The erlin2 T65I mutation inhibits erlin1/2 complex–mediated inositol 1,4,5-trisphosphate receptor ubiquitination and phosphatidylinositol 3-phosphate binding von Wright, Forrest A., Bonzerato, Caden G., Sliter, Danielle A., Wojcikiewicz, Richard J.H.

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Bok: real killer or bystander with non-apoptotic roles? von Bonzerato, Caden G, Wojcikiewicz, Richard J H

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Identification of the Bok Interactome Using Proximity Labeling von Szczesniak, Laura M, Bonzerato, Caden G, Wojcikiewicz, Richard J H

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Endogenous Bok is stable at the endoplasmic reticulum membrane and does not mediate proteasome inhibitor-induced apoptosis von Bonzerato, Caden G, Keller, Katherine R, Schulman, Jacqualyn J, Gao, Xiaokong, Szczesniak, Laura M, Wojcikiewicz, Richard J H

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Binding of the erlin1/2 complex to the third intralumenal loop of IP3R1 triggers its ubiquitin-proteasomal degradation von Gao, Xiaokong, Bonzerato, Caden G., Wojcikiewicz, Richard J.H.

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The erlin1/erlin2 complex binds to and stabilizes phosphatidylinositol 3-phosphate and regulates autophagy von Hua, Fanghui, Bonzerato, Caden G., Keller, Katherine R., Guo, Dandan, Luo, Juntao, Wojcikiewicz, Richard J.H.

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The ubiquitin-proteasome pathway inhibitor TAK-243 has major effects on calcium handling in mammalian cells von Gao, Xiaokong, Keller, Katherine R., Bonzerato, Caden G., Li, Peng, Laemmerhofer, Michael, Wojcikiewicz, Richard J.H.

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Bok binds to a largely disordered loop in the coupling domain of type 1 inositol 1,4,5-trisphosphate receptor von Szczesniak, Laura M., Bonzerato, Caden G., Schulman, Jacqualyn J., Bah, Alaji, Wojcikiewicz, Richard J.H.

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Binding of the erlin1/2 complex to the third intralumenal loop of IP 3 R1 triggers its ubiquitin-proteasomal degradation von Gao, Xiaokong, Bonzerato, Caden G, Wojcikiewicz, Richard J H

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