provider: falcon
model: Edison Scientific Literature
cached: false
start_time: '2026-02-08T20:24:34.568934'
end_time: '2026-02-08T20:31:55.312574'
duration_seconds: 440.75
template_file: templates/gene_research_go_focused.md
template_variables:
organism: human
gene_id: MEX3B
gene_symbol: MEX3B
uniprot_accession: Q6ZN04
protein_description: 'RecName: Full=RNA-binding protein MEX3B; AltName: Full=RING
finger and KH domain-containing protein 3; AltName: Full=RING finger protein 195;'
gene_info: Name=MEX3B; Synonyms=KIAA2009, RKHD3, RNF195;
organism_full: Homo sapiens (Human).
protein_family: Not specified in UniProt
protein_domains: KH-I_MEX3_rpt1. (IPR047228); KH-I_MEX3_rpt2. (IPR047226); KH_dom.
(IPR004087); KH_dom_type_1. (IPR004088); KH_dom_type_1_sf. (IPR036612)
provider_config:
timeout: 600
max_retries: 3
parameters:
allowed_domains: []
temperature: 0.1
citation_count: 25

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: Q6ZN04
• Protein Description: RecName: Full=RNA-binding protein MEX3B; AltName: Full=RING finger and KH domain-containing protein 3; AltName: Full=RING finger protein 195;
• Gene Information: Name=MEX3B; Synonyms=KIAA2009, RKHD3, RNF195;
• Organism (full): Homo sapiens (Human).
• Protein Family: Not specified in UniProt
• Key Domains: KH-I_MEX3_rpt1. (IPR047228); KH-I_MEX3_rpt2. (IPR047226); KH_dom. (IPR004087); KH_dom_type_1. (IPR004088); KH_dom_type_1_sf. (IPR036612)

MANDATORY VERIFICATION STEPS:

1. Check if the gene symbol "MEX3B" 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 'MEX3B' 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 MEX3B (gene ID: MEX3B, UniProt: Q6ZN04) 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: Q6ZN04
• Protein Description: RecName: Full=RNA-binding protein MEX3B; AltName: Full=RING finger and KH domain-containing protein 3; AltName: Full=RING finger protein 195;
• Gene Information: Name=MEX3B; Synonyms=KIAA2009, RKHD3, RNF195;
• Organism (full): Homo sapiens (Human).
• Protein Family: Not specified in UniProt
• Key Domains: KH-I_MEX3_rpt1. (IPR047228); KH-I_MEX3_rpt2. (IPR047226); KH_dom. (IPR004087); KH_dom_type_1. (IPR004088); KH_dom_type_1_sf. (IPR036612)

MANDATORY VERIFICATION STEPS:

1. Check if the gene symbol "MEX3B" 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 'MEX3B' 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 MEX3B (gene ID: MEX3B, UniProt: Q6ZN04) 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
- Identity verified: MEX3B (gene symbol), human protein with UniProt accession Q6ZN04, described as an RNA-binding protein with KH domains and a C3HC4-type RING finger consistent with dual RNA-binding and E3 ubiquitin ligase functions. Domain architecture and roles are supported by recent structural/biophysical and review literature focused on human MEX3 family members, including MEX3B (KH1/KH2 at N-terminus; C3HC4/RING at C-terminus) (yang2024molecularmechanismof pages 1-2, lederer2021oncogenicpotentialof pages 4-5). The organism context is Homo sapiens.

Comprehensive research report

Key concepts and definitions
- Protein family and domains: Human MEX3B is a member of the MEX-3 family of RNA-binding proteins characterized by two tandem KH domains (KH1 and KH2) mediating sequence-specific RNA recognition and a C3HC4 (RING) domain conferring E3 ubiquitin ligase activity at the C-terminus. This dual-function architecture underlies its roles in post-transcriptional mRNA regulation and post-translational ubiquitination of substrate proteins (Communications Biology, 2024; Biology review, 2021) (yang2024molecularmechanismof pages 1-2, lederer2021oncogenicpotentialof pages 4-5). URL: https://doi.org/10.1038/s42003-024-05845-y; https://doi.org/10.3390/biology10050415.
- Mechanistic theme: MEX3B binds target mRNAs through the tandem KH domains to regulate stability/translation and can, in other contexts, act as an E3 ligase via the RING, sometimes assembled by lncRNA scaffolds such as HOTAIR to ubiquitinate specific proteins (IJMS review, 2020; Biology review, 2021) (jasinskibergner2020theroleof pages 9-12, lederer2021oncogenicpotentialof pages 4-5). URL: https://doi.org/10.3390/ijms21155209; https://doi.org/10.3390/biology10050415.

Recent developments and latest research (emphasis 2023–2024)
- High-resolution RNA-recognition mechanism for HLA-A: A 2024 structural/biophysical study defined the sequence-specific HLA-A 3′UTR binding by hMEX3B. The authors mapped a high-affinity 12-nt motif (CUGAGCUGUAAC) and showed the tandem KH1/2 binds ~100× more strongly than single KH domains. NMR/SAXS and mutagenesis revealed variable-loop threonine/arginine pairs that are essential for RNA recognition in vitro and in cells. Functionally, MEX3B binding promotes degradation of substrate mRNAs and reduces HLA-A surface expression, supporting a mechanism of tumor immune escape (Communications Biology, Feb 2024) (yang2024molecularmechanismof pages 1-2). URL: https://doi.org/10.1038/s42003-024-05845-y.
- Innate immunity—TLR3 co-receptor role reinforced: A 2024 review on RNA-binding proteins (RBPs) in antiviral signaling specifically lists Mex3B (RNF195) as a RING-type RBP acting as a co-receptor for TLR3 in endosomes that interacts with viral dsRNA to potentiate signaling, placing MEX3B among RBPs that modulate PRR activation via co-receptor functions and ubiquitination (Virology Journal, Sep 2024) (li2024thernabindingproteins pages 9-11). URL: https://doi.org/10.1186/s12985-024-02503-x.
- Cancer immunotherapy resistance: Authoritative reviews continue to highlight MEX3B as a tumor-intrinsic regulator of antigen presentation by binding the HLA-A 3′UTR, thereby reducing HLA-A and contributing to anti–PD-1 resistance—a mechanism discovered in melanoma models and now contextualized more broadly across cancers (IJMS 2020; expert commentary in Clinical Cancer Research 2018; 2024 Communications Biology supports the binding mechanism) (jasinskibergner2020theroleof pages 9-12, yang2024molecularmechanismof pages 1-2). URLs: https://doi.org/10.3390/ijms21155209; https://doi.org/10.1038/s42003-024-05845-y.
- Pan-cancer context (2023): Bioinformatic analyses in NSCLC and other tumors integrate TCGA resources and consistently implicate the MEX3 family (including MEX3B) in tumor biology and immune correlates, supporting clinical relevance and prompting mechanistic follow-up (Molecular Biotechnology, Dec 2023) (zhang2023investigationofthe pages 11-12). URL: https://doi.org/10.1007/s12033-022-00638-2.

Primary function, biochemical activities, and substrate/target specificity
- RNA-binding specificity and validated RNA targets:
- HLA-A 3′UTR: hMEX3B binds a defined 12-nt motif within the HLA-A 3′UTR via the tandem KH domains, with mutations in KH variable loops abolishing binding and function. This binding promotes mRNA decay and reduces HLA-A surface presentation, mechanistically linking MEX3B to immune evasion (Communications Biology, 2024) (yang2024molecularmechanismof pages 1-2).
- Broader target class: Reviews indicate MEX-3 proteins frequently target immune-relevant mRNAs and 3′UTRs; MEX3B has been repeatedly associated with MHC-I pathway regulation, notably HLA-A. Additional putative APM targets have been hypothesized, but require direct validation (IJMS review, 2020) (jasinskibergner2020theroleof pages 9-12).
- E3 ubiquitin ligase activity and validated protein substrates:
- MEX3B is reported to ubiquitinate and promote degradation of specific proteins, including SNUPN (Snurportin-1), SUZ12, and RUNX3, in complexes that require the lncRNA HOTAIR as a molecular scaffold. This lncRNA-dependent assembly connects MEX3B’s RING E3 activity to specific substrates relevant to chromatin regulation and tumor suppression (Biology review summarizing primary literature; see also seminal HOTAIR scaffold work) (lederer2021oncogenicpotentialof pages 4-5, lederer2021oncogenicpotentialof pages 11-12). URLs: https://doi.org/10.3390/biology10050415; https://doi.org/10.1038/ncomms3939.
- Ubiquitin linkage types: While K48- and K63-linked chains are common regulators in related RNP granule biology and innate pathways, specific chain linkages installed by MEX3B on its validated substrates remain insufficiently defined in the human literature surveyed here (lederer2021oncogenicpotentialof pages 4-5).

Cellular and subcellular localization where MEX3B functions
- Cytoplasmic RNP granules: MEX-3 family proteins, including MEX3B, are enriched in cytoplasmic processing bodies (P-bodies) and participate in post-transcriptional control in RNA–protein condensates. MEX3 proteins can shuttle between cytoplasm and nucleus. These localizations are congruent with MEX3B’s mRNA-decay and translational control activities and with lncRNA-scaffolded E3 functions (Biology review 2021; IJMS review 2020) (lederer2021oncogenicpotentialof pages 4-5, jasinskibergner2020theroleof pages 9-12).
- Endosomal context: As a TLR3 co-receptor RBP, Mex3B is implicated at endosomal compartments where TLR3 engages viral dsRNA, positioning MEX3B to influence innate signaling (Virology Journal 2024) (li2024thernabindingproteins pages 9-11).

Pathway roles—innate immune signaling and antigen presentation
- TLR3 signaling: Mex3B is described as a co-receptor facilitating TLR3 sensing of dsRNA in endosomes, contributing positively to antiviral innate responses. This co-receptor role places Mex3B upstream of TRIF recruitment and downstream IRF3/NF-κB activation cascades that induce type I/III interferons and inflammatory cytokines (Virology Journal 2024) (li2024thernabindingproteins pages 9-11).
- RLR (RIG-I/MDA5/MAVS) context: Reviews class Mex3B among RBPs that modulate PRRs, though direct human mechanistic data on MEX3B’s control of RIG-I/MDA5/MAVS are less resolved relative to TLR3. The theme is that RBP–E3 ligase coupling can tune PRR activation via co-receptor or ubiquitin-dependent processes (Virology Journal 2024) (li2024thernabindingproteins pages 9-11).
- Antigen presentation: MEX3B directly represses HLA-A expression at the mRNA level via 3′UTR binding, yielding reduced MHC-I surface expression and antigen display. This directly links MEX3B to tumor immune evasion (Communications Biology 2024; IJMS 2020 review of the 2018 discovery) (yang2024molecularmechanismof pages 1-2, jasinskibergner2020theroleof pages 9-12).

Current applications and real-world implementations
- Biomarker and resistance mechanism in immuno-oncology: MEX3B’s suppression of HLA-A provides a tumor-intrinsic mechanism of resistance to T cell–mediated therapies (e.g., anti–PD-1). This mechanism has been highlighted in expert commentaries and reviews as actionable biology for patient stratification and as a rationale for targeting post-transcriptional repression to restore antigen presentation (Clinical Cancer Research commentary 2018; IJMS 2020; Communications Biology 2024 mechanism) (jasinskibergner2020theroleof pages 9-12, yang2024molecularmechanismof pages 1-2).
- Pan-cancer bioinformatics and target discovery: Analyses integrating TCGA resources in 2023 underscore the MEX3 family (including MEX3B) in tumor biology and immunity, motivating translational research into MEX3B as a biomarker/modulator of immune microenvironments (Molecular Biotechnology 2023) (zhang2023investigationofthe pages 11-12). URL: https://doi.org/10.1007/s12033-022-00638-2.

Expert opinions and analysis from authoritative sources
- Consensus view: Authoritative reviews in tumor immunology and RNA biology position MEX3B as a key post-transcriptional regulator of MHC-I antigen presentation with direct implications for immune checkpoint therapy response, and as a TLR3 co-receptor RBP in innate antiviral sensing. These functions are coherent with its KH/RING domain architecture and subcellular granule/endosomal localizations (IJMS 2020; Virology Journal 2024; Biology 2021 overview) (jasinskibergner2020theroleof pages 9-12, li2024thernabindingproteins pages 9-11, lederer2021oncogenicpotentialof pages 4-5).
- Mechanistic clarity improved in 2024: The 2024 structural work provides the most precise molecular map to date for MEX3B–mRNA recognition (HLA-A motif and essential KH residues), filling a longstanding gap in defining paralog- and target-specific RNA contacts (Communications Biology 2024) (yang2024molecularmechanismof pages 1-2).

Relevant statistics and quantitative data
- RNA-binding affinity: Tandem KH1/2 of hMEX3B binds an optimized HLA-A 3′UTR 12-nt motif roughly 100-fold more strongly than individual KH domains, per NMR/SAXS-guided biophysical measurements (Communications Biology, Feb 2024) (yang2024molecularmechanismof pages 1-2).
- Clinical correlations: Reviews summarizing the original melanoma discovery report that elevated MEX3B correlates with non-response to PD-1 blockade, consistent with reduced HLA-A levels. While effect-size metrics (e.g., HRs/AUCs) are not enumerated in the 2020–2024 reviews cited here, the 2024 mechanistic paper reinforces the direct biochemical basis for the observed immunotherapy resistance phenotype (jasinskibergner2020theroleof pages 9-12, yang2024molecularmechanismof pages 1-2).

Open questions and caveats
- Substrate linkage specificity: For MEX3B’s validated protein substrates (e.g., SNUPN, RUNX3, SUZ12), ubiquitin chain types and E2 partners remain to be fully defined in human systems. The role of lncRNA scaffolds (e.g., HOTAIR) appears critical for substrate selection but the generality of this mechanism across targets requires further testing (lederer2021oncogenicpotentialof pages 4-5, lederer2021oncogenicpotentialof pages 11-12).
- Transcriptome-wide RNA target maps: Family-wide CLIP/RIP datasets remain limited; additional high-resolution crosslinking studies will be valuable to define the full MEX3B targetome beyond HLA-A (lederer2021oncogenicpotentialof pages 4-5).

Embedded summary table
| Feature | Key findings | Primary sources (year, journal, URL) |
|---|---|---|
| Identity & domains | Two N‑terminal KH domains (KH1/KH2); C3HC4 (RING) at C‑terminus; dual RNA‑binding + E3 ligase architecture | Yang et al., 2024, Communications Biology — https://doi.org/10.1038/s42003-024-05845-y; Lederer et al., 2021, Biology — https://doi.org/10.3390/biology10050415 (yang2024molecularmechanismof pages 1-2, lederer2021oncogenicpotentialof pages 4-5) |
| RNA‑binding motif & targets | High‑affinity 12‑nt HLA‑A 3'UTR motif (CUGAGCUGUAAC); tandem KH1+KH2 bind ~100× stronger than single KH; family reports tie MEX3 proteins to TAPBP/tapasin 3'UTR regulation | Yang et al., 2024, Communications Biology — https://doi.org/10.1038/s42003-024-05845-y; Jasinski‑Bergner et al., 2020, IJMS — https://doi.org/10.3390/ijms21155209 (yang2024molecularmechanismof pages 1-2, jasinskibergner2020theroleof pages 9-12) |
| E3 ligase activity & substrates | Validated ubiquitination targets reported: SNUPN (Snurportin‑1), RUNX3, SUZ12; many ubiquitination events reported to require lncRNA HOTAIR as scaffold | Lederer et al., 2021, Biology — https://doi.org/10.3390/biology10050415; Yoon et al., 2013, Nat Commun — https://doi.org/10.1038/ncomms3939 (lederer2021oncogenicpotentialof pages 4-5, lederer2021oncogenicpotentialof pages 11-12) |
| Subcellular localization | Enriched in processing bodies (P‑bodies); shuttles nucleus ⇄ cytoplasm; implicated in RNP granules/stress responses | Lederer et al., 2021, Biology — https://doi.org/10.3390/biology10050415; Jasinski‑Bergner et al., 2020, IJMS — https://doi.org/10.3390/ijms21155209 (lederer2021oncogenicpotentialof pages 4-5, jasinskibergner2020theroleof pages 9-12) |
| Innate immunity roles | Reported as a TLR3 co‑receptor in endosomes; implicated (family/parallel evidence) in modulating RIG‑I/MDA5/MAVS signaling and antiviral sensing | Li et al., 2024, Virology Journal — https://doi.org/10.1186/s12985-024-02503-x; related mechanistic reviews (li2024thernabindingproteins pages 9-11, jasinskibergner2020theroleof pages 9-12) |
| Cancer & immunotherapy relevance | Binds HLA‑A 3'UTR → decreased HLA‑A mRNA/protein and reduced antigen presentation; associated with resistance to anti–PD‑1 immunotherapy (Clin Cancer Res 2018); 2024 structural work elucidates binding motif/mechanism | Huang et al., 2018, Clin Cancer Res — https://doi.org/10.1158/1078-0432.ccr-17-2483; Yang et al., 2024, Communications Biology — https://doi.org/10.1038/s42003-024-05845-y (lederer2021oncogenicpotentialof pages 11-12, yang2024molecularmechanismof pages 1-2, jasinskibergner2020theroleof pages 9-12) |

Table: Compact, citation‑backed summary of human MEX3B features: domains, RNA motif/targets, E3 substrates, localization, innate‑immunity roles, and cancer/immunotherapy relevance (2023–2024 emphasis).

Conclusion—precise role for human MEX3B (Q6ZN04)
- MEX3B is a human KH/RING dual-function protein that recognizes specific 3′UTR motifs (now defined for HLA-A) to destabilize transcripts and reduce antigen presentation, and that can serve as an E3 ligase for discrete substrates, often in HOTAIR-scaffolded complexes. It localizes to cytoplasmic RNA granules and endosomal compartments where it participates in post-transcriptional control and innate immune sensing, respectively. Mechanistically, MEX3B is directly implicated in tumor immune evasion and resistance to checkpoint blockade through downregulation of HLA-A. The 2024 biophysical study provides definitive sequence and structural determinants of HLA-A targeting by MEX3B, offering a concrete foundation for therapeutic strategies to restore antigen presentation or modulate innate sensing in cancer and infection (yang2024molecularmechanismof pages 1-2, jasinskibergner2020theroleof pages 9-12, li2024thernabindingproteins pages 9-11, lederer2021oncogenicpotentialof pages 4-5).

References

1. (yang2024molecularmechanismof pages 1-2): Kanglong Yang, Guanglin Chen, Fan Yu, Xianyang Fang, Jiahai Zhang, Zhiyong Zhang, Yunyu Shi, and Liang Zhang. Molecular mechanism of specific hla-a mrna recognition by the rna-binding-protein hmex3b to promote tumor immune escape. Communications Biology, Feb 2024. URL: https://doi.org/10.1038/s42003-024-05845-y, doi:10.1038/s42003-024-05845-y. This article has 6 citations and is from a peer-reviewed journal.

2. (lederer2021oncogenicpotentialof pages 4-5): Marcell Lederer, Simon Müller, Markus Glaß, Nadine Bley, Christian Ihling, Andrea Sinz, and Stefan Hüttelmaier. Oncogenic potential of the dual-function protein mex3a. Biology, May 2021. URL: https://doi.org/10.3390/biology10050415, doi:10.3390/biology10050415. This article has 22 citations and is from a poor quality or predatory journal.

3. (jasinskibergner2020theroleof pages 9-12): Simon Jasinski-Bergner, André Steven, and Barbara Seliger. The role of the rna-binding protein family mex-3 in tumorigenesis. International Journal of Molecular Sciences, 21:5209, Jul 2020. URL: https://doi.org/10.3390/ijms21155209, doi:10.3390/ijms21155209. This article has 26 citations and is from a poor quality or predatory journal.

4. (li2024thernabindingproteins pages 9-11): Jianguo Li, Jingge Yu, Ao Shen, Suwen Lai, Zhiping Liu, and Tian-Sheng He. The rna-binding proteins regulate innate antiviral immune signaling by modulating pattern recognition receptors. Virology Journal, Sep 2024. URL: https://doi.org/10.1186/s12985-024-02503-x, doi:10.1186/s12985-024-02503-x. This article has 8 citations and is from a peer-reviewed journal.

5. (zhang2023investigationofthe pages 11-12): Ming Zhang, Linfeng Cao, Gouxin Hou, Xiaodong Lv, and Jingjing Deng. Investigation of the potential correlation between rna-binding proteins in the evolutionarily conserved mex3 family and non-small-cell lung cancer. Molecular Biotechnology, 65:1263-1274, Dec 2023. URL: https://doi.org/10.1007/s12033-022-00638-2, doi:10.1007/s12033-022-00638-2. This article has 13 citations and is from a peer-reviewed journal.

6. (lederer2021oncogenicpotentialof pages 11-12): Marcell Lederer, Simon Müller, Markus Glaß, Nadine Bley, Christian Ihling, Andrea Sinz, and Stefan Hüttelmaier. Oncogenic potential of the dual-function protein mex3a. Biology, May 2021. URL: https://doi.org/10.3390/biology10050415, doi:10.3390/biology10050415. This article has 22 citations and is from a poor quality or predatory journal.

Citations

1. yang2024molecularmechanismof pages 1-2
2. li2024thernabindingproteins pages 9-11
3. zhang2023investigationofthe pages 11-12
4. jasinskibergner2020theroleof pages 9-12
5. lederer2021oncogenicpotentialof pages 4-5
6. lederer2021oncogenicpotentialof pages 11-12
7. https://doi.org/10.1038/s42003-024-05845-y;
8. https://doi.org/10.3390/biology10050415.
9. https://doi.org/10.3390/ijms21155209;
10. https://doi.org/10.1038/s42003-024-05845-y.
11. https://doi.org/10.1186/s12985-024-02503-x.
12. https://doi.org/10.1007/s12033-022-00638-2.
13. https://doi.org/10.3390/biology10050415;
14. https://doi.org/10.1038/ncomms3939.
15. https://doi.org/10.3390/biology10050415
16. https://doi.org/10.3390/ijms21155209
17. https://doi.org/10.1038/ncomms3939
18. https://doi.org/10.1186/s12985-024-02503-x;
19. https://doi.org/10.1158/1078-0432.ccr-17-2483;
20. https://doi.org/10.1038/s42003-024-05845-y
21. https://doi.org/10.1038/s42003-024-05845-y,
22. https://doi.org/10.3390/biology10050415,
23. https://doi.org/10.3390/ijms21155209,
24. https://doi.org/10.1186/s12985-024-02503-x,
25. https://doi.org/10.1007/s12033-022-00638-2,