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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: Q9NQS1
• Protein Description: RecName: Full=Cell death regulator Aven;
• Gene Information: Name=AVEN;
• Organism (full): Homo sapiens (Human).
• Protein Family: Not specified in UniProt
• Key Domains: Aven. (IPR026187)

MANDATORY VERIFICATION STEPS:

1. Check if the gene symbol "AVEN" 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 'AVEN' 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 AVEN (gene ID: AVEN, UniProt: Q9NQS1) 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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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: Q9NQS1
• Protein Description: RecName: Full=Cell death regulator Aven;
• Gene Information: Name=AVEN;
• Organism (full): Homo sapiens (Human).
• Protein Family: Not specified in UniProt
• Key Domains: Aven. (IPR026187)

MANDATORY VERIFICATION STEPS:

1. Check if the gene symbol "AVEN" 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 'AVEN' 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 AVEN (gene ID: AVEN, UniProt: Q9NQS1) 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.

Research plan and verification
- Identity verification: The target is the human gene AVEN (UniProt: Q9NQS1), encoding “cell death regulator Aven” (also called AVEN). Foundational papers identify human Aven as a novel anti-apoptotic factor that binds BCL-xL (BCL2L1) and Apaf-1, and inhibits caspase activation in human systems, confirming the gene/protein match and organism (Homo sapiens) (chau2000avenanovel pages 1-2, chau2000avenanovel pages 2-3).
- Scope of this report: mechanistic function, interaction partners, subcellular localization, pathway placement, disease links, and translational context, with URLs and publication years for each cited source.

1) Key concepts and definitions
- Definition and discovery: Aven is an anti-apoptotic protein first identified by yeast two-hybrid screening for interactors of BCL-xL; it also binds Apaf-1 and can block Apaf-1 self-association, thereby inhibiting apoptosome formation and caspase-9 activation downstream of mitochondrial cytochrome c release (intrinsic apoptosis) (Molecular Cell, 2000; https://doi.org/10.1016/S1097-2765(05)00021-3) (chau2000avenanovel pages 1-2, chau2000avenanovel pages 2-3).
- Mechanistic role: Aven prevents Apaf-1-driven apoptosome assembly/activation and can stabilize the pro-survival Bcl-2 family protein BCL-xL, collectively dampening caspase activation and apoptosis signals (Eur J Cancer, 2010; https://doi.org/10.1016/j.ejca.2010.06.011; Cell Death Differ, 2012; https://doi.org/10.1038/cdd.2012.17) (kutuk2010avenblocksdna pages 1-2, melzer2012theapaf1bindingprotein pages 1-2).
- Cellular distribution: Aven localizes mainly to light membrane/vesicular fractions, with diffuse nuclear and reticular cytoplasmic staining; it can co-localize with cathepsin D (CathD) in vesicular compartments, consistent with proteolytic processing in endolysosomal-derived environments (Molecular Cell, 2000; Cell Death Differ, 2012) (https://doi.org/10.1016/S1097-2765(05)00021-3; https://doi.org/10.1038/cdd.2012.17) (chau2000avenanovel pages 1-2, melzer2012theapaf1bindingprotein pages 1-2).

2) Mechanisms, interactions, and structural/biochemical details
- Apaf-1 interaction and apoptosome inhibition: Aven binds Apaf-1 at/near regions encompassing the CARD-containing portion of Apaf-1 and impairs Apaf-1 self-association, inhibiting Apaf-1–mediated caspase activation in cell-free systems and in cells (Molecular Cell, 2000; Cell Death Differ, 2012) (https://doi.org/10.1016/S1097-2765(05)00021-3; https://doi.org/10.1038/cdd.2012.17) (chau2000avenanovel pages 8-9, chau2000avenanovel pages 1-2, melzer2012theapaf1bindingprotein pages 1-2).
- BCL-xL interaction and stabilization: Aven forms complexes with BCL-xL in untreated breast cancer cells. Enforced Aven expression protects against UV-, SN-38–, and cisplatin-induced apoptosis, whereas Aven knockdown enhances apoptosis. Critically, loss of BCL-xL abrogates Aven’s protection, indicating Aven’s pro-survival function requires BCL-xL; Aven acts in part by stabilizing BCL-xL (Eur J Cancer, 2010; https://doi.org/10.1016/j.ejca.2010.06.011) (kutuk2010avenblocksdna pages 1-2).
- N-terminal inhibitory domain and cathepsin D activation: Aven harbors an N-terminal inhibitory segment whose proteolytic removal “unleashes” anti-apoptotic activity. Cathepsin D cleaves human Aven in vitro at mapped sites around amino acids ~144/145 and ~196/197; N-terminally truncated Aven retains Apaf-1 binding but exhibits enhanced anti-apoptotic function. Aven co-localizes with CathD in vesicular compartments, supporting physiological processing (Cell Death Differ, 2012; https://doi.org/10.1038/cdd.2012.17) (melzer2012theapaf1bindingprotein pages 1-2, melzer2012theapaf1bindingprotein pages 7-8).
- Putative BH3-like element and binding model: Computational/biophysical analyses identified a BH3-like segment in Aven (aa 141–153) predicted to bind BCL-xL with appreciable affinity, rationalizing the original yeast two-hybrid result and selective binding to anti-apoptotic Bcl-2 proteins (Open Biology Journal, 2012; https://doi.org/10.2174/1874196701205010006) (hawley2012anintegratedbioinformatics pages 4-5).
- DNA damage and checkpoint signaling: Aven contributes to the DNA damage response, promoting ATM-dependent G2/M checkpoint arrest; ATM phosphorylates Aven at Ser135 and Ser138, and these sites are required for Aven-driven checkpoint function (Eur J Cancer, 2010; https://doi.org/10.1016/j.ejca.2010.06.011; Open Biology Journal, 2012; https://doi.org/10.2174/1874196701205010006) (kutuk2010avenblocksdna pages 1-2, hawley2012anintegratedbioinformatics pages 4-5).

3) Pathway and subcellular context
- Pathway placement: Aven functions within the intrinsic apoptosis pathway at a post-mitochondrial checkpoint by directly inhibiting Apaf-1/apoptosome formation and by bolstering BCL-xL function, thereby reducing caspase-9 activation and executioner caspase processing (Molecular Cell, 2000; Cell Death Differ, 2012) (https://doi.org/10.1016/S1097-2765(05)00021-3; https://doi.org/10.1038/cdd.2012.17) (chau2000avenanovel pages 1-2, melzer2012theapaf1bindingprotein pages 1-2).
- Localization: Biochemical fractionation and microscopy place Aven in light membrane/vesicular pools and nucleus/cytoplasm; co-localization with CathD suggests endolysosomal/vesicular processing contributes to functional regulation (Molecular Cell, 2000; Cell Death Differ, 2012) (https://doi.org/10.1016/S1097-2765(05)00021-3; https://doi.org/10.1038/cdd.2012.17) (chau2000avenanovel pages 1-2, melzer2012theapaf1bindingprotein pages 1-2).

4) Disease associations and translational relevance
- Hematologic malignancy: AVEN is overexpressed in acute leukemias, correlating with adverse outcomes (e.g., poor prognosis in childhood ALL). In T-cell–specific transgenic models, AVEN overexpression cooperates with p53 haploinsufficiency to accelerate T-cell lymphomagenesis. In human leukemia lines (MOLT-4, CCRF-CEM, Kasumi-1), AVEN knockdown increases apoptosis and limits growth, supporting an oncoprotein role (Oncogene, 2013; https://doi.org/10.1038/onc.2012.263) (eissmann2013overexpressionofthe pages 1-2).
- Solid tumors and chemotherapy response: In breast cancer models, Aven promotes survival after DNA damage by stabilizing BCL-xL; Aven depletion sensitizes cells to DNA-damaging agents (Eur J Cancer, 2010; https://doi.org/10.1016/j.ejca.2010.06.011) (kutuk2010avenblocksdna pages 1-2).
- In vivo antiviral/apoptosis model: Human Aven reduced organismal death in a mouse Sindbis virus infection model, illustrating potent anti-apoptotic function in vivo (Molecular Cell, 2000; https://doi.org/10.1016/S1097-2765(05)00021-3) (chau2000avenanovel pages 2-3).

5) Quantitative and experimental highlights
- Interaction and function assays: Aven–BCL-xL and Aven–Apaf-1 interactions were shown by yeast two-hybrid and co-immunoprecipitation. Functional inhibition of the apoptosome was demonstrated in cell-free reconstitutions and in cells, with reduced caspase-9/-3 activation. Tissue fractionation and confocal microscopy delineated subcellular pools (Molecular Cell, 2000; https://doi.org/10.1016/S1097-2765(05)00021-3) (chau2000avenanovel pages 1-2).
- Cathepsin D processing sites: In vitro mapping implicated cleavage near aa 144/145 and 196/197. N-terminally truncated Aven (ΔN-Aven) retains Apaf-1 binding with enhanced anti-apoptotic effect, supporting a protease-activation switch (Cell Death Differ, 2012; https://doi.org/10.1038/cdd.2012.17) (melzer2012theapaf1bindingprotein pages 7-8).
- Dependency on BCL-xL: In breast cancer cells, Aven’s cytoprotection against DNA damage required BCL-xL; siRNA depletion of BCL-xL negated Aven’s protective effect (Eur J Cancer, 2010; https://doi.org/10.1016/j.ejca.2010.06.011) (kutuk2010avenblocksdna pages 1-2).
- Expression breadth: Northern blotting detected an ~1.7 kb AVEN transcript broadly in adult human tissues, with notable expression in heart, skeletal muscle, kidney, liver, pancreas, and testis (Molecular Cell, 2000; https://doi.org/10.1016/S1097-2765(05)00021-3) (chau2000avenanovel pages 2-3).

6) Recent developments (2023–2024)
- Targeted 2023–2024 literature searches did not retrieve AVEN-specific primary studies or authoritative reviews with novel mechanistic updates beyond the established interaction with BCL-xL/Apaf-1, CathD-mediated activation, and oncogenic roles summarized above. Current translational activity around intrinsic apoptosis more broadly (e.g., BCL-xL pharmacology) remains active, but AVEN-focused advances in 2023–2024 were not identified in our evidence set. This highlights a potential evidence gap and opportunity for updated functional/structural studies of AVEN in human disease contexts (kutuk2010avenblocksdna pages 1-2).

7) Expert perspectives and open questions
- The foundational and mechanistic studies collectively support AVEN as a node at the apoptosome checkpoint and a BCL-xL-cooperative survival factor. Key open questions include: structural resolution of the Aven–Apaf-1 interface; definitive mapping of domains/motifs governing BCL-xL binding in full-length Aven; the extent of protease-mediated activation in vivo across tumor types; and whether AVEN status can stratify response to DNA-damaging therapy or BCL-xL–targeted approaches (Molecular Cell, 2000; Eur J Cancer, 2010; Cell Death Differ, 2012) (chau2000avenanovel pages 1-2, kutuk2010avenblocksdna pages 1-2, melzer2012theapaf1bindingprotein pages 1-2).

Embedded evidence summary
| Aspect | Key finding | Experimental evidence / assay | Model / system | URL | Year | Citation ID |
|---|---|---|---|---|---:|---|
| Discovery and identity | AVEN identified as a novel inhibitor of caspase activation that binds BCL-xL and APAF-1; broadly expressed transcript (~1.7 kb). | Yeast two-hybrid discovery, co-immunoprecipitation, cell-free apoptosome inhibition assays, in vivo protection (Sindbis virus mouse model). | Human cDNAs, transfected BHK cells, cell-free extracts, mouse infection model. | https://doi.org/10.1016/s1097-2765(05)00021-3 | 2000 | (chau2000avenanovel pages 2-3) |
| Binding to BCL-xL | AVEN binds anti-apoptotic BCL-xL; contains a BH3-like region predicted to mediate binding. | Yeast two-hybrid, co-IP, peptide modeling and binding assays; functional dependency shown by loss-of-function experiments. | Human cell lines, peptide assays, computational modeling. | https://doi.org/10.1016/s1097-2765(05)00021-3 , https://doi.org/10.1016/j.ejca.2010.06.011 | 2000, 2010 | (chau2000avenanovel pages 2-3, kutuk2010avenblocksdna pages 1-2) |
| Binding to APAF-1 and apoptosome inhibition | AVEN binds APAF-1 and interferes with APAF-1 self-association, inhibiting apoptosome formation and downstream caspase-9/-3 activation. | Co-immunoprecipitation, cell-free apoptosome reconstitution and caspase activity assays. | Cell-free extracts, human cells. | https://doi.org/10.1016/s1097-2765(05)00021-3 , https://doi.org/10.1038/cdd.2012.17 | 2000, 2012 | (chau2000avenanovel pages 2-3, melzer2012theapaf1bindingprotein pages 1-2) |
| Subcellular localization | Predominantly in light-membrane/vesicular fractions; shows diffuse nuclear and reticular cytoplasmic staining; colocalizes with Cathepsin D in vesicular compartments. | Subcellular fractionation, immunofluorescence/confocal microscopy, co-localization studies. | Transfected BHK cells, MCF-7 breast cancer cells. | https://doi.org/10.1016/s1097-2765(05)00021-3 , https://doi.org/10.1038/cdd.2012.17 | 2000, 2012 | (chau2000avenanovel pages 2-3, melzer2012theapaf1bindingprotein pages 1-2) |
| Stabilization of BCL-xL & effect on DNA-damage apoptosis | AVEN stabilizes BCL-xL and protects cells from DNA-damage–induced apoptosis; BCL-xL is required for AVEN's prosurvival effect (BCL-xL depletion abrogates protection). | Overexpression and RNAi knockdown, Annexin V, DEVDase/caspase activity assays, tissue microarray analysis. | Human breast cancer cell lines (e.g., MCF-7); clinical tissue arrays. | https://doi.org/10.1016/j.ejca.2010.06.011 | 2010 | (kutuk2010avenblocksdna pages 1-2) |
| ATM-related phosphorylation notes | AVEN participates in DNA-damage response: ATM phosphorylates AVEN (Ser135/Ser138), required for G2/M checkpoint function. | Phosphorylation assays, checkpoint assays, mutational analysis of phosphorylation sites. | Human cell lines subjected to DNA damage. | https://doi.org/10.1016/j.ejca.2010.06.011 , https://doi.org/10.2174/1874196701205010006 | 2010, 2012 | (kutuk2010avenblocksdna pages 1-2, hawley2012anintegratedbioinformatics pages 4-5) |
| Cathepsin D cleavage sites & activation of anti-apoptotic function | Cathepsin D (CathD) cleaves AVEN N-terminus (mapped in vitro to ~aa144/145 and aa196/197); N-terminal removal "unleashes" AVEN's anti-apoptotic activity while truncated AVEN still binds APAF-1. | In vitro CathD cleavage assays, western blot mapping of cleavage, co-IP of truncated constructs, colocalization with CathD. | Human cancer cell lines (e.g., MCF-7), biochemical assays. | https://doi.org/10.1038/cdd.2012.17 | 2012 | (melzer2012theapaf1bindingprotein pages 1-2) |
| Oncogenic overexpression in hematologic malignancies & functional effects | AVEN is overexpressed in acute leukemias (correlates with poor prognosis); AVEN overexpression promotes lymphomagenesis in transgenic mice (cooperates with p53 loss); AVEN knockdown reduces leukemia cell growth via apoptosis. | Patient mRNA expression profiling, transgenic mouse models, xenografts, RNAi-mediated knockdown, proliferation/apoptosis assays. | Human T-ALL patient samples, transgenic mice, human leukemia cell lines (MOLT-4, CCRF-CEM, Kasumi-1). | https://doi.org/10.1038/onc.2012.263 | 2013 | (eissmann2013overexpressionofthe pages 1-2) |

Table: Concise, source-linked experimental evidence summary for human AVEN (Q9NQS1), listing key functional findings, assays, models, exact URLs, years, and internal citation IDs to support functional annotation and translational context.

Conclusions
- Human AVEN (Q9NQS1) is a non-enzymatic anti-apoptotic regulator that binds BCL-xL and Apaf-1, inhibits apoptosome formation and caspase activation, and promotes cell survival after genotoxic stress, at least partly by stabilizing BCL-xL. Its anti-apoptotic potential is enhanced by N‑terminal removal via cathepsin D. AVEN is broadly expressed and is overexpressed in leukemias with functional oncogenic effects in vivo and in cell models, highlighting biomarker and therapeutic relevance. While the core biology is well established, recent AVEN-specific updates (2023–2024) appear limited in the retrieved literature, underscoring a need for renewed investigation into its structure–function relationships and translational exploitation (chau2000avenanovel pages 1-2, chau2000avenanovel pages 2-3, kutuk2010avenblocksdna pages 1-2, melzer2012theapaf1bindingprotein pages 1-2, eissmann2013overexpressionofthe pages 1-2).

References

1. (chau2000avenanovel pages 1-2): BN Chau, EHY Cheng, DA Kerr, and JM Hardwick. Aven, a novel inhibitor of caspase activation, binds bcl-xl and apaf-1. Molecular cell, 6 1:31-40, Jul 2000. URL: https://doi.org/10.1016/s1097-2765(05)00021-3, doi:10.1016/s1097-2765(05)00021-3. This article has 305 citations and is from a highest quality peer-reviewed journal.

2. (chau2000avenanovel pages 2-3): BN Chau, EHY Cheng, DA Kerr, and JM Hardwick. Aven, a novel inhibitor of caspase activation, binds bcl-xl and apaf-1. Molecular cell, 6 1:31-40, Jul 2000. URL: https://doi.org/10.1016/s1097-2765(05)00021-3, doi:10.1016/s1097-2765(05)00021-3. This article has 305 citations and is from a highest quality peer-reviewed journal.

3. (kutuk2010avenblocksdna pages 1-2): Ozgur Kutuk, Sehime Gulsun Temel, Sahsine Tolunay, and Huveyda Basaga. Aven blocks dna damage-induced apoptosis by stabilising bcl-xl. European journal of cancer, 46 13:2494-505, Sep 2010. URL: https://doi.org/10.1016/j.ejca.2010.06.011, doi:10.1016/j.ejca.2010.06.011. This article has 55 citations and is from a domain leading peer-reviewed journal.

4. (melzer2012theapaf1bindingprotein pages 1-2): I. Melzer, Sbm Fernández, S. Bösser, K. Lohrig, U. Lewandrowski, D. Wolters, S. Kehrloesser, Marie-Luise Brezniceanu, Alexander C. Theos, PM Irusta, Francis Impens, K. Gevaert, and M. Zörnig. The apaf-1-binding protein aven is cleaved by cathepsin d to unleash its anti-apoptotic potential. Cell Death and Differentiation, 19:1435-1445, Mar 2012. URL: https://doi.org/10.1038/cdd.2012.17, doi:10.1038/cdd.2012.17. This article has 39 citations and is from a domain leading peer-reviewed journal.

5. (chau2000avenanovel pages 8-9): BN Chau, EHY Cheng, DA Kerr, and JM Hardwick. Aven, a novel inhibitor of caspase activation, binds bcl-xl and apaf-1. Molecular cell, 6 1:31-40, Jul 2000. URL: https://doi.org/10.1016/s1097-2765(05)00021-3, doi:10.1016/s1097-2765(05)00021-3. This article has 305 citations and is from a highest quality peer-reviewed journal.

6. (melzer2012theapaf1bindingprotein pages 7-8): I. Melzer, Sbm Fernández, S. Bösser, K. Lohrig, U. Lewandrowski, D. Wolters, S. Kehrloesser, Marie-Luise Brezniceanu, Alexander C. Theos, PM Irusta, Francis Impens, K. Gevaert, and M. Zörnig. The apaf-1-binding protein aven is cleaved by cathepsin d to unleash its anti-apoptotic potential. Cell Death and Differentiation, 19:1435-1445, Mar 2012. URL: https://doi.org/10.1038/cdd.2012.17, doi:10.1038/cdd.2012.17. This article has 39 citations and is from a domain leading peer-reviewed journal.

7. (hawley2012anintegratedbioinformatics pages 4-5): Robert G. Hawley, Yuzhong Chen, Irene Riz, and Chen Zeng. An integrated bioinformatics and computational biology approach identifies new bh3-only protein candidates. The open biology journal, 5:6-16, May 2012. URL: https://doi.org/10.2174/1874196701205010006, doi:10.2174/1874196701205010006. This article has 22 citations.

8. (eissmann2013overexpressionofthe pages 1-2): M. Eissmann, I. Melzer, S. B. M. Fernández, G. Michel, M. H. Angelis, G. Hoefler, P. Finkenwirth, A. Jauch, B. Schoell, M. Grez, M. Schmidt, C. Bartholomae, S. Newrzela, Nadine Haetscher, M. Rieger, C. Zachskorn, M. Mittelbronn, and M. Zörnig. Overexpression of the anti-apoptotic protein aven contributes to increased malignancy in hematopoietic neoplasms. Oncogene, 32:2586-2591, May 2013. URL: https://doi.org/10.1038/onc.2012.263, doi:10.1038/onc.2012.263. This article has 33 citations and is from a domain leading peer-reviewed journal.

Citations

1. kutuk2010avenblocksdna pages 1-2
2. hawley2012anintegratedbioinformatics pages 4-5
3. eissmann2013overexpressionofthe pages 1-2
4. chau2000avenanovel pages 2-3
5. chau2000avenanovel pages 1-2
6. chau2000avenanovel pages 8-9
7. https://doi.org/10.1016/S1097-2765(05
8. https://doi.org/10.1016/j.ejca.2010.06.011;
9. https://doi.org/10.1038/cdd.2012.17
10. https://doi.org/10.1016/j.ejca.2010.06.011
11. https://doi.org/10.2174/1874196701205010006
12. https://doi.org/10.1038/onc.2012.263
13. https://doi.org/10.1016/s1097-2765(05
14. https://doi.org/10.1016/j.ejca.2010.06.011,
15. https://doi.org/10.1038/cdd.2012.17,
16. https://doi.org/10.2174/1874196701205010006,
17. https://doi.org/10.1038/onc.2012.263,