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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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.
Identity is verified. The requested target is human OLFML2A (olfactomedin-like 2A), encoding olfactomedin-like protein 2A/photomedin-1, UniProt Q68BL7. Literature places the gene at 9q33.3 and clearly distinguishes it from OLFML2B/photomedin-2 and from OLFM2, a different olfactomedin-family gene. OLFML2A and OLFML2B form a distinct olfactomedin subfamily characterized by a Ser/Thr-rich region preceding the C-terminal OLF domain. Thus, the retrieved literature matches the requested human protein and not a similarly named paralog. (tomarev2009olfactomedindomaincontainingproteins pages 7-8)
The best-supported primary annotation is: OLFML2A is a secreted, non-enzymatic extracellular-matrix/matricellular glycoprotein that oligomerizes and preferentially binds sulfated glycosaminoglycans, especially chondroitin sulfate-E (CS-E) and heparin. It is therefore more plausibly an organizer or modulator of glycosaminoglycan-rich extracellular environments than an enzyme, transporter, or canonical soluble signaling ligand. Its endogenous receptor, physiological binding partners, and indispensable organism-level function remain unknown. (cardenasleon2022matricellularproteinsin pages 11-12, tomarev2009olfactomedindomaincontainingproteins pages 7-8)
Recent work has concentrated mainly on cancer transcriptomics. Cell experiments support an AP-1→OLFML2A axis contributing to triple-negative breast-cancer phenotypes, whereas 2023 AML studies report prognostic associations but do not establish mechanism. No validated clinical assay, approved drug, or OLFML2A-directed clinical implementation was identified. (zhao2021olfml2aisnecessary pages 4-8, zhao2021olfml2aisnecessary pages 3-4, lu2023olfml2aoverexpressionpredicts pages 3-4, lu2023olfml2aoverexpressionpredicts pages 4-5)
The gene symbol, protein description, organism, and domains supplied in the query are mutually consistent:
This target must not be confused with OLFML2B, which is photomedin-2 and is located at 1q23.3, or OLFM2, which has separate adipose/metabolic literature. Some older summaries contain inconsistent chromosome or protein-length entries; the explicit 9q33.3 assignment and current Q68BL7 identity should control interpretation. (tomarev2009olfactomedindomaincontainingproteins pages 26-27, tomarev2009olfactomedindomaincontainingproteins pages 7-8)
OLFML2A has no demonstrated catalytic reaction, substrate turnover, ion transport, or small-molecule transport activity. The evidence instead identifies it as a secreted extracellular glycoprotein with matricellular properties. “Matricellular” denotes extracellular proteins that bind matrix constituents and modulate cell–matrix interactions rather than serving primarily as load-bearing fibrils such as collagen. (cardenasleon2022matricellularproteinsin pages 11-12, tomarev2009olfactomedindomaincontainingproteins pages 7-8)
Among extracellular-matrix components tested in foundational photomedin studies, Olfml2 proteins bound preferentially to chondroitin sulfate-E and heparin. CS-E is a highly sulfated glycosaminoglycan motif capable of concentrating proteins and modifying their availability within extracellular matrices. This is the strongest substrate-like specificity known for OLFML2A, although “ligand” is more appropriate than “substrate,” because no chemical conversion has been shown. (tomarev2009olfactomedindomaincontainingproteins pages 7-8)
The physiological consequence remains unresolved. Plausible functions include anchoring OLFML2A in sulfated proteoglycan-rich matrices, organizing multivalent extracellular complexes, or regulating local accessibility of signaling proteins. These are mechanistic inferences from biochemical binding and oligomerization—not demonstrated endogenous pathways.
Olfml2 proteins form disulfide-linked homodimers and higher oligomers, with N-terminal determinants required for assembly. Photomedin-1 is proteolytically cleaved after secretion; the resulting C-terminal fragment retains the intact OLF domain but cannot form dimers. This suggests that the N-terminal region governs multimeric avidity or matrix assembly, whereas cleavage could change extracellular distribution or binding behavior. The responsible protease and physiological regulation of this event are unknown. (tomarev2009olfactomedindomaincontainingproteins pages 7-8)
These foundational observations were substantially derived from rodent photomedins and heterologous expression systems. They align with human sequence/domain annotations, but endogenous human binding constants, cleavage sites, and native complex composition have not been established.
The precursor annotation, experimental secretion, and extracellular-matrix binding collectively place OLFML2A’s principal site of action outside the cell, after synthesis through the secretory pathway. It is not established as a transmembrane protein or intracellular enzyme. (tomarev2009olfactomedindomaincontainingproteins pages 7-8)
Human ocular tissue provides direct localization evidence. RT-PCR detected OLFML2A transcripts in retina, cornea, and lens, but not iris or sclera in the 2016 study. Retinal immunofluorescence detected protein in the ganglion-cell, inner-nuclear, and outer-nuclear layers, with no reported signal in the inner plexiform layer, rod layer, or retinal pigment epithelium. (perezibave2016olfactomedinlike2a pages 4-5)
This study established tissue and layer-level presence, not subcellular localization. It did not determine whether staining represented secreted matrix, cell-associated extracellular protein, or protein within the secretory pathway. Moreover, OLFML2A and OLFML2B had similar tissue-level RT-PCR patterns, so antibody specificity is important when assigning retinal protein distributions. The human pattern also differed in detail from older rodent observations, where Olfml2a was reported predominantly in the photoreceptor layer. (perezibave2016olfactomedinlike2a pages 4-5, tomarev2009olfactomedindomaincontainingproteins pages 7-8)
The convergence of secretion, sulfated-glycosaminoglycan binding, oligomerization, and expression in matrix-producing contexts supports a role in ECM organization or signaling modulation. Reviews consequently discuss OLFML2A as a matricellular protein, but its role in normal cutaneous wound healing remains insufficiently defined. (cardenasleon2022matricellularproteinsin pages 11-12, tomarev2009olfactomedindomaincontainingproteins pages 7-8)
Transcriptomic studies frequently assign OLFML2A to ECM, fibrosis, adhesion, or stromal gene programs. Such co-expression is consistent with the biochemical annotation but does not establish a specific receptor or pathway.
The clearest gene-specific regulatory mechanism was reported in TNBC cell models. In BT549 cells, overlap of expression changes after c-Jun knockdown, Fra-1 knockdown, and treatment with the AP-1 inhibitor T-5224 yielded 136 shared genes—79 upregulated and 57 downregulated. ChIP-PCR supported recruitment of c-Jun and Fra-1 to the OLFML2A locus, while T-5224 reduced OLFML2A RNA and protein. This supports direct or near-direct transcriptional regulation of OLFML2A by AP-1. (zhao2021olfml2aisnecessary pages 3-4)
OLFML2A siRNA reduced proliferation, wound closure, and invasion and increased apoptosis in BT549 and Hs578T cells. T-5224 produced similar phenotypes at 15 µM in BT549 and 40 µM in Hs578T cells. The authors therefore proposed an AP-1–OLFML2A axis contributing to TNBC progression. (zhao2021olfml2aisnecessary pages 4-8, zhao2021olfml2aisnecessary pages 2-3)
A related RNA-interference study found that OLFML2A silencing altered 1,140 genes—428 upregulated and 712 downregulated—and implicated cell-cycle, cytoskeletal, DNA-damage/p53, integrin, HGF, and NGF-associated programs. These are downstream transcriptomic responses, not evidence that OLFML2A physically binds those signaling components. (gao2022genechipexpressionprofiling pages 1-6)
Important limitations are the absence of a genetic rescue experiment, limited in-vivo validation, uncertain extracellular receptor/ligand mechanism, and possible broad effects of high-micromolar T-5224. Accordingly, AP-1 regulation is better supported than the precise route by which extracellular OLFML2A affects proliferation or migration.
A 2023 AML analysis associated OLFML2A-correlated genes with cGMP–PKG, adrenergic, aldosterone, melanogenesis, and parathyroid-hormone pathways. These are enrichment results and should not be interpreted as demonstrated biochemical pathways of OLFML2A. (lu2023olfml2aoverexpressionpredicts pages 3-4)
Claims that OLFML2A regulates Wnt/β-catenin in glioma appear in secondary discussion, but the retrieved evidence did not provide the underlying experimental paper in sufficient detail. This pathway should therefore be treated as provisional rather than part of the core annotation. (lu2023olfml2aoverexpressionpredicts pages 6-8)
In a TCGA analysis of 115 TNBC cases with survival data, higher OLFML2A expression was associated with more advanced AJCC/T/M features and poorer overall survival. Kaplan–Meier Plotter analyses also associated higher expression with poorer recurrence-free and distant-metastasis-free survival. (zhao2021olfml2aisnecessary pages 4-8, zhao2021olfml2aisnecessary pages 3-4)
These retrospective bulk-RNA observations are compatible with the cell-line perturbation results, but they do not prove tumor-cell autonomy. Because OLFML2A is an extracellular-matrix/stromal gene, bulk tumor RNA may partly measure fibroblast abundance or fibrosis rather than expression by malignant cells. Prospective validation, a locked clinical cutoff, and independent multivariable testing are needed.
Lu et al., published February 2023, analyzed 151 TCGA-AML cases, divided into 75 low- and 76 high-expression cases. High OLFML2A was associated with worse overall survival: HR 2.36, 95% CI 1.53–3.64; P<0.001. The reported discrimination between AML and normal samples was AUC 0.977, 95% CI 0.960–0.994. OLFML2A expression was also associated with cytogenetic risk (P=0.035), detailed cytogenetic category (P=0.014), and FLT3 mutation status (P=0.005). (lu2023olfml2aoverexpressionpredicts pages 4-5, lu2023olfml2aoverexpressionpredicts pages 6-8)
Subgroup results included HR 3.35 for cases with >20% marrow blasts, HR 2.06 in intermediate cytogenetic risk, HR 3.08 in FAB-M1, and HR 4.09 in FAB-M4. (lu2023olfml2aoverexpressionpredicts pages 5-6)
However, the paper contains an important internal inconsistency: its abstract states that high-expression patients had longer survival, whereas its title, Kaplan–Meier curve, HR, and results text indicate worse survival with high expression. The latter interpretation is supported by the quantitative results. The analysis also relies mainly on one public cohort, lacks prospective or protein-level validation, and does not establish causality in AML cells. (lu2023olfml2aoverexpressionpredicts pages 3-4, lu2023olfml2aoverexpressionpredicts pages 4-5)
A separate 2023 computational study included OLFML2A in a five-gene AML prognostic model, but natural-compound “docking” to OLFML2A is hypothesis-generating only; no validated drug-binding site, biochemical affinity, cellular target engagement, or therapeutic efficacy was demonstrated.
Human ocular expression makes eye biology plausible, and OLFML2A was among genes reported as altered in transcriptomic/m6A analyses of pterygium. This remains an association rather than evidence that OLFML2A initiates pterygium or that targeting it is therapeutic.
Open Targets lists heterogeneous, low-scoring associations with diverticular disease, skin cancer, brain aneurysm, and Ascher syndrome; representative scores ranged from approximately 0.109 to 0.317. These aggregate links should not be considered validated Mendelian or therapeutic relationships. (OpenTargets Search: -OLFML2A)
OLFML2A currently has no established clinical application. Specifically, the retrieved evidence did not identify:
Current applications are research-stage: inclusion in prognostic expression signatures, use as a candidate ECM/stromal marker, and preclinical investigation as an AP-1-regulated cancer dependency. Patent or multigene-panel inclusion would indicate commercial interest, not clinical validity.
The evidence hierarchy is summarized below.
| Topic | Best-supported finding | Evidence type | Confidence / limitation |
|---|---|---|---|
| Identity and disambiguation | Human OLFML2A encodes olfactomedin-like protein 2A (photomedin-1), the target corresponding to Q68BL7; it is distinct from OLFML2B/photomedin-2 and OLFM2. The human gene is reported at 9q33.3, and OLFML2A/2B form a separate olfactomedin-family subfamily with a distinctive Ser/Thr-rich region preceding the OLF domain. (tomarev2009olfactomedindomaincontainingproteins pages 7-8) | Curated protein information plus comparative phylogenetic/domain analysis | High for identity and paralog distinction. Some older summaries contain inconsistent chromosomal or protein-length annotations, so current UniProt/HGNC records should control nomenclature. |
| Extracellular biochemical role | OLFML2A is a secreted glycoprotein that can form disulfide-linked homodimers and higher oligomers through determinants in its N-terminal region. After secretion, photomedin-1 can be proteolytically cleaved; the resulting C-terminal OLF-domain fragment does not dimerize. Olfml2 proteins preferentially bound chondroitin sulfate-E (CS-E) and heparin among tested extracellular-matrix components. (tomarev2009olfactomedindomaincontainingproteins pages 7-8) | Direct recombinant/cell biochemical experiments summarized in an authoritative olfactomedin-family review | Moderate–high for secretion, assembly, cleavage, and glycosaminoglycan binding. Foundational experiments were largely conducted with rodent photomedins or heterologous expression; endogenous human binding constants, physiological partners, and the functional consequence of CS-E binding remain unresolved. |
| Primary functional interpretation | The strongest molecular interpretation is that OLFML2A is a non-enzymatic, secreted ECM/matricellular glycoprotein, probably organizing or modulating glycosaminoglycan-rich extracellular environments rather than catalyzing a reaction or transporting a substrate. (cardenasleon2022matricellularproteinsin pages 11-12, tomarev2009olfactomedindomaincontainingproteins pages 7-8) | Biochemical binding plus domain/family inference | Moderate. No catalytic activity, receptor, definitive downstream signaling mechanism, or indispensable physiological function has been established. |
| Ocular expression and localization | Human OLFML2A transcript was detected by RT-PCR in retina, cornea, and lens. Retinal immunofluorescence detected protein in the ganglion-cell, inner-nuclear, and outer-nuclear layers, but not in the inner plexiform layer, rod layer, or retinal pigment epithelium in that study. (perezibave2016olfactomedinlike2a pages 4-5) | Human-tissue RT-PCR and immunofluorescence | Moderate for ocular presence and layer-level localization. The study was descriptive, did not establish extracellular versus intracellular distribution at subcellular resolution, and did not define ocular function; antibodies also require paralog-specific validation. |
| AP-1–OLFML2A axis in TNBC | In BT549/Hs578T triple-negative breast-cancer models, ChIP-PCR supported recruitment of c-Jun and Fra-1 to OLFML2A, and AP-1 inhibitor T-5224 reduced OLFML2A expression. OLFML2A knockdown inhibited proliferation, migration, and invasion and increased apoptosis, supporting OLFML2A as an AP-1-regulated contributor to the cultured-cell phenotype. (zhao2021olfml2aisnecessary pages 4-8, zhao2021olfml2aisnecessary pages 3-4, zhao2021olfml2aisnecessary pages 2-3) | ChIP-PCR, RNA/protein measurements, siRNA perturbation, and in-vitro phenotypic assays | Moderate for a cell-line AP-1→OLFML2A relationship; low for therapeutic translation. T-5224 required 15–40 µM in these models, may have broader effects, and the study lacked genetic rescue, endogenous ligand/receptor mechanism, robust in-vivo validation, and clinical testing of OLFML2A-directed therapy. |
| TNBC prognostic association | Among 115 TCGA TNBC cases, higher OLFML2A expression was associated with more advanced clinicopathological features and poorer survival; other retrospective datasets also linked higher expression with poorer recurrence-free and distant-metastasis-free survival. (zhao2021olfml2aisnecessary pages 4-8, zhao2021olfml2aisnecessary pages 3-4) | Retrospective transcriptomic survival association | Low–moderate. This is not evidence that tumor-cell OLFML2A is independently causal: bulk RNA can reflect fibroblast/ECM content, and prospective external validation or a clinically locked cutoff was not reported. |
| AML association | In a 151-case TCGA-AML analysis (75 low, 76 high), high OLFML2A expression was associated with worse overall survival (HR 2.36, 95% CI 1.53–3.64; P<0.001) and distinguished AML from normal samples with reported AUC 0.977, 95% CI 0.960–0.994. It was also associated with cytogenetic risk and FLT3 mutation status. (lu2023olfml2aoverexpressionpredicts pages 3-4, lu2023olfml2aoverexpressionpredicts pages 4-5, lu2023olfml2aoverexpressionpredicts pages 6-8) | Retrospective bulk-transcriptomic and clinical association | Low–moderate as a candidate biomarker. The publication contains internally inconsistent wording about survival, relies principally on one public cohort, and provides no demonstration that OLFML2A drives AML biology or that circulating/secreted protein measurement has diagnostic value. |
| Clinical and application status | OLFML2A currently has no validated diagnostic assay, approved drug, clinically established therapeutic indication, or demonstrated clinical-trial application. Database disease links are low-scoring and heterogeneous, and reported uses remain exploratory biomarker signatures or preclinical target hypotheses. (OpenTargets Search: -OLFML2A, cardenasleon2022matricellularproteinsin pages 11-12) | Target-disease database evidence and literature appraisal | High confidence that clinical validation is absent in the reviewed evidence. Proposed cancer, fibrosis, ocular, and immune applications should not be interpreted as established medical utility. |
Table: Evidence-ranked summary of human OLFML2A Q68BL7, separating direct biochemical and cell-based findings from retrospective transcriptomic associations. It highlights the likely extracellular matricellular role and the absence of a validated clinical application.
The most defensible annotation is narrower than many bioinformatic publications imply. OLFML2A is best described as a secreted, oligomeric olfactomedin-domain ECM glycoprotein with preferential affinity for CS-E and heparin. Its broader structural role is likely to be matricellular—organizing or modulating sulfated extracellular matrices and thereby influencing cell adhesion, migration, or local signaling—rather than acting as a core load-bearing matrix polymer. (cardenasleon2022matricellularproteinsin pages 11-12, tomarev2009olfactomedindomaincontainingproteins pages 7-8)
The AP-1/TNBC work supplies credible evidence that OLFML2A can influence cancer-cell behavior, but it does not yet connect the extracellular protein’s CS-E binding to a receptor or intracellular signaling cascade. AML and other recent reports chiefly show that OLFML2A RNA covaries with prognosis or tissue state. Given its ECM association, these signals may reflect stromal composition as much as malignant-cell biology.
Priority experiments are: endogenous human-protein purification and glycoproteomics; quantitative CS-E/heparin binding; identification of receptors and native matrix partners; mapping of the cleavage site and protease; rescue with cleavage-resistant and oligomerization-deficient mutants; spatial transcriptomic/proteomic separation of stromal and malignant sources; and conditional animal models. Until those studies are available, OLFML2A should be considered a mechanistically plausible but incompletely characterized extracellular regulator, not a validated therapeutic target.
References
(tomarev2009olfactomedindomaincontainingproteins pages 7-8): Stanislav I. Tomarev and Naoki Nakaya. Olfactomedin domain-containing proteins: possible mechanisms of action and functions in normal development and pathology. Molecular Neurobiology, 40:122-138, Jun 2009. URL: https://doi.org/10.1007/s12035-009-8076-x, doi:10.1007/s12035-009-8076-x. This article has 177 citations and is from a peer-reviewed journal.
(cardenasleon2022matricellularproteinsin pages 11-12): Claudia Griselda Cárdenas-León, Kristina Mäemets-Allas, Mariliis Klaas, Heli Lagus, Esko Kankuri, and Viljar Jaks. Matricellular proteins in cutaneous wound healing. Frontiers in Cell and Developmental Biology, Nov 2022. URL: https://doi.org/10.3389/fcell.2022.1073320, doi:10.3389/fcell.2022.1073320. This article has 33 citations.
(zhao2021olfml2aisnecessary pages 4-8): Qian Zhao, Kaixin Zhang, Yong Li, Yaxuan Ren, Jikang Shi, Yulu Gu, Shuang Qiu, Sainan Liu, Yi Cheng, Yichun Qiao, and Yawen Liu. Olfml2a is necessary for anti-triple negative breast cancer effect of selective activator protein‐1 inhibitor t-5224. Aug 2021. URL: https://doi.org/10.1016/j.tranon.2021.101100, doi:10.1016/j.tranon.2021.101100. This article has 18 citations and is from a peer-reviewed journal.
(zhao2021olfml2aisnecessary pages 3-4): Qian Zhao, Kaixin Zhang, Yong Li, Yaxuan Ren, Jikang Shi, Yulu Gu, Shuang Qiu, Sainan Liu, Yi Cheng, Yichun Qiao, and Yawen Liu. Olfml2a is necessary for anti-triple negative breast cancer effect of selective activator protein‐1 inhibitor t-5224. Aug 2021. URL: https://doi.org/10.1016/j.tranon.2021.101100, doi:10.1016/j.tranon.2021.101100. This article has 18 citations and is from a peer-reviewed journal.
(lu2023olfml2aoverexpressionpredicts pages 3-4): Xuan Lu, Ying Li, Yan Yang, Wanchuan Zhuang, Xingxing Chai, and Chen Gong. Olfml2a overexpression predicts an unfavorable prognosis in patients with aml. Journal of Oncology, 2023:1-12, Feb 2023. URL: https://doi.org/10.1155/2023/6017852, doi:10.1155/2023/6017852. This article has 6 citations.
(lu2023olfml2aoverexpressionpredicts pages 4-5): Xuan Lu, Ying Li, Yan Yang, Wanchuan Zhuang, Xingxing Chai, and Chen Gong. Olfml2a overexpression predicts an unfavorable prognosis in patients with aml. Journal of Oncology, 2023:1-12, Feb 2023. URL: https://doi.org/10.1155/2023/6017852, doi:10.1155/2023/6017852. This article has 6 citations.
(tomarev2009olfactomedindomaincontainingproteins pages 26-27): Stanislav I. Tomarev and Naoki Nakaya. Olfactomedin domain-containing proteins: possible mechanisms of action and functions in normal development and pathology. Molecular Neurobiology, 40:122-138, Jun 2009. URL: https://doi.org/10.1007/s12035-009-8076-x, doi:10.1007/s12035-009-8076-x. This article has 177 citations and is from a peer-reviewed journal.
(perezibave2016olfactomedinlike2a pages 4-5): Diana Cristina Pérez-Ibave, Rafael González-Alvarez, Margarita de La Luz Martinez-Fierro, Gabriel Ruiz-Ayma, Maricela Luna-Muñoz, Laura Elia Martínez-De-Villarreal, María De Lourdes Garza-Rodríguez, Diana Reséndez-Pérez, Jibran Mohamed-Noriega, Raquel Garza-Guajardo, Víctor Manuel Bautista-De-Lucío, Karim Mohamed-Noriega, Oralia Barboza-Quintana, Carlos Arámburo-De-La-Hoz, Hugo Alberto Barrera-Saldaña, and Irám Pablo Rodríguez-Sánchez. Olfactomedin-like 2 a and b (olfml2a and olfml2b) expression profile in primates (human and baboon). Biological Research, Nov 2016. URL: https://doi.org/10.1186/s40659-016-0101-8, doi:10.1186/s40659-016-0101-8. This article has 14 citations and is from a peer-reviewed journal.
(zhao2021olfml2aisnecessary pages 2-3): Qian Zhao, Kaixin Zhang, Yong Li, Yaxuan Ren, Jikang Shi, Yulu Gu, Shuang Qiu, Sainan Liu, Yi Cheng, Yichun Qiao, and Yawen Liu. Olfml2a is necessary for anti-triple negative breast cancer effect of selective activator protein‐1 inhibitor t-5224. Aug 2021. URL: https://doi.org/10.1016/j.tranon.2021.101100, doi:10.1016/j.tranon.2021.101100. This article has 18 citations and is from a peer-reviewed journal.
(gao2022genechipexpressionprofiling pages 1-6): Xiufei Gao, Zimei Yang, Chuchu Xu, Qing-hong Yu, Mengqian Wang, Jiaqing Song, Chunyu Wu, and Ming-cang Chen. Genechip expression profiling identified olfml2a as a potential therapeutic target in tnbc cells. Annals of Translational Medicine, 10:274-274, Mar 2022. URL: https://doi.org/10.21037/atm-22-757, doi:10.21037/atm-22-757. This article has 12 citations.
(lu2023olfml2aoverexpressionpredicts pages 6-8): Xuan Lu, Ying Li, Yan Yang, Wanchuan Zhuang, Xingxing Chai, and Chen Gong. Olfml2a overexpression predicts an unfavorable prognosis in patients with aml. Journal of Oncology, 2023:1-12, Feb 2023. URL: https://doi.org/10.1155/2023/6017852, doi:10.1155/2023/6017852. This article has 6 citations.
(lu2023olfml2aoverexpressionpredicts pages 5-6): Xuan Lu, Ying Li, Yan Yang, Wanchuan Zhuang, Xingxing Chai, and Chen Gong. Olfml2a overexpression predicts an unfavorable prognosis in patients with aml. Journal of Oncology, 2023:1-12, Feb 2023. URL: https://doi.org/10.1155/2023/6017852, doi:10.1155/2023/6017852. This article has 6 citations.
(OpenTargets Search: -OLFML2A): Open Targets Query (-OLFML2A, 5 results). Buniello, A. et al. (2025). Open Targets Platform: facilitating therapeutic hypotheses building in drug discovery. Nucleic Acids Research.