Search Results - "Iwase, Reina"

The structural basis of PTEN regulation by multi-site phosphorylation by Dempsey, Daniel R., Viennet, Thibault, Iwase, Reina, Park, Eunyoung, Henriquez, Stephanie, Chen, Zan, Jeliazkov, Jeliazko R., Palanski, Brad A., Phan, Kim L., Coote, Paul, Gray, Jeffrey J., Eck, Michael J., Gabelli, Sandra B., Arthanari, Haribabu, Cole, Philip A.

“…Phosphatase and tensin homolog (PTEN) is a phosphatidylinositol-3,4,5-triphosphate (PIP 3 ) phospholipid phosphatase that is commonly mutated or silenced in…”
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Dynamic regulation of inter-organelle communication by ubiquitylation controls skeletal muscle development and disease onset by Mansur, Arian, Joseph, Remi, Kim, Euri S, Jean-Beltran, Pierre M, Udeshi, Namrata D, Pearce, Cadence, Jiang, Hanjie, Iwase, Reina, Milev, Miroslav P, Almousa, Hashem A, McNamara, Elyshia, Widrick, Jeffrey, Perez, Claudio, Ravenscroft, Gianina, Sacher, Michael, Cole, Philip A, Carr, Steven A, Gupta, Vandana A

“…Ubiquitin-proteasome system (UPS) dysfunction is associated with the pathology of a wide range of human diseases, including myopathies and muscular atrophy…”
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Interaction Energetics and Druggability of the Protein–Protein Interaction between Kelch-like ECH-Associated Protein 1 (KEAP1) and Nuclear Factor Erythroid 2 Like 2 (Nrf2) by Zhong, Mengqi, Lynch, Andrew, Muellers, Samantha N, Jehle, Stefan, Luo, Lingqi, Hall, David R, Iwase, Reina, Carolan, James P, Egbert, Megan, Wakefield, Amanda, Streu, Kristina, Harvey, Christine M, Ortet, Paula C, Kozakov, Dima, Vajda, Sandor, Allen, Karen N, Whitty, Adrian

“…Development of small molecule inhibitors of protein–protein interactions (PPIs) is hampered by our poor understanding of the druggability of PPI target sites…”
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Semisynthetic Approach to the Analysis of Tumor Suppressor PTEN Ubiquitination by Iwase, Reina, Dempsey, Daniel R., Whedon, Samuel D., Jiang, Hanjie, Palanski, Brad A., Deng, Bedphiny, Cole, Philip A.

“…Phosphatase and tensin homologue (PTEN) tumor suppressor protein is a PIP3 lipid phosphatase that is subject to multifaceted post-translational modifications…”
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