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1. 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
FEBS Journal, ISSN 1742-464X, 03/2016, Volume 283, Issue 6, pp. 1107 - 1123
Novel structure of sphingomyelinase phosphodiesterase like 3a ( SMPDL 3a) revealed a conserved calcineurin like phosphodiesterase domain with a binuclear... 
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 | 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 | HYPOTHETICAL PROTEIN | ARABIDOPSIS-THALIANA | CRYSTAL-STRUCTURE | POLYKETIDE SYNTHASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | TETRACENOMYCIN-F2 CYCLASE | PLANT POLYKETIDES | ALDOL CONDENSATION | AROMATIC POLYKETIDES | FUNCTIONAL-ANALYSIS | STREPTOMYCES-GLAUCESCENS | Enzymes | Hydrolases | Phospholipids | Nucleotides | Analysis | Lipids | Genetic disorders | Molecular biology | Index Medicus
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2. 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
Journal of Biological Chemistry, ISSN 0021-9258, 11/2014, Volume 289, Issue 47, pp. 32895 - 32913
Cholesterol-loaded foam cell macrophages are prominent in atherosclerotic lesions and play complex roles in both inflammatory signaling and lipid metabolism,... 
ATHEROSCLEROTIC LESIONS | GENE | BIOCHEMISTRY & MOLECULAR BIOLOGY | CD39 | RECEPTOR | FUNCTIONAL-CHARACTERIZATION | DISULFIDE BOND | ECTO-APYRASE | SECRETION | EXPRESSION | APOLIPOPROTEIN-E | 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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3. 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 (Online), ISSN 1536-2442, 09/2018, Volume 18, Issue 5
Sphingomyelin phosphodiesterase (SMPD) is a hydrolase that plays a major role in metabolic reactions involving sphingomyelin. Here, we describe an analysis of... 
NORTH CHINA | ACTIVATOR PROTEINS | ENTOMOLOGY | Sphingomyelin phosphodiesterase | MODELS | NEUTRAL SPHINGOMYELINASE | PURIFICATION | DISEASE | GENE-EXPRESSION | ALKALINE SPHINGOMYELINASE | bumblebee | Bombus lantschouensis | cloning | gene expression | BRAIN | 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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4. 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
The mouse mutation fragilitas ossium (fro) leads to a syndrome of severe osteogenesis and dentinogenesis imperfecta with no detectable collagen defect.... 
FORM | FRO/FRO | MINERALIZATION | GENETICS & HEREDITY | BRITTLE BONE-DISEASE | CERAMIDE | FRAGILITAS-OSSIUM | 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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5. Full Text Sphingomyelinase-Like Phosphodiesterase 3b Expression Levels Determine Podocyte Injury Phenotypes in Glomerular Disease
by Yoo, TH and Pedigo, CE and Guzman, J and Correa-Medina, M and Wei, CL and Villarreal, R and Mitrofanova, A and Leclercq, F and Faul, C and Li, J and Kretzler, M and Nelson, RG and Lehto, M and Forsblom, C and Groop, PH and Reiser, J and Burke, GW and Fornoni, A and Merscher, S
JOURNAL OF THE AMERICAN SOCIETY OF NEPHROLOGY, ISSN 1046-6673, 01/2015, Volume 26, Issue 1, pp. 133 - 147
Diabetic kidney disease (DKD) is the most common cause of ESRD in the United States. Podocyte injury is an important feature of DKD that is likely to be caused... 
KIDNEY-DISEASE | CELLS | ACTIVATOR | PERMEABILITY | KINASE | SUPAR LEVELS | UROLOGY & NEPHROLOGY | UROKINASE RECEPTOR | HUMAN DIABETIC-NEPHROPATHY | FOCAL SEGMENTAL GLOMERULOSCLEROSIS | TNF RECEPTORS 1 | Oligonucleotide Array Sequence Analysis | Humans | Kidney Glomerulus - injuries | Receptors, Urokinase Plasminogen Activator - blood | Integrins - metabolism | Integrin alphaVbeta3 - metabolism | Sphingomyelin Phosphodiesterase - metabolism | HEK293 Cells | Female | Cyclic Nucleotide Phosphodiesterases, Type 3 - metabolism | Kidney Diseases - metabolism | Mice, Transgenic | Neuropeptides - metabolism | Kidney Glomerulus - pathology | Podocytes - pathology | Gene Expression Regulation, Enzymologic | Podocytes - cytology | Phenotype | Animals | rho GTP-Binding Proteins - metabolism | Mice | Mice, Inbred BALB C | rac1 GTP-Binding Protein - metabolism | Apoptosis | Cell Movement | Index Medicus | FSGS | glomerular disease | proteinuria | diabetic nephropathy | podocyte | Basic Research
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6. Full Text Sphingomyelin phosphodiesterase 1 (SMPD1) mediates the attenuation of myocardial infarction-induced cardiac fibrosis by astaxanthin
by Shi, Yu and Lin, Peng and Wang, Xiaoning and Zou, Guangmei and Li, Kefeng
Biochemical and Biophysical Research Communications, ISSN 0006-291X, 09/2018, Volume 503, Issue 2, pp. 637 - 643
Uncontrolled cardiac fibrosis following myocardial infarction (MI) is a critical pathological change leading to heart failure. Current pharmacotherapies are... 
Myocardial infarction | Cardiac fibrosis | Lipidomics | Astaxanthin | SMPD1 | TGF-BETA | BIOCHEMISTRY & MOLECULAR BIOLOGY | LIVER FIBROSIS | HEART | INHIBITION | BIOPHYSICS | METABOLISM | PATHWAY | ACID SPHINGOMYELINASE | Mice, Inbred C57BL | Male | Myocardium - pathology | Cardiotonic Agents - pharmacology | Myocardial Infarction - metabolism | Xanthophylls - therapeutic use | Cardiotonic Agents - therapeutic use | Animals | Myocardial Infarction - drug therapy | Signal Transduction - drug effects | Fibrinolytic Agents - therapeutic use | Myocardial Infarction - pathology | Myocardium - metabolism | Sphingomyelin Phosphodiesterase - metabolism | Fibrosis | Heart - drug effects | Xanthophylls - pharmacology | Molecular Docking Simulation | Enzymes | Medical colleges | Phospholipids | Transforming growth factors | Heart attack | Antioxidants | Analysis | Collagen | Physiological aspects | Ceramides | Bone morphogenetic proteins | Cardiology | Index Medicus
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7. Full Text Sphingomyelin Phosphodiesterase 3 Enhances Cytodifferentiation of Periodontal Ligament Cells
by Miyauchi, S and Kitagaki, J and Masumoto, R and Imai, A and Kobayashi, K and Nakaya, A and Kawai, S and Fujihara, C and Asano, Y and Yamashita, M and Yanagita, M and Yamada, S and Kitamura, M and Murakami, S
Journal of Dental Research, ISSN 0022-0345, 3/2017, Volume 96, Issue 3, pp. 339 - 346
Sphingomyelin phosphodiesterase 3 (Smpd3), which encodes neutral sphingomyelinase 2 (nSMase2), is a key molecule for skeletal development as well as for the... 
molecular biology | aggressive periodontitis | cell biology | calcification | single nucleotide polymorphism | genome-wide association study | MOUSE | BONE MINERALIZATION | RELEASE | SPHINGOSINE 1-PHOSPHATE | SMPD3 | NEUTRAL SPHINGOMYELINASE | DENTISTRY, ORAL SURGERY & MEDICINE | SPHINGOSINE-1-PHOSPHATE | DISEASE | INHIBITOR | Aggressive Periodontitis - enzymology | Cell Line | Sphingomyelin Phosphodiesterase - genetics | Gene Expression | Genome-Wide Association Study | Collagen Type I - metabolism | Osteocalcin - metabolism | Humans | Japan | Alkaline Phosphatase - metabolism | Cells, Cultured | Immunoblotting | Male | Osteopontin - metabolism | Aggressive Periodontitis - genetics | Periodontal Ligament - cytology | Phenotype | Calcification, Physiologic | Adult | Female | Cell Differentiation | Polymorphism, Single Nucleotide | Sphingomyelin Phosphodiesterase - physiology | Real-Time Polymerase Chain Reaction | Index Medicus | Dentistry
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8. 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
(−)-Epigallocatechin-3- -gallate (EGCG), a polyphenol in green tea, induces apoptosis in acute myeloid leukemia (AML) cells without affecting normal cells. In... 
Laminin receptor | cGMP | Epigallocatechin-3-O-gallate | Acute myeloid leukemia | Acid sphingomyelinase | Apoptosis | AML | Epigallocatechin-3 | acid sphingomyelinase | EGCG | PDE | acute myeloid leukemia | gallate | (−)-epigallocatechin-3 | 67-kDa laminin receptor | ASM | phosphodiesterase | 67LR | TEA POLYPHENOL EGCG | PROTEIN | BIOCHEMISTRY & MOLECULAR BIOLOGY | RAI STAGE 0 | DEATH | CELL BIOLOGY | TRIAL | GREEN TEA | BIOPHYSICS | SPHINGOMYELINASE | CHRONIC LYMPHOCYTIC-LEUKEMIA | PATIENT | 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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9. Full Text Biochemical and Molecular Characterization of a Novel Choline-specific Glycerophosphodiester Phosphodiesterase Belonging to the Nucleotide Pyrophosphatase/Phosphodiesterase Family
by Hideki Sakagami and Junken Aoki and Yumiko Natori and Kiyotaka Nishikawa and Yoshiyuki Kakehi and Yasuhiro Natori and Hiroyuki Arai
Journal of Biological Chemistry, ISSN 0021-9258, 06/2005, Volume 280, Issue 24, pp. 23084 - 23093
Nucleotide pyrophosphatases/phosphodiesterases (NPPs) are ubiquitous membrane-associated or secreted ectoenzymes that release nucleoside 5′-monophosphate... 
LYSOPHOSPHOLIPASE-D | PLASMA | MEMBRANE GLYCOPROTEIN PC-1 | LYSOPHOSPHATIDIC ACID | CELL MOTILITY | INSULIN-RESISTANCE | BIOCHEMISTRY & MOLECULAR BIOLOGY | IDENTIFICATION | CATALYTIC SITE | AUTOTAXIN | EXPRESSION | Immunohistochemistry | Models, Chemical | Humans | Kidney - enzymology | Brain - enzymology | Phosphorylcholine - analogs & derivatives | Phylogeny | RNA, Messenger - metabolism | Tissue Distribution | Glycerylphosphorylcholine - chemistry | Time Factors | Swine | Base Sequence | Cell Membrane - metabolism | Antibodies, Monoclonal - chemistry | Amino Acid Sequence | Fatty Acids - chemistry | Sphingomyelin Phosphodiesterase - chemistry | Recombinant Proteins - chemistry | Type C Phospholipases - chemistry | Reverse Transcriptase Polymerase Chain Reaction | Sequence Analysis, DNA | Blotting, Western | Pyrophosphatases - metabolism | Sphingosine - analogs & derivatives | Models, Biological | Phosphorylcholine - chemistry | Mice | HeLa Cells | Kinetics | Nephrons - metabolism | Sphingosine - chemistry | Cell Movement | Species Specificity | Molecular Sequence Data | Transfection | Sphingomyelin Phosphodiesterase - metabolism | Phospholipids - metabolism | Sphingomyelin Phosphodiesterase - physiology | Protein Structure, Tertiary | Lysophosphatidylcholines - metabolism | Pyrophosphatases - chemistry | Hydrolysis | Sequence Homology, Amino Acid | Phosphoric Diester Hydrolases | Blotting, Northern | Myocardium - enzymology | Animals | Protein Binding | Cations | Lysophosphatidylcholines - chemistry | Microscopy, Fluorescence | Index Medicus
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10. 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
FASEB Journal, ISSN 0892-6638, 02/2017, Volume 31, Issue 2, pp. 771 - 780
The molecular mechanisms responsible for the development of proteinuria and glomerulosclerosis in radiation nephropathy remain largely unknown. Podocytes are... 
Ceramide | Lipids | Radioprotection | Cancer | lipids | CANCER CELLS | BIOCHEMISTRY & MOLECULAR BIOLOGY | SPHINGOLIPIDS | NEPHROPATHY | TRANSPLANTATION | CELL BIOLOGY | ACID CERAMIDASE | ceramide | radioprotection | INHIBITION | PATHWAY | DISEASE | BIOLOGY | RESISTANCE | cancer | EXPRESSION | 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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11. Full Text Urinary excretion of sphingomyelinase phosphodiesterase acid‐like 3b in children with intractable nephrotic syndrome
by Watanabe, Shojiro and Tsugawa, Koji and Tsuruga, Kazushi and Imaizumi, Tadaatsu and Tanaka, Hiroshi
Pediatrics International, ISSN 1328-8067, 10/2017, Volume 59, Issue 10, pp. 1112 - 1115
Rituximab ( RTX ), a specific antibody to human CD 20, has been successfully used to treat intractable nephrotic syndrome ( NS ). Recent studies have suggested... 
sphingomyelinase phosphodiesterase acid‐like 3b | nephrotic syndrome | rituximab | podocyte | sphingomyelinase phosphodiesterase acid-like 3b | PEDIATRICS | Biomarkers - urine | Nephrotic Syndrome - urine | Humans | Child, Preschool | Male | Treatment Outcome | Nephrotic Syndrome - drug therapy | Case-Control Studies | Nephrotic Syndrome - immunology | Rituximab - therapeutic use | Adolescent | Sphingomyelin Phosphodiesterase - urine | Adult | Female | Drug Monitoring | Child | Immunologic Factors - therapeutic use | Nephrotic syndrome | Urine | Excretion | Medical services | Rituximab | Patients | Sphingomyelin phosphodiesterase | Acids | Biopsy | CD20 antigen | Remission | Adults | Children | Immunoreactivity | Phosphodiesterase | Index Medicus
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12. 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
Niemann–Pick disease (NPD) is a lysosomal storage disorder that results from the deficiency of a lysosomal enzyme, acid sphingomyelinase. Niemann–Pick disease... 
SMPD1 gene | Turkish population | Niemann–Pick disease | Novel mutation | Niemann-Pick disease | B PATIENTS | GENETICS & HEREDITY | DISULFIDE BOND | HUMAN ACID SPHINGOMYELINASE | IDENTIFICATION | 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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13. 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
Journal of Biological Chemistry, ISSN 0021-9258, 11/2016, Volume 291, Issue 46, pp. 24054 - 24064
The enzyme acid sphingomyelinase-like phosphodiesterase 3B (SMPDL3B) was shown to act as a negative regulator of innate immune signaling, affecting cellular... 
BIOCHEMISTRY & MOLECULAR BIOLOGY | lipid metabolism | substrate specificity | crystal structure | sphingomyelinase | PHENIX | cell surface enzyme | SMPDL3B | PROTEOMIC ANALYSIS | IDENTIFICATION | PHOSPHATIDYLCHOLINE | 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
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14. Full Text Structural basis for nucleotide hydrolysis by the acid sphingomyelinase-like phosphodiesterase SMPDL3A
by Gorelik, Alexei and Illes, Katalin and Superti-Furga, Giulio and Nagar, Bhushan
Journal of Biological Chemistry, ISSN 0021-9258, 03/2016, Volume 291, Issue 12, pp. 6376 - 6385
Sphingomyelin phosphodiesterase, acid-like 3A (SMPDL3A) is a member of a small family of proteins founded by the well characterized lysosomal enzyme, acid... 
LYSOSOMAL PROTEINS | SYSTEM | MECHANISM | HUMAN MACROPHAGES | BIOCHEMISTRY & MOLECULAR BIOLOGY | nucleoside | enzyme catalysis | INDUCTION | nucleotide metabolism | GENE | DISEASE | crystal structure | sphingomyelinase | CALCINEURIN | PROTEOMIC ANALYSIS | RECEPTORS | zinc | SMPDL3A | Amino Acid Sequence | Cell Line | Catalytic Domain | Biocatalysis | Sphingomyelin Phosphodiesterase - chemistry | Protein Structure, Secondary | Humans | Adenosine Monophosphate - chemistry | Models, Molecular | Molecular Sequence Data | Substrate Specificity | Crystallography, X-Ray | Zinc - chemistry | Hydrolysis | Animals | Protein Binding | Mice | Kinetics | Adenosine Triphosphate - chemistry | Index Medicus | Enzymology
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