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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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.
Target identity: The body of evidence retrieved is consistent with human FBXO2 (also called Fbs1 in the lectin-type F-box literature) being a glycan-binding F-box protein that functions as the substrate-recognition subunit of an SCF (SKP1–CUL1–RBX1–F-box) E3 ubiquitin ligase. This matches the UniProt-provided description “F-box only protein 2” for Homo sapiens, and aligns with UniProt-listed domains (F-box plus a C-terminal sugar-binding/galactose-binding–like fold) because the literature describes an N-terminal F-box (SKP1-binding) and a C-terminal substrate-binding domain (SBD) that binds the innermost N-glycan core (Man3GlcNAc2). (suzuki2021foldingandquality pages 15-16, yoshida2019sugarrecognizingubiquitinligases pages 2-4)
FBXO2 is best understood as a substrate-recognition adaptor that confers specificity to an SCF E3 ligase complex (SKP1–CUL1–RBX1–FBXO2). In this architecture, the F-box binds SKP1, which bridges to CUL1/RBX1, while FBXO2’s C-terminal region binds the substrate; ubiquitin transfer is executed by the RBX1-associated E2 enzyme. (suzuki2021foldingandquality pages 15-16, yoshida2018cytosolicnglycanstriggers pages 5-6)
A central concept for FBXO2/Fbs1 is that it recognizes a glycan-based degradation signal (“sugar degron”): it binds the innermost N-glycan core (described as Man3GlcNAc2 / innermost GlcNAc2 moiety) using a small hydrophobic pocket in its SBD, with preference for high-mannose N-glycans and denatured/misfolded glycoproteins (where the core glycan becomes accessible). (yoshida2019sugarrecognizingubiquitinligases pages 2-4, yoshida2018cytosolicnglycanstriggers pages 5-6)
Visual evidence: Structural and schematic support for FBXO2/Fbs1 domain organization, SCF assembly, and Man3GlcNAc2 recognition pocket are shown in Yoshida et al. 2019 (Figures summarizing domain map/SCF model and glycan-binding pocket). (yoshida2019sugarrecognizingubiquitinligases media c9dd2277)
Although N-glycoproteins are produced in the ER/secretory pathway, lectin-type F-box proteins such as FBXO2 are described as operating in the nucleocytoplasmic compartment, where they can recognize retrotranslocated ER glycoproteins and promote their ubiquitination as part of ER-associated degradation (ERAD) and broader proteostasis mechanisms. (yoshida2019sugarrecognizingubiquitinligases pages 2-4, yoshida2019sugarrecognizingubiquitinligases pages 4-5)
Authoritative reviews describe SCF(Fbs1/FBXO2) and SCF(Fbs2) as binding the innermost N-glycan core and acting on ERAD substrates. Examples of glycoprotein targets/processes cited in the mechanistic literature include integrin β1, TCRα, asialoglycoprotein receptor H2a, and CFTRΔF508 as glycoproteins in the orbit of Fbs1/Fbs2-mediated quality control. (yoshida2019sugarrecognizingubiquitinligases pages 4-5)
Reviews summarizing primary work report that FBXO2/Fbs1 can modulate the amyloid pathway by promoting degradation of BACE1 (β-secretase) and by regulating APP levels/processing; FBXO2 is described as neuron/brain enriched in these accounts. (suzuki2021foldingandquality pages 15-16, yoshida2019sugarrecognizingubiquitinligases pages 5-6)
A 2024 preprint further leverages this biology to build a human iPSC-derived cortical neuron model in which early downregulation of FBXO2 is reported to lead to Aβ aggregation, tau hyperphosphorylation, and neuronal network impairment, positioning FBXO2 reduction as a potential driver of sporadic AD-like phenotypes in vitro (note: preprint, not yet peer reviewed). URL and date: bioRxiv (Sep 2024) https://doi.org/10.1101/2024.09.01.610673. (xue2024skp2mediatedfbxo2proteasomal pages 1-5)
A peer-reviewed primary study (JCI Insight, Oct 2020; https://doi.org/10.1172/jci.insight.136676) reports that Fbxo2 functions as part of an SCF complex and mediates clearance of damaged lysosomes in CNS contexts. Loss of Fbxo2 delayed clearance of damaged lysosomes and reduced viability after lysosomal damage in mouse primary cortical cultures; in an NPC disease model, Fbxo2 deficiency exacerbated neurodegeneration and reduced survival. (liu2020fbxo2mediatesclearance pages 1-2)
Direct localization evidence in human cancer cells is available from a 2024 study in papillary thyroid carcinoma (PTC), where immunofluorescence localized FBXO2 mainly to the cytoplasm of PTC cells. (Scientific Reports, Sep 2024; https://doi.org/10.1038/s41598-024-73455-z). (guo2024fbxo2promotesthe pages 3-5)
A Neuro-Oncology study (Jul 2023; https://doi.org/10.1093/neuonc/noac169) used SWATH-MS proteomics across paired primary and recurrent glioblastomas and identified FBXO2 as consistently upregulated at recurrence, validated by immunohistochemistry. Functionally, FBXO2 knockout in human glioma cells conferred a survival benefit in orthotopic xenograft mouse models and reduced invasive growth in organotypic brain slice cultures, consistent with a protumorigenic role in this context. FBXO2 expression was reported enriched in the tumor infiltration zone, and FBXO2-positive cancer cells associated with synaptic signaling programs. (buehler2023quantitativeproteomiclandscapes pages 1-2)
A Scientific Reports paper (Sep 2024; https://doi.org/10.1038/s41598-024-73455-z) reports that FBXO2 is overexpressed in PTC and that FBXO2 binds p53 and promotes p53 ubiquitination and degradation. Experimentally, the study used co-immunoprecipitation/GST pulldown and ubiquitination assays (MG132-treated cells; p53 IP; ubiquitin detection) and showed that FBXO2 knockdown reduced proliferation and increased apoptosis, with xenograft tumor growth suppressed upon FBXO2 targeting. Clinically, FBXO2 expression correlated with tumor size and metastatic/invasive features (as reported by the authors). (guo2024fbxo2promotesthe pages 7-8, guo2024fbxo2promotesthe pages 2-3)
A bioRxiv preprint (Mar 2024; https://doi.org/10.1101/2024.03.28.586926) proposes FBXO2 acts as a tumor suppressor in HCC by binding and promoting ubiquitination/proteasomal degradation of Hsp47/SERPINH1. A key quantitative datapoint reported is that FBXO2 protein was frequently downregulated in HCC tissues by IHC: 149/258 tumors classified as low FBXO2 (P<0.001). The authors also describe a regulatory mechanism in which DNA-PKcs-mediated phosphorylation at S17 enables SKP2-mediated ubiquitination (at K79) and proteasomal degradation of FBXO2. (xue2024skp2mediatedfbxo2proteasomal pages 5-8, xue2024skp2mediatedfbxo2proteasomal pages 11-14)
A Heliyon study (Apr 2024; https://doi.org/10.1016/j.heliyon.2024.e28490) integrated scRNA-seq and bulk RNA-seq and identified FBXO2 as a candidate biomarker associated with chemoresistance. The authors describe FBXO2 as an ER-associated F-box component implicated in protein processing in the ER, report higher FBXO2 expression in malignant epithelial cells, and present functional evidence that silencing FBXO2 lowered cisplatin IC50 in A2780 and SKOV3 ovarian cancer cell lines. The study further reports that high FBXO2 associates with worse overall and disease-free survival in their computational analyses. (lai2024integratedanalysisof pages 10-11)
Recent studies position FBXO2 as a potential biomarker or stratification variable in multiple cancers:
- Glioblastoma: FBXO2 abundance increases at recurrence and correlates with infiltrative-zone programs; FBXO2 genetic loss reduces tumor aggressiveness in models, making it a candidate dependency/biomarker for recurrence biology. (buehler2023quantitativeproteomiclandscapes pages 1-2)
- HGSOC: FBXO2 is proposed as a biomarker for chemoresistance and prognosis, with supporting in vitro cisplatin-sensitization upon knockdown. (lai2024integratedanalysisof pages 10-11)
- PTC: FBXO2 expression correlates with aggressive clinicopathologic features and mechanistically impacts p53 stability, suggesting diagnostic/prognostic relevance. (guo2024fbxo2promotesthe pages 7-8)
From an E3-ligase biology perspective, FBXO2 is not a catalytic enzyme but a specificity factor; thus, interventions could conceptually target (i) its substrate-binding interface (glycan pocket / substrate docking), (ii) its SCF assembly (F-box–SKP1 interaction), or (iii) upstream regulatory nodes that tune FBXO2 abundance (e.g., the SKP2 axis proposed in HCC). The 2019 mechanistic synthesis emphasizes that identifying physiological substrates and complex components is essential for understanding pathophysiological roles—an argument that remains salient given context-dependent oncogenic vs tumor-suppressive roles across cancers. (yoshida2019sugarrecognizingubiquitinligases pages 5-6, xue2024skp2mediatedfbxo2proteasomal pages 11-14)
Mechanistic reviews by Yoshida/Tanaka and colleagues provide a coherent expert framework: cytosolic exposure of N-glycans (from ER retrotranslocation or membrane damage) is interpreted as a signal of unwanted proteins/organelles, and lectin-type SCF complexes (including SCF(Fbs1/FBXO2)) translate this signal into ubiquitination and degradation (proteasome and, in related paralogs, autophagy). These reviews highlight structural determinants of glycan recognition and caution that detailed physiological substrate mapping is still needed to understand tissue- and disease-specific outcomes. (yoshida2019sugarrecognizingubiquitinligases pages 2-4, yoshida2018cytosolicnglycanstriggers pages 5-6)
A concise cross-study summary is provided in the table below.
| FBXO2/Fbs1 role | Key substrate(s) / process | Main evidence type | Recent source(s) (2023–2024) | Foundational source(s) | Year(s) | DOI / URL | Citation |
|---|---|---|---|---|---|---|---|
| SCF-type F-box substrate receptor for glycoprotein quality control; binds innermost Man3GlcNAc2 N-glycan core via substrate-binding domain after SKP1 association through the F-box domain | Recognition of misfolded/high-mannose glycoproteins in ERAD; broad lectin-like glycan sensing rather than classical enzyme catalysis | Structural biology, SCF complex modeling, glycan-binding biochemistry, review synthesis | — | Yoshida et al., Front Physiol (2019); Suzuki & Fujihira, Comprehensive Glycoscience (2021) | 2019, 2021 | https://doi.org/10.3389/fphys.2019.00104 ; https://doi.org/10.1016/B978-0-12-409547-2.14947-9 | (yoshida2019sugarrecognizingubiquitinligases pages 2-4, suzuki2021foldingandquality pages 15-16, yoshida2019sugarrecognizingubiquitinligases media c9dd2277) |
| Glycan-directed ER-associated degradation adaptor in the cytosol/nucleocytoplasm | ERAD substrates cited for Fbs1/Fbs2 pathway include CFTRΔF508, TCRα, integrin β1, asialoglycoprotein receptor H2a | Review of primary ERAD studies; substrate lists from prior cell-based and biochemical work | HGSOC biomarker study links FBXO2 to ER protein processing and chemoresistance-related ER pathways | Yoshida et al., Front Physiol (2019); Yoshida & Tanaka, BioEssays (2018) | 2018, 2019, 2024 | https://doi.org/10.3389/fphys.2019.00104 ; https://doi.org/10.1002/bies.201700215 ; https://doi.org/10.1016/j.heliyon.2024.e28490 | (yoshida2019sugarrecognizingubiquitinligases pages 4-5, yoshida2018cytosolicnglycanstriggers pages 5-6, lai2024integratedanalysisof pages 10-11) |
| Neuron-enriched SCF adaptor regulating APP pathway glycoproteins | APP is a reported FBXO2 substrate; FBXO2 also reduces BACE1 levels, lowering amyloidogenic processing | In vitro/in vivo substrate studies, knockout mouse/neuron experiments, disease-focused reviews | 2024 preprint: FBXO2 downregulation in human iPSC-derived neurons induces Aβ aggregation and tau hyperphosphorylation | Atkin et al., J Biol Chem (2014); Suzuki & Fujihira (2021); Yoshida et al. (2019) | 2014, 2019, 2021, 2024 | https://doi.org/10.1074/jbc.M113.515056 ; https://doi.org/10.3389/fphys.2019.00104 ; https://doi.org/10.1016/B978-0-12-409547-2.14947-9 ; https://doi.org/10.1101/2024.09.01.610673 | (suzuki2021foldingandquality pages 15-16, yoshida2019sugarrecognizingubiquitinligases pages 4-5, yoshida2019sugarrecognizingubiquitinligases pages 5-6) |
| Metabolic regulator when induced in liver; still acting through ubiquitin-ligase substrate recognition rather than catalysis | Insulin receptor ubiquitination reported in obese liver context, disrupting glucose homeostasis | Review synthesis of prior mechanistic studies | — | Yoshida & Tanaka, BioEssays (2018) | 2018 | https://doi.org/10.1002/bies.201700215 | (yoshida2018cytosolicnglycanstriggers pages 5-6) |
| CNS lysosomal quality-control factor; glycan-binding F-box protein in an SCF complex | Damaged lysosome clearance / lysophagy in CNS; loss delays damaged lysosome clearance and reduces viability after lysosomal injury | Mouse primary cortical culture assays, NPC human fibroblast sensitivity assays, knockout disease model | — | Liu et al., JCI Insight (2020) | 2020 | https://doi.org/10.1172/jci.insight.136676 | (liu2020fbxo2mediatesclearance pages 1-2) |
| Recurrent glioblastoma-associated FBXO2 program, likely via tumor–microenvironment interactions | Increased FBXO2 abundance in recurrent glioblastoma; enriched in tumor infiltration zone; associated with synaptic signaling processes | SWATH-MS proteomics, immunohistochemistry, CRISPR/KO, orthotopic xenografts, organotypic brain slices | Buehler et al., Neuro-Oncology (2023) | — | 2023 | https://doi.org/10.1093/neuonc/noac169 | (buehler2023quantitativeproteomiclandscapes pages 1-2) |
| Oncogenic FBXO2 in papillary thyroid carcinoma acting through ubiquitin-mediated substrate turnover | p53 direct binding, ubiquitination, and degradation; FBXO2 overexpression correlates with tumor size, lymph-node metastasis, and invasion; mainly cytoplasmic localization in PTC cells | Co-IP, GST pulldown, in vivo ubiquitination assay, IF/IHC, xenografts, proliferation/apoptosis assays | Guo et al., Scientific Reports (2024) | — | 2024 | https://doi.org/10.1038/s41598-024-73455-z | (guo2024fbxo2promotesthe pages 7-8, guo2024fbxo2promotesthe pages 2-3, guo2024fbxo2promotesthe pages 3-5) |
| Tumor-suppressive FBXO2 in hepatocellular carcinoma through degradation of a pro-fibrotic chaperone | Hsp47/SERPINH1 ubiquitination and proteasomal degradation; FBXO2 protein low in 149/258 HCCs; low FBXO2 associated with advanced stage and worse median survival | Human tumor IHC, ubiquitination and half-life studies, phospho-regulation analysis, hepatocyte-specific knockout mice, metastasis assays | Xue et al., bioRxiv (2024) | — | 2024 | https://doi.org/10.1101/2024.03.28.586926 | (xue2024skp2mediatedfbxo2proteasomal pages 5-8, xue2024skp2mediatedfbxo2proteasomal pages 1-5, xue2024skp2mediatedfbxo2proteasomal pages 11-14) |
| Candidate biomarker/therapeutic target in ovarian chemoresistance with ER-processing links | High FBXO2 associated with worse OS/DFS; FBXO2 knockdown lowers cisplatin IC50 in A2780 and SKOV3 cells | scRNA-seq + bulk RNA-seq integration, survival analysis, cisplatin-response assays, knockdown | Lai et al., Heliyon (2024) | — | 2024 | https://doi.org/10.1016/j.heliyon.2024.e28490 | (lai2024integratedanalysisof pages 10-11) |
Table: This table summarizes the best-supported molecular roles, substrates/processes, and evidence types for human FBXO2/Fbs1, contrasting recent 2023–2024 disease studies with foundational mechanistic literature on SCF assembly and glycan recognition.
Open Targets lists disease associations for FBXO2 including hepatocellular carcinoma, papillary thyroid carcinoma, hearing loss/deafness, and neurodegenerative disease, with underlying evidence including recent literature links (via PubMed IDs) and functional genomics screens. This supports that FBXO2 is repeatedly implicated across cancer and neurological phenotypes, though the mechanistic directionality is context dependent. (OpenTargets Search: -FBXO2)
Note on evidence quality: Two key 2024 items are preprints (bioRxiv) and should be interpreted as provisional until peer-reviewed; core mechanistic aspects of FBXO2 glycan recognition and SCF adaptor function are supported by peer-reviewed reviews and established structural work summarized therein. (yoshida2019sugarrecognizingubiquitinligases pages 2-4, yoshida2018cytosolicnglycanstriggers pages 5-6)
References
(suzuki2021foldingandquality pages 15-16): Tadashi Suzuki and Haruhiko Fujihira. Folding and quality control of glycoproteins. Comprehensive Glycoscience, pages 1-28, Dec 2021. URL: https://doi.org/10.1016/b978-0-12-409547-2.14947-9, doi:10.1016/b978-0-12-409547-2.14947-9. This article has 12 citations.
(yoshida2019sugarrecognizingubiquitinligases pages 2-4): Yukiko Yoshida, Tsunehiro Mizushima, and Keiji Tanaka. Sugar-recognizing ubiquitin ligases: action mechanisms and physiology. Frontiers in Physiology, Feb 2019. URL: https://doi.org/10.3389/fphys.2019.00104, doi:10.3389/fphys.2019.00104. This article has 31 citations.
(yoshida2018cytosolicnglycanstriggers pages 5-6): Yukiko Yoshida and Keiji Tanaka. Cytosolic n-glycans: triggers for ubiquitination directing proteasomal and autophagic degradation: molecular systems for monitoring cytosolic n-glycans as signals for unwanted proteins and organelles. BioEssays : news and reviews in molecular, cellular and developmental biology, Feb 2018. URL: https://doi.org/10.1002/bies.201700215, doi:10.1002/bies.201700215. This article has 19 citations.
(yoshida2019sugarrecognizingubiquitinligases media c9dd2277): Yukiko Yoshida, Tsunehiro Mizushima, and Keiji Tanaka. Sugar-recognizing ubiquitin ligases: action mechanisms and physiology. Frontiers in Physiology, Feb 2019. URL: https://doi.org/10.3389/fphys.2019.00104, doi:10.3389/fphys.2019.00104. This article has 31 citations.
(yoshida2019sugarrecognizingubiquitinligases pages 4-5): Yukiko Yoshida, Tsunehiro Mizushima, and Keiji Tanaka. Sugar-recognizing ubiquitin ligases: action mechanisms and physiology. Frontiers in Physiology, Feb 2019. URL: https://doi.org/10.3389/fphys.2019.00104, doi:10.3389/fphys.2019.00104. This article has 31 citations.
(yoshida2019sugarrecognizingubiquitinligases pages 5-6): Yukiko Yoshida, Tsunehiro Mizushima, and Keiji Tanaka. Sugar-recognizing ubiquitin ligases: action mechanisms and physiology. Frontiers in Physiology, Feb 2019. URL: https://doi.org/10.3389/fphys.2019.00104, doi:10.3389/fphys.2019.00104. This article has 31 citations.
(xue2024skp2mediatedfbxo2proteasomal pages 1-5): Cailin Xue, Fei Yang, Guojian Bao, Jiawu Yan, Rao Fu, Minglu Zhang, Jialu Ding, Jiale Feng, Jianbo Han, Xihu Qin, Hua Su, and Beicheng Sun. Skp2-mediated fbxo2 proteasomal degradation drives hepatocellular carcinoma progression via stabilizing hsp47. bioRxiv, Mar 2024. URL: https://doi.org/10.1101/2024.03.28.586926, doi:10.1101/2024.03.28.586926. This article has 0 citations.
(liu2020fbxo2mediatesclearance pages 1-2): Elaine A. Liu, Mark L. Schultz, Chisaki Mochida, Chan Chung, Henry L. Paulson, and Andrew P. Lieberman. Fbxo2 mediates clearance of damaged lysosomes and modifies neurodegeneration in the niemann-pick c brain. JCI Insight, Oct 2020. URL: https://doi.org/10.1172/jci.insight.136676, doi:10.1172/jci.insight.136676. This article has 53 citations and is from a domain leading peer-reviewed journal.
(guo2024fbxo2promotesthe pages 3-5): Wenke Guo, Yaoqiang Ren, and Xinguang Qiu. Fbxo2 promotes the progression of papillary thyroid carcinoma through the p53 pathway. Scientific Reports, Sep 2024. URL: https://doi.org/10.1038/s41598-024-73455-z, doi:10.1038/s41598-024-73455-z. This article has 9 citations and is from a peer-reviewed journal.
(buehler2023quantitativeproteomiclandscapes pages 1-2): Marcel Buehler, Xiao Yi, Weigang Ge, Peter Blattmann, Elisabeth Rushing, Guido Reifenberger, Joerg Felsberg, Charles Yeh, Jacob E Corn, Luca Regli, Junyi Zhang, Ann Cloos, Vidhya M Ravi, Benedikt Wiestler, Dieter Henrik Heiland, Ruedi Aebersold, Michael Weller, Tiannan Guo, and Tobias Weiss. Quantitative proteomic landscapes of primary and recurrent glioblastoma reveal a protumorigeneic role for fbxo2-dependent glioma-microenvironment interactions. Neuro-oncology, 25:290-302, Jul 2023. URL: https://doi.org/10.1093/neuonc/noac169, doi:10.1093/neuonc/noac169. This article has 32 citations and is from a domain leading peer-reviewed journal.
(guo2024fbxo2promotesthe pages 7-8): Wenke Guo, Yaoqiang Ren, and Xinguang Qiu. Fbxo2 promotes the progression of papillary thyroid carcinoma through the p53 pathway. Scientific Reports, Sep 2024. URL: https://doi.org/10.1038/s41598-024-73455-z, doi:10.1038/s41598-024-73455-z. This article has 9 citations and is from a peer-reviewed journal.
(guo2024fbxo2promotesthe pages 2-3): Wenke Guo, Yaoqiang Ren, and Xinguang Qiu. Fbxo2 promotes the progression of papillary thyroid carcinoma through the p53 pathway. Scientific Reports, Sep 2024. URL: https://doi.org/10.1038/s41598-024-73455-z, doi:10.1038/s41598-024-73455-z. This article has 9 citations and is from a peer-reviewed journal.
(xue2024skp2mediatedfbxo2proteasomal pages 5-8): Cailin Xue, Fei Yang, Guojian Bao, Jiawu Yan, Rao Fu, Minglu Zhang, Jialu Ding, Jiale Feng, Jianbo Han, Xihu Qin, Hua Su, and Beicheng Sun. Skp2-mediated fbxo2 proteasomal degradation drives hepatocellular carcinoma progression via stabilizing hsp47. bioRxiv, Mar 2024. URL: https://doi.org/10.1101/2024.03.28.586926, doi:10.1101/2024.03.28.586926. This article has 0 citations.
(xue2024skp2mediatedfbxo2proteasomal pages 11-14): Cailin Xue, Fei Yang, Guojian Bao, Jiawu Yan, Rao Fu, Minglu Zhang, Jialu Ding, Jiale Feng, Jianbo Han, Xihu Qin, Hua Su, and Beicheng Sun. Skp2-mediated fbxo2 proteasomal degradation drives hepatocellular carcinoma progression via stabilizing hsp47. bioRxiv, Mar 2024. URL: https://doi.org/10.1101/2024.03.28.586926, doi:10.1101/2024.03.28.586926. This article has 0 citations.
(lai2024integratedanalysisof pages 10-11): Wenwen Lai, Ruixiang Xie, Chen Chen, Weiming Lou, Haiyan Yang, Libin Deng, Quqin Lu, and Xiaoli Tang. Integrated analysis of scrna-seq and bulk rna-seq identifies fbxo2 as a candidate biomarker associated with chemoresistance in hgsoc. Apr 2024. URL: https://doi.org/10.1016/j.heliyon.2024.e28490, doi:10.1016/j.heliyon.2024.e28490. This article has 8 citations.
(OpenTargets Search: -FBXO2): Open Targets Query (-FBXO2, 35 results). Buniello, A. et al. (2025). Open Targets Platform: facilitating therapeutic hypotheses building in drug discovery. Nucleic Acids Research.