Molecular basis for the catalytic mechanism of human neutral sphingomyelinases 1 (hSMPD2)
Molecular basis for the catalytic mechanism of human neutral sphingomyelinases 1 (hSMPD2)
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Author / Creator
Yi, Jingbo , Qi, Boya , Yin, Jian , Li, Ruochong , Chen, Xudong , Hu, Junhan , Li, Guohui , Zhang, Sensen , Zhang, Yuebin and Yang, Maojun
Publisher
London: Nature Publishing Group UK
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Language
English
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Publisher
London: Nature Publishing Group UK
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Enzymatic breakdown of sphingomyelin by sphingomyelinase (SMase) is the main source of the membrane lipids, ceramides, which are involved in many cellular physiological processes. However, the full-length structure of human neutral SMase has not been resolved; therefore, its catalytic mechanism remains unknown. Here, we resolve the structure of hum...
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Full title
Molecular basis for the catalytic mechanism of human neutral sphingomyelinases 1 (hSMPD2)
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TN_cdi_doaj_primary_oai_doaj_org_article_af97935e67f44be8858b2e1f52c7a7dc
Permalink
https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_af97935e67f44be8858b2e1f52c7a7dc
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ISSN
2041-1723
E-ISSN
2041-1723
DOI
10.1038/s41467-023-43580-w