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| http://purl.uniprot.org/citations/23046545 | http://www.w3.org/2000/01/rdf-schema#comment | "NSMase2 is associated to the plasma membrane, whereas ASMase is predominantly lysosomal; both hydrolyze sphingomyelin (SM) to ceramide and phosphocholine. Although SM accumulated in both ASMase(-/-) and fro/fro (NSMase2(-/-)) fibroblasts, the reduction of ceramides was more dramatic in fro/fro cells. ASMase mRNA, protein and enzyme activity were substantially elevated in fro/fro fibroblasts. In contrast, NSMase2 activity was unaffected in ASMase(-/-) fibroblasts. ASMase(-/-) cells showed normal cell cycling whereas fro/fro cells grew slowly and were arrested in G1/G0 and could be corrected by transfection with smpd3 gene. This suggests two distinct subcellular pathways for SM catabolism with distinct functions."xsd:string |
| http://purl.uniprot.org/citations/23046545 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.febslet.2012.09.039"xsd:string |
| http://purl.uniprot.org/citations/23046545 | http://purl.uniprot.org/core/author | "Qin J."xsd:string |
| http://purl.uniprot.org/citations/23046545 | http://purl.uniprot.org/core/author | "Dawson G."xsd:string |
| http://purl.uniprot.org/citations/23046545 | http://purl.uniprot.org/core/date | "2012"xsd:gYear |
| http://purl.uniprot.org/citations/23046545 | http://purl.uniprot.org/core/name | "FEBS Lett"xsd:string |
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| http://purl.uniprot.org/citations/23046545 | http://purl.uniprot.org/core/title | "Evidence for coordination of lysosomal (ASMase) and plasma membrane (NSMase2) forms of sphingomyelinase from mutant mice."xsd:string |
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