Research Topics
Genomes and Genes | Silke WiesnerSummaryAffiliation: University of Toronto Country: Canada Publications
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Detail Information
Publications
Autoinhibition of the HECT-type ubiquitin ligase Smurf2 through its C2 domainSilke Wiesner
Hospital for Sick Children, 555 University Avenue, Toronto, Ontario M5G 1X8, Canada
Cell 130:651-62. 2007..Thus, interactions between C2 and HECT domains autoinhibit a subset of HECT-type E3s to protect them and their substrates from futile degradation in cells...
The ubiquitin binding region of the Smurf HECT domain facilitates polyubiquitylation and binding of ubiquitylated substratesAbiodun A Ogunjimi
Center for Systems Biology, Samuel Lunenfeld Research Institute, Mount Sinai Hospital, Toronto, Ontario M5G 1X5, Canada
J Biol Chem 285:6308-15. 2010..Our findings suggest the UBS promotes polyubiquitylation by stabilizing ubiquitylated substrate binding to the HECT domain...
Structural studies of FF domains of the transcription factor CA150 provide insights into the organization of FF domain tandem arraysJames M Murphy
Samuel Lunenfeld Research Institute, Mount Sinai Hospital, Toronto, Ontario, Canada
J Mol Biol 393:409-24. 2009....
An exchange-free measure of 15N transverse relaxation: an NMR spectroscopy application to the study of a folding intermediate with pervasive chemical exchangeD Flemming Hansen
Department of Medical Genetics, The University of Toronto, Toronto, Ontario, Canada, M5S 1A8
J Am Chem Soc 129:11468-79. 2007....
A change in conformational dynamics underlies the activation of Eph receptor tyrosine kinasesSilke Wiesner
Structural Biology and Biochemistry, Hospital for Sick Children, Toronto, Ontario, Canada
EMBO J 25:4686-96. 2006....
Fractional 13C enrichment of isolated carbons using [1-13C]- or [2- 13C]-glucose facilitates the accurate measurement of dynamics at backbone Calpha and side-chain methyl positions in proteinsPatrik Lundström
Department of Medical Genetics, The University of Toronto, Toronto, ON, Canada, M5S 1A8
J Biomol NMR 38:199-212. 2007..The utility of the labeling is established by recording (13)C R (1rho) and CPMG-based experiments on a number of different protein systems...
The structure of Prp40 FF1 domain and its interaction with the crn-TPR1 motif of Clf1 gives a new insight into the binding mode of FF domainsAlexander Gasch
Structural Biology Program, EMBL Heidelberg, Meyerhofstrasse 1, 69117 Heidelberg, Germany
J Biol Chem 281:356-64. 2006..Our results also revealed that not all FF domains in Prp40 are functionally equivalent. We proposed that at least two different interaction surfaces exist in FF domains that have evolved to recognize distinct binding motifs...
NMR Assignment Reveals an alpha-Helical Fold for the F-Actin Binding Domain of Human Bcr-Abl/c-AblSilke Wiesner
J Biomol NMR 32:335. 2005
Structural basis for the cytoskeletal association of Bcr-Abl/c-AblOliver Hantschel
Center for Molecular Medicine of the Austrian Academy of Sciences, Lazarettgasse 19/3, 1090 Vienna, Austria
Mol Cell 19:461-73. 2005..We propose that these interactions represent a major determinant for both Bcr-Abl and c-Abl localization...
Solution structure and ligand recognition of the WW domain pair of the yeast splicing factor Prp40Silke Wiesner
Structural Biology Programme, EMBL Heidelberg, Meyerhofstr 1, 69117 Heidelberg, Germany
J Mol Biol 324:807-22. 2002..In contrast, no interaction was observed between the Prp40 WW domains and the CTD repeats used in this work...
Interactions between the three CIN85 SH3 domains and ubiquitin: implications for CIN85 ubiquitinationIrina Bezsonova
Department of Chemistry, University of Toronto, 80 St George Street, Toronto, ON, Canada M5S 1A8
Biochemistry 47:8937-49. 2008..These results suggest that competition between Cbl and ubiquitin binding to CIN85 regulates Cbl function and EGFR endocytosis...
WW and SH3 domains, two different scaffolds to recognize proline-rich ligandsMaria J Macias
Structural and Computational Biology Program, EMBL Heidelberg, Heidelberg, Germany
FEBS Lett 513:30-7. 2002..The binding surface of the modeled WW domain of Npw38 protein shows a remarkable similarity to the SH3 domain of Sem5 protein, confirming biochemical data on similar binding predilections of both domains...
