ArticleProtein science : a publication of the Protein Society1994
Acid sphingomyelinase possesses a domain homologous to its activator proteins: saposins B and D.
Article in Protein science : a publication of the Protein Society, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- Article
- Acid Sphingomyelinase Deficiency: A Clinical and Immunological Perspective.International journal of molecular sciences · 2021Review
- Antiviral Activity of a Turbot (Marine drugs · 2019Article
- Characterization of Sphingomyelin Phosphodiesterase Expression in Bumblebee (Bombus lantschouensis).Journal of insect science (Online) · 2018Article
- Acid sphingomyelinase activity is regulated by membrane lipids and facilitates cholesterol transfer by NPC2.Journal of lipid research · 2014Article
- Sphingomyelin phosphodiesterase acid-like 3A (SMPDL3A) is a novel nucleotide phosphodiesterase regulated by cholesterol in human macrophages.The Journal of biological chemistry · 2014Article
- Roles and regulation of secretory and lysosomal acid sphingomyelinase.Cellular signalling · 2009Review
- A short guided tour through functional and structural features of saposin-like proteins.The Biochemical journal · 2005Review
- A model of the acid sphingomyelinase phosphoesterase domain based on its remote structural homolog purple acid phosphatase.Protein science : a publication of the Protein Society · 2004Article
- J3-crystallin of the jellyfish lens: similarity to saposins.Proceedings of the National Academy of Sciences of the United States of America · 2001Article
- Saposins and their interaction with lipids.Neurochemical research · 1999Review
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Abstract
An N-terminal region of the acid sphingomyelinase sequence (residues 89-165) is shown to be homologous to saposin-type sequences. By analogy with the known functions of saposins, this sphingomyelinase saposin-type domain may possess lipid-binding and/or sphingomyelinase-activator properties. This finding may prove to be important in the understanding of Niemann-Pick disease, which results from sphingomyelinase deficiency.
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