Kicking down the ladder： adding cleavable features to genetically encoded photocrosslinkers
Protein-protein interactions（PPIs）play vital roles in biological processes.However,the discovery of transient and biologically relevant PPIs remain a formidable challenge using conventional strategies such as co-immunoprecipitation（CoIP）,yeast two hybrids（Y2H）and Forster resonance energy transfer（FR...
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| Veröffentlicht in: | Science China. Chemistry 2017-02, Vol.60 (2), p.167-169 |
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| creator | Lin, Zhi Xie, Xiao Chen, Peng R. |
| description | Protein-protein interactions（PPIs）play vital roles in biological processes.However,the discovery of transient and biologically relevant PPIs remain a formidable challenge using conventional strategies such as co-immunoprecipitation（CoIP）,yeast two hybrids（Y2H）and Forster resonance energy transfer（FRET）[1].Genetically encoded photocrosslinkers have recently emerged as a powerful approach for probing intracellular PPIs with the capability for in situ studies,low perturbation to cells as well as the wide generality.This facile strategy also demonstrated an advantage of high spatiotemporal resolution,which offers a robust capture strategy for the discovery of transient and/or weak PPIs with lowered false-positive backgrounds[2]. |
| doi_str_mv | 10.1007/s11426-016-0452-6 |
| format | Article |
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Xie, Xiao ; Chen, Peng R.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c343t-4c03655c9ef9d0fd5334669408660d28ec1462cc68f718d3a20c5bb3fbfdb8f53</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2017</creationdate><topic>Amino acids</topic><topic>Chemical bonds</topic><topic>Chemistry</topic><topic>Chemistry and Materials Science</topic><topic>Chemistry/Food Science</topic><topic>Design</topic><topic>Genetic code</topic><topic>Interfaces</topic><topic>Peptides</topic><topic>Perspectives</topic><topic>Proteins</topic><topic>Science</topic><topic>Selenium</topic><topic>Transfer RNA</topic><topic>交联剂</topic><topic>免疫共沉淀</topic><topic>基因编码</topic><topic>特征</topic><topic>蛋白质-蛋白质相互作用</topic><topic>裂解</topic><topic>质子泵抑制剂</topic><topic>酵母双杂交</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Lin, Zhi</creatorcontrib><creatorcontrib>Xie, Xiao</creatorcontrib><creatorcontrib>Chen, Peng R.</creatorcontrib><collection>中文科技期刊数据库</collection><collection>中文科技期刊数据库-CALIS站点</collection><collection>中文科技期刊数据库-7.0平台</collection><collection>中文科技期刊数据库- 镜像站点</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Science Database (Alumni Edition)</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Technology Collection</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Materials Science & Engineering Collection</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>ProQuest Central</collection><collection>Technology Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Materials Science Collection</collection><collection>ProQuest Central Korea</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>Materials Science Database</collection><collection>Science Database</collection><collection>Materials Science Collection</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>ProQuest Central Basic</collection><jtitle>Science China. 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China Chem</stitle><addtitle>SCIENCE CHINA Chemistry</addtitle><date>2017-02-01</date><risdate>2017</risdate><volume>60</volume><issue>2</issue><spage>167</spage><epage>169</epage><pages>167-169</pages><issn>1674-7291</issn><eissn>1869-1870</eissn><abstract>Protein-protein interactions（PPIs）play vital roles in biological processes.However,the discovery of transient and biologically relevant PPIs remain a formidable challenge using conventional strategies such as co-immunoprecipitation（CoIP）,yeast two hybrids（Y2H）and Forster resonance energy transfer（FRET）[1].Genetically encoded photocrosslinkers have recently emerged as a powerful approach for probing intracellular PPIs with the capability for in situ studies,low perturbation to cells as well as the wide generality.This facile strategy also demonstrated an advantage of high spatiotemporal resolution,which offers a robust capture strategy for the discovery of transient and/or weak PPIs with lowered false-positive backgrounds[2].</abstract><cop>Beijing</cop><pub>Science China Press</pub><doi>10.1007/s11426-016-0452-6</doi><tpages>3</tpages></addata></record> |
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| subjects | Amino acids Chemical bonds Chemistry Chemistry and Materials Science Chemistry/Food Science Design Genetic code Interfaces Peptides Perspectives Proteins Science Selenium Transfer RNA 交联剂 免疫共沉淀 基因编码 特征 蛋白质-蛋白质相互作用 裂解 质子泵抑制剂 酵母双杂交 |
| title | Kicking down the ladder： adding cleavable features to genetically encoded photocrosslinkers |
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