Sicheri, Frank - University of Toronto - Department of Biochemistry

研究领域

Our research is directed at furthering the understanding of protein kinase regulation with a particular focus towards the underlying structural mechanism that imparts specificity to signalling function. We seek to uncover the structural basis for novel catalytic switching, substrate recognition and down-stream phosphoregulatory mechanisms. In addition, we are interested in uncovering the structure and function of new proteins and activities that impact protein kinase function. These efforts have recently led our lab into the area of ubiquitin directed proteolysis. Our long-term goal is to make use of what we learn about protein kinases and phosphoregulatory systems to develop drugs to treat human disease.

近期论文

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MOB1 mediated phospho-recognition in the core mammalian Hippo pathway. Couzens AL, Xiong S, Knight JD, Mao DY, Guettler S, Picaud S, Kurinov I, Filippakopoulos P, Sicheri F, Gingras AC. Mol Cell Proteomics. 2017 Apr 3. pii: mcp.M116.065490. doi: 10.1074/mcp.M116.065490. [Epub ahead of print] PMID: 28373298 Free Article Similar articles Select item 28373297 Regulation of protein interactions by MOB1 phosphorylation. Xiong S, Couzens AL, Kean MJ, Mao DY, Guettler S, Kurinov I, Gingras AC, Sicheri F. Mol Cell Proteomics. 2017 Apr 3. pii: mcp.M117.068130. doi: 10.1074/mcp.M117.068130. [Epub ahead of print] PMID: 28373297 Free Article Similar articles Select item 28276594 Structural and functional characterization of a ubiquitin variant engineered for tight and specific binding to an alpha-helical ubiquitin interacting motif. Manczyk N, Yates BP, Veggiani G, Ernst A, Sicheri F, Sidhu SS. Protein Sci. 2017 Mar 9. doi: 10.1002/pro.3155. [Epub ahead of print] PMID: 28276594 Similar articles Select item 28115697 Mechanism of catalysis, E2 recognition, and autoinhibition for the IpaH family of bacterial E3 ubiquitin ligases. Keszei AF, Sicheri F.