首页> The Journal of biological chemistry> The GP(Y/F) domain of TF1 integrase multimerizes when present in a fragment, and substitutions in this domain reduce enzymatic activity of the full-length protein

The GP(Y/F) domain of TF1 integrase multimerizes when present in a fragment, and substitutions in this domain reduce enzymatic activity of the full-length protein

导出原文传递

翻译打印收藏纠错

第一作者： Ebina H

作者： Ebina H ^[1] ; Chatterjee AG ; Judson RL ; Levin HL

作者单位： NICHD, Sect Eukaryot Transposable Elements, Lab Gene Regulat & Dev, NIH, Bethesda, MD 20892 USA ^[1]

关键词 HUMAN-IMMUNODEFICIENCY-VIRUS TERMINAL REPEAT-RETROTRANSPOSON RETROVIRAL DNA INTEGRATION TYPE-1 INTEGRASE HIV-1 INTEGRASE FISSION YEAST CONCERTED INTEGRATION FUNCTIONAL DOMAINS CATALYTIC DOMAIN SELF-ASSOCIATION

发布时间 2013-11-20

翻译满意度评价：

准确一般字义偏差语意偏离译文作用小提交

浏览0

The Journal of biological chemistry

2008年283卷23期

15965-15974页

相似文献

中文期刊
外文期刊
学位论文
会议论文

浏览0

点击下载本期目录封面

The Journal of biological chemistry

2008年283卷23期

15965-15974页

检索历史清除

The GP(Y/F) domain of TF1 integrase multimerizes when present in a fragment, and substitutions in this domain reduce enzymatic activity of the full-length protein

The Journal of biological chemistry

相似文献

同项目论文

The Journal of biological chemistry

相关期刊

参考文献：
指定格式：	NoteExpress EndNote RefWorks NoteFirst

检索历史 清除

The GP(Y/F) domain of TF1 integrase multimerizes when present in a fragment, and substitutions in this domain reduce enzymatic activity of the full-length protein

The Journal of biological chemistry

相似文献

同项目论文

The Journal of biological chemistry

相关期刊

检索历史清除