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  • Structure of human nSMase2 reveals an interdomain allosteric activation mechanism for ceramide generation.

Structure of human nSMase2 reveals an interdomain allosteric activation mechanism for ceramide generation.

Proceedings of the National Academy of Sciences of the United States of America (2017-06-28)
Michael V Airola, Prajna Shanbhogue, Achraf A Shamseddine, Kip E Guja, Can E Senkal, Rohan Maini, Nana Bartke, Bill X Wu, Lina M Obeid, Miguel Garcia-Diaz, Yusuf A Hannun
ABSTRACT

Neutral sphingomyelinase 2 (nSMase2, product of the

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Sigma-Aldrich
O-(4-Nitrophenylphosphoryl)choline