基本信息
浏览量:77
职业迁徙
个人简介
We combine structural biology, cell biology and biochemical reconstitutions to address the molecular workings of multi-protein ubiquitin ligase complexes. In particular, we are interested in protein complexes and pathways that contribute to the control of gene expression and are frequently associated with human disease and cancer.
Research:
The Ubiquitin Proteasome System (UPS) is involved in virtually any cellular process and frequently implicated in human pathologies. Ubiquitin, through the action of a three-enzyme cascade (E1, E2 and E3), is covalently attached to substrate proteins. The posttranslational modification with ubiquitin can serve a multitude of functions depending on the type and length of the ubiquitin chain attached to the substrate, including the control of protein abundance via proteasomal degradation. The human genome encodes for more than 600 E3 ligases, which confer specificity in the ubiquitin signaling cascade. While the process of ubiquitin transfer is well understood, the biological function and molecular mechanisms of the majority of ubiquitin ligases remain obscure.
We combine structural biology, cell biology and biochemical reconstitutions to address the molecular workings of multi-protein ubiquitin ligase complexes. In particular, we are interested in protein complexes and pathways that contribute to the control of gene expression and are frequently associated with human disease and cancer. Intimate understanding of the structure allows us to dissect the complex mechanisms that underlie function and regulation of such molecules and to probe their biology in a cellular context.
We seek to leverage our molecular understanding to propose and test new avenues of therapeutic intervention. We are also interested in small molecules targeting the UPS such as the anti-cancer therapeutics thalidomide and derivatives. As before, we utilize a broad toolset of structural biology, proteomics, cell biology and biochemical reconstitutions to elucidate their activities and precise mode of action.
Research:
The Ubiquitin Proteasome System (UPS) is involved in virtually any cellular process and frequently implicated in human pathologies. Ubiquitin, through the action of a three-enzyme cascade (E1, E2 and E3), is covalently attached to substrate proteins. The posttranslational modification with ubiquitin can serve a multitude of functions depending on the type and length of the ubiquitin chain attached to the substrate, including the control of protein abundance via proteasomal degradation. The human genome encodes for more than 600 E3 ligases, which confer specificity in the ubiquitin signaling cascade. While the process of ubiquitin transfer is well understood, the biological function and molecular mechanisms of the majority of ubiquitin ligases remain obscure.
We combine structural biology, cell biology and biochemical reconstitutions to address the molecular workings of multi-protein ubiquitin ligase complexes. In particular, we are interested in protein complexes and pathways that contribute to the control of gene expression and are frequently associated with human disease and cancer. Intimate understanding of the structure allows us to dissect the complex mechanisms that underlie function and regulation of such molecules and to probe their biology in a cellular context.
We seek to leverage our molecular understanding to propose and test new avenues of therapeutic intervention. We are also interested in small molecules targeting the UPS such as the anti-cancer therapeutics thalidomide and derivatives. As before, we utilize a broad toolset of structural biology, proteomics, cell biology and biochemical reconstitutions to elucidate their activities and precise mode of action.
研究兴趣
论文共 168 篇作者统计合作学者相似作者
按年份排序按引用量排序主题筛选期刊级别筛选合作者筛选合作机构筛选
时间
引用量
主题
期刊级别
合作者
合作机构
Sandi Radko-Juettner,Hong Yue,Jacquelyn A. Myers, Raymond D. Carter, Alexis N. Robertson,Priya Mittal,Zhexin Zhu,Baranda S. Hansen,Katherine A. Donovan,Moritz Hunkeler,Wojciech Rosikiewicz,Zhiping Wu,
NATURE (2024)
Sandi Radko-Juettner,Hong Yue,Jacquelyn A Myers, Raymond D Carter, Alexis N Robertson,Priya Mittal,Zhexin Zhu,Baranda S Hansen,Katherine A Donovan,Moritz Hunkeler,Wojciech Rosikiewicz,Zhiping Wu,
Natureno. 8012 (2024): E12-E12
Sandi Radko-Juettner,Hong Yue,Jacquelyn A. Myers, Raymond D. Carter, Alexis N. Robertson,Priya Mittal,Zhexin Zhu,Baranda S. Hansen,Katherine A. Donovan,Moritz Hunkeler,Wojciech Rosikiewicz,Zhiping Wu,
Sandi Radko-Juettner,Hong Yue,Jacquelyn A Myers, Raymond D Carter, Alexis N Robertson,Priya Mittal,Zhexin Zhu,Baranda S Hansen,Katherine A Donovan,Moritz Hunkeler,Wojciech Rosikiewicz,Zhiping Wu,
Natureno. 8007 (2024): 442-449
Yingpeng Liu,Radoslaw P. Nowak,Jianwei Che,Katherine A. Donovan, Fidel Huerta, Hu Liu,Rebecca J. Metivier,Eric S. Fischer,Lyn H. Jones
RSC MEDICINAL CHEMISTRYno. 2 (2024): 607-611
Nature Chemistryno. 2 (2024): 218-228
Sandi Radko-Juettner,Hong Yue,Jacquelyn A. Myers, Raymond D. Carter, Alexis N. Robertson,Priya Mittal,Zhexin Zhu,Baranda S. Hansen,Katherine A. Donovan,Moritz Hunkeler,Wojciech Rosikiewicz,Zhiping Wu,
Naturepp.1-8, (2024)
Hlib Razumkov, Zixuan Jiang, Kheewoong Baek,Inchul You, Qixiang Geng,Katherine A. Donovan, Michelle T. Tang,Rebecca J. Metivier,Nada Mageed, Pooreum Seo,Zhengnian Li,Woong Sub Byun,
biorxiv(2024)
Hai-Tsang Huang,Ryan J. Lumpkin, Ryan W. Tsai, Shuyao Su, Xu Zhao,Yuan Xiong,James Chen,Nada Mageed,Katherine A. Donovan,Eric S. Fischer,William R. Sellers
Nature Chemical Biologypp.1-10, (2024)
Hai-Tsang Huang,Ryan J. Lumpkin, Ryan W. Tsai,Katherine A. Donovan, Shuyao Su, Xu Zhao, James Chen,Eric S. Fischer, William R. Sellers
Cancer Researchno. 6_Supplement (2024): 3885-3885
加载更多
作者统计
合作学者
合作机构
D-Core
- 合作者
- 学生
- 导师
数据免责声明
页面数据均来自互联网公开来源、合作出版商和通过AI技术自动分析结果,我们不对页面数据的有效性、准确性、正确性、可靠性、完整性和及时性做出任何承诺和保证。若有疑问,可以通过电子邮件方式联系我们:report@aminer.cn