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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.
Research Interests
Papers共 174 篇Author StatisticsCo-AuthorSimilar Experts
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Natureno. 8012 (2024): E12-E12
NATURE (2024)
Paul M.C. Park, Jiho Park,Jared Brown,Moritz Hunkeler,Shourya S. Roy Burman,Katherine A. Donovan,Hojong Yoon, Radosław P. Nowak, Mikołaj Słabicki,Benjamin L. Ebert,Eric S. Fischer
Molecular Cellno. 13 (2024): 2511-2524.e8
Natureno. 8007 (2024): 442-449
RSC MEDICINAL CHEMISTRYno. 2 (2024): 607-611
Han-Yuan Liu,Zhengnian Li, Theresia Reindl,Zhixiang He, Xueer Qiu, Ryan P Golden,Katherine A Donovan, Adam Bailey,Eric S Fischer,Tinghu Zhang,Nathanael S Gray,Priscilla L Yang
Nature communicationsno. 1 (2024): 5179-5179
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 the preprint server for biology (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)
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