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Molecular basis for the catalytic mechanism of human neutral sphingomyelinases 1 (hSMPD2)

Molecular basis for the catalytic mechanism of human neutral sphingomyelinases 1 (hSMPD2)

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_af97935e67f44be8858b2e1f52c7a7dc

Molecular basis for the catalytic mechanism of human neutral sphingomyelinases 1 (hSMPD2)

About this item

Full title

Molecular basis for the catalytic mechanism of human neutral sphingomyelinases 1 (hSMPD2)

Publisher

London: Nature Publishing Group UK

Journal title

Nature communications, 2023-11, Vol.14 (1), p.7755-7755, Article 7755

Language

English

Formats

Publication information

Publisher

London: Nature Publishing Group UK

More information

Scope and Contents

Contents

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...

Alternative Titles

Full title

Molecular basis for the catalytic mechanism of human neutral sphingomyelinases 1 (hSMPD2)

Identifiers

Primary Identifiers

Record Identifier

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

Other Identifiers

ISSN

2041-1723

E-ISSN

2041-1723

DOI

10.1038/s41467-023-43580-w

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