E
Enrico O. Purisima
Researcher at National Research Council
Publications - 91
Citations - 3835
Enrico O. Purisima is an academic researcher from National Research Council. The author has contributed to research in topics: Solvation & Cathepsin L. The author has an hindex of 30, co-authored 87 publications receiving 3601 citations. Previous affiliations of Enrico O. Purisima include François Rabelais University.
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Journal ArticleDOI
Small molecule obatoclax (GX15-070) antagonizes MCL-1 and overcomes MCL-1-mediated resistance to apoptosis
Mai Nguyen,Richard C. Marcellus,Anne Roulston,Mark F. Watson,Lucile Serfass,S.R. Murthy Madiraju,Daniel Goulet,Jean Viallet,Laurent Bélec,Xavier Billot,Stephane Acoca,Enrico O. Purisima,Adrian Wiegmans,Leonie A. Cluse,Ricky W. Johnstone,Pierre Beauparlant,Gordon C. Shore +16 more
TL;DR: Findings support a rational clinical development opportunity for the compound in cancer indications or treatments where MCL-1 contributes to resistance to cell killing.
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Role of the occluding loop in cathepsin B activity.
Chantal Illy,Omar Quraishi,Omar Quraishi,Jing Wang,Enrico O. Purisima,Thierry Vernet,John S. Mort +6 more
TL;DR: The results suggest that the endopeptidase activity of cathepsin B is an evolutionary remnant since, as a consequence of its membership in the papain family, the propeptide must be able to bind unobstructed through the full length of the active site cleft.
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A simple yet accurate boundary element method for continuum dielectric calculations
TL;DR: It is shown that the limiting factor in accuracy is not the evaluation of integrals involving the interaction between boundary elements but rather a proper estimation of the self‐polarization of a patch upon itself, and a sum rule is derived that allows us to calculate this important self‐ polarization term in a self‐consistent and simple way.
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Molecular dynamics-solvated interaction energy studies of protein-protein interactions: the MP1-p14 scaffolding complex.
Qizhi Cui,Traian Sulea,Joseph D. Schrag,Christine Munger,Ming-Ni Hung,Marwen Naim,Miroslaw Cygler,Miroslaw Cygler,Enrico O. Purisima +8 more
TL;DR: The sensitized protein-protein interface afforded by the p14(Y56A) mutation identified here has practical applications in screening-based discovery of first-generation small-molecule hits for further development into specific modulators of the mitogen-activated protein kinase signaling pathway.
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MicroRNAs preferentially target the genes with high transcriptional regulation complexity.
TL;DR: Gene ontology analysis reveals that the genes with higher cis-regulation complexity are more coordinately regulated by TFs at the transcriptional level and by miRNAs at the post-transcriptional level, which is a potentially novel discovery of mechanism for coordinated regulation of gene expression.