{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,18]],"date-time":"2026-08-18T13:26:38Z","timestamp":1787059598700,"version":"build-2736575974"},"reference-count":56,"publisher":"American Chemical Society (ACS)","issue":"16","license":[{"start":{"date-parts":[[2026,8,7]],"date-time":"2026-08-07T00:00:00Z","timestamp":1786060800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100001659","name":"Deutsche Forschungsgemeinschaft","doi-asserted-by":"publisher","award":["AR 376\/22-1"],"award-info":[{"award-number":["AR 376\/22-1"]}],"id":[{"id":"10.13039\/501100001659","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000057","name":"National Institute of General Medical Sciences","doi-asserted-by":"publisher","award":["R35GM118128"],"award-info":[{"award-number":["R35GM118128"]}],"id":[{"id":"10.13039\/100000057","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000057","name":"National Institute of General Medical Sciences","doi-asserted-by":"publisher","award":["R35GM128666"],"award-info":[{"award-number":["R35GM128666"]}],"id":[{"id":"10.13039\/100000057","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2026,8,18]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>Neutral sphingomyelinase 2 (nSMase2) is a membrane-bound enzyme that hydrolyzes sphingomyelin (SM) into ceramide and phosphocholine. By generating the bioactive lipid ceramide, nSMase2 plays a critical role in cell stress responses and in regulating exosomes that package and transfer pathogenic factors, including tau protein and amyloid \u03b2. Thus, nSMase2 has been implicated in Alzheimer\u2019s disease and other neurological disorders. However, current tools to measure nSMase2 activity are limited, in particular those that could be used in therapeutic development. Here we developed a high-throughput assay to measure human nSMase2 activity. The assay uses a sphingomyelin substrate analogue with a FRET donor and acceptor pair attached to the headgroup and acyl-chain, respectively. Using recombinant human nSMase2, we sensitively detected both wild-type and mutant activity and demonstrated inhibition by the known nSMase2 inhibitor GW4869. The assay captures the major hallmarks of nSMase2 regulation by anionic lipids and displays sensitivity capable of detecting nSMase2 activity from cell lysates. Together, this assay enables rapid screening of nSMase2 inhibitors to support future therapeutic development.<\/jats:p>","DOI":"10.1021\/acs.biochem.6c00322","type":"journal-article","created":{"date-parts":[[2026,8,7]],"date-time":"2026-08-07T15:01:34Z","timestamp":1786114894000},"page":"2548-2556","source":"Crossref","is-referenced-by-count":0,"title":["Development\nof a FRET-Based Assay for Human Neutral\nSphingomyelinase 2"],"prefix":"10.1021","volume":"65","author":[{"ORCID":"https:\/\/orcid.org\/0009-0007-4377-5681","authenticated-orcid":true,"given":"Khalayi Martha","family":"Aywa","sequence":"first","affiliation":[{"name":"Stony Brook University , , ,","place":["Stony Brook, New York, United States, 11794"]},{"name":"Stony Brook University Cancer Center , , ,","place":["Stony Brook, New York, United States, 11794"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Christian","family":"Kappe","sequence":"additional","affiliation":[{"name":"Humboldt-Universita\u0308t zu Berlin , , Brook-Taylor-Strasse 2 , ,","place":["Berlin, Germany, 12489"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Botheina","family":"Ghandour","sequence":"additional","affiliation":[{"name":"Stony Brook University Cancer Center , , ,","place":["Stony Brook, New York, United States, 11794"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Shujuan","family":"Gao","sequence":"additional","affiliation":[{"name":"Stony Brook University , , ,","place":["Stony Brook, New York, United States, 11794"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Christoph","family":"Arenz","sequence":"additional","affiliation":[{"name":"Humboldt-Universita\u0308t zu Berlin , , Brook-Taylor-Strasse 2 , ,","place":["Berlin, Germany, 12489"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yusuf A.","family":"Hannun","sequence":"additional","affiliation":[{"name":"Stony Brook University , , ,","place":["Stony Brook, New York, United States, 11794"]},{"name":"Stony Brook University Cancer Center , , ,","place":["Stony Brook, New York, United States, 11794"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-4981-1253","authenticated-orcid":true,"given":"Michael V.","family":"Airola","sequence":"additional","affiliation":[{"name":"Stony Brook University , , ,","place":["Stony Brook, New York, United States, 11794"]},{"name":"Stony Brook University Cancer Center , , ,","place":["Stony Brook, New York, United States, 11794"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"316","published-online":{"date-parts":[[2026,8,7]]},"reference":[{"issue":"5294","key":"2026081808121807500_cit1","doi-asserted-by":"publisher","first-page":"1855","DOI":"10.1126\/science.274.5294.1855","article-title":"Functions\nof ceramide in coordinating cellular responses to stress","volume":"274","author":"Hannun","year":"1996","journal-title":"Science"},{"issue":"3","key":"2026081808121807500_cit2","doi-asserted-by":"publisher","first-page":"285","DOI":"10.1002\/1097-4652(200009)184:3&lt;285::AID-JCP2&gt;3.0.CO;2-3","article-title":"Compartmentalization\nof ceramide\nsignaling: physical foundations and biological effects","volume":"184","author":"Kolesnick","year":"2000","journal-title":"J. Cell Physiol"},{"issue":"3","key":"2026081808121807500_cit3","doi-asserted-by":"publisher","first-page":"202","DOI":"10.1016\/S0022-2275(20)40138-5","article-title":"Sphingomyelinase\nin normal human spleens and in spleens\nfrom subjects with Niemann-Pick disease","volume":"8","author":"Schneider","year":"1967","journal-title":"J.\nLipid Res."},{"issue":"5","key":"2026081808121807500_cit4","doi-asserted-by":"publisher","first-page":"506","DOI":"10.1016\/S0022-2275(20)41749-3","article-title":"Sphingomyelinase Activity at Ph 7.4\nin Human-Brain\nand a Comparison to Activity at Ph 5.0","volume":"17","author":"Rao","year":"1976","journal-title":"J. Lipid\nRes."},{"issue":"2","key":"2026081808121807500_cit5","doi-asserted-by":"publisher","first-page":"339","DOI":"10.1016\/0005-2760(69)90192-1","article-title":"The presence\nof spingomyelin- and ceramide-cleaving enzymes in the small intestinal\ntract","volume":"176","author":"Nilsson","year":"1969","journal-title":"Biochim. Biophys. Acta"},{"issue":"4","key":"2026081808121807500_cit6","doi-asserted-by":"publisher","first-page":"823","DOI":"10.1002\/hep.510260403","article-title":"Purification\nof a newly identified alkaline sphingomyelinase\nin human bile and effects of bile salts and phosphatidylcholine on\nenzyme activity","volume":"26","author":"Duan","year":"1997","journal-title":"Hepatology"},{"issue":"1","key":"2026081808121807500_cit7","doi-asserted-by":"publisher","first-page":"27","DOI":"10.1139\/o03-091","article-title":"Acid and neutral\nsphingomyelinases: roles and mechanisms\nof regulation","volume":"82","author":"Marchesini","year":"2004","journal-title":"Biochem Cell Biol."},{"issue":"1","key":"2026081808121807500_cit8","doi-asserted-by":"publisher","first-page":"484","DOI":"10.1016\/S0021-9258(18)52461-3","article-title":"Identification of sphingomyelin\nturnover as an effector mechanism for the action of tumor necrosis\nfactor alpha and gamma-interferon. Specific role in cell differentiation","volume":"266","author":"Kim","year":"1991","journal-title":"J. Biol. Chem."},{"issue":"11","key":"2026081808121807500_cit9","doi-asserted-by":"publisher","first-page":"2443","DOI":"10.1194\/jlr.M700227-JLR200","article-title":"Regulation\nof neutral\nsphingomyelinase-2 by GSH: a new insight to the role of oxidative\nstress in aging-associated inflammation","volume":"48","author":"Rutkute","year":"2007","journal-title":"J.\nLipid Res."},{"issue":"9","key":"2026081808121807500_cit10","doi-asserted-by":"publisher","first-page":"968","DOI":"10.1096\/fj.03-0875fje","article-title":"Expression\nof neutral sphingomyelinase-2 (NSMase-2) in primary rat hepatocytes\nmodulates IL-beta-induced JNK activation","volume":"18","author":"Karakashian","year":"2004","journal-title":"FASEB\nJ."},{"issue":"3","key":"2026081808121807500_cit11","doi-asserted-by":"publisher","first-page":"900","DOI":"10.1016\/j.bbrc.2006.04.013","article-title":"nSMase2 activation and trafficking\nare modulated by oxidative stress to induce apoptosis","volume":"344","author":"Levy","year":"2006","journal-title":"Biochem. Biophys. Res. Commun."},{"issue":"2","key":"2026081808121807500_cit12","doi-asserted-by":"publisher","first-page":"296","DOI":"10.1093\/cvr\/cvn349","article-title":"Activation\nof neutral sphingomyelinase is involved\nin acute hypoxic pulmonary vasoconstriction","volume":"82","author":"Cogolludo","year":"2008","journal-title":"Cardiovasc. Res."},{"issue":"11","key":"2026081808121807500_cit13","doi-asserted-by":"publisher","first-page":"5895","DOI":"10.1073\/pnas.97.11.5895","article-title":"Cloning and characterization\nof the mammalian brain-specific, Mg2+-dependent neutral sphingomyelinase","volume":"97","author":"Hofmann","year":"2000","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"issue":"6220","key":"2026081808121807500_cit14","doi-asserted-by":"publisher","DOI":"10.1126\/science.1260419","article-title":"Proteomics. Tissue-based map of the human proteome","volume":"347","author":"Uhlen","year":"2015","journal-title":"Science"},{"issue":"24","key":"2026081808121807500_cit15","doi-asserted-by":"publisher","first-page":"25101","DOI":"10.1074\/jbc.M313662200","article-title":"Role for mammalian\nneutral sphingomyelinase 2 in confluence-induced\ngrowth arrest of MCF7 cells","volume":"279","author":"Marchesini","year":"2004","journal-title":"J. Biol. Chem."},{"issue":"4","key":"2026081808121807500_cit16","doi-asserted-by":"publisher","first-page":"456","DOI":"10.1016\/S0022-2275(20)40599-1","article-title":"The subcellular localization of neutral sphingomyelinase\nin rat liver","volume":"20","author":"Hostetler","year":"1979","journal-title":"J. Lipid Res."},{"issue":"28","key":"2026081808121807500_cit17","doi-asserted-by":"publisher","first-page":"E5549","DOI":"10.1073\/pnas.1705134114","article-title":"Structure of human nSMase2 reveals an interdomain\nallosteric activation mechanism for ceramide generation","volume":"114","author":"Airola","year":"2017","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"issue":"12","key":"2026081808121807500_cit18","doi-asserted-by":"publisher","first-page":"4554","DOI":"10.1073\/pnas.0406380102","article-title":"Neutral sphingomyelinase 2 (smpd3)\nin the control of\npostnatal growth and development","volume":"102","author":"Stoffel","year":"2005","journal-title":"Proc. Natl.\nAcad. Sci. U. S. A."},{"issue":"51","key":"2026081808121807500_cit19","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.2212879119","article-title":"Temporal changes\nin plasma membrane lipid content induce endocytosis to regulate developmental\nepithelial-to-mesenchymal transition","volume":"119","author":"Piacentino","year":"2022","journal-title":"Proc.\nNatl. Acad. Sci. U. S. A."},{"issue":"5867","key":"2026081808121807500_cit20","doi-asserted-by":"publisher","first-page":"1244","DOI":"10.1126\/science.1153124","article-title":"Ceramide triggers budding\nof exosome vesicles into multivesicular endosomes","volume":"319","author":"Trajkovic","year":"2008","journal-title":"Science"},{"issue":"5","key":"2026081808121807500_cit21","doi-asserted-by":"publisher","DOI":"10.1242\/jcs.259324","article-title":"Neutral sphingomyelinase\n2 controls exosome secretion by counteracting V-ATPase-mediated endosome\nacidification","volume":"135","author":"Choezom","year":"2022","journal-title":"J. Cell Sci."},{"issue":"11","key":"2026081808121807500_cit22","doi-asserted-by":"publisher","first-page":"1584","DOI":"10.1038\/nn.4132","article-title":"Depletion of microglia and inhibition of exosome synthesis halt tau\npropagation","volume":"18","author":"Asai","year":"2015","journal-title":"Nat. Neurosci"},{"issue":"8","key":"2026081808121807500_cit23","doi-asserted-by":"publisher","first-page":"1792","DOI":"10.1016\/j.neurobiolaging.2014.02.012","article-title":"Exosome reduction\nin vivo is associated with lower amyloid plaque load in the 5XFAD\nmouse model of Alzheimer\u2019s disease","volume":"35","author":"Dinkins","year":"2014","journal-title":"Neurobiol\nAging"},{"issue":"9","key":"2026081808121807500_cit24","doi-asserted-by":"publisher","first-page":"4716","DOI":"10.1182\/blood-2007-10-113068","article-title":"Mutations\nin the neutral\nsphingomyelinase gene SMPD3 implicate the ceramide pathway in human\nleukemias","volume":"111","author":"Kim","year":"2008","journal-title":"Blood"},{"issue":"7","key":"2026081808121807500_cit25","doi-asserted-by":"publisher","first-page":"1479","DOI":"10.1161\/ATVBAHA.118.311208","article-title":"nSMase2 (Type 2-Neutral Sphingomyelinase) Deficiency\nor Inhibition by GW4869 Reduces Inflammation and Atherosclerosis in\nApoe(\u2212\/\u2212) Mice","volume":"38","author":"Lallemand","year":"2018","journal-title":"Arterioscler Thromb\nVasc Biol."},{"issue":"3","key":"2026081808121807500_cit26","doi-asserted-by":"publisher","first-page":"537","DOI":"10.3233\/JAD-2011-111202","article-title":"Increased\nceramide in brains with Alzheimer\u2019s and other neurodegenerative\ndiseases","volume":"29","author":"Filippov","year":"2012","journal-title":"J. Alzheimers Dis"},{"issue":"1","key":"2026081808121807500_cit27","doi-asserted-by":"publisher","first-page":"109","DOI":"10.1186\/1742-2094-10-109","article-title":"Early activation of\nnSMase2\/ceramide pathway in astrocytes\nis involved in ischemia-associated neuronal damage via inflammation\nin rat hippocampi","volume":"10","author":"Gu","year":"2013","journal-title":"J. Neuroinflammation"},{"issue":"5","key":"2026081808121807500_cit28","doi-asserted-by":"publisher","first-page":"1869","DOI":"10.1016\/S0002-9440(10)64463-X","article-title":"Intraneuronal Alzheimer abeta42 accumulates in multivesicular\nbodies and is associated with synaptic pathology","volume":"161","author":"Takahashi","year":"2002","journal-title":"Am. J. Pathol."},{"issue":"33","key":"2026081808121807500_cit29","doi-asserted-by":"publisher","first-page":"8653","DOI":"10.1523\/JNEUROSCI.1429-16.2016","article-title":"Neutral Sphingomyelinase-2\nDeficiency Ameliorates Alzheimer\u2019s\nDisease Pathology and Improves Cognition in the 5XFAD Mouse","volume":"36","author":"Dinkins","year":"2016","journal-title":"J. Neurosci."},{"key":"2026081808121807500_cit30","doi-asserted-by":"publisher","DOI":"10.1016\/j.nbd.2023.105987","article-title":"Neuronal\ndeletion of nSMase2 reduces\nthe production of Abeta and directly protects neurons","volume":"177","author":"Tohumeken","year":"2023","journal-title":"Neurobiol Dis"},{"issue":"11","key":"2026081808121807500_cit31","doi-asserted-by":"publisher","first-page":"1118","DOI":"10.1038\/ncb1313","article-title":"Regulation of cholesterol\nand sphingomyelin metabolism by amyloid-beta and presenilin","volume":"7","author":"Grimm","year":"2005","journal-title":"Nat. Cell Biol."},{"issue":"38","key":"2026081808121807500_cit32","doi-asserted-by":"publisher","first-page":"12676","DOI":"10.1523\/JNEUROSCI.1243-10.2010","article-title":"Fibrillar amyloid-beta-activated\nhuman astroglia kill primary human\nneurons via neutral sphingomyelinase: implications for Alzheimer\u2019s\ndisease","volume":"30","author":"Jana","year":"2010","journal-title":"J. Neurosci."},{"issue":"7","key":"2026081808121807500_cit33","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pone.0021643","article-title":"Metabolomics in early Alzheimer\u2019s\ndisease: identification of altered plasma sphingolipidome using shotgun\nlipidomics","volume":"6","author":"Han","year":"2011","journal-title":"PLoS One"},{"issue":"7","key":"2026081808121807500_cit34","doi-asserted-by":"publisher","first-page":"2070","DOI":"10.1073\/pnas.0305799101","article-title":"Involvement of oxidative\nstress-induced abnormalities in ceramide and cholesterol metabolism\nin brain aging and Alzheimer\u2019s disease","volume":"101","author":"Cutler","year":"2004","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"2026081808121807500_cit35","doi-asserted-by":"publisher","first-page":"65","DOI":"10.1016\/bs.apha.2024.10.015","article-title":"Neutral sphingomyelinase\n2: A promising drug target for CNS disease","volume":"102","author":"Huang","year":"2025","journal-title":"Adv. Pharmacol."},{"issue":"7","key":"2026081808121807500_cit36","doi-asserted-by":"publisher","first-page":"1323","DOI":"10.1016\/j.febslet.2007.02.046","article-title":"Analysis of membrane topology of\nneutral sphingomyelinase\n2","volume":"581","author":"Tani","year":"2007","journal-title":"FEBS Lett."},{"issue":"16","key":"2026081808121807500_cit37","doi-asserted-by":"publisher","first-page":"13775","DOI":"10.1074\/jbc.M212262200","article-title":"Biochemical\nproperties of mammalian\nneutral sphingomyelinase 2 and its role in sphingolipid metabolism","volume":"278","author":"Marchesini","year":"2003","journal-title":"J. Biol. Chem."},{"issue":"25","key":"2026081808121807500_cit38","doi-asserted-by":"publisher","first-page":"22362","DOI":"10.1074\/jbc.M110.156471","article-title":"Identification of\nnovel anionic phospholipid\nbinding domains in neutral sphingomyelinase 2 with selective binding\npreference","volume":"286","author":"Wu","year":"2011","journal-title":"J. Biol. Chem."},{"issue":"43","key":"2026081808121807500_cit39","doi-asserted-by":"publisher","first-page":"41128","DOI":"10.1074\/jbc.M206747200","article-title":"Inhibition of tumor\nnecrosis factor-induced cell death\nin MCF7 by a novel inhibitor of neutral sphingomyelinase","volume":"277","author":"Luberto","year":"2002","journal-title":"J. Biol. Chem."},{"issue":"3","key":"2026081808121807500_cit40","doi-asserted-by":"publisher","first-page":"2027","DOI":"10.3390\/ijms24032027","article-title":"Inhibition of\nNeutral Sphingomyelinase\n2 by Novel Small Molecule Inhibitors Results in Decreased Release\nof Extracellular Vesicles by Vascular Smooth Muscle Cells and Attenuated\nCalcification","volume":"24","author":"Pavlic","year":"2023","journal-title":"Int. J. Mol. Sci."},{"issue":"5","key":"2026081808121807500_cit41","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pone.0124481","article-title":"Cambinol,\na novel inhibitor of neutral sphingomyelinase\n2 shows neuroprotective properties","volume":"10","author":"Figuera-Losada","year":"2015","journal-title":"PLoS One"},{"key":"2026081808121807500_cit42","first-page":"164","article-title":"[18] Sphingomyelinase\nassay using radiolabeled substrate","volume-title":"Methods\nin enzymology","author":"Liu","year":"2000"},{"issue":"5","key":"2026081808121807500_cit43","doi-asserted-by":"publisher","first-page":"815","DOI":"10.1016\/S0022-2275(20)30124-3","article-title":"High-precision\nfluorescence assay for sphingomyelinase activity of isolated enzymes\nand cell lysates","volume":"43","author":"Loidl","year":"2002","journal-title":"J. Lipid Res."},{"key":"2026081808121807500_cit44","doi-asserted-by":"publisher","first-page":"113","DOI":"10.1007\/978-1-0716-0814-2_7","article-title":"Methods to\nCharacterize Synthesis and Degradation of Sphingomyelin at the Plasma\nMembrane and Its Impact on Lipid Raft Dynamics","volume":"2187","author":"Nikolova-Karakashian","year":"2021","journal-title":"Methods Mol. Biol."},{"issue":"12","key":"2026081808121807500_cit45","doi-asserted-by":"publisher","first-page":"1665","DOI":"10.1016\/j.bbalip.2013.08.007","article-title":"Endocytosis and intracellular processing\nof BODIPY-sphingomyelin by murine CATH.a neurons","volume":"1831","author":"Nusshold","year":"2013","journal-title":"Biochim. Biophys. Acta"},{"issue":"1","key":"2026081808121807500_cit46","doi-asserted-by":"publisher","first-page":"7755","DOI":"10.1038\/s41467-023-43580-w","article-title":"Molecular basis for\nthe catalytic mechanism of human neutral sphingomyelinases 1 (hSMPD2)","volume":"14","author":"Yi","year":"2023","journal-title":"Nat. Commun."},{"issue":"2","key":"2026081808121807500_cit47","doi-asserted-by":"publisher","first-page":"162","DOI":"10.1006\/abio.1997.2391","article-title":"A stable nonfluorescent\nderivative of resorufin for the fluorometric determination of trace\nhydrogen peroxide: applications in detecting the activity of phagocyte\nNADPH oxidase and other oxidases","volume":"253","author":"Zhou","year":"1997","journal-title":"Anal. Biochem."},{"issue":"8","key":"2026081808121807500_cit48","doi-asserted-by":"publisher","first-page":"911","DOI":"10.1139\/o59-099","article-title":"A rapid method of total lipid extraction and purification","volume":"37","author":"Bligh","year":"1959","journal-title":"Can. J. Biochem Physiol"},{"issue":"10","key":"2026081808121807500_cit49","doi-asserted-by":"publisher","first-page":"2790","DOI":"10.1002\/anie.201611706","article-title":"Amplification\nof a FRET Probe by Lipid-Water Partition for the Detection of Acid\nSphingomyelinase in Live Cells","volume":"56","author":"Pinkert","year":"2017","journal-title":"Angew. Chem.,\nInt. Ed. Engl."},{"issue":"26","key":"2026081808121807500_cit50","doi-asserted-by":"publisher","first-page":"5780","DOI":"10.1002\/chem.202000133","article-title":"A Novel Visible Range FRET Probe\nfor Monitoring Acid Sphingomyelinase\nActivity in Living Cells","volume":"26","author":"Kappe","year":"2020","journal-title":"Chemistry"},{"key":"2026081808121807500_cit51","doi-asserted-by":"publisher","DOI":"10.1016\/j.bmc.2021.116303","article-title":"Synthesis and characterization of a new two photon excitable acid\nsphingomyelinase FRET probe","volume":"44","author":"Mohamed","year":"2021","journal-title":"Bioorg. Med. Chem."},{"key":"2026081808121807500_cit52","doi-asserted-by":"publisher","first-page":"152","DOI":"10.1016\/j.chemphyslip.2018.09.014","article-title":"FRET probes for measuring sphingolipid\nmetabolizing enzyme activity","volume":"216","author":"Mohamed","year":"2018","journal-title":"Chem. Phys. Lipids"},{"key":"2026081808121807500_cit53","doi-asserted-by":"publisher","DOI":"10.1007\/978-0-387-46312-4","volume-title":"Principles of Fluorescence\nSpectroscopy","author":"Lakowicz","year":"2006"},{"issue":"1","key":"2026081808121807500_cit54","doi-asserted-by":"publisher","first-page":"7456","DOI":"10.1038\/s41467-024-51874-w","article-title":"Trifunctional sphingomyelin\nderivatives enable nanoscale resolution of sphingomyelin turnover\nin physiological and infection processes via expansion microscopy","volume":"15","author":"Ruhling","year":"2024","journal-title":"Nat. Commun."},{"issue":"8","key":"2026081808121807500_cit55","doi-asserted-by":"publisher","DOI":"10.1016\/j.jlr.2024.100584","article-title":"A comprehensive\nmeasure of Golgi sphingolipid flux using NBD C(6)-ceramide: evaluation\nof sphingolipid inhibitors","volume":"65","author":"Lee","year":"2024","journal-title":"J. Lipid Res."},{"issue":"4","key":"2026081808121807500_cit56","doi-asserted-by":"publisher","first-page":"320","DOI":"10.1007\/s12017-010-8120-z","article-title":"Mammalian neutral sphingomyelinases:\nregulation and roles in cell signaling responses","volume":"12","author":"Wu","year":"2010","journal-title":"Neuromolecular Med."}],"container-title":["Biochemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/pubs.acs.org\/doi\/pdf\/10.1021\/acs.biochem.6c00322","content-type":"application\/pdf","content-version":"vor","intended-application":"unspecified"},{"URL":"https:\/\/pubs.acs.org\/bichaw\/article-pdf\/65\/16\/2548\/66459576\/acs.biochem.6c00322.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/pubs.acs.org\/bichaw\/article-pdf\/65\/16\/2548\/66459576\/acs.biochem.6c00322.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,8,18]],"date-time":"2026-08-18T12:46:33Z","timestamp":1787057193000},"score":1,"resource":{"primary":{"URL":"https:\/\/pubs.acs.org\/bichaw\/article\/65\/16\/2548\/5250376\/Development-of-a-FRET-Based-Assay-for-Human"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,8,7]]},"references-count":56,"journal-issue":{"issue":"16","published-online":{"date-parts":[[2026,8,7]]},"published-print":{"date-parts":[[2026,8,18]]}},"URL":"https:\/\/doi.org\/10.1021\/acs.biochem.6c00322","relation":{},"ISSN":["0006-2960","1520-4995"],"issn-type":[{"value":"0006-2960","type":"print"},{"value":"1520-4995","type":"electronic"}],"subject":[],"published":{"date-parts":[[2026,8,7]]}}}