期刊文献+

泛素调节的蛋白质降解——2004年诺贝尔化学奖简介 被引量:6

Ubiquitin-mediated Protein Degradation The Introduction of the Nobel Prize in Chemistry 2004
在线阅读 下载PDF
导出
摘要 20 0 4年诺贝尔化学奖颁给了 3位发现细胞是如何摧毁蛋白质的科学家———阿龙·切哈诺沃、阿夫拉姆·赫什科和欧文·罗斯。本文详细介绍了他们的发现 ,重点介绍了泛素调节下蛋白质降解所需要的各种物质及其机理。 The Nobel Prize in Chemistry 2004 was awarded to three scientists: Aaron Ciechanover, Avram Hershko and Irwin Rose. They succeeded in showing how proteins are destroyed in cells. The article introduce their discovery, especially the substances wanted in the course of the ubiquitin-mediated protein degradation and the mechanism.
出处 《化学教育》 CAS 2004年第11期6-7,32,共3页 Chinese Journal of Chemical Education
关键词 泛素 蛋白质降解 2004年诺贝尔化学奖 蛋白酶体 the Nobel Prize, ubiquitin-mediate, protein degradation
  • 相关文献

参考文献6

二级参考文献16

  • 1Xiao ling S,J Biol Chem,1996年,271卷,42期,26410页
  • 2Desalle LM,Pagano M.Regulation of the G1 to S transition by the ubiquitin pathway.Febs Lett,2001,490(3),179~189
  • 3Kornitzer D,Ciechanover A.Modes of regulation of ubiquitin-mediated protein degradation.J Cell Physiol,2000,182(1),1~11
  • 4Saitoh H,Hinchey J.Functional heterogeneity of small ubiquitin-related protein modifiers SUMO-1 versus SUMO-2/3.J Biol chem,2000,275(9),6252~6258
  • 5Schwakz SE,Matuschewski K,Liakopoulos D,et al.The ubiquitin-like proteins SMT3 and SUMO-1 are conjugated by the UBC9 E2 enzyme.Proc Natl Acad Sci USA,1998,95(2),560~564
  • 6Joazeiro CA,Weissman AW.RING finger proteins:mediators of ubiquitin ligase activity.Cell,2000,102(5),549~552
  • 7Wan HI,Aaron DA,Fetter RD,et al.Highwire regulates synaptic growth in Drosophila.Neuron,2000,26(2),313~329
  • 8Strickland E,Hakalq K,Thomas PJ,et al.Recognition of misfolding proteins by PA700,the regulatory subcomplex of the 26 S proteasome.J Biol Chem,2000,275(8),5565~5572
  • 9Lord JM,Davey J,Frigerio L.Endoplasmic reticulum-associated protein degradation.Semin Cell Dev Biol,2000,11(3),159~164
  • 10Tomoda K,Kubota Y,Kato J.Degradation of the cyclin-dependent-kinase inhibitor p27Kip1 is instigated by Jab1.Nature,1999,398(6723),160~165

共引文献21

同被引文献199

引证文献6

二级引证文献44

相关作者

内容加载中请稍等...

相关机构

内容加载中请稍等...

相关主题

内容加载中请稍等...

浏览历史

内容加载中请稍等...
;
使用帮助 返回顶部