Affinage

BOK

Bcl-2-related ovarian killer protein · UniProt Q9UMX3

Length
212 aa
Mass
23.3 kDa
Annotated
2026-06-09
88 papers in source corpus 35 papers cited in narrative 35 extracted findings
Cross-family judge vs UniProt: Affinage preferred faithfulness: 9/9 claims corpus-supported (100%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

BOK is a pro-apoptotic BCL-2 family effector that links endoplasmic reticulum/Golgi membrane biology to mitochondrial outer membrane permeabilization (MOMP) and intrinsic apoptosis (PMID:9356461, PMID:23429263, PMID:26949185). It was originally defined by a BH1/BH2/BH3-domain architecture lacking BH4 and a selective heterodimerization pattern with anti-apoptotic Mcl-1, Bfl-1, and BHRF1 but not Bcl-2, Bcl-xL, or Bcl-w (PMID:9356461). Endogenous BOK is tail-anchored at the ER and Golgi membranes (PMID:23429263), where it binds strongly and constitutively to inositol-1,4,5-trisphosphate receptors, preferring IP3R1/IP3R2, through a high-affinity site within the largely disordered IP3R1 coupling-domain loop (residues ~1898–1940) (PMID:23884412, PMID:33773141). Through this interaction BOK suppresses IP3R-mediated Ca2+ release—an inhibition relieved by PKA-mediated Ser-8 phosphorylation that weakens BOK–IP3R1 binding (PMID:39810210)—and establishes ER–mitochondria proximity and the ER-to-mitochondria Ca2+ transfer required for ER-stress-induced apoptosis (PMID:33691099). Consistent with this ER-centric role, Bok-deficient cells are selectively defective in apoptosis triggered by ER stressors and show an attenuated unfolded protein response and reduced chaperone availability (PMID:26015568, PMID:36060797). BOK can act as a non-canonical MOMP effector that triggers cytochrome c release independently of BAX and BAK; its activity is metastability-driven rather than dependent on activator BH3 ligands, and a stabilizing helix-α1 glycine substitution inhibits permeabilization (PMID:26949185, PMID:29768206). BOK is held at low abundance by AMFR/gp78-mediated ubiquitylation and VCP/p97-dependent proteasomal degradation, with IP3R binding stabilizing the protein, so that stabilization (by proteasome/VCP/gp78 impairment or loss of degradation machinery) permits BOK-driven apoptosis (PMID:26949185, PMID:36601536). Beyond cell death, BOK promotes mitochondrial fusion and regulates mitochondrial morphology and bioenergetics (PMID:27098698, PMID:30976095), and it enhances uridine monophosphate synthetase (UMPS) activity to support uridine biosynthesis, chemosensitivity to 5-fluorouracil, and genomic stability (PMID:31311867, PMID:41611842). Its pro-apoptotic activity is restrained by anti-apoptotic partners through both BH3-groove and transmembrane-domain interactions, the latter mediating selective inhibition by MCL-1 and by BCL-2 at the ER membrane (PMID:30127460, PMID:39048751).

Mechanistic history

Synthesis pass · year-by-year structured walk · 25 steps
  1. 1997 High

    Established BOK as a distinct pro-apoptotic BCL-2 family member, defining its domain content and an unusual selective binding to a subset of anti-apoptotic proteins.

    Evidence Yeast two-hybrid screening and mammalian overexpression/rescue assays

    PMID:9356461

    Open questions at the time
    • Did not address endogenous localization or physiological function
    • Heterodimerization specificity not mapped to structural determinants
  2. 1998 High

    Showed heterodimerization with anti-apoptotic proteins is dispensable for BOK killing, decoupling its pro-apoptotic activity from BH3-mediated binding.

    Evidence Splice-variant and BH3 mutagenesis with in vitro binding and cell-death assays

    PMID:9804769

    Open questions at the time
    • Mechanism of killing independent of dimerization not defined
    • Endogenous relevance of the splice variant not established
  3. 2004 Medium

    Placed BOK in the p53-dependent DNA-damage apoptosis pathway upstream of cytochrome c release.

    Evidence p53 activation, protein-synthesis inhibition, and cytochrome c translocation assays in tumor cells

    PMID:15102863

    Open questions at the time
    • No BOK knockout validation of the requirement
    • Direct vs indirect role in cytochrome c release unresolved
  4. 2006 Medium

    Identified transcriptional (E2F) and post-translational (Crm1-mediated nuclear export) controls on BOK abundance and localization.

    Evidence ChIP/luciferase promoter analysis and leptomycin B/Co-IP localization studies

    PMID:16302269 PMID:16772296

    Open questions at the time
    • Functional consequence of nuclear BOK pool unclear
    • Cell-cycle coupling of BOK function not demonstrated
  5. 2013 High

    Defined BOK as a tail-anchored ER/Golgi membrane protein that constitutively binds IP3R1/2 at a discrete coupling-domain site and protects IP3Rs from proteolysis.

    Evidence Subcellular fractionation, microscopy, reciprocal Co-IP, domain mapping, and protease-protection assays

    PMID:23429263 PMID:23884412

    Open questions at the time
    • Functional consequence of IP3R binding for Ca2+ signaling not yet measured
    • Relationship between membrane localization and MOMP activity unresolved
  6. 2013 Medium

    Demonstrated in vivo that BOK overlaps functionally with BAX (not BAK) in physiological apoptosis using compound knockout mice.

    Evidence Bok/Bax and Bok/Bak compound knockout mice with ovarian histology

    PMID:23744350

    Open questions at the time
    • Molecular basis of BAX-overlap not defined
    • Tissue specificity of overlapping function not generalized
  7. 2015 High

    Established a selective, non-redundant requirement for BOK in ER-stress-induced apoptosis that BAX and BAK cannot compensate.

    Evidence Bok-/- MEFs challenged with multiple ER stressors plus UPR readouts and in vivo challenge

    PMID:26015568

    Open questions at the time
    • Mechanistic link between ER localization and apoptotic execution not yet defined
    • Whether the effect requires IP3R binding untested at this stage
  8. 2016 High

    Defined BOK as a constitutively active, BAX/BAK-independent MOMP effector whose activity is governed primarily by gp78/VCP-dependent proteasomal degradation.

    Evidence BAX/BAK-DKO cells, ubiquitylation assays, gp78/VCP knockdown, and MOMP/apoptosis readouts

    PMID:26949185 PMID:27076518

    Open questions at the time
    • Whether endogenous BOK acts this way under physiological conditions later contested
    • Structural basis of constitutive activity not resolved here
  9. 2016 High

    Revealed a non-apoptotic, MCL-1-dependent role for BOK in neuronal mitochondrial bioenergetics and calcium homeostasis under metabolic stress.

    Evidence Bok-/- neurons with calcium imaging, bioenergetics, MCL-1 rescue, and in vivo seizure/ischemia models

    PMID:27098698

    Open questions at the time
    • Mechanism by which BOK maintains MCL-1 levels unclear
    • Connection between bioenergetic and apoptotic roles not unified
  10. 2017 Medium

    Mapped multiple layers of BOK abundance control: post-transcriptional repression by TRIM28 and miR-296-5p, ER-associated DNAJB12/gp78 turnover, and a MAL/MRTF-SRF transcriptional input.

    Evidence RNA pulldown/reporter assays, Co-IP of degradation complexes, and ChIP/reporter promoter analysis

    PMID:22185759 PMID:28536268 PMID:29156771 PMID:30471638

    Open questions at the time
    • Relative contribution of each regulatory layer in vivo unknown
    • Integration of transcriptional and degradative control not defined
  11. 2017 Medium

    Tested BOK's intrinsic membrane-permeabilizing activity, showing it forms toroidal pores in liposomes but fails to permeabilize native BAX/BAK-null mitochondria.

    Evidence Recombinant BOKΔC liposome and isolated-mitochondria permeabilization assays with cBID/BCL-XL

    PMID:28064468

    Open questions at the time
    • Additional factors required for mitochondrial activity unidentified
    • Negative mitochondrial result leaves native mechanism unresolved
  12. 2018 High

    Provided a structural basis for BOK activation as a metastability-driven process distinct from BH3-ligand-driven BAX/BAK activation.

    Evidence NMR structure of the BOK BCL-2 core, stability/denaturation assays, mutagenesis, and reconstituted MOMP

    PMID:29768206

    Open questions at the time
    • Physiological trigger that exposes the metastable conformation unknown
    • Structure of full-length membrane-embedded BOK not determined
  13. 2018 High

    Confirmed structural similarity to BAX/BAK and demonstrated overlapping developmental cell-death function in triple-knockout mice.

    Evidence Structural comparison and Bok/Bax/Bak triple-knockout developmental phenotyping

    PMID:29775594

    Open questions at the time
    • Tissue-level mechanism of the developmental requirement undefined
    • Quantitative contribution of BOK vs BAX/BAK not parsed
  14. 2018 Medium

    Localized inhibition of BOK by anti-apoptotic proteins to both BH3-groove and transmembrane-domain interactions, especially with MCL-1, and revealed BOK's role in CER-driven mitochondrial fission.

    Evidence Domain-deletion/mutagenesis apoptosis and interaction assays; gain/loss-of-function fission assays with DRP1/MFN2 readouts

    PMID:29463805 PMID:30127460

    Open questions at the time
    • TMD interaction structure not resolved in these studies
    • Mechanistic link between BOK and DRP1/MFN2 regulation unclear
  15. 2019 High

    Uncovered two non-canonical BOK functions: positive regulation of UMPS-driven uridine biosynthesis/5-FU sensitivity and promotion of mitochondrial fusion.

    Evidence Bok-/- cells/mice with UMPS activity and 5-FU sensitivity assays; CRISPR-KO mitochondrial fusion-rate, bioenergetics, and rescue with IP3R-binding-deficient mutant

    PMID:30976095 PMID:31311867

    Open questions at the time
    • Mechanism by which BOK enhances UMPS activity not defined
    • How fusion regulation relates to IP3R binding only partially separated
  16. 2020 Medium

    Showed transmembrane-domain heterooligomerization between MCL-1 and BOK occurs at mitochondria and modulates MAM contacts and BOK-dependent death.

    Evidence Split-GFP TMD interaction assay, localization analysis, MD simulation, and BOK-dependent death readouts

    PMID:33093207

    Open questions at the time
    • Structural detail of TMD heterooligomers limited to simulation
    • Physiological stoichiometry of TMD complexes unknown
  17. 2021 High

    Demonstrated that the BOK–IP3R interaction specifically governs ER-to-mitochondria Ca2+ transfer and MAM composition required for ER-stress apoptosis, separable from mere organelle proximity.

    Evidence Bok-/- MEFs, proximity ligation, inducible ER-mitochondria linkers, IP3R-binding mutant rescue, and MAM proteomics

    PMID:33691099

    Open questions at the time
    • Identity of MAM proteins functionally dependent on BOK not fully resolved
    • How Ca2+ transfer couples to MOMP execution undefined
  18. 2021 Medium

    Refined the BOK proximal interactome, confirming proximity to fission (Drp1) and ER-PM (Stim1) machinery and a TMD-dependent physical interaction with MCL-1 distinct from BAK.

    Evidence TurboID proximity labeling/MS, Co-IP, and TMD-deletion mutants

    PMID:34136494

    Open questions at the time
    • Functional consequence of most proximal partners untested
    • Endogenous vs overexpression interactome differences not parsed
  19. 2021 High

    Defined the BOK–IP3R1 binding interface at atomic detail, showing high-affinity multivalent binding to a disordered IP3R1 loop.

    Evidence Disorder prediction, in vitro pulldown with purified proteins/peptides, Kd measurement, and mutagenesis

    PMID:33773141

    Open questions at the time
    • BOK surface mediating binding not co-mapped here
    • Whether binding alters IP3R channel gating not tested in this study
  20. 2022 Medium

    Established IP3R binding as the dominant determinant of endogenous BOK stability and challenged the model of endogenous BOK as a proteasome-controlled constitutive MOMP effector.

    Evidence IP3R-knockout cells, proteasome inhibition, ubiquitylation and stability assays, and TMD mutants

    PMID:36601536

    Open questions at the time
    • Reconciliation with gp78/VCP degradation model incomplete
    • Context determining when endogenous BOK is apoptotically active unclear
  21. 2022 Medium

    Linked BOK to ER proteostasis by showing it sustains the unfolded protein response and chaperone availability.

    Evidence UPR reporter cells and FRAP of GRP78/BiP-eGFP in Bok-deficient cells/neurons

    PMID:36060797

    Open questions at the time
    • Mechanism by which BOK modulates BiP/UPR not defined
    • Whether the effect requires IP3R binding untested
  22. 2022 High

    Identified BOK as a host target hijacked by SARS-CoV-2 M protein to drive BAX/BAK-independent apoptosis via inhibition of BOK ubiquitination.

    Evidence CRISPR-KO/rescue, Co-IP, ubiquitination and domain-deletion assays, and in vivo lentiviral model

    PMID:35022571

    Open questions at the time
    • Generalizability beyond M protein to other viral contexts unknown
    • BH2-domain interaction interface not structurally resolved
  23. 2025 High

    Demonstrated direct functional suppression of IP3R1-mediated Ca2+ mobilization by BOK and identified PKA Ser-8 phosphorylation as a switch reversing this suppression.

    Evidence Ca2+ sensor assays with GPCR stimulation, in vitro PKA phosphorylation of purified proteins, MS, and phosphomimetic mutagenesis

    PMID:39810210

    Open questions at the time
    • Upstream signals controlling PKA-dependent BOK phosphorylation unknown
    • Physiological settings where this switch operates undefined
  24. 2024 High

    Resolved a TMD-mediated mechanism by which anti-apoptotic BCL-2 inhibits BOK at the ER membrane.

    Evidence Split-luciferase TMD interaction in cells, MD simulation of heterotetramers, BCL-2-TMD mutagenesis, and apoptosis assays

    PMID:39048751

    Open questions at the time
    • Structural model rests on simulation rather than experimental structure
    • Relative contribution of TMD vs BH3-groove inhibition in cells not quantified
  25. 2026 Medium

    Connected BOK's UMPS-regulatory activity to genomic stability, creating an ATR-inhibitor synthetic lethality in p53-deficient cancer cells, and identified additional transcriptional and protein-stability regulators.

    Evidence UMPS activity assays, Bok-deficient NSCLC cells with ATR inhibitor, BOK-BH3 peptide rescue, and EGR3 ChIP/reporter analysis

    PMID:41611842 PMID:42097002

    Open questions at the time
    • Molecular basis of BOK-UMPS activation still undefined
    • Direct mechanism linking UMP synthesis to DNA-damage prevention incomplete

Open questions

Synthesis pass · forward-looking unresolved questions
  • How BOK integrates its ER/IP3R-bound Ca2+-regulatory role, its metastable MOMP-effector activity, and its non-apoptotic metabolic and mitochondrial-dynamics functions into a single physiological program remains unresolved.
  • No structure of full-length, membrane-embedded or IP3R-bound BOK
  • The physiological trigger that converts stable ER-resident BOK into an active MOMP effector is unknown
  • Whether the UMPS/uridine and apoptotic functions are mechanistically linked is undefined

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0005198 structural molecule activity 3 GO:0098772 molecular function regulator activity 3 GO:0140096 catalytic activity, acting on a protein 2
Localization
GO:0005739 mitochondrion 5 GO:0005783 endoplasmic reticulum 5 GO:0005794 Golgi apparatus 1
Pathway
R-HSA-5357801 Programmed Cell Death 3 R-HSA-1430728 Metabolism 2 R-HSA-8953897 Cellular responses to stimuli 2
Partners
AMFRBCL2DNAJB12ITPR1ITPR2MCL1UMPSVCP

Evidence

Reading pass · 35 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
1997 BOK (Bcl-2-related ovarian killer) was identified as a pro-apoptotic BCL-2 family member containing BH1, BH2, and BH3 domains and a C-terminal transmembrane region but lacking the BH4 domain. In yeast two-hybrid assays, BOK interacted selectively with Mcl-1, BHRF1, and Bfl-1, but not with Bcl-2, Bcl-xL, or Bcl-w—a heterodimerization pattern distinct from other pro-apoptotic members (Bax, Bak, Bik). Overexpression of BOK in mammalian cells induced apoptosis that was blocked by P35 and suppressed by co-expression of Mcl-1 or BHRF1 but not Bcl-2. Yeast two-hybrid, mammalian cell overexpression, co-expression rescue assay Proceedings of the National Academy of Sciences of the United States of America High 9356461
1998 A naturally occurring splicing variant of BOK (Bok-S) with a 43-residue deletion fusing the N-terminal half of BH3 to the C-terminal half of BH1 retained apoptosis-inducing activity but lost the ability to dimerize with anti-apoptotic proteins in vitro. Additional BH3 domain mutations in Bok-L also abolished heterodimerization without impairing pro-apoptotic function, indicating that heterodimerization with anti-apoptotic proteins is not required for BOK-mediated cell killing. Site-directed mutagenesis, in vitro binding assay, mammalian cell overexpression/apoptosis assay The Journal of biological chemistry High 9804769
2004 In human neuroblastoma and breast cancer cells, DNA damage-induced apoptosis required new protein synthesis, p53 accumulation, and p53-dependent induction of BOK and NOXA genes, with cytochrome c translocation not dependent on BAX. This placed BOK downstream of p53 and upstream of cytochrome c release in the DNA-damage intrinsic apoptosis pathway. Protein synthesis inhibition, p53 activation assays, cytochrome c translocation assay, gene expression analysis The Journal of biological chemistry Medium 15102863
2006 BOK expression is cell cycle-regulated: Bok RNA is low in quiescent cells and rises upon serum stimulation. The mouse Bok promoter contains a conserved E2F binding site (−43 to −49); serum-dependent activation requires this site, and endogenous E2F1 and E2F3 associate with the Bok promoter in vivo by chromatin immunoprecipitation. RT-PCR, luciferase reporter assay, chromatin immunoprecipitation (ChIP), promoter cloning The Journal of biological chemistry Medium 16772296
2006 Human BOK contains a leucine-rich nuclear export signal (NES) within its BH3 domain. BOK is present in both nucleus and cytoplasm; treatment with leptomycin B (Crm1 inhibitor) increases nuclear BOK. Crm1 co-immunoprecipitates wild-type BOK but not a NES-mutant BOK. Mutation of the NES increases nuclear localization and apoptotic activity, indicating that nuclear export of BOK is a regulated process mediated by Crm1. Western blot fractionation, leptomycin B treatment, site-directed mutagenesis, co-immunoprecipitation, immunocytochemistry Molecular carcinogenesis Medium 16302269
2013 Endogenous BOK localizes predominantly to the membranes of the Golgi apparatus and ER (and associated membranes) via a C-terminal tail-anchor transmembrane domain. Overexpression of full-length BOK causes early fragmentation of ER and Golgi compartments. BOK-deficient cells showed abnormal responses to the Golgi/ER stressor brefeldin A. Enforced BOK expression in BAX/BAK-proficient cells activates the intrinsic apoptotic pathway, but BOK fails to kill cells lacking both BAX and BAK. Subcellular fractionation, immunofluorescence/confocal microscopy, BOK truncation constructs, Bok-/- MEFs, apoptosis assays Cell death and differentiation High 23429263
2013 BOK binds strongly and constitutively to inositol 1,4,5-trisphosphate receptors (IP3Rs) in cells. BOK preferentially binds IP3R1 and IP3R2 but barely IP3R3. The binding site maps to a small region within the IP3R coupling domain (amino acids 1895–1903 of IP3R1). Essentially all cellular BOK is IP3R-bound in cells expressing substantial IP3Rs. BOK protects IP3Rs from proteolytic cleavage (by chymotrypsin in vitro and by caspase-3 in vivo) and regulates IP3R expression levels. Persistent IP3-dependent signaling triggers co-degradation of BOK and IP3R via the ubiquitin-proteasome pathway. Co-immunoprecipitation, in vitro pulldown, chymotrypsin protection assay, caspase-3 cleavage assay in apoptotic cells, IP3R truncation mutants The Journal of biological chemistry High 23884412
2013 Loss of BOK combined with loss of BAX in Bok-/-Bax-/- female mice resulted in abnormally increased numbers of oocytes from different developmental stages in aged animals, indicating an overlapping pro-apoptotic function of BOK and BAX in age-related follicular atresia. Combined loss of BOK and BAK showed no noticeable phenotypic defects. Genetic knockout mouse model, histological analysis of ovaries Cell death & disease Medium 23744350
2015 Bok-/- cells are selectively defective in apoptotic responses to ER stress stimuli (thapsigargin, A23187, brefeldin A, DTT, geldanamycin, bortezomib) but not to other apoptotic stimuli (etoposide, staurosporine, UV). BOK's predominant subcellular localization at the ER is consistent with this selective role. BAX and BAK cannot compensate for this ER stress apoptosis defect in BOK-deficient cells. Bok-/- cells also show diminished ATF4 and CHOP activation after ER stress. Bok-/- mouse embryonic fibroblasts, multiple ER stressor treatments, apoptosis assays, unfolded protein response (UPR) activation analysis, in vivo thapsigargin challenge Proceedings of the National Academy of Sciences of the United States of America High 26015568
2016 BOK is a bona fide effector of mitochondrial outer membrane permeabilization (MOMP) that can trigger apoptosis in the absence of both BAX and BAK. Unlike BAX/BAK, BOK is constitutively active and unresponsive to antagonism by anti-apoptotic BCL-2 proteins. BOK is controlled at the level of protein stability: it is ubiquitylated by the AMFR/gp78 E3 ubiquitin ligase complex and targeted for proteasomal degradation in a VCP/p97-dependent manner. When proteasome function, VCP, or gp78 is compromised, BOK is stabilized and induces MOMP independently of other BCL-2 proteins. BAX/BAK double-knockout cells, proteasome inhibition, gp78/VCP knockdown, ubiquitylation assay, MOMP assay, apoptosis assay Cell High 26949185
2016 BOK induces cytochrome c release and apoptosis independently of BAX and BAK in multiple cell systems. Endogenous BOK levels modulate apoptotic responses to chemotherapeutic drugs in ovarian carcinoma cells as shown by RNAi and targeted gene deletion of BOK. BAX/BAK-deficient cell systems, siRNA knockdown, CRISPR gene deletion, cytochrome c release assay, apoptosis assay Journal of cell science Medium 27076518
2016 In neurons, BOK is not required for staurosporine-, proteasome inhibition-, or excitotoxicity-induced apoptosis. Instead, BOK-deficient neurons are more sensitive to oxygen/glucose deprivation and seizure-induced injury. BOK deficiency reduces neuronal MCL-1 protein levels and causes disrupted mitochondrial bioenergetics and calcium homeostasis in response to excitotoxic stimuli, which could be rescued by MCL-1 overexpression. BOK-deficient neurons activate poly ADP-ribose polymerase-dependent cell death. Bok-/- neurons, single-cell calcium imaging, mitochondrial bioenergetics assay, MCL-1 overexpression rescue, in vivo seizure model, cell death pathway analysis The Journal of neuroscience High 27098698
2017 Recombinant BOK (BOK∆C) permeabilizes liposomes mimicking mitochondrial outer membrane composition, forming large stable toroidal pores. Pore formation is enhanced by cBID and is refractory to BCL-XL. However, isolated mitochondria from Bax-/-Bak-/- cells were resistant to BOK-induced cytochrome c release even in the presence of cBID, suggesting that BOK's direct MOMP activity at native mitochondria requires additional factors or regulation. In vitro liposome permeabilization assay, isolated mitochondria cytochrome c release assay, recombinant protein, cBID/BCL-XL addition The FEBS journal Medium 28064468
2017 DNAJB12 (JB12), an ER-associated Hsp40 protein, is required to maintain BOK at low levels and is detected in complexes with JB12 and gp78. JB12 is degraded by ER-associated degradation complexes (containing HERP, Sel1L, gp78) during severe ER stress. JB12 knockdown leads to BOK accumulation and activation of Caspase 3, 7, and 9, sensitizing cells to proteotoxic agents. Co-immunoprecipitation, siRNA knockdown, caspase activation assay, proteasome inhibition The Journal of biological chemistry Medium 28536268
2017 Myocardin-related transcription factor MAL/MRTF-A directly induces Bok transcription via a CArG-like box in the Bok promoter in an SRF-dependent and actin-regulated manner. Chromatin immunoprecipitation confirms inducible recruitment of MAL and SRF to the Bok promoter. MAL-dependent Bok induction occurs downstream of TNF and staurosporin stimulation. Luciferase reporter assay, ChIP, actin drug (latrunculin) treatment, siRNA knockdown Cell cycle (Georgetown, Tex.) Medium 22185759
2018 NMR structure of the BCL-2 core of human BOK reveals a conserved BCL-2 architecture with an atypical hydrophobic groove that undergoes conformational exchange. The BCL-2 core of BOK spontaneously associates with purified mitochondria and releases cytochrome c. Alanine substitution of a unique glycine in helix α1 stabilizes BOK and significantly inhibits MOMP, liposome permeabilization, and cell death. Activated BID does not activate WT BOK or the stabilized mutant, supporting a metastability-driven (rather than BH3 ligand-driven) mechanism of BOK activation. NMR structure determination, thermal shift assay, urea denaturation, in vitro MOMP assay with purified mitochondria, liposome permeabilization assay, alanine mutagenesis, cell death assay Cell reports High 29768206
2018 BOK structural analysis reveals close resemblance to BAX and BAK. Triple-knockout (Bok-/-Bax-/-Bak-/-) mice exhibit more severe developmental defects and die earlier than Bax-/-Bak-/- mice, demonstrating that BOK has overlapping roles with BAX and BAK during developmental cell death in vivo. Structural analysis, triple-knockout mouse generation, developmental phenotype analysis Cell High 29775594
2018 The ceramide (CER)/BOK axis promotes mitochondrial fission in preeclamptic placentae. BOK expression is increased by CER 16:0. Loss- and gain-of-function experiments showed BOK positively regulates phospho-DRP1/DRP1 and MFN2 expression and localizes mitochondrial fission events to ER/MAM compartments. The BH3 and transmembrane domains of BOK are required for this regulation of fission. Loss- and gain-of-function experiments, CER treatment, DRP1/MFN2 expression analysis, transmission electron microscopy, BOK domain deletion constructs Cell death & disease Medium 29463805
2018 The BH3 domain leucine-1 mutation (L70E) in BOK does not block apoptosis induction, but when combined with transmembrane domain deletion, the Bok(L70E)ΔTM double mutant shows enhanced pro-apoptotic activity by abolishing interaction with anti-apoptotic proteins, especially MCL-1. Deletion of the C-terminal transmembrane domain reduces pro-apoptotic function of BOK. The transmembrane domain thus contributes to BOK's interaction with and inhibition by MCL-1. Site-directed mutagenesis, domain deletion constructs, apoptosis assay, interaction analysis Scientific reports Medium 30127460
2019 BOK is a positive regulator of uridine monophosphate synthetase (UMPS) activity. BOK expression enhances UMPS enzymatic activity, cell proliferation, and chemosensitivity to 5-fluorouracil (5-FU). Genetic deletion of Bok results in chemoresistance to 5-FU in cell lines and in vivo. Cancers resistant to 5-FU down-regulate BOK expression. Bok-/- cells and mice, UMPS activity assay, 5-FU sensitivity assay, cell proliferation assay Proceedings of the National Academy of Sciences of the United States of America Medium 31311867
2019 Deletion of BOK expression by CRISPR/Cas9 significantly reduces mitochondrial fusion rate, resulting in mitochondrial fragmentation. This fragmentation phenotype is reversed by exogenous wild-type BOK and by an IP3R binding-deficient BOK mutant. BOK deletion also enhances mitochondrial spare respiratory capacity and membrane potential. BOK deletion does not alter IP3R-mediated Ca2+ signaling or Ca2+ influx into mitochondria. BOK deletion does not alter responsiveness to various apoptotic stimuli. CRISPR/Cas9 knockout, mitochondrial morphology analysis, mitochondrial fusion rate assay (photoactivatable GFP), Ca2+ mobilization assay, bioenergetics assay, BOK rescue constructs Cell death and differentiation High 30976095
2020 The transmembrane domain (TMD) of MCL-1 forms homooligomers in the mitochondrial membrane and induces cell death in a BOK-dependent manner. The BOK TMD oligomers localize preferentially to the ER, while heterooligomerization between MCL-1 TMD and BOK TMD occurs predominantly at the mitochondrial membrane. Co-expression of MCL-1 and BOK TMDs increases ER-mitochondrial associated membrane (MAM) contacts. Cancer-associated somatic mutations in MCL-1 TMD alter the TMD interaction pattern. Split-GFP TMD interaction assay, subcellular localization analysis, BOK-dependent cell death assay, molecular dynamics simulation, mutant analysis Proceedings of the National Academy of Sciences of the United States of America Medium 33093207
2021 BOK is necessary for baseline mitochondrial calcium levels and stimulus-induced calcium transfer from the ER to the mitochondria. Bok-/- MEFs have decreased proximity of the ER to the mitochondria and altered protein composition of mitochondria-associated membranes (MAMs). Drug-inducible ER-mitochondria linkers can overcome the proximity defect but fail to rescue thapsigargin-induced calcium transfer or apoptosis in Bok-/- cells. A BOK mutant unable to interact with IP3R restores ER-mitochondrial proximity but not calcium transfer, MAM protein composition, or apoptosis, showing that the BOK-IP3R interaction specifically governs calcium transfer. Bok-/- MEFs, mitochondrial calcium assay, ER-mitochondrial proximity assay (proximity ligation), chemically inducible organelle linkers, BOK IP3R-binding mutant, MAM proteomics, apoptosis assay Cell reports High 33691099
2021 Proximity labeling (TurboID-Bok) revealed that Bok is proximal to proteins involved in mitochondrial fission (e.g., Drp1) and ER-plasma membrane junctions (e.g., Stim1). Among BCL-2 family members, Bok is proximal only to Mcl-1. When overexpressed, Mcl-1 and Bok interact physically and functionally in a manner dependent on the transmembrane domain of Bok. The Bok interactome is largely distinct from those of Mcl-1 and Bak. TurboID proximity labeling, mass spectrometry, co-immunoprecipitation, transmembrane domain deletion mutants Frontiers in cell and developmental biology Medium 34136494
2021 Bok binds to a largely disordered loop in IP3R1 between α helices 72 and 73 (residues 1882–1957). The high-affinity binding site maps to amino acids 1898–1940 (Kd ~65 nM as measured with purified proteins and IP3R1-derived peptides). Binding is mediated by multivalent interactions with both the central low-disorder region and flanking high-disorder regions. Small deletions in the predicted transient helical elements (residues ~1914–1926) block Bok binding. Bioinformatic disorder prediction, in vitro pulldown with purified Bok and IP3R1 peptides, IP3R1 deletion/point mutants, membrane recruitment assay in cells Biochemical and biophysical research communications High 33773141
2022 SARS-CoV-2 membrane (M) protein stabilizes BOK by inhibiting its ubiquitination and promotes BOK mitochondrial translocation. The endodomain of M protein is required for interaction with BOK. The BH2 domain of BOK is required for interaction with M protein and for pro-apoptotic activity. M protein can induce MOMP-independent apoptosis via BOK in the absence of BAX and BAK. BOK knockout (CRISPR) increases cellular resistance to M protein-induced apoptosis; BOK re-expression restores it. CRISPR/Cas9 BOK knockout, co-immunoprecipitation, ubiquitination assay, domain deletion mutants, apoptosis assay in BAX/BAK-deficient cells, in vivo lentiviral infection model Cell death and differentiation High 35022571
2022 BOK-deficient cells have an attenuated unfolded protein response (UPR) across all three UPR signaling branches upon ER stress induction. FRAP experiments with GRP78/BiP-eGFP demonstrated that GRP78 motility is significantly lower in BOK-deficient cells, indicating more BiP is bound to unfolded proteins (reduced chaperone availability), establishing BOK as a regulator of ER proteostasis. UPR reporter cell lines, FRAP microscopy with GRP78-eGFP, Bok-/- neurons and cell lines Frontiers in cell and developmental biology Medium 36060797
2022 Endogenous Bok is stable at the ER membrane and its stability is critically dependent on the presence of IP3Rs. In the absence of IP3Rs, endogenous Bok is rapidly degraded by the ubiquitin-proteasome pathway. Proteasome inhibitor-induced apoptosis is not mediated by endogenous Bok. Charged residues in the transmembrane region of Bok affect its stability, ability to interact with Mcl-1, and pro-apoptotic activity when over-expressed. This study reports that endogenous Bok does not play a major role in apoptotic signaling (negative finding regarding BOK as a constitutively active MOMP effector governed purely by proteasomal degradation). IP3R knockout cells, proteasome inhibition, ubiquitylation assay, Bok stability assays, transmembrane domain mutants, apoptosis assays Frontiers in cell and developmental biology Medium 36601536
2024 The transmembrane domain (TMD) of anti-apoptotic BCL-2 interacts with the TMD of BOK at the ER membrane, as demonstrated by split-luciferase assay in living cells and confirmed by molecular dynamics simulations showing stable BOK-TMD/BCL-2-TMD heterotetramers. Mutation of BCL-2-TMD at predicted key residues abolishes interaction with BOK-TMD. Inhibition of BOK-induced apoptosis by BCL-2 depends specifically on their TMD interaction, revealing a novel TMD-mediated apoptosis regulation mechanism. Split luciferase assay in living cells, molecular dynamics simulation, site-directed mutagenesis of BCL-2-TMD, subcellular localization, apoptosis assay EMBO reports High 39048751
2025 BOK directly suppresses IP3R1-mediated Ca2+ mobilization. Specifically, Bok accelerates the post-maximal decline in GPCR-induced cytosolic Ca2+ by suppressing IP3R-dependent Ca2+ release from the ER. This effect requires the Bok-IP3R interaction (only seen with IP3Rs that bind Bok, e.g., IP3R1). Ser-8 phosphorylation of BOK by cAMP-dependent protein kinase weakens Bok-IP3R1 interaction and reverses Bok's suppressive effect on IP3R1-mediated Ca2+ mobilization. Fluorescent Ca2+-sensitive dye and genetically encoded Ca2+ sensor assays, PKA phosphorylation of purified proteins, mass spectrometry, phosphomimetic substitution (Ser-8), GPCR agonist stimulation, IP3R1-expressing cell systems Cell communication and signaling High 39810210
2017 BOK expression is negatively regulated post-transcriptionally by TRIM28 binding to conserved AU/U-rich elements in the human BOK 3' UTR. TRIM28 was identified as a key regulatory component by proteomics approaches, and its recruitment to the 3' UTR results in dramatic reduction of BOK expression. Proteomics/mass spectrometry identification, RNA pulldown, reporter assay, TRIM28 knockdown iScience Medium 30471638
2017 miR-296-5p regulates BOK expression by binding to its 3' UTR in breast cancer cells. Ectopic BOK expression induces MCL-1 upregulation, while MCL-1 silencing reduces BOK levels, forming a regulatory feedback loop. Glycogen synthase kinase (GSK3) α/β interacts with BOK and regulates its protein level post-translationally. 3'-UTR luciferase reporter assay, co-immunoprecipitation (GSK3-BOK), BOK/MCL-1 siRNA knockdown, Western blot Oncotarget Medium 29156771
2025 BCL-B interacts directly with BOK and can mitigate BOK-mediated cell death. This interaction promotes sublethal MOMP, generating apoptosis-flatliners that serve as drug-tolerant persister cells with enhanced invasiveness via EMT. Co-immunoprecipitation, sublethal MOMP assay, apoptosis-flatliner identification, EMT assay Cells Low 39996719
2026 BOK interacts with and increases UMPS enzymatic activity to promote UMP synthesis. BOK deficiency increases baseline DNA damage and p53 activation. In p53-deficient NSCLC cells, BOK loss elevates DNA damage and increases dependence on ATR-mediated repair, creating a synthetic lethal interaction with the ATR inhibitor ceralasertib. The DNA damage in BOK-deficient cells was rescued by a cell-permeable BOK-BH3-derived peptide, linking BOK's effect on genomic stability to its UMPS-regulatory function. UMPS activity assay, Bok-deficient NSCLC cell lines, ATR inhibitor (ceralasertib) treatment, DNA damage markers, BOK-BH3 peptide rescue, p53-deficient cell models Cell death and differentiation Medium 41611842
2026 EGR3 is a transcription factor that directly binds to the BOK gene promoter to transcriptionally activate BOK expression, as demonstrated by ChIP and dual luciferase reporter assays. BOK promotes mitochondrial apoptosis in response to arsenic exposure downstream of EGR3. ChIP, dual luciferase reporter assay, EGR3/BOK overexpression/knockdown, apoptosis assay Phytomedicine Medium 42097002

Source papers

Stage 0 corpus · 88 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
1997 Bok is a pro-apoptotic Bcl-2 protein with restricted expression in reproductive tissues and heterodimerizes with selective anti-apoptotic Bcl-2 family members. Proceedings of the National Academy of Sciences of the United States of America 285 9356461
2016 BOK Is a Non-canonical BCL-2 Family Effector of Apoptosis Regulated by ER-Associated Degradation. Cell 223 26949185
2018 Embryogenesis and Adult Life in the Absence of Intrinsic Apoptosis Effectors BAX, BAK, and BOK. Cell 171 29775594
2020 BAX, BAK, and BOK: A Coming of Age for the BCL-2 Family Effector Proteins. Cold Spring Harbor perspectives in biology 146 31570337
2004 BOK and NOXA are essential mediators of p53-dependent apoptosis. The Journal of biological chemistry 123 15102863
2017 Control of mitochondrial physiology and cell death by the Bcl-2 family proteins Bax and Bok. Neurochemistry international 117 28315370
2015 BCL-2 family member BOK promotes apoptosis in response to endoplasmic reticulum stress. Proceedings of the National Academy of Sciences of the United States of America 113 26015568
2013 Intracellular localization of the BCL-2 family member BOK and functional implications. Cell death and differentiation 111 23429263
2012 BCL-2 family member BOK is widely expressed but its loss has only minimal impact in mice. Cell death and differentiation 96 22281706
2018 Ceramide-induced BOK promotes mitochondrial fission in preeclampsia. Cell death & disease 92 29463805
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 cleavage. The Journal of biological chemistry 87 23884412
2022 SARS-CoV-2 membrane protein causes the mitochondrial apoptosis and pulmonary edema via targeting BOK. Cell death and differentiation 82 35022571
2021 BOK controls apoptosis by Ca2+ transfer through ER-mitochondrial contact sites. Cell reports 68 33691099
2013 Consequences of the combined loss of BOK and BAK or BOK and BAX. Cell death & disease 59 23744350
2019 Bok regulates mitochondrial fusion and morphology. Cell death and differentiation 58 30976095
2014 Anthocyanin accumulation and transcriptional regulation of anthocyanin biosynthesis in purple bok choy (Brassica rapa var. chinensis). Journal of agricultural and food chemistry 57 25419600
2013 Placental autophagy regulation by the BOK-MCL1 rheostat. Autophagy 54 24113155
2018 Intrinsic Instability of BOK Enables Membrane Permeabilization in Apoptosis. Cell reports 50 29768206
2016 Bok Is Not Pro-Apoptotic But Suppresses Poly ADP-Ribose Polymerase-Dependent Cell Death Pathways and Protects against Excitotoxic and Seizure-Induced Neuronal Injury. The Journal of neuroscience : the official journal of the Society for Neuroscience 49 27098698
2009 A natural antisense transcript, BOKAS, regulates the pro-apoptotic activity of human Bok. International journal of oncology 49 19287972
2019 Raptinal bypasses BAX, BAK, and BOK for mitochondrial outer membrane permeabilization and intrinsic apoptosis. Cell death & disease 46 31324752
1998 A splicing variant of the Bcl-2 member Bok with a truncated BH3 domain induces apoptosis but does not dimerize with antiapoptotic Bcl-2 proteins in vitro. The Journal of biological chemistry 46 9804769
2020 The Multifaceted Roles of the BCL-2 Family Member BOK. Frontiers in cell and developmental biology 44 33043006
2017 The membrane activity of BOK involves formation of large, stable toroidal pores and is promoted by cBID. The FEBS journal 41 28064468
2017 Endoplasmic reticulum stress-induced degradation of DNAJB12 stimulates BOK accumulation and primes cancer cells for apoptosis. The Journal of biological chemistry 41 28536268
2006 Bok, Bcl-2-related Ovarian Killer, Is Cell Cycle-regulated and Sensitizes to Stress-induced Apoptosis. The Journal of biological chemistry 41 16772296
2009 Mtd/Bok takes a swing: proapoptotic Mtd/Bok regulates trophoblast cell proliferation during human placental development and in preeclampsia. Cell death and differentiation 39 19942931
2022 The BCL-2 family member BID plays a role during embryonic development in addition to its BH3-only protein function by acting in parallel to BAX, BAK and BOK. The EMBO journal 38 35758142
2016 Bok is a genuine multi-BH-domain protein that triggers apoptosis in the absence of Bax and Bak. Journal of cell science 38 27076518
2020 Mcl-1 and Bok transmembrane domains: Unexpected players in the modulation of apoptosis. Proceedings of the National Academy of Sciences of the United States of America 37 33093207
2019 BCL-2 family protein BOK is a positive regulator of uridine metabolism in mammals. Proceedings of the National Academy of Sciences of the United States of America 34 31311867
2015 Impact of the combined loss of BOK, BAX and BAK on the hematopoietic system is slightly more severe than compound loss of BAX and BAK. Cell death & disease 34 26492371
2006 Nuclear translocation of the pro-apoptotic Bcl-2 family member Bok induces apoptosis. Molecular carcinogenesis 33 16302269
2017 BOK promotes chemical-induced hepatocarcinogenesis in mice. Cell death and differentiation 30 29229991
2017 BOK displays cell death-independent tumor suppressor activity in non-small-cell lung carcinoma. International journal of cancer 28 28744854
2018 Avicularin reversed multidrug-resistance in human gastric cancer through enhancing Bax and BOK expressions. Biomedicine & pharmacotherapy = Biomedecine & pharmacotherapie 26 29635130
2010 WNT signaling controls expression of pro-apoptotic BOK and BAX in intestinal cancer. Biochemical and biophysical research communications 25 21184732
2019 Effects of bok choy on the dissipation of dibutyl phthalate (DBP) in mollisol and its possible mechanisms of biochemistry and microorganisms. Ecotoxicology and environmental safety 24 31201960
2010 Regulation of cell death in human fetal and adult ovaries--role of Bok and Bcl-X(L). Molecular and cellular endocrinology 24 20673843
2022 Modeling apoptosis resistance in CHO cells with CRISPR-mediated knockouts of Bak1, Bax, and Bok. Biotechnology and bioengineering 23 35180317
2021 Development of a nanobody-based ELISA for the detection of the insecticides cyantraniliprole and chlorantraniliprole in soil and the vegetable bok choy. Analytical and bioanalytical chemistry 21 33580830
2020 The Mysteries around the BCL-2 Family Member BOK. Biomolecules 21 33291826
2006 Effects of endocrine disruptor di-n-butyl phthalate on the growth of Bok choy (Brassica rapa subsp. chinensis). Chemosphere 21 16824579
2021 CEBPA-AS1 Knockdown Alleviates Oxygen-Glucose Deprivation/Reperfusion-Induced Neuron Cell Damage by the MicroRNA 24-3p/BOK Axis. Molecular and cellular biology 20 34001648
2017 Novel post-transcriptional and post-translational regulation of pro-apoptotic protein BOK and anti-apoptotic protein Mcl-1 determine the fate of breast cancer cells to survive or die. Oncotarget 20 29156771
2001 The expression and regulation of Bcl-2-related ovarian killer (Bok) mRNA in the developing and adult rat testis. European journal of endocrinology 20 11720903
2012 Myocardin-related transcription factor A regulates expression of Bok and Noxa and is involved in apoptotic signalling. Cell cycle (Georgetown, Tex.) 18 22185759
2025 Allelopathic effects of tree peony extracts on bok choy, spinach and tatsoi. Scientific reports 16 41365932
2018 Contribution of BH3-domain and Transmembrane-domain to the Activity and Interaction of the Pore-forming Bcl-2 Proteins Bok, Bak, and Bax. Scientific reports 16 30127460
2018 How do root exudates of bok choy promote dibutyl phthalate adsorption on mollisol? Ecotoxicology and environmental safety 15 29879573
2024 BCL-2 and BOK regulate apoptosis by interaction of their C-terminal transmembrane domains. EMBO reports 14 39048751
2021 Identification of the Bok Interactome Using Proximity Labeling. Frontiers in cell and developmental biology 13 34136494
2023 Bok: real killer or bystander with non-apoptotic roles? Frontiers in cell and developmental biology 12 37123400
2016 BOK: Oddball of the BCL-2 Family. Trends in cell biology 12 27156889
2022 The BCL-2 family member BOK promotes KRAS-driven lung cancer progression in a p53-dependent manner. Oncogene 11 35091677
2019 Role of B-Cell Lymphoma 2 Ovarian Killer (BOK) in Acute Toxicity of Human Lung Epithelial Cells Caused by Cadmium Chloride. Medical science monitor : international medical journal of experimental and clinical research 10 31323016
2018 Negative Regulation of BOK Expression by Recruitment of TRIM28 to Regulatory Elements in Its 3' Untranslated Region. iScience 10 30471638
2015 Molecular profiles and pathogen-induced transcriptional responses of prawn B cell lymphoma-2 related ovarian killer protein (BOK). Fish & shellfish immunology 10 25982403
2001 The expression of Bok is regulated by serum in HC11 mammary epithelial cells. Molecules and cells 10 11804337
2014 Hypoxia-inducible regulation of placental BOK expression. The Biochemical journal 9 24806027
2022 BOK controls ER proteostasis and physiological ER stress responses in neurons. Frontiers in cell and developmental biology 8 36060797
2022 Endogenous Bok is stable at the endoplasmic reticulum membrane and does not mediate proteasome inhibitor-induced apoptosis. Frontiers in cell and developmental biology 8 36601536
2021 Bok binds to a largely disordered loop in the coupling domain of type 1 inositol 1,4,5-trisphosphate receptor. Biochemical and biophysical research communications 8 33773141
2004 Ge-Jee-Bok-Ryung-Hwan induces apoptosis in human cervical carcinoma HeLa cells--an endoplasmic reticulum stress pathway--. Life sciences 8 15474552
2023 Necrostatin-1 prevents skeletal muscle ischemia reperfusion injury by regulating Bok-mediated apoptosis. Journal of the Chinese Medical Association : JCMA 7 36599139
2019 BOK promotes erythropoiesis in a mouse model of myelodysplastic syndrome. Annals of hematology 7 31203423
2023 Assessment of CuO NPs on soil microbial community structure based on phospholipid fatty acid techniques and phytotoxicity of bok choy seedlings. Plant physiology and biochemistry : PPB 6 36989987
2017 There is something about BOK we just don't get yet. The FEBS journal 6 28262002
2004 Role of Mtd/Bok in normal and neoplastic B-cell development in the bursa of Fabricius. Developmental and comparative immunology 6 15177115
2025 Root and foliar uptake, bidirectional translocation, subcellular distribution, and metabolism of tire wear particle-derived p-phenylenediamines and their quinones in Chinese cabbage and bok choy. Environmental pollution (Barking, Essex : 1987) 5 40588154
2016 Identification of the Bcl-2 family protein gene BOK from orange-spotted grouper (Epinephelus coioides) involved in SGIV infection. Fish & shellfish immunology 4 26994672
2016 Cell Biology: ERADicating Survival with BOK. Current biology : CB 4 27269726
2024 Non-thermal plasma enhances growth and salinity tolerance of bok choy (Brassica rapa subsp. chinensis) in hydroponic culture. Frontiers in plant science 3 39376241
2024 BcWRKY25-BcWRKY33A-BcLRP1/BcCOW1 module promotes root development for improved salt tolerance in Bok choy. Horticulture research 3 39850370
2021 BOK-MCL1 transmembrane interactions: a challenging target for cancer therapy. Molecular & cellular oncology 3 33553610
2024 Physiological and Transcriptomic Responses of Bok Choy to Heat Stress. Plants (Basel, Switzerland) 2 38674501
2021 Loss of BOK Has a Minor Impact on Acetaminophen Overdose-Induced Liver Damage in Mice. International journal of molecular sciences 2 33807047
2026 Loss of BOK increases vulnerability of p53 deficient non-small cell lung cancer cells to ATR inhibition through its role in uridine metabolism. Cell death and differentiation 1 41611842
2025 BCL-B Promotes Lung Cancer Invasiveness by Direct Inhibition of BOK. Cells 1 39996719
2024 Interactive effects of microplastics and cadmium on soil properties, microbial communities and bok choy growth. The Science of the total environment 1 39395501
2023 Up-regulation of BOK-AS1, FAM215A and FEZF1-AS1 lncRNAs and their potency as moderate diagnostic biomarkers in gastric cancer. Pathology, research and practice 1 37364417
2026 Gastrodin alleviates high fructose-induced podocyte mitochondria-mediated apoptosis by inhibiting NLRP6 to facilitate TRIM7-triggered Bok mRNA degradation. International journal of biological sciences 0 41608624
2026 Molecular Hydrogen Improves Storage Quality of Bok Choy by Reducing Water Loss and Maintaining Cell Wall Integrity. Plants (Basel, Switzerland) 0 41754355
2026 Dynamics and drivers of last-resort antibiotic resistance genes during pilot-scale aerobic fermentation of municipal sludge and subsequent bok choy pot trials. Journal of hazardous materials 0 41962374
2026 Vitamin K2 (MK7) alleviates arsenic-induced cardiac hypertrophy by suppressing the EGR3/BOK mitochondrial apoptosis pathway. Phytomedicine : international journal of phytotherapy and phytopharmacology 0 42097002
2025 Phosphorylation of Bok at Ser-8 blocks its ability to suppress IP3R-mediated calcium mobilization. Cell communication and signaling : CCS 0 39810210
2025 Low BOK Expression Promotes Epithelial-Mesenchymal Transition and Migration via the Wnt Signaling Pathway in Breast Cancer Cells. International journal of molecular sciences 0 40806384
2023 Discovery and Comprehensive Characterization of Novel Circular RNAs of the Apoptosis-Related BOK Gene in Human Ovarian and Prostate Cancer Cells, Using Nanopore Sequencing. Non-coding RNA 0 37888203

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