Molecular basis for the catalytic mechanism of human neutral sphingomyelinases 1 (hSMPD2)
Abstract 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 mecha...
Main Authors: | Jingbo Yi, Boya Qi, Jian Yin, Ruochong Li, Xudong Chen, Junhan Hu, Guohui Li, Sensen Zhang, Yuebin Zhang, Maojun Yang |
---|---|
Format: | Article |
Language: | English |
Published: |
Nature Portfolio
2023-11-01
|
Series: | Nature Communications |
Online Access: | https://doi.org/10.1038/s41467-023-43580-w |
Similar Items
-
Exosomes mediate Zika virus transmission through SMPD3 neutral Sphingomyelinase in cortical neurons
by: Wenshuo Zhou, et al.
Published: (2019-01-01) -
mRNA Expression of <i>SMPD1</i> Encoding Acid Sphingomyelinase Decreases upon Antidepressant Treatment
by: Cosima Rhein, et al.
Published: (2021-05-01) -
SMPD1 expression profile and mutation landscape help decipher genotype–phenotype association and precision diagnosis for acid sphingomyelinase deficiency
by: Ruisong Wang, et al.
Published: (2023-03-01) -
Neutral Sphingomyelinase 2 Inhibition Limits Hepatic Steatosis and Inflammation
by: Fatema Al-Rashed, et al.
Published: (2024-03-01) -
Characterization of a Neutral Sphingomyelinase Activity in Human Serum and Plasma
by: Christiane Mühle, et al.
Published: (2023-01-01)