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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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.
The target protein is human Akirin-2, encoded by AKIRIN2 (synonym C6orf166) and assigned to the akirin protein family (UniProt accession Q53H80, per user-provided context). The literature retrieved here is consistent with an evolutionarily conserved, primarily nuclear, non-enzymatic transcriptional cofactor/adaptor termed Akirin2/Akirin-2 (mammals) and Akirin (invertebrates), which lacks an obvious DNA-binding motif and functions via protein–protein interactions to connect signaling-dependent transcription factors (notably NF-κB pathway outputs) to chromatin remodeling machinery (tartey2016akirin2mediatedtranscriptionalcontrol pages 5-6, tartey2016akirin2mediatedtranscriptionalcontrol pages 1-2, tartey2016akirin2mediatedtranscriptionalcontrol pages 6-8).
Scope note: Much mechanistic evidence comes from mouse immune cells and Drosophila; these are used to infer human function because the mechanism is described as conserved and directly discussed in the mammalian Akirin2 context (tartey2016akirin2mediatedtranscriptionalcontrol pages 5-6, bonnay2014akirinspecifiesnfκb pages 2-3).
AKIRIN2 is best understood as a signal-responsive transcriptional cofactor/adaptor rather than an enzyme, receptor, or transporter. It is described as a highly conserved nuclear protein required for NF-κB-dependent gene expression, but importantly it contributes to selective induction of a subset of NF-κB target genes rather than serving as a universal NF-κB co-activator (tartey2016akirin2mediatedtranscriptionalcontrol pages 5-6, tartey2016akirin2mediatedtranscriptionalcontrol pages 10-11).
Mechanistically, AKIRIN2 is described as linking transcriptional programs to chromatin remodeling, particularly SWI/SNF (BAF) complexes (tartey2016akirin2mediatedtranscriptionalcontrol pages 1-2, tartey2016akirin2mediatedtranscriptionalcontrol pages 6-8).
A recurring concept is that Akirin proteins confer NF-κB target gene selectivity by enabling recruitment of SWI/SNF remodelers at specific promoters. In Drosophila, Akirin physically connects the NF-κB transcription factor Relish with the SWI/SNF component BAP60, supporting a promoter-bound complex that preferentially activates a subset of immune effector genes (bonnay2014akirinspecifiesnfκb pages 9-11, bonnay2014akirinspecifiesnfκb pages 2-3). The mechanism is presented as evolutionarily conserved, with mammalian Akirin-2 binding BAF60 homologs (bonnay2014akirinspecifiesnfκb pages 9-11).
Akirin2 is summarized as lacking obvious DNA-binding motifs, with regions consistent with protein–protein interaction roles (including conserved helical regions), and having an N-terminal nuclear localization signal, consistent with its nuclear cofactor role (tartey2016akirin2mediatedtranscriptionalcontrol pages 5-6).
A major experimentally supported model is that Akirin2 helps drive transcription of specific inflammatory genes by bridging NF-κB pathway components to SWI/SNF chromatin remodelers (tartey2016akirin2mediatedtranscriptionalcontrol pages 1-2, tartey2016akirin2mediatedtranscriptionalcontrol pages 10-11).
IκBζ (NFKBIZ)–Akirin2–SWI/SNF axis: In macrophage contexts, IκBζ is reported to bind Akirin2 (via Akirin2’s C-terminal region) and to cooperate with Akirin2 and Brg1 (SWI/SNF) to support promoter recruitment and activation of inflammatory genes including Il6 and Il12b after innate immune stimulation (e.g., LPS/IL-1β/TLR signaling) (tartey2016akirin2mediatedtranscriptionalcontrol pages 6-8, tartey2016akirin2mediatedtranscriptionalcontrol pages 10-11).
This places AKIRIN2 within the nuclear stage of NF-κB response, acting downstream of receptor signaling to implement chromatin remodeling–dependent transcriptional programs (tartey2016akirin2mediatedtranscriptionalcontrol pages 5-6, tartey2016akirin2mediatedtranscriptionalcontrol pages 6-8).
In B cells, Akirin2 is described as required for recruitment of Brg1 to promoters such as Myc and Ccnd2 after CD40 stimulation, supporting expression of proliferative and survival genes (e.g., Myc, Ccnd1/2, Bcl2, Bcl-xL) and thereby influencing B-cell proliferation/survival and antibody responses (tartey2016akirin2mediatedtranscriptionalcontrol pages 6-8, tartey2016akirin2mediatedtranscriptionalcontrol pages 8-10).
Akirin2 is described as essential for embryonic development, with knockout lethality by embryonic day E9.5 in mice, consistent with a fundamental role in transcriptional regulation (tartey2016akirin2mediatedtranscriptionalcontrol pages 5-6).
Akirin2-dependent genes are summarized as enriched among promoters with lower CpG-island density, suggesting that some promoters may require Akirin2-dependent SWI/SNF remodeling for activation, providing one mechanistic explanation for selective NF-κB gene induction (tartey2016akirin2mediatedtranscriptionalcontrol pages 5-6, tartey2016akirin2mediatedtranscriptionalcontrol pages 6-8).
Akirin2 is repeatedly described as nuclear in mechanistic reviews, consistent with its role in transcriptional control and chromatin remodeling (tartey2016akirin2mediatedtranscriptionalcontrol pages 5-6, tartey2016akirin2mediatedtranscriptionalcontrol pages 1-2, tartey2016akirin2mediatedtranscriptionalcontrol pages 10-11). In a cancer drug-resistance context (CML), increased nuclear accumulation of Akirin-2 in imatinib-resistant cells was reported (without numeric fold-change in retrieved excerpts) (karabay2018expressionanalysisof pages 7-7).
A 2024 chemoproteomics study (Burton & Backus, Communications Chemistry, published Apr 2024; https://doi.org/10.1038/s42004-024-01162-x) reported AKIRIN2 Cys3 among “uniquely liganded” cysteines detected by their sCIP-TMT workflow, and noted this residue is proximal to a 20S proteasome binding motif (burton2024functionalizingtandemmass pages 5-7).
Quantitatively in that dataset: they report 29 uniquely liganded cysteines in the study; and that 760/789 liganded cysteines had prior support in CysDB, highlighting that AKIRIN2 Cys3 belonged to a small set of newly observed ligandable sites (burton2024functionalizingtandemmass pages 5-7). Figure evidence for AKIRIN2 Cys3 being listed among uniquely liganded cysteines is shown in their Figure 5C (burton2024functionalizingtandemmass media b5b8243d, burton2024functionalizingtandemmass media 0c97aa47).
Interpretation: This is not direct functional enzymology (AKIRIN2 is not an enzyme) but provides chemical tractability/ligandability data that could enable future chemical biology tools (burton2024functionalizingtandemmass pages 5-7).
A 2024 study (Luo et al., Antioxidants & Redox Signaling, Dec 2024; https://doi.org/10.1089/ars.2023.0409) derived a “core NRF2” transcriptional signature from seven RNA-seq datasets and reported that AKIRIN2 was primarily upregulated in drug-mediated NRF2 activation contexts, but not consistently upregulated in some cancer cohort/cell line datasets (e.g., TCGA LUAD/NSCLC analyses mentioned in the excerpt) (luo2024acorenrf2 pages 4-7).
Interpretation: This supports AKIRIN2 as a context-dependent oxidative-stress/Nrf2-responsive transcript in some settings, but does not by itself establish direct NRF2 binding at AKIRIN2 regulatory elements (luo2024acorenrf2 pages 4-7).
A 2024 review on IκBζ (Yamazaki, Cells, Aug 2024; https://doi.org/10.3390/cells13171467) reinforces that IκBζ supports selective NF-κB target gene induction through SWI/SNF-dependent chromatin remodeling (including examples such as IL6/LCN2 and dependence on BRG1 recruitment), which is mechanistically consistent with the previously described IκBζ–Akirin2–SWI/SNF framework (yamazaki2024thenuclearnfκb pages 4-6). However, the retrieved excerpt does not explicitly mention Akirin2/AKIRIN2 by name, so it mainly strengthens the pathway background rather than directly updating AKIRIN2-specific mechanisms (yamazaki2024thenuclearnfκb pages 4-6).
AKIRIN2 has been linked to tumor phenotypes in multiple models. A review summary describes Akirin2 as implicated as an oncogene and notes overexpression in tumor cell lines, where knockdown/antisense approaches reduced growth/tumorigenicity/metastasis in models and increased cell death susceptibility in glioblastoma lines (tartey2016akirin2mediatedtranscriptionalcontrol pages 5-6). In chronic myeloid leukemia models, increased nuclear accumulation of Akirin-2 in imatinib-resistant cells was proposed as a potential biomarker (karabay2018expressionanalysisof pages 7-7).
Implementation status: These are primarily preclinical or biomarker-proposal level findings; no AKIRIN2-targeted therapy is established in the retrieved evidence.
The 2024 sCIP-TMT chemoproteomics finding (AKIRIN2 Cys3 ligandability) provides a practical foothold for developing covalent probes to interrogate AKIRIN2 function or interactions in cells (burton2024functionalizingtandemmass pages 5-7, burton2024functionalizingtandemmass media b5b8243d).
The 2024 NRF2 signature work includes AKIRIN2 as a conditional NRF2-induced gene in drug-activation settings, implying AKIRIN2 may appear in transcriptomic readouts of oxidative-stress responses in some perturbation screens (luo2024acorenrf2 pages 4-7).
A focused immunology review explicitly frames Akirin2 as a central nuclear cofactor that mediates transcriptional programs by recruiting SWI/SNF chromatin remodeling, emphasizing its role as a bridge linking signaling-induced transcription factors to chromatin remodeling machinery and driving selective NF-κB-dependent transcription (Tartey & Takeuchi, Crit Rev Immunol, Jan 2016, https://doi.org/10.1615/critrevimmunol.2017019629) (tartey2016akirin2mediatedtranscriptionalcontrol pages 1-2, tartey2016akirin2mediatedtranscriptionalcontrol pages 10-11). Although not new, this remains one of the clearest authoritative mechanistic syntheses in the retrieved corpus.
A key conceptual advance from the Drosophila EMBO Journal study is the “molecular selector” model—Akirin defining NF-κB target subset choice via chromatin remodeling—explicitly presented as conserved in mammals, supporting its relevance to human AKIRIN2 annotation (Bonnay et al., EMBO J, Sep 2014, https://doi.org/10.15252/embj.201488456) (bonnay2014akirinspecifiesnfκb pages 9-11, bonnay2014akirinspecifiesnfκb pages 2-3).
| Functional claim | Mechanism/partners/pathway | Cell/tissue/model | Key experimental evidence type | Quantitative/statistical detail (if available) | Primary source with publication date and URL/DOI | Notes (strength/limitations/species ambiguity) |
|---|---|---|---|---|---|---|
| Human AKIRIN2 (UniProt Q53H80) is the conserved nuclear Akirin-2 protein in the akirin family and functions primarily as a transcriptional cofactor rather than a DNA-binding enzyme or receptor | Lacks obvious DNA/RNA-binding motifs; contains N-terminal nuclear localization signal and conserved helical regions; acts through protein-protein interactions to couple NF-κB-responsive factors to chromatin remodeling machinery | Mammals/human ortholog context summarized from mouse and immune-cell studies | Review synthesis of KO/knockdown, promoter studies, interaction studies | Mouse Akirin2 knockout causes embryonic lethality by E9.5 | Tartey & Takeuchi, Crit Rev Immunol (Jan 2016), https://doi.org/10.1615/CritRevImmunol.2017019629 (tartey2016akirin2mediatedtranscriptionalcontrol pages 5-6, tartey2016akirin2mediatedtranscriptionalcontrol pages 1-2) | Strong mechanistic review grounded in primary studies; some evidence is from mouse rather than direct human experiments |
| AKIRIN2 is required for selective, not global, NF-κB-dependent transcription | Bridges NF-κB pathway output to SWI/SNF (BAF/Brg1) chromatin remodeling, enabling induction of specific inflammatory genes after TLR/IL-1/TNF signaling | Mouse embryonic fibroblasts, macrophages, B cells | Genetic KO/conditional deletion, promoter recruitment, transcriptional analysis | Selective defect in a subset of inducible genes rather than pan-NF-κB failure; promoters with lower CpG-island density are enriched among Akirin2-dependent genes | Tartey & Takeuchi, Crit Rev Immunol (Jan 2016), https://doi.org/10.1615/CritRevImmunol.2017019629 (tartey2016akirin2mediatedtranscriptionalcontrol pages 5-6, tartey2016akirin2mediatedtranscriptionalcontrol pages 6-8, tartey2016akirin2mediatedtranscriptionalcontrol pages 8-10, tartey2016akirin2mediatedtranscriptionalcontrol pages 10-11) | High-value functional annotation for human AKIRIN2 by orthology/conservation; quantitative fold changes were not provided in the retrieved excerpts |
| AKIRIN2 cooperates with IκBζ (NFKBIZ) and SWI/SNF to activate inflammatory promoters | IκBζ binds the C-terminal region of Akirin2; IκBζ-Akirin2-SWI/SNF complex interacts with NF-κB p50 and supports recruitment to Il6 and Il12b promoters after LPS/IL-1β/TLR stimulation | Macrophages | ChIP/recruitment studies, interaction mapping, stimulus-response transcription assays | No numeric recruitment values in retrieved excerpt; mechanistic link reported for Il6 and Il12b promoters | Tartey & Takeuchi, Crit Rev Immunol (Jan 2016), https://doi.org/10.1615/CritRevImmunol.2017019629 (tartey2016akirin2mediatedtranscriptionalcontrol pages 6-8, tartey2016akirin2mediatedtranscriptionalcontrol pages 10-11) | Strong pathway-specific mechanism; evidence is largely from mouse/immune-cell literature but directly relevant to conserved human AKIRIN2 function |
| AKIRIN2 supports B-cell activation and survival programs | Required for Brg1 recruitment to Myc and Ccnd2 promoters after CD40 stimulation; supports expression of Myc, Ccnd1, Ccnd2, Bcl2 and Bcl-xL | B cells | Conditional deletion, promoter recruitment, transcriptional profiling | Loss of Akirin2 severely impairs T-cell-dependent and T-cell-independent antibody responses; decreased splenic follicular and marginal zone B cells | Tartey & Takeuchi, Crit Rev Immunol (Jan 2016), https://doi.org/10.1615/CritRevImmunol.2017019629 (tartey2016akirin2mediatedtranscriptionalcontrol pages 6-8, tartey2016akirin2mediatedtranscriptionalcontrol pages 8-10) | Useful for immune-function annotation; retrieved evidence did not include exact cell-count statistics |
| Akirin proteins act as molecular selectors that confer NF-κB target-gene specificity through chromatin remodeling, a mechanism conserved to mammals | In Drosophila, Akirin binds Relish and BAP60 (SWI/SNF/BAP), forming a bridge to remodel chromatin at selected promoters; authors note conservation with mouse Akirin-2 binding BAF60 homologs | Drosophila innate immune system with mammalian conservation inference | Genome-wide expression analysis, proteomics, interaction studies, infection phenotyping | Akirin required for 9 of 41 Relish-dependent immune-related genes; Akirin alone required for 31 genes independently of Relish; loss caused derepression/overexpression of 205 genes | Bonnay et al., EMBO Journal (Sep 2014), https://doi.org/10.15252/embj.201488456 (bonnay2014akirinspecifiesnfκb pages 9-11, bonnay2014akirinspecifiesnfκb pages 2-3) | Not human-specific, but highly informative for conserved Akirin biology; should be used as evolutionary/mechanistic support, not as sole human evidence |
| AKIRIN2 contains a newly observed ligandable cysteine near a proteasome-related motif, suggesting potential chemical tractability | Chemoproteomics identified AKIRIN2 Cys3 as a uniquely liganded cysteine; text notes proximity to the 20S proteasome binding motif | Human proteome-scale chemoproteomics dataset | Chemoproteomics (sCIP-TMT), Figure 5C | 29 uniquely liganded cysteines identified in study; 760/789 liganded cysteines had prior CysDB support, placing AKIRIN2 Cys3 among newly observed sites | Burton & Backus, Communications Chemistry (Apr 2024), https://doi.org/10.1038/s42004-024-01162-x (burton2024functionalizingtandemmass pages 5-7, burton2024functionalizingtandemmass media b5b8243d, burton2024functionalizingtandemmass media 0c97aa47) | Important recent finding, but it does not establish AKIRIN2 biochemical function or therapeutic efficacy; ligandability ≠ validated drug target |
| AKIRIN2 can behave as a conditional NRF2-responsive gene in some pharmacologic activation contexts | AKIRIN2 was induced mainly in drug-mediated NRF2 activation datasets, but not consistently in TCGA LUAD or NSCLC cell-line analyses; thus not part of the most universal core NRF2 output | Multiple transcriptomic datasets including pharmacologic CDDO-2P-Im treatment and genetic KEAP1-knockout models | RNA-seq / transcriptomic meta-analysis | Seven transcriptomic databases used to derive a 15-gene candidate NRF2 core set; AKIRIN2 highlighted as conditionally induced rather than universally upregulated | Luo et al., Antioxidants & Redox Signaling (Dec 2024), https://doi.org/10.1089/ars.2023.0409 (luo2024acorenrf2 pages 4-7) | Recent and useful for regulatory context; this is association/expression evidence, not proof of direct NRF2 binding to AKIRIN2 regulatory DNA |
| 2024 IκBζ review reinforces the SWI/SNF-dependent selective NF-κB transcription mechanism relevant to AKIRIN2, but the retrieved excerpt does not explicitly mention Akirin2 | IκBζ promotes BRG1/SWI/SNF recruitment and chromatin remodeling at secondary NF-κB target genes such as IL6/LCN2, with p50 preference and promoter motif selectivity | Inflammatory gene regulation context | Review synthesis of ChIP/ATAC/structural studies | BRG1 recruitment to Lcn2 promoter is abolished without IκBζ; no AKIRIN2-specific quantitative measure in excerpt | Yamazaki, Cells (Aug 2024), https://doi.org/10.3390/cells13171467 (yamazaki2024thenuclearnfκb pages 4-6) | Useful contextual support for the IκBζ arm of the pathway; limitation: excerpt did not directly mention AKIRIN2, so it supports pathway context more than direct annotation |
| FBI1/Akirin2 has tumor-related functions in liver-cancer models, but this evidence is not specific to human AKIRIN2 and should be interpreted cautiously | Reported as a 14-3-3β-binding protein that sustains ERK1/2 activation by suppressing MKP-1; silencing FBI1/Akirin2 increases Lu/BCAM expression, consistent with Lu/BCAM as a possible downstream target | Rat hepatoma / rat liver cancer cells | Review citing functional silencing/overexpression studies | No exact effect sizes in retrieved excerpt; claim is qualitative (increased Lu/BCAM on Akirin2 silencing; reduced colony formation/migration/invasion with Lu/BCAM overexpression) | Jin et al., Int J Mol Sci (Jul 2024), https://doi.org/10.3390/ijms25137268 (jin2024theroleof pages 5-6, jin2024theroleof pages 8-10) | Important caveat: these findings concern rat cells/ortholog context and FBI1 alias usage; not sufficient alone for direct human AKIRIN2 functional annotation |
| AKIRIN2 has been implicated in cancer-associated phenotypes and nuclear accumulation in resistance states | Conserved nuclear NF-κB cofactor; increased nuclear AKIRIN2 reported in imatinib-resistant CML cells; related literature links AKIRIN2/FBI1 to tumorigenicity/metastasis and glioblastoma chemosensitivity | Human CML cells; broader tumor-cell literature summarized | Expression analysis, nuclear protein localization, literature synthesis | Increased nuclear accumulation in resistant cells reported, but no exact fold-change in retrieved excerpt | Karabay et al., Hematology (Jun 2018), https://doi.org/10.1080/10245332.2018.1488795 (karabay2018expressionanalysisof pages 7-7) | Human disease relevance is suggestive, but this is downstream/association-heavy and not the strongest source for core molecular function |
Table: This table summarizes experimentally supported and recent literature-based functional annotation evidence for human AKIRIN2 (UniProt Q53H80), including core mechanism, pathway context, localization/function in immune transcription, and recent 2024 omics/chemoproteomics findings. It also flags species and evidence-strength limitations where the literature is indirect or ortholog-based.
Across mechanistic immunology literature and conserved invertebrate models, the primary function of human AKIRIN2 (Akirin-2; Q53H80) is best annotated as a nuclear transcriptional cofactor/adaptor that confers selective activation of NF-κB-dependent gene programs by partnering with IκBζ (NFKBIZ) and recruiting SWI/SNF (BAF/BRG1) chromatin remodeling complexes to specific promoters (tartey2016akirin2mediatedtranscriptionalcontrol pages 6-8, tartey2016akirin2mediatedtranscriptionalcontrol pages 10-11). Recent 2024 work extends AKIRIN2’s practical research relevance by identifying AKIRIN2 Cys3 as a ligandable site in human proteome chemoproteomics (potential for probe development) and by situating AKIRIN2 as a context-dependent NRF2-responsive gene in pharmacologic activation datasets (burton2024functionalizingtandemmass pages 5-7, luo2024acorenrf2 pages 4-7).
References
(tartey2016akirin2mediatedtranscriptionalcontrol pages 5-6): Sarang Tartey and Osamu Takeuchi. Akirin2-mediated transcriptional control by recruiting swi/snf complex in b cells. Critical reviews in immunology, 36 5:395-406, Jan 2016. URL: https://doi.org/10.1615/critrevimmunol.2017019629, doi:10.1615/critrevimmunol.2017019629. This article has 8 citations and is from a peer-reviewed journal.
(tartey2016akirin2mediatedtranscriptionalcontrol pages 1-2): Sarang Tartey and Osamu Takeuchi. Akirin2-mediated transcriptional control by recruiting swi/snf complex in b cells. Critical reviews in immunology, 36 5:395-406, Jan 2016. URL: https://doi.org/10.1615/critrevimmunol.2017019629, doi:10.1615/critrevimmunol.2017019629. This article has 8 citations and is from a peer-reviewed journal.
(tartey2016akirin2mediatedtranscriptionalcontrol pages 6-8): Sarang Tartey and Osamu Takeuchi. Akirin2-mediated transcriptional control by recruiting swi/snf complex in b cells. Critical reviews in immunology, 36 5:395-406, Jan 2016. URL: https://doi.org/10.1615/critrevimmunol.2017019629, doi:10.1615/critrevimmunol.2017019629. This article has 8 citations and is from a peer-reviewed journal.
(bonnay2014akirinspecifiesnfκb pages 2-3): François Bonnay, Xuan‐Hung Nguyen, Eva Cohen‐Berros, Laurent Troxler, Eric Batsche, Jacques Camonis, Osamu Takeuchi, Jean‐Marc Reichhart, and Nicolas Matt. Akirin specifies nf-κb selectivity of drosophila innate immune response via chromatin remodeling. The EMBO Journal, 33:2349-2362, Sep 2014. URL: https://doi.org/10.15252/embj.201488456, doi:10.15252/embj.201488456. This article has 124 citations.
(tartey2016akirin2mediatedtranscriptionalcontrol pages 10-11): Sarang Tartey and Osamu Takeuchi. Akirin2-mediated transcriptional control by recruiting swi/snf complex in b cells. Critical reviews in immunology, 36 5:395-406, Jan 2016. URL: https://doi.org/10.1615/critrevimmunol.2017019629, doi:10.1615/critrevimmunol.2017019629. This article has 8 citations and is from a peer-reviewed journal.
(bonnay2014akirinspecifiesnfκb pages 9-11): François Bonnay, Xuan‐Hung Nguyen, Eva Cohen‐Berros, Laurent Troxler, Eric Batsche, Jacques Camonis, Osamu Takeuchi, Jean‐Marc Reichhart, and Nicolas Matt. Akirin specifies nf-κb selectivity of drosophila innate immune response via chromatin remodeling. The EMBO Journal, 33:2349-2362, Sep 2014. URL: https://doi.org/10.15252/embj.201488456, doi:10.15252/embj.201488456. This article has 124 citations.
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(jin2024theroleof pages 8-10): Juan Jin, Qinqin Guo, and Zhibin Yan. The role of lutheran/basal cell adhesion molecule in hematological diseases and tumors. International Journal of Molecular Sciences, 25:7268, Jul 2024. URL: https://doi.org/10.3390/ijms25137268, doi:10.3390/ijms25137268. This article has 6 citations.