Human acid sphingomyelinase structures provide insight to molecular basis of Niemann-Pick disease.
about
Sphingolipids and their metabolism in physiology and disease.Structure of human nSMase2 reveals an interdomain allosteric activation mechanism for ceramide generation.Synthesis and evaluation of xanthone derivatives as acid sphingomyelinase inhibitors: potential treatment for UV-induced skin damage.Crystal structure of the mammalian lipopolysaccharide detoxifier.The mechanism of glycosphingolipid degradation revealed by a GALC-SapA complex structure.Structural basis for the activation of acid ceramidase.
P2860
Human acid sphingomyelinase structures provide insight to molecular basis of Niemann-Pick disease.
description
2016 nî lūn-bûn
@nan
2016年の論文
@ja
2016年論文
@yue
2016年論文
@zh-hant
2016年論文
@zh-hk
2016年論文
@zh-mo
2016年論文
@zh-tw
2016年论文
@wuu
2016年论文
@zh
2016年论文
@zh-cn
name
Human acid sphingomyelinase st ...... basis of Niemann-Pick disease.
@en
type
label
Human acid sphingomyelinase st ...... basis of Niemann-Pick disease.
@en
prefLabel
Human acid sphingomyelinase st ...... basis of Niemann-Pick disease.
@en
P2093
P2860
P356
P1476
Human acid sphingomyelinase st ...... basis of Niemann-Pick disease.
@en
P2093
Huawei Qiu
Matthew C Metcalf
Ronnie R Wei
Scott C Garman
Tim Edmunds
Yan-Feng Zhou
P2860
P2888
P356
10.1038/NCOMMS13082
P407
P577
2016-10-11T00:00:00Z
P6179
1020424291