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The Journal of Biological Chemistry|July 26, 2013
The Bcl-2 protein family member Bok binds to the coupling domain of inositol 1,4,5-trisphosphate receptors and protects them from proteolytic cleavageJacqualyn J Schulman, Forrest A Wright, Thomas Kaufmann, et al.Biochemical and Biophysical Research Communications|March 27, 2021
Bok binds to a largely disordered loop in the coupling domain of type 1 inositol 1,4,5-trisphosphate receptorLaura M Szczesniak, Caden G Bonzerato, Jacqualyn J Schulman, et al.Frontiers in Cell and Developmental Biology|January 5, 2023
Endogenous Bok is stable at the endoplasmic reticulum membrane and does not mediate proteasome inhibitor-induced apoptosisCaden G Bonzerato, Katherine R Keller, Jacqualyn J Schulman, et al.The Journal of Biological Chemistry|April 8, 2016
The Stability and Expression Level of Bok Are Governed by Binding to Inositol 1,4,5-Trisphosphate ReceptorsJacqualyn J Schulman, Forrest A Wright, Xiaobing Han, et al.Cell Death and Differentiation|April 13, 2019
Bok regulates mitochondrial fusion and morphologyJacqualyn J Schulman, Laura M Szczesniak, Eric N Bunker, et al.Pageof 1