The Bcl-2 Protein Family Member Bok Binds to the Coupling Domain of Inositol 1,4,5-Trisphosphate Receptors and Protects Them from Proteolytic Cleavage by Schulman, Jacqualyn J., Wright, Forrest A., Kaufmann, Thomas, Wojcikiewicz, Richard J.H.

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The Stability and Expression Level of Bok Are Governed by Binding to Inositol 1,4,5-Trisphosphate Receptors by Schulman, Jacqualyn J., Wright, Forrest A., Han, Xiaobing, Zluhan, Eric J., Szczesniak, Laura M., 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 by Bonzerato, Caden G, Keller, Katherine R, Schulman, Jacqualyn J, Gao, Xiaokong, Szczesniak, Laura M, Wojcikiewicz, Richard J H

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Bok regulates mitochondrial fusion and morphology by Schulman, Jacqualyn J., Szczesniak, Laura M., Bunker, Eric N., Nelson, Heather A., Roe, Michael W., Wagner, Larry E., Yule, David I., 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 by Szczesniak, Laura M., Bonzerato, Caden G., Schulman, Jacqualyn J., Bah, Alaji, Wojcikiewicz, Richard J.H.

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c-Abl Mediated Tyrosine Phosphorylation of Aha1 Activates Its Co-chaperone Function in Cancer Cells by Dunn, Diana M., Woodford, Mark R., Truman, Andrew W., Jensen, Sandra M., Schulman, Jacqualyn, Caza, Tiffany, Remillard, Taylor C., Loiselle, David, Wolfgeher, Donald, Blagg, Brian S.J., Franco, Lucas, Haystead, Timothy A., Daturpalli, Soumya, Mayer, Matthias P., Trepel, Jane B., Morgan, Rhodri M.L., Prodromou, Chrisostomos, Kron, Stephen J., Panaretou, Barry, Stetler-Stevenson, William G., Landas, Steve K., Neckers, Len, Bratslavsky, Gennady, Bourboulia, Dimitra, Mollapour, Mehdi

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