | Phylogeny | Disulfides - chemistry | Sphingomyelin Phosphodiesterase - metabolism | Niemann-Pick Diseases - enzymology | Conserved Sequence | Niemann-Pick Diseases - genetics | Amino Acid Sequence | Catalytic Domain | Sphingomyelin Phosphodiesterase - chemistry | Mutant Proteins - genetics | Models, Molecular | Mutant Proteins - metabolism | Glycosylation | Static Electricity | Sequence Homology, Amino Acid | Point Mutation | Mutant Proteins - chemistry | Protein Conformation | Enzymes | Hydrolases | Phospholipids | Nucleotides | Analysis | Lipids | Genetic disorders | Molecular biology | Index Medicus | Medicin och hälsovetenskap
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3. Full Text Phosphodiesterase 5 inhibitor acts as a potent agent sensitizing acute myeloid leukemia cells to 67-kDa laminin receptor-dependent apoptosis
by Kumazoe, Motofumi and Kim, Yoonhee and Bae, Jaehoon and Takai, Mika and Murata, Motoki and Suemasu, Yumi and Sugihara, Kaori and Yamashita, Shuya and Tsukamoto, Shuntaro and Huang, Yuhui and Nakahara, Kanami and Yamada, Koji and Tachibana, Hirofumi
FEBS letters, ISSN 0014-5793, 09/2013, Volume 587, Issue 18, pp. 3052 - 3057
Laminin receptor | cGMP | Epigallocatechin-3-O-gallate | Acute myeloid leukemia | Acid sphingomyelinase | Apoptosis | AML | acid sphingomyelinase | EGCG | (−)-epigallocatechin-3-O-gallate | PDE | acute myeloid leukemia | 67-kDa laminin receptor | ASM | phosphodiesterase | 67LR | Biochemistry & Molecular Biology | Biophysics | Life Sciences & Biomedicine | Science & Technology | Cell Biology | Receptors, Laminin - metabolism | Sphingomyelin Phosphodiesterase - genetics | Receptors, Laminin - agonists | Apoptosis - drug effects | Humans | Leukemia, Myeloid, Acute - metabolism | Receptors, Laminin - genetics | Sphingomyelin Phosphodiesterase - metabolism | Oncogene Protein v-akt - genetics | Leukemia, Myeloid, Acute - drug therapy | Nitric Oxide Synthase Type III - metabolism | Catechin - pharmacology | Oncogene Protein v-akt - metabolism | Phosphodiesterase 5 Inhibitors - pharmacology | Cyclic Nucleotide Phosphodiesterases, Type 5 - metabolism | Signal Transduction | Leukemia, Myeloid, Acute - pathology | Gene Expression Regulation, Leukemic - drug effects | Enzyme Activation - drug effects | Nitric Oxide Synthase Type III - genetics | Drug Synergism | Cyclic GMP - metabolism | Cyclic Nucleotide Phosphodiesterases, Type 5 - genetics | HL-60 Cells | Catechin - analogs & derivatives | Primary Cell Culture | Leukemia, Myeloid, Acute - genetics | Antimitotic agents | Catechin | Laminin | Antineoplastic agents | Index Medicus
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4. Full Text The LC3-conjugation machinery specifies the loading of RNA-binding proteins into extracellular vesicles
by Leidal, Andrew M and Huang, Hector H and Marsh, Timothy and Solvik, Tina and Zhang, Dachuan and Ye, Jordan and Kai, FuiBoon and Goldsmith, Juliet and Liu, Jennifer Y and Huang, Yu-Hsin and Monkkonen, Teresa and Vlahakis, Ariadne and Huang, Eric J and Goodarzi, Hani and Yu, Li and Wiita, Arun P and Debnath, Jayanta
Nature cell biology, ISSN 1465-7392, 02/2020, Volume 22, Issue 2, pp. 187 - 199
Life Sciences & Biomedicine | Science & Technology | Cell Biology | Autophagosomes - chemistry | RNA-Binding Proteins - genetics | Sphingomyelin Phosphodiesterase - genetics | Receptors, Estrogen - metabolism | Extracellular Vesicles - chemistry | Lysosomes - chemistry | Microtubule-Associated Proteins - genetics | Microtubule-Associated Proteins - metabolism | Humans | Adaptor Proteins, Vesicular Transport - deficiency | Adaptor Proteins, Vesicular Transport - genetics | Gene Expression Profiling | Intracellular Signaling Peptides and Proteins - metabolism | Extracellular Vesicles - metabolism | Lysosomes - metabolism | Biological Transport | Sphingomyelin Phosphodiesterase - metabolism | HEK293 Cells | RNA, Small Untranslated - genetics | Autophagy - genetics | Proteomics - methods | Autophagy-Related Proteins - genetics | Intracellular Signaling Peptides and Proteins - genetics | RNA, Small Untranslated - metabolism | Autophagy-Related Proteins - deficiency | Biotinylation | Receptors, Estrogen - genetics | Matrix Attachment Region Binding Proteins - metabolism | Gene Expression Regulation | Nuclear Matrix-Associated Proteins - metabolism | Autophagosomes - metabolism | Autophagy-Related Protein 7 - genetics | Heterogeneous-Nuclear Ribonucleoprotein K - genetics | RNA-Binding Proteins - classification | Heterogeneous-Nuclear Ribonucleoprotein K - metabolism | Animals | Nuclear Matrix-Associated Proteins - genetics | Matrix Attachment Region Binding Proteins - genetics | RAW 264.7 Cells | Mice | RNA-Binding Proteins - metabolism | Autophagy-Related Protein 7 - deficiency | RNA | Binding proteins | Protein binding | Binding | Cargo | Profiling | Target recognition | Secretion | Secretome | Ribonucleic acid--RNA | Autophagy | Machinery | Sphingomyelin phosphodiesterase | Proteins | Ribonucleoprotein K | Vesicles | RNA-binding protein | Proteomics | Packaging | Conjugation | Phagocytosis | Index Medicus
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5. Full Text Sphingomyelinase‐like phosphodiesterase 3b mediates radiation‐induced damage of renal podocytes
by Ahmad, Anis and Mitrofanova, Alla and Bielawski, Jacek and Yang, Yidong and Marples, Brian and Fornoni, Alessia and Zeidan, Youssef H
The FASEB journal, ISSN 0892-6638, 02/2017, Volume 31, Issue 2, pp. 771 - 780
lipids | ceramide | radioprotection | cancer | Ceramide | Lipids | Radioprotection | Cancer | Biochemistry & Molecular Biology | Biology | Life Sciences & Biomedicine - Other Topics | Life Sciences & Biomedicine | Science & Technology | Cell Biology | Sphingomyelin Phosphodiesterase - genetics | Cyclic Nucleotide Phosphodiesterases, Type 3 - genetics | Ceramides - metabolism | Podocytes - metabolism | Down-Regulation | Humans | Mice, Inbred C57BL | Immunologic Factors - administration & dosage | Gene Expression Regulation, Enzymologic | Rituximab - administration & dosage | Rituximab - pharmacology | Animals | Podocytes - radiation effects | Sphingomyelin Phosphodiesterase - metabolism | Mice | Cyclic Nucleotide Phosphodiesterases, Type 3 - metabolism | Immunologic Factors - pharmacology | Phosphates | Change detection | Pathogenesis | Radiation | Sphingolipids | Remodeling | Caspase-3 | Cytosol | Sphingosine 1-phosphate | Actin | Radiation injuries | Pretreatment | Phosphodiesterase | Radiation effects | Kidneys | Ezrin | Rituximab | Caspase | Pseudopodia | Radiation dosage | Sphingomyelin phosphodiesterase | Molecular modelling | Nephropathy | CD20 antigen | Irradiation | Cytoskeleton | Radiation damage | Proteinuria | Index Medicus | Research
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6. Full Text A deletion in the gene encoding sphingomyelin phosphodiesterase 3 ( Smpd3 ) results in osteogenesis and dentinogenesis imperfecta in the mouse
by Goldberg, Michel and Poirier, Christophe and Auge, Nathalie and Guénet, Jean-Louis and Opsahl, Sibylle and Aubin, Isabelle and Negre-Salvayre, Anne and Adams, Carolyn P and Bishop, Colin E and Septier, Dominique and Salvayre, Robert
Nature genetics, ISSN 1061-4036, 08/2005, Volume 37, Issue 8, pp. 803 - 805
Life Sciences & Biomedicine | Genetics & Heredity | Science & Technology | Animals | Sphingomyelin Phosphodiesterase | Mice, Mutant Strains | Gene Deletion | Osteogenesis Imperfecta - genetics | Dentinogenesis Imperfecta - enzymology | Mice | Mutation | Osteogenesis Imperfecta - enzymology | Dentinogenesis Imperfecta - genetics | Complications and side effects | Gene mutations | Osteogenesis imperfecta | Physiological aspects | Genetic aspects | Diagnosis | Research | Phosphodiesterases | Risk factors | Index Medicus
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7. Full Text Crystal structure of the acid sphingomyelinase-like phosphodiesterase SMPDL3B provides insights into determinants of substrate specificity
by Gorelik, Alexei and Heinz, Leonhard X and Illes, Katalin and Superti-Furga, Giulio and Nagar, Bhushan
The Journal of biological chemistry, ISSN 0021-9258, 11/2016, Volume 291, Issue 46, pp. 24054 - 24064
Life Sciences & Biomedicine | Biochemistry & Molecular Biology | Science & Technology | Adenosine Diphosphate - genetics | Choline - metabolism | Cyclic Nucleotide Phosphodiesterases, Type 3 - chemistry | Cyclic Nucleotide Phosphodiesterases, Type 3 - genetics | Sphingomyelins - metabolism | Protein Structure, Secondary | Substrate Specificity | Adenosine Triphosphate - genetics | Crystallography, X-Ray | Adenosine Diphosphate - chemistry | Choline - chemistry | Spodoptera | Sphingomyelins - genetics | Sf9 Cells | Animals | Adenosine Triphosphate - metabolism | Protein Domains | Sphingomyelins - chemistry | Mice | Adenosine Diphosphate - metabolism | Cyclic Nucleotide Phosphodiesterases, Type 3 - metabolism | Adenosine Triphosphate - chemistry | Choline - genetics | Index Medicus | Protein Structure and Folding | lipid metabolism | substrate specificity | crystal structure | sphingomyelinase | cell surface enzyme | SMPDL3B
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8. Full Text Characterization of Sphingomyelin Phosphodiesterase Expression in Bumblebee (Bombus lantschouensis)
by Han, Lei and Ding, Guiling and Liu, Yanjie and Huang, Jiaxing and Wu, Jie
Journal of insect science (Tucson, Ariz.), ISSN 1536-2442, 09/2018, Volume 18, Issue 5
Life Sciences & Biomedicine | Entomology | Science & Technology | Amino Acid Sequence | Sphingomyelin Phosphodiesterase - genetics | Sphingomyelin Phosphodiesterase - chemistry | Molecular Conformation | Insect Proteins - genetics | Gene Expression Profiling | Phylogeny | Bees | Reproduction | Animals | Gene Expression Regulation, Developmental | Insect Proteins - chemistry | Sphingomyelin Phosphodiesterase - metabolism | Insect Proteins - metabolism | Physiological aspects | Enzymes | Bumblebees | Gene expression | Genetic regulation | Analysis | Index Medicus
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9. Full Text Analysis of the sphingomyelin phosphodiesterase 1 gene (SMPD1) in Turkish Niemann–Pick disease patients: Mutation profile and description of a novel mutation
by Aykut, A and Karaca, E and Onay, H and Kalkan Ucar, S and Coker, M and Cogulu, O and Ozkinay, F
Gene, ISSN 0378-1119, 09/2013, Volume 526, Issue 2, pp. 484 - 486
SMPD1 gene | Turkish population | Niemann–Pick disease | Novel mutation | Niemann-Pick disease | Life Sciences & Biomedicine | Genetics & Heredity | Science & Technology | Sphingomyelin Phosphodiesterase - genetics | Genetic Association Studies | Exons | Humans | Child, Preschool | Infant | Male | Codon | Turkey | Female | Niemann-Pick Diseases - diagnosis | Mutation | Child | Niemann-Pick Diseases - genetics | Infant, Newborn | Amino Acid Substitution | Pick's disease | Analysis | Genes | Genetic research | Phospholipids | Genetic aspects | Index Medicus
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10. Full Text Oncogenic ras-driven cancer cell vesiculation leads to emission of double-stranded DNA capable of interacting with target cells
by Lee, Tae Hoon and Chennakrishnaiah, Shilpa and Audemard, Eric and Montermini, Laura and Meehan, Brian and Rak, Janusz
Biochemical and biophysical research communications, ISSN 0006-291X, 08/2014, Volume 451, Issue 2, pp. 295 - 301
Chromatin | Extracellular vesicle | Sphingomyelinase | Ras | DNA | Oncogene | Biochemistry & Molecular Biology | Biophysics | Life Sciences & Biomedicine | Science & Technology | Exosomes - metabolism | Chromatin - metabolism | Sphingomyelin Phosphodiesterase - genetics | Intestinal Mucosa - metabolism | DNA, Neoplasm - metabolism | Proto-Oncogene Proteins p21(ras) - genetics | Humans | Exosomes - genetics | Cell Transformation, Neoplastic - genetics | Sphingomyelin Phosphodiesterase - metabolism | Exosomes - ultrastructure | Cell Line | Microscopy, Electron, Transmission | Antigens, Polyomavirus Transforming - genetics | Intestinal Mucosa - ultrastructure | Rats | DNA - metabolism | Cell Transformation, Neoplastic - metabolism | Sphingomyelin Phosphodiesterase - deficiency | DNA - genetics | Animals | Cell Line, Tumor | Mice | DNA, Neoplasm - genetics | Mutation | Genes, ras | Genome, Human | Chromatin - genetics | Genetic aspects | Cancer | Index Medicus | HUMAN POPULATIONS | ONCOGENES | CHROMATIN | NEOPLASMS | RETENTION | EV RANGE | RATS | CELL PROLIFERATION | TUMOR CELLS | 60 APPLIED LIFE SCIENCES | FIBROBLASTS | MUTANTS | BIOLOGICAL MARKERS | TRANSIENTS | UPTAKE | MICE | BRAIN
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