ArticleNature communications2016
Human acid sphingomyelinase structures provide insight to molecular basis of Niemann-Pick disease.
Article in Nature communications, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 53 citations in OpenAlex.
- Targeting of Acid Sphingomyelinase, a Lysosomal Membrane Protein, Using Apolipoprotein E3-containing Nanodiscs.The Journal of membrane biology · 2026Article
- The Acid sphingomyelinase/ceramide System in Idiopathic Inflammatory Myopathies: a Potential Treatment Target.Inflammation · 2026Review
- Proteomic Profiling of an Exosome-Enriched Extracellular Vesicle Fraction and Structural Characterization of SMPDL3A in the Carcinogenic Liver FlukeInternational journal of molecular sciences · 2026Article
- A case of acid sphingomyelinase deficiency type B with prominent histiocytes with engulfed nucleated cells and compound heterozygosity.Journal of hematopathology · 2025Article
- Theoretical Study of Sphingomyelinases fromPathogens (Basel, Switzerland) · 2025Article
- Acidic sphingomyelinase interactions with lysosomal membranes and cation amphiphilic drugs: A molecular dynamics investigation.Computational and structural biotechnology journal · 2024Article
- Human Saposin B Ligand Binding and Presentation to α-Galactosidase A.bioRxiv : the preprint server for biology · 2024Article
- Molecular docking as a tool for the discovery of novel insight about the role of acid sphingomyelinase inhibitors in SARS- CoV-2 infectivity.BMC public health · 2024Review
- Molecular basis for the catalytic mechanism of human neutral sphingomyelinases 1 (hSMPD2).Nature communications · 2023Article
- Oxidative stress induces lysosomal membrane permeabilization and ceramide accumulation in retinal pigment epithelial cells.Disease models & mechanisms · 2023Article
- Inhibition of chitin deacetylases to attenuate plant fungal diseases.Nature communications · 2023Article
- Repurposing FIASMAs against Acid Sphingomyelinase for COVID-19: A Computational Molecular Docking and Dynamic Simulation Approach.Molecules (Basel, Switzerland) · 2023Article
- Article
- Discovery of a dual-action small molecule that improves neuropathological features of Alzheimer's disease mice.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- New Molecular Targets for Antidepressant Drugs.Pharmaceuticals (Basel, Switzerland) · 2021Review
- Acid Sphingomyelinase, a Lysosomal and Secretory Phospholipase C, Is Key for Cellular Phospholipid Catabolism.International journal of molecular sciences · 2021Review
- In Silico Analysis of the Molecular-Level Impact of SMPD1 Variants on Niemann-Pick Disease Severity.International journal of molecular sciences · 2021Article
- Small Molecule Inhibitors Targeting Biosynthesis of Ceramide, the Central Hub of the Sphingolipid Network.Journal of medicinal chemistry · 2021Review
- Fenofibrate increases very-long-chain sphingolipids and improves blood glucose homeostasis in NOD mice.Diabetologia · 2019Article
- Molecular models should not be published without the corresponding atomic coordinates.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Acid sphingomyelinase (ASM) hydrolyzes sphingomyelin to ceramide and phosphocholine, essential components of myelin in neurons. Genetic alterations in ASM lead to ASM deficiency (ASMD) and have been linked to Niemann-Pick disease types A and B. Olipudase alfa, a recombinant form of human ASM, is being developed as enzyme replacement therapy to treat the non-neurological manifestations of ASMD. Here we present the human ASM holoenzyme and product bound structures encompassing all of the functional domains. The catalytic domain has a metallophosphatase fold, and two zinc ions and one reaction product phosphocholine are identified in a histidine-rich active site. The structures reveal the underlying catalytic mechanism, in which two zinc ions activate a water molecule for nucleophilic attack of the phosphodiester bond. Docking of sphingomyelin provides a model that allows insight into the selectivity of the enzyme and how the ASM domains collaborate to complete hydrolysis. Mapping of known mutations provides a basic understanding on correlations between enzyme dysfunction and phenotypes observed in ASMD patients.
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Registered trials
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