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Page 1
Bok regulates mitochondrial fusion and morphology.
Cell Death Differ. 2019 Dec;26(12):2682-2694. doi: 10.1038/s41418-019-0327-4. Epub 2019 Apr 11.
Cell Death Differ. 2019.
PMID: 30976095
Free PMC article.
Endogenous Bok is stable at the endoplasmic reticulum membrane and does not mediate proteasome inhibitor-induced apoptosis.
Bonzerato CG, Keller KR, Schulman JJ, Gao X, Szczesniak LM, Wojcikiewicz RJH.
Bonzerato CG, et al. Among authors: schulman jj.
Front Cell Dev Biol. 2022 Dec 19;10:1094302. doi: 10.3389/fcell.2022.1094302. eCollection 2022.
Front Cell Dev Biol. 2022.
PMID: 36601536
Free PMC article.
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Bok binds to a largely disordered loop in the coupling domain of type 1 inositol 1,4,5-trisphosphate receptor.
Szczesniak LM, Bonzerato CG, Schulman JJ, Bah A, Wojcikiewicz RJH.
Szczesniak LM, et al. Among authors: schulman jj.
Biochem Biophys Res Commun. 2021 May 14;553:180-186. doi: 10.1016/j.bbrc.2021.03.047. Epub 2021 Mar 24.
Biochem Biophys Res Commun. 2021.
PMID: 33773141
Free PMC article.
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The Stability and Expression Level of Bok Are Governed by Binding to Inositol 1,4,5-Trisphosphate Receptors.
Schulman JJ, Wright FA, Han X, Zluhan EJ, Szczesniak LM, Wojcikiewicz RJ.
Schulman JJ, et al.
J Biol Chem. 2016 May 27;291(22):11820-8. doi: 10.1074/jbc.M115.711242. Epub 2016 Apr 6.
J Biol Chem. 2016.
PMID: 27053113
Free PMC article.
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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.
Schulman JJ, Wright FA, Kaufmann T, Wojcikiewicz RJH.
Schulman JJ, et al.
J Biol Chem. 2013 Aug 30;288(35):25340-25349. doi: 10.1074/jbc.M113.496570. Epub 2013 Jul 24.
J Biol Chem. 2013.
PMID: 23884412
Free PMC article.
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