James G. Omichinski

Affiliations: 
Faculte de medecine Université de Montréal, Montréal, Canada 
Area:
Molecular Biology, Biochemistry
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"James Omichinski"
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Publications

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Lussier-Price M, Mascle XH, Cappadocia L, et al. (2020) Characterization of a C-Terminal SUMO-Interacting Motif Present in Select PIAS-Family Proteins. Structure (London, England : 1993). 28: 573-585.e5
Mascle XH, Gagnon C, Wahba HM, et al. (2019) Acetylation of SUMO1 Alters Interactions with the SIMs of PML and Daxx in a Protein-Specific Manner. Structure (London, England : 1993)
Sakaguchi T, Janairo JIB, Lussier-Price M, et al. (2017) Oligomerization enhances the binding affinity of a silver biomineralization peptide and catalyzes nanostructure formation. Scientific Reports. 7: 1400
Lecoq L, Raiola L, Chabot PR, et al. (2017) Structural characterization of interactions between transactivation domain 1 of the p65 subunit of NF-κB and transcription regulatory factors. Nucleic Acids Research
Desrochers G, Cappadocia L, Lussier-Price M, et al. (2017) Molecular Basis of Interactions Between SH3 Domain-Containing Proteins and the Proline-Rich Region of the Ubiquitin Ligase Itch. The Journal of Biological Chemistry
Desrochers G, Lussier-Price M, Omichinski JG, et al. (2016) Correction to Multiple Src Homology 3 Binding to the Ubiquitin Ligase Itch Conserved Proline-Rich Region. Biochemistry. 55: 3174
Wahba H, Lecoq L, Stevenson MJ, et al. (2016) Structural and biochemical characterization of a copper-binding mutant of the organomercurial lyase MerB: Insight into the key role of the active site aspartic acid in both Hg-carbon bond cleavage and metal-binding specificity. Biochemistry
Riahi N, Cappadocia L, Henry O, et al. (2016) Soluble expression, purification and functional characterization of a coil peptide composed of a positively charged and hydrophobic motif. Amino Acids. 48: 567-77
Desrochers G, Lussier-Price M, Omichinski JG, et al. (2015) Multiple Src Homology 3 Binding to the Ubiquitin Ligase Itch Conserved Proline-Rich Region. Biochemistry. 54: 7345-54
Cyr N, de la Fuente C, Lecoq L, et al. (2015) A ΩXaV motif in the Rift Valley fever virus NSs protein is essential for degrading p62, forming nuclear filaments and virulence. Proceedings of the National Academy of Sciences of the United States of America. 112: 6021-6
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