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template_file: templates/gene_research_go_focused.md
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organism: human
gene_id: BCL2L12
gene_symbol: BCL2L12
uniprot_accession: Q9HB09
protein_description: 'RecName: Full=Bcl-2-like protein 12 {ECO:0000305}; Short=Bcl2-L-12;
AltName: Full=Bcl-2-related proline-rich protein;'
gene_info: Name=BCL2L12 {ECO:0000312|HGNC:HGNC:13787}; Synonyms=BPR;
organism_full: Homo sapiens (Human).
protein_family: Belongs to the Bcl-2 family. .
protein_domains: Bcl-2-like_sf. (IPR036834)
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citation_count: 17

Question

Gene Research for Functional Annotation

⚠️ CRITICAL: Gene/Protein Identification Context

BEFORE YOU BEGIN RESEARCH: You MUST verify you are researching the CORRECT gene/protein. Gene symbols can be ambiguous, especially for less well-characterized genes from non-model organisms.

Target Gene/Protein Identity (from UniProt):

• UniProt Accession: Q9HB09
• Protein Description: RecName: Full=Bcl-2-like protein 12 {ECO:0000305}; Short=Bcl2-L-12; AltName: Full=Bcl-2-related proline-rich protein;
• Gene Information: Name=BCL2L12 {ECO:0000312|HGNC:HGNC:13787}; Synonyms=BPR;
• Organism (full): Homo sapiens (Human).
• Protein Family: Belongs to the Bcl-2 family. .
• Key Domains: Bcl-2-like_sf. (IPR036834)

MANDATORY VERIFICATION STEPS:

1. Check if the gene symbol "BCL2L12" matches the protein description above
2. Verify the organism is correct: Homo sapiens (Human).
3. Check if protein family/domains align with what you find in literature
4. If you find literature for a DIFFERENT gene with the same or similar symbol, STOP

If Gene Symbol is Ambiguous or You Cannot Find Relevant Literature:

DO NOT PROCEED WITH RESEARCH ON A DIFFERENT GENE. Instead:
- State clearly: "The gene symbol 'BCL2L12' is ambiguous or literature is limited for this specific protein"
- Explain what you found (e.g., "Found extensive literature on a different gene with the same symbol in a different organism")
- Describe the protein based ONLY on the UniProt information provided above
- Suggest that the protein function can be inferred from domain/family information

Research Target:

Please provide a comprehensive research report on the gene BCL2L12 (gene ID: BCL2L12, UniProt: Q9HB09) in human.

The research report should be a detailed narrative explaining the function, biological processes, and localization of the gene product. Citations should be given for all claims.

You should prioritize authoritative reviews and primary scientific literature when conducting research. You can supplement
this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.

We are specifically interested in the primary function of the gene - for enzymes, what reaction is catalyzed, and what is the substrate specificity? For transporters, what is the substrate? For structural proteins or adapters, what is the broader structural role? For signaling molecules, what is the role in the pathway.

We are interested in where in or outside the cell the gene product carries out its function.

We are also interested in the signaling or biochemical pathways in which the gene functions. We are less interested in broad pleiotropic effects, except where these elucidate the precise role.

Include evidence where possible. We are interested in both experimental evidence as well as inference from structure, evolution, or bioinformatic analysis. Precise studies should be prioritized over high-throughput, where available.

Output

Question: You are an expert researcher providing comprehensive, well-cited information.

Provide detailed information focusing on:
1. Key concepts and definitions with current understanding
2. Recent developments and latest research (prioritize 2023-2024 sources)
3. Current applications and real-world implementations
4. Expert opinions and analysis from authoritative sources
5. Relevant statistics and data from recent studies

Format as a comprehensive research report with proper citations. Include URLs and publication dates where available.
Always prioritize recent, authoritative sources and provide specific citations for all major claims.

Gene Research for Functional Annotation

⚠️ CRITICAL: Gene/Protein Identification Context

BEFORE YOU BEGIN RESEARCH: You MUST verify you are researching the CORRECT gene/protein. Gene symbols can be ambiguous, especially for less well-characterized genes from non-model organisms.

Target Gene/Protein Identity (from UniProt):

• UniProt Accession: Q9HB09
• Protein Description: RecName: Full=Bcl-2-like protein 12 {ECO:0000305}; Short=Bcl2-L-12; AltName: Full=Bcl-2-related proline-rich protein;
• Gene Information: Name=BCL2L12 {ECO:0000312|HGNC:HGNC:13787}; Synonyms=BPR;
• Organism (full): Homo sapiens (Human).
• Protein Family: Belongs to the Bcl-2 family. .
• Key Domains: Bcl-2-like_sf. (IPR036834)

MANDATORY VERIFICATION STEPS:

1. Check if the gene symbol "BCL2L12" matches the protein description above
2. Verify the organism is correct: Homo sapiens (Human).
3. Check if protein family/domains align with what you find in literature
4. If you find literature for a DIFFERENT gene with the same or similar symbol, STOP

If Gene Symbol is Ambiguous or You Cannot Find Relevant Literature:

DO NOT PROCEED WITH RESEARCH ON A DIFFERENT GENE. Instead:
- State clearly: "The gene symbol 'BCL2L12' is ambiguous or literature is limited for this specific protein"
- Explain what you found (e.g., "Found extensive literature on a different gene with the same symbol in a different organism")
- Describe the protein based ONLY on the UniProt information provided above
- Suggest that the protein function can be inferred from domain/family information

Research Target:

Please provide a comprehensive research report on the gene BCL2L12 (gene ID: BCL2L12, UniProt: Q9HB09) in human.

The research report should be a detailed narrative explaining the function, biological processes, and localization of the gene product. Citations should be given for all claims.

You should prioritize authoritative reviews and primary scientific literature when conducting research. You can supplement
this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.

We are specifically interested in the primary function of the gene - for enzymes, what reaction is catalyzed, and what is the substrate specificity? For transporters, what is the substrate? For structural proteins or adapters, what is the broader structural role? For signaling molecules, what is the role in the pathway.

We are interested in where in or outside the cell the gene product carries out its function.

We are also interested in the signaling or biochemical pathways in which the gene functions. We are less interested in broad pleiotropic effects, except where these elucidate the precise role.

Include evidence where possible. We are interested in both experimental evidence as well as inference from structure, evolution, or bioinformatic analysis. Precise studies should be prioritized over high-throughput, where available.

Plan and verification summary
- Identity check: The target matches human BCL2L12 (Bcl-2-like protein 12), also known as Bcl2L12, an atypical Bcl-2 family member with proline-rich regions and a C-terminal BH2-like feature; literature places it prominently in human glioblastoma biology, consistent with a Homo sapiens protein (reviewed in glioma context) (kouri2012theroleof pages 4-5, stegh2011beyondeffectorcaspase pages 3-4). Domain reports in primary and review works converge on a proline-rich protein with PxxP motifs, a single C-terminal BH2 domain, and a BH3-like motif—consistent with a Bcl-2 family classification (kouri2012theroleof pages 4-5, yang2015bcl2l12witha pages 1-2, yang2015bcl2l12witha pages 12-13).

Comprehensive research report on BCL2L12 (UniProt: Q9HB09)

1) Key concepts and definitions
- Gene/protein and family: BCL2L12 encodes Bcl-2-like protein 12, an atypical Bcl-2 family protein. Unlike canonical prosurvival Bcl-2 proteins, BCL2L12 is proline-rich and is characterized by PxxP motifs and a single C-terminal BH2 domain; it lacks BH1/BH3/BH4 and a transmembrane region, yet carries a BH3-like motif that mediates interactions with antiapoptotic Bcl-2 homologs (Kouri et al., 2012; Yang et al., 2015; URL: https://doi.org/10.1100/2012/838916; https://doi.org/10.3892/ijo.2015.2838) (kouri2012theroleof pages 4-5, yang2015bcl2l12witha pages 1-2).
- Cellular roles: BCL2L12 functions as a dual-site apoptosis regulator. In the cytoplasm, it blocks post-mitochondrial apoptosis signaling by inhibiting effector caspases. In the nucleus, it binds and neutralizes p53 transcriptional activity, limiting the induction of p53 target genes and apoptosis (Stegh & DePinho, 2011; URL: https://doi.org/10.4161/cc.10.1.14365) (stegh2011beyondeffectorcaspase pages 3-4, stegh2011beyondeffectorcaspase pages 1-3).
- Localization: Detected in both cytoplasm and nucleus in glioma models and tissues; nuclear complexes with p53 are functionally important (Stegh & DePinho, 2011; URL: https://doi.org/10.4161/cc.10.1.14365) (stegh2011beyondeffectorcaspase pages 3-4, stegh2011beyondeffectorcaspase pages 1-3).

2) Recent developments and latest research (emphasis on mechanisms and regulatory insights)
Note: Our retrieved, citable corpus is dominated by foundational primary studies and reviews up to 2015. We summarize the current mechanistic understanding below and, where possible, include quantitative results from those sources. More recent 2023–2024 items relevant to nanotherapy and splicing regulation were identified in searches, but we were unable to retrieve full evidence for direct citation here; therefore, this section reflects earlier, still-current mechanistic studies and explicitly notes the evidence gap for 2023–2024.
- GSK3β regulation and Ser156 phosphorylation: BCL2L12 directly interacts with GSK3β; GSK3β phosphorylates BCL2L12 at Ser156. The S156A mutant loses antiapoptotic function, and LiCl (a GSK3β inhibitor) reduces BCL2L12-mediated survival signaling in glioblastoma cells (Chou et al., 2012; URL: https://doi.org/10.4161/cc.11.3.19051) (chou2012gsk3betaregulatesbcl2l12 pages 1-2).
- BH3-like motif function and interaction specificity: A BH3-like segment within BCL2L12 mediates binding to Bcl-2/Bcl-xL; mutating key hydrophobic residues (e.g., L213, L217) restores apoptosis signaling (cleaved PARP, caspase-3 activation, cytochrome c release), supporting a model in which BCL2L12’s BH3-like region underpins its antiapoptotic interactions (Yang et al., 2015; URL: https://doi.org/10.3892/ijo.2015.2838) (yang2015bcl2l12witha pages 1-2, yang2015bcl2l12witha pages 12-13).
- Post-mitochondrial blockade of apoptosis: BCL2L12 inhibits effector caspases downstream of mitochondrial permeabilization and apoptosome assembly; it binds caspase-7 directly and reduces caspase-3 activation in part via αB-crystallin upregulation (reviewed in Stegh & DePinho, 2011; URL: https://doi.org/10.4161/cc.10.1.14365) (stegh2011beyondeffectorcaspase pages 3-4, stegh2011beyondeffectorcaspase pages 1-3).
- Nuclear inhibition of p53 tumor suppressor: BCL2L12 forms complexes with p53 in the nucleus, blunting p53’s transcriptional activation of targets such as p21, DR5, Noxa, and PUMA, and reducing p53 stability. This mechanism suppresses DNA damage–induced apoptosis and senescence programs (Stegh & DePinho, 2011; URL: https://doi.org/10.4161/cc.10.1.14365) (stegh2011beyondeffectorcaspase pages 1-3).
- Isoforms and expression in GBM: Two major isoforms are described. Full-length BCL2L12 (~334 aa) and a truncated splice isoform BCL2L12A (~176 aa, lacks exon 3). mRNA overexpression in glioblastoma was reported at approximately 52% for BCL2L12, 76% for BCL2L12A, and 86% for either isoform (Chou et al., 2012; URL: https://doi.org/10.4161/cc.11.3.19051) (chou2012gsk3betaregulatesbcl2l12 pages 1-2).

3) Current applications and real-world implementations
- Biomarker applications in hematologic malignancy: In a qRT-PCR study of 65 CLL patients vs. 23 controls, BCL2L12 mRNA was significantly elevated in CLL, showed strong discriminatory performance in ROC analysis, predicted CLL presence by logistic regression, and high expression associated with advanced clinical stage and shorter overall survival (Papageorgiou et al., 2011; URL: https://doi.org/10.1634/theoncologist.2010-0349) (papageorgiou2011thenovelmember pages 1-2).
- Therapeutic concepts in GBM (preclinical): Mechanistic studies suggest BCL2L12 contributes to chemoradiation resistance by blocking caspase activation and neutralizing p53. Strategies proposed include disrupting BCL2L12–p53 interactions, inhibiting BCL2L12’s BH3-like binding surface, and pairing BH3 mimetics (e.g., ABT-737) with temozolomide to overcome resistance (Yang et al., 2015; Stegh & DePinho, 2011; URLs: https://doi.org/10.3892/ijo.2015.2838; https://doi.org/10.4161/cc.10.1.14365) (yang2015bcl2l12witha pages 12-13, stegh2011beyondeffectorcaspase pages 3-4, stegh2011beyondeffectorcaspase pages 1-3).

4) Expert opinions and analysis from authoritative sources
- Authoritative reviews emphasize BCL2L12 as an “atypical” Bcl-2 family oncoprotein that operates both in the cytoplasm (effector caspase blockade) and nucleus (p53 antagonism), thereby conferring potent apoptosis resistance and promoting necrotic outcomes in glioblastoma contexts. Elevated expression is frequent in primary GBM by tissue analysis (Stegh & DePinho, 2011; review perspective; URL: https://doi.org/10.4161/cc.10.1.14365) (stegh2011beyondeffectorcaspase pages 3-4, stegh2011beyondeffectorcaspase pages 1-3).
- In malignant astrocytic gliomas, BCL2L12 is highlighted as a critical modulator of therapy response with mechanistic placement downstream of mitochondrial permeabilization and upstream of executioner caspase activity and p53-driven transcription, making it a rational target to sensitize GBM to cytotoxic therapies (Kouri et al., 2012; URL: https://doi.org/10.1100/2012/838916) (kouri2012theroleof pages 4-5).

5) Relevant statistics and data from recent studies (from accessible evidence)
- Glioblastoma overexpression: Reviews summarizing tissue microarray data report robust BCL2L12 expression in a high fraction of primary GBM specimens (Stegh & DePinho, 2011; URL: https://doi.org/10.4161/cc.10.1.14365) (stegh2011beyondeffectorcaspase pages 3-4). While the review context indicates very high prevalence, precise numerical breakdowns vary by cohort and method; in parallel, mRNA-level overexpression of splice isoforms was quantified at 52% (BCL2L12), 76% (BCL2L12A), and 86% for either transcript in GBM (Chou et al., 2012; URL: https://doi.org/10.4161/cc.11.3.19051) (chou2012gsk3betaregulatesbcl2l12 pages 1-2).
- CLL cohort: In a clinical cohort of 65 CLL patients, BCL2L12 mRNA was significantly elevated vs. 23 controls; ROC and multivariate models supported diagnostic value, and high BCL2L12 predicted shorter overall survival (Papageorgiou et al., 2011; URL: https://doi.org/10.1634/theoncologist.2010-0349) (papageorgiou2011thenovelmember pages 1-2).

Primary molecular functions and pathway placement (focused synthesis)
- Effector caspase inhibition: BCL2L12 acts downstream of cytochrome c/apoptosome formation to inhibit caspase-7 directly and attenuate caspase-3 activity, effecting a post-mitochondrial block that shifts death outcomes and fosters therapy resistance (Stegh & DePinho, 2011; URL: https://doi.org/10.4161/cc.10.1.14365) (stegh2011beyondeffectorcaspase pages 3-4, stegh2011beyondeffectorcaspase pages 1-3).
- p53 pathway antagonism: Nuclear BCL2L12 complexes with p53, diminishes p53 stability, and prevents p53 binding to target promoters, impairing canonical p53 responses to genotoxic stress (Stegh & DePinho, 2011; URL: https://doi.org/10.4161/cc.10.1.14365) (stegh2011beyondeffectorcaspase pages 1-3).
- BH3-like interactions: The BH3-like motif is required for binding to Bcl-2/Bcl-xL; mutations in the motif restore apoptotic signaling, indicating that this interface is a potential therapeutic target (Yang et al., 2015; URL: https://doi.org/10.3892/ijo.2015.2838) (yang2015bcl2l12witha pages 1-2, yang2015bcl2l12witha pages 12-13).
- Regulation: GSK3β binds and phosphorylates BCL2L12 at S156, which is necessary for its antiapoptotic activity; pharmacologic GSK3β inhibition (e.g., LiCl) reduces BCL2L12-mediated survival, implicating kinase control as a regulatory node (Chou et al., 2012; URL: https://doi.org/10.4161/cc.11.3.19051) (chou2012gsk3betaregulatesbcl2l12 pages 1-2).
- Isoforms: Full-length BCL2L12 and BCL2L12A (exon 3 skipping) are both expressed; BCL2L12A lacks the S156 site and BH2-containing region, with distinct functional properties and prevalent expression in GBM (Chou et al., 2012; URL: https://doi.org/10.4161/cc.11.3.19051) (chou2012gsk3betaregulatesbcl2l12 pages 1-2).

Cellular localization
- BCL2L12 operates in both the cytoplasm and nucleus. Cytoplasmic activity underlies effector caspase blockade; nuclear activity involves direct interference with p53-mediated transcription (Stegh & DePinho, 2011; URL: https://doi.org/10.4161/cc.10.1.14365) (stegh2011beyondeffectorcaspase pages 3-4, stegh2011beyondeffectorcaspase pages 1-3).

Disease associations and translational relevance
- Glioblastoma: High-level BCL2L12 expression is a defining feature of many GBM samples, and functional data place BCL2L12 as a driver of therapy resistance via caspase inhibition and p53 suppression. Targeting BCL2L12 (protein–protein interfaces, kinase regulation, RNA interference) is a rational strategy to improve apoptotic responses in GBM (Stegh & DePinho, 2011; Kouri et al., 2012; Yang et al., 2015; URLs: https://doi.org/10.4161/cc.10.1.14365; https://doi.org/10.1100/2012/838916; https://doi.org/10.3892/ijo.2015.2838) (stegh2011beyondeffectorcaspase pages 3-4, kouri2012theroleof pages 4-5, yang2015bcl2l12witha pages 12-13).
- Hematologic malignancy: Elevated BCL2L12 mRNA in CLL correlates with advanced disease and worse survival, supporting its potential as a biomarker (Papageorgiou et al., 2011; URL: https://doi.org/10.1634/theoncologist.2010-0349) (papageorgiou2011thenovelmember pages 1-2).

Embedded evidence summary table
| Topic | Key finding (1–2 sentences) | Model/context | Source (authors, year) | URL | Pub date (Month Year) | Citation ID |
|---|---|---:|---|---|---:|---|
| Identity & family | BCL2L12 encodes a proline-rich, atypical Bcl-2 family protein (~334 aa) that lacks classical BH1/BH3/BH4 and transmembrane motifs but is implicated in tumorigenesis and therapy resistance. | Human tissues and glioma specimens | Kouri F.M. et al., 2012 | https://doi.org/10.1100/2012/838916 | Feb 2012 | pqac-00000006 |
| Domain architecture | Contains multiple PxxP proline-rich motifs, a single C-terminal BH2 domain and a 12-residue BH3-like motif that mediates interactions with Bcl-2/Bcl-xL. | Sequence/functional mapping; glioma cell assays | Yang M.-C. et al., 2015 | https://doi.org/10.3892/ijo.2015.2838 | Mar 2015 | pqac-00000002 |
| Subcellular localization | Localizes to both cytoplasm and nucleus; nuclear BCL2L12 forms complexes with p53 and cytoplasmic protein mediators to exert anti-apoptotic effects. | GBM cell lines and tissue microarrays | Stegh A.H. & DePinho R.A., 2011 | https://doi.org/10.4161/cc.10.1.14365 | Jan 2011 | pqac-00000000 |
| Primary molecular function — effector caspase inhibition | Blocks post-mitochondrial apoptosis by inhibiting effector caspases (directly inhibiting caspase-7 and attenuating caspase-3 activation), producing apoptosis resistance. | Functional assays in glioma models (caspase readouts) | Stegh A.H. et al. (reviewed), 2011 | https://doi.org/10.4161/cc.10.1.14365 | Jan 2011 | pqac-00000000 |
| Primary molecular function — p53 modulation | Interacts with and neutralizes p53 transactivation, reducing p53 stability and preventing binding to target promoters (e.g., p21, PUMA, Noxa), thereby attenuating p53-dependent apoptosis. | GBM models; promoter/transactivation assays | Stegh A.H. & DePinho R.A., 2011 | https://doi.org/10.4161/cc.10.1.14365 | Jan 2011 | pqac-00000003 |
| Mechanisms (post-mitochondrial blockade; BH3-like interactions) | Acts downstream of mitochondria to block apoptosome/effector activity; a minimal region (≈residues 192–220; L213/L217 critical) contains the BH3-like motif required for binding anti-apoptotic Bcl-2 homologs. | Mutational mapping and U87MG glioma assays | Yang M.-C. et al., 2015 | https://doi.org/10.3892/ijo.2015.2838 | Mar 2015 | pqac-00000004 |
| Regulation (GSK3β phosphorylation S156; LiCl sensitivity) | GSK3β phosphorylates BCL2L12 at Ser156; S156 phosphorylation is required for anti-apoptotic activity and GSK3β inhibition (e.g., LiCl) reduces BCL2L12-mediated survival. | Yeast two-hybrid, phosphorylation mutants, GBM cell lines | Chou C.-H. et al., 2012 | https://doi.org/10.4161/cc.11.3.19051 | Feb 2012 | pqac-00000001 |
| Isoforms (BCL2L12 and BCL2L12A) | Two main transcripts: full-length (~334 aa) and truncated BCL2L12A (lacks exon 3, ~176 aa); expression in GBM reported as mRNA overexpression in ~52% (BCL2L12), 76% (BCL2L12A), and 86% for either isoform. | GBM tumor expression profiling | Chou C.-H. et al., 2012 | https://doi.org/10.4161/cc.11.3.19051 | Feb 2012 | pqac-00000001 |
| Pathway placement | Functions at the intersection of intrinsic (mitochondrial) apoptosis and p53 tumor-suppressor signaling, contributing to therapy resistance in glioma models. | Review synthesis and functional studies in glioma | Kouri F.M. et al., 2012 | https://doi.org/10.1100/2012/838916 | Feb 2012 | pqac-00000006 |
| Disease associations / biomarkers | Overexpressed in primary glioblastoma (high frequency in tumor specimens) and elevated BCL2L12 mRNA in CLL (n=65) associates with advanced stage and shorter overall survival (qRT‑PCR study). | GBM tissue analyses; CLL patient cohort (65 patients vs 23 controls) | Stegh A.H. review 2011; Papageorgiou S.G. et al., 2011 | https://doi.org/10.4161/cc.10.1.14365 ; https://doi.org/10.1634/theoncologist.2010-0349 | Jan 2011 ; Sep 2011 | pqac-00000003, pqac-00000005 |

Table: Compact table summarizing key molecular features, mechanisms, regulation, isoforms, pathway placement, and disease associations for human BCL2L12 (UniProt Q9HB09) with primary literature links and context IDs for traceability.

Gaps and limitations
- Despite targeted searches, we could not retrieve citable 2023–2024 full-text evidence within the current tool context. Consequently, the latest translational advances (e.g., nanotechnology-enabled delivery targeting BCL2L12, splicing-factor modulation of BCL2L12, or newer clinical datasets) are not detailed here. The mechanistic conclusions above are grounded in earlier, peer-reviewed human studies that remain widely cited. We recommend updating with 2023–2024 sources as they become accessible to confirm whether newer clinical cohorts or therapeutic platforms (e.g., BH3 mimetics, kinase modulators, nucleic acid therapeutics) have produced validated efficacy/signature data specific to BCL2L12 in GBM or other cancers (stegh2011beyondeffectorcaspase pages 3-4, chou2012gsk3betaregulatesbcl2l12 pages 1-2, yang2015bcl2l12witha pages 1-2, stegh2011beyondeffectorcaspase pages 1-3, yang2015bcl2l12witha pages 12-13, papageorgiou2011thenovelmember pages 1-2, kouri2012theroleof pages 4-5, yang2015bcl2l12witha pages 13-13).

References (URLs and publication dates)
- Stegh A.H. & DePinho R.A. Beyond effector caspase inhibition. Cell Cycle. Jan 2011. URL: https://doi.org/10.4161/cc.10.1.14365 (stegh2011beyondeffectorcaspase pages 3-4, stegh2011beyondeffectorcaspase pages 1-3)
- Chou C.-H. et al. GSK3β regulates Bcl2L12 and Bcl2L12A anti-apoptosis signaling in glioblastoma and is inhibited by LiCl. The FASEB Journal/Cell Cycle report. Feb 2012. URL: https://doi.org/10.4161/cc.11.3.19051 (chou2012gsk3betaregulatesbcl2l12 pages 1-2)
- Yang M.-C. et al. Bcl2L12 with a BH3-like domain in regulating apoptosis and TMZ-induced autophagy. Int J Oncol. Mar 2015. URL: https://doi.org/10.3892/ijo.2015.2838 (yang2015bcl2l12witha pages 1-2, yang2015bcl2l12witha pages 12-13)
- Kouri F.M., Jensen S.A., Stegh A.H. The Role of Bcl-2 Family Proteins in Therapy Responses of Malignant Astrocytic Gliomas: Bcl2L12 and Beyond. The Scientific World Journal. Feb 2012. URL: https://doi.org/10.1100/2012/838916 (kouri2012theroleof pages 4-5)
- Papageorgiou S.G. et al. BCL2L12 elevated in CLL: biomarker value. The Oncologist. Sep 2011. URL: https://doi.org/10.1634/theoncologist.2010-0349 (papageorgiou2011thenovelmember pages 1-2)

Citations
- Identity, localization, dual mechanism (caspases and p53): (stegh2011beyondeffectorcaspase pages 3-4, stegh2011beyondeffectorcaspase pages 1-3)
- Domain architecture, BH3-like motif function: (kouri2012theroleof pages 4-5, yang2015bcl2l12witha pages 1-2, yang2015bcl2l12witha pages 12-13)
- Regulation (GSK3β, S156; LiCl sensitivity): (chou2012gsk3betaregulatesbcl2l12 pages 1-2)
- Isoforms and GBM expression percentages: (chou2012gsk3betaregulatesbcl2l12 pages 1-2)
- Biomarker in CLL with cohort statistics: (papageorgiou2011thenovelmember pages 1-2)

References

1. (kouri2012theroleof pages 4-5): Fotini M. Kouri, Samuel A. Jensen, and Alexander H. Stegh. The role of bcl-2 family proteins in therapy responses of malignant astrocytic gliomas: bcl2l12 and beyond. The Scientific World Journal, 2012:1-8, Feb 2012. URL: https://doi.org/10.1100/2012/838916, doi:10.1100/2012/838916. This article has 65 citations.

2. (stegh2011beyondeffectorcaspase pages 3-4): Alexander H. Stegh and Ronald A. DePinho. Beyond effector caspase inhibition. Cell Cycle, 10:33-38, Jan 2011. URL: https://doi.org/10.4161/cc.10.1.14365, doi:10.4161/cc.10.1.14365. This article has 90 citations and is from a peer-reviewed journal.

3. (yang2015bcl2l12witha pages 1-2): MING-CHANG YANG, JOON-KHIM LOH, YI-YANG LI, WEN-SHENG HUANG, CHIA-HUA CHOU, JIIN-TSUEY CHENG, YENG-TSENG WANG, ANN-SHUNG LIEU, SHEN-LONG HOWNG, YI-REN HONG, and AN-KUO CHOU. Bcl2l12 with a bh3-like domain in regulating apoptosis and tmz-induced autophagy: a prospective combination of abt-737 and tmz for treating glioma. International journal of oncology, 46 3:1304-16, Mar 2015. URL: https://doi.org/10.3892/ijo.2015.2838, doi:10.3892/ijo.2015.2838. This article has 35 citations and is from a peer-reviewed journal.

4. (yang2015bcl2l12witha pages 12-13): MING-CHANG YANG, JOON-KHIM LOH, YI-YANG LI, WEN-SHENG HUANG, CHIA-HUA CHOU, JIIN-TSUEY CHENG, YENG-TSENG WANG, ANN-SHUNG LIEU, SHEN-LONG HOWNG, YI-REN HONG, and AN-KUO CHOU. Bcl2l12 with a bh3-like domain in regulating apoptosis and tmz-induced autophagy: a prospective combination of abt-737 and tmz for treating glioma. International journal of oncology, 46 3:1304-16, Mar 2015. URL: https://doi.org/10.3892/ijo.2015.2838, doi:10.3892/ijo.2015.2838. This article has 35 citations and is from a peer-reviewed journal.

5. (stegh2011beyondeffectorcaspase pages 1-3): Alexander H. Stegh and Ronald A. DePinho. Beyond effector caspase inhibition. Cell Cycle, 10:33-38, Jan 2011. URL: https://doi.org/10.4161/cc.10.1.14365, doi:10.4161/cc.10.1.14365. This article has 90 citations and is from a peer-reviewed journal.

6. (chou2012gsk3betaregulatesbcl2l12 pages 1-2): Chia-Hua Chou, An-Kuo Chou, Ching-Chih Lin, Wei-Jay Chen, Chih-Chang Wei, Ming-Chang Yang, Ching-Mei Hsu, For-Wey Lung, Joon-Khim Loh, Shen-Long Howng, and Yi-Ren Hong. Gsk3beta regulates bcl2l12 and bcl2l12a anti‐apoptosis signaling in glioblastoma and is inhibited by licl. The FASEB Journal, 26:532-542, Feb 2012. URL: https://doi.org/10.4161/cc.11.3.19051, doi:10.4161/cc.11.3.19051. This article has 43 citations.

7. (papageorgiou2011thenovelmember pages 1-2): Sotirios G. Papageorgiou, Christos K. Kontos, Vassiliki Pappa, Hellinida Thomadaki, Frida Kontsioti, John Dervenoulas, Efstathios Papageorgiou, Theofanis Economopoulos, and Andreas Scorilas. The novel member of the bcl2 gene family, bcl2l12, is substantially elevated in chronic lymphocytic leukemia patients, supporting its value as a significant biomarker. The oncologist, 16 9:1280-91, Sep 2011. URL: https://doi.org/10.1634/theoncologist.2010-0349, doi:10.1634/theoncologist.2010-0349. This article has 44 citations.

8. (yang2015bcl2l12witha pages 13-13): MING-CHANG YANG, JOON-KHIM LOH, YI-YANG LI, WEN-SHENG HUANG, CHIA-HUA CHOU, JIIN-TSUEY CHENG, YENG-TSENG WANG, ANN-SHUNG LIEU, SHEN-LONG HOWNG, YI-REN HONG, and AN-KUO CHOU. Bcl2l12 with a bh3-like domain in regulating apoptosis and tmz-induced autophagy: a prospective combination of abt-737 and tmz for treating glioma. International journal of oncology, 46 3:1304-16, Mar 2015. URL: https://doi.org/10.3892/ijo.2015.2838, doi:10.3892/ijo.2015.2838. This article has 35 citations and is from a peer-reviewed journal.

Citations

1. stegh2011beyondeffectorcaspase pages 1-3
2. papageorgiou2011thenovelmember pages 1-2
3. kouri2012theroleof pages 4-5
4. stegh2011beyondeffectorcaspase pages 3-4
5. https://doi.org/10.1100/2012/838916;
6. https://doi.org/10.3892/ijo.2015.2838
7. https://doi.org/10.4161/cc.10.1.14365
8. https://doi.org/10.4161/cc.11.3.19051
9. https://doi.org/10.1634/theoncologist.2010-0349
10. https://doi.org/10.3892/ijo.2015.2838;
11. https://doi.org/10.1100/2012/838916
12. https://doi.org/10.4161/cc.10.1.14365;
13. https://doi.org/10.1100/2012/838916,
14. https://doi.org/10.4161/cc.10.1.14365,
15. https://doi.org/10.3892/ijo.2015.2838,
16. https://doi.org/10.4161/cc.11.3.19051,
17. https://doi.org/10.1634/theoncologist.2010-0349,