Structural and mechanistic basis for a new mode of glycosyltransferase inhibition.
Structural and mechanistic basis for a new mode of glycosyltransferase inhibition.
复制标题
DOI:
10.1038/nchembio.343
复制
发表时间:
2010-05
影响因子:
14.8
通讯作者:
Wagner, Gerd K.
中科院分区:
文献类型:
--
作者:
Pesnot, Thomas;Jorgensen, Rene;Palcic, Monica M.;Wagner, Gerd K.
Glycosyltransferases are carbohydrate-active enzymes with essential roles in numerous important biological processes. We have developed a novel donor analogue for galactosyltransferases which locks a representative target enzyme in a catalytically inactive conformation, thus almost completely abolishing sugar transfer. Results with other galactosyltransferases suggest that this novel and unique mode of glycosyltransferase inhibition is, very likely, generally applicable to other members of this very important enzyme family also.
登录
查看更多内容
影响因子:
14.8
作者:
Liu, Y;Gray, NS
通讯作者:
Gray, NS
DOI:
10.1038/nri2417
发表时间:
2008-11
期刊:
Nature reviews. Immunology
影响因子:
--
作者:
通讯作者:
--
影响因子:
11.4
作者:
Gastinel, LN;Cambillau, C;Bourne, Y
通讯作者:
Bourne, Y
影响因子:
3.2
作者:
Pesnot, Thomas;Wagner, Gerd K.
通讯作者:
Wagner, Gerd K.
影响因子:
4.9
作者:
Collier, Alice;Wagner, Gerd K.
通讯作者:
Wagner, Gerd K.