Affinage

NANOS3

Nanos homolog 3 · UniProt P60323

Length
173 aa
Mass
18.8 kDa
Annotated
2026-06-10
45 papers in source corpus 20 papers cited in narrative 20 extracted findings
Cross-family judge vs UniProt: Affinage preferred faithfulness: 9/9 claims corpus-supported (100%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

NANOS3 is a zinc-finger RNA-binding protein that acts as a post-transcriptional regulator to specify and maintain the germ cell lineage (PMID:18436203, PMID:21421998). Its central biochemical activity is the assembly of a high-affinity ribonucleoprotein complex with the RNA-binding protein DND1, which jointly recognizes an AUGAAUU heptanucleotide motif (N3-DRE) in target mRNA 3'UTRs; a 1.7-Å crystal structure of the DND1–NANOS3–CDK1 N3-DRE complex shows that NANOS3 has no intrinsic sequence specificity on its own but contributes a continuous RNA-binding surface that, together with DND1, builds a high-information recognition motif to repress targets such as Cdk1 in primordial germ cells (PGCs) (PMID:41040373). NANOS3 also partners with Pumilio-family proteins (PUM2, PUM1) to form translational-repressor complexes, including PUM1-dependent 3'UTR repression of the G2/M regulator FOXM1 (PMID:18089289, PMID:35743036), and couples target mRNAs to deadenylation by directly binding the CCR4-NOT subunit CNOT8 (PMID:25416063). The protein localizes to stress granules and processing bodies (P-bodies), where it represses target translation, and in human PGC-like cells it bridges DND1 to the translational repressor 4E-T to silence SOX4 mRNA (PMID:19861488, PMID:40410171). Functionally, NANOS3 maintains germ cells by suppressing both Bax-dependent and Bax-independent apoptosis, and germline-restricted expression is enforced by 3'UTR-mediated mRNA destabilization in somatic cells (PMID:18436203, PMID:20174582). In spermatogonia it blocks retinoic acid–driven differentiation to sustain progenitor expansion and is stabilized by PTBP1 binding to Nanos3 mRNA (PMID:32624547, PMID:35394008). Hypomorphic and zinc-finger missense mutations in NANOS3 are associated with primary ovarian insufficiency, with PGC population size set by NANOS3 protein dosage (PMID:24091668, PMID:25054146). In a context-dependent manner NANOS3 can also act as a translational activator: in zebrafish PGCs the Nanos3–Dnd1 complex activates translation of its own RNAs via an eIF3 interaction, forming a positive feedback loop required to prevent germ cell transdifferentiation (PMID:42026270). Beyond the germline, NANOS3 promotes proliferation, invasion, and stemness programs in lung cancer and glioblastoma cells (PMID:25904364, PMID:32508533).

Mechanistic history

Synthesis pass · year-by-year structured walk · 19 steps
  1. 1999 High

    Established the founding mechanistic model that a NANOS-3 family protein operates by partnering with an RNA-binding protein to control germline fate, rather than acting alone.

    Evidence Yeast two-hybrid, in vitro binding and deletion-mutant analysis of C. elegans NOS-3 with FBF

    PMID:10508609

    Open questions at the time
    • Done in C. elegans, not vertebrate NANOS3
    • fem-3 mRNA repression inferred, not directly demonstrated as the molecular output
    • no structural basis for the interaction
  2. 2007 Medium

    Identified a conserved Pumilio partner for mammalian NANOS3 and linked it to cell-cycle delay and maintenance of undifferentiated spermatogonia, framing NANOS3 as a translational repressor controlling progenitor state.

    Evidence Co-IP with Pumilio2, G1-accumulation cell cycle analysis and retinoic acid treatment in mouse testis

    PMID:18089289

    Open questions at the time
    • Direct mRNA targets of the NANOS3-PUM2 complex not defined
    • interaction assay rigor limited
    • mechanism linking complex to G1 arrest unresolved
  3. 2008 High

    Demonstrated that NANOS3's core in vivo role is germ cell survival, acting through both Bax-dependent and Bax-independent apoptotic suppression.

    Evidence Nanos3/Bax double-knockout mice with lineage tracing and apoptosis quantification

    PMID:18436203

    Open questions at the time
    • Molecular identity of the Bax-independent pathway unknown
    • no direct mRNA targets linking NANOS3 to apoptotic regulators
  4. 2010 High

    Resolved how germline-restricted NANOS3 expression is achieved, showing the 3'UTR enforces germ-cell specificity via somatic mRNA destabilization.

    Evidence Transgenic reporter constructs with WT/truncated 3'UTR and mRNA stability assays in mouse

    PMID:20174582

    Open questions at the time
    • Trans-acting factors mediating somatic destabilization not identified
    • does not address NANOS3 protein function
  5. 2009 High

    Placed NANOS3 protein in stress granules and P-bodies, localizing its repressive activity to cytoplasmic RNP condensates.

    Evidence NANOS3-EGFP transgenic mice with confocal co-localization (TIAL1, p-eIF2α, DCP1A) and functional rescue

    PMID:19861488

    Open questions at the time
    • Functional consequence of granule/P-body localization not tested here
    • no target mRNAs assigned to these compartments
  6. 2011 Medium

    Extended the germ-cell maintenance role to human ESC-derived germ cells, linking NANOS3 to pluripotency and meiotic gene programs.

    Evidence Morpholino and shRNA knockdown with immunofluorescence and gene expression analysis in hESC-derived germ cells

    PMID:21421998

    Open questions at the time
    • Direct vs indirect effect on the affected genes unresolved
    • nuclear co-localization with DNA mechanistically unexplained
    • single lab
  7. 2013 Medium

    Connected NANOS3 to human disease and established that germ cell number is set by NANOS3 protein dosage, via a destabilizing POI mutation.

    Evidence POI patient mutation screening, protein stability Western blot, mouse dosage analysis

    PMID:24091668

    Open questions at the time
    • Causality limited to a hypomorph mechanism
    • molecular targets downstream of dosage not defined
    • single lab
  8. 2014 Medium

    Linked a zinc-finger missense mutation to loss of anti-apoptotic function, supporting RNA-binding via the C2HC motif as essential for activity.

    Evidence In vitro apoptosis assays (flow cytometry, confocal) and in silico modelling of the p.Glu120Lys mutant

    PMID:25054146

    Open questions at the time
    • RNA-binding disruption inferred from modelling, not measured
    • physiological relevance in vivo not established
    • single lab
  9. 2014 Medium

    Defined the biochemical route to mRNA degradation, showing NANOS3 directly engages the CCR4-NOT deadenylase via CNOT8, distinguishing it from NANOS2.

    Evidence Co-IP in mouse germ cells, NANOS2 zinc-finger mutant transgenics, double-mutant phenotyping

    PMID:25416063

    Open questions at the time
    • Direct deadenylation of specific targets not demonstrated
    • single lab
  10. 2020 Medium

    Placed DND1 genetically and physically in the NANOS3 pathway for suppressing teratoma formation from PGCs.

    Evidence Dnd1/Nanos3 double-mutant mice with teratoma incidence quantification

    PMID:32339196

    Open questions at the time
    • Molecular targets of the DND1-NANOS3 complex not yet identified here
    • strain-specific (129 background)
  11. 2020 Medium

    Identified PTBP1 as an upstream stabilizer of Nanos3 mRNA, embedding NANOS3 in a regulatory network governing spermatogonial homeostasis.

    Evidence RIP of PTBP1 on Nanos3 mRNA, RNA-seq in Ptbp1-KO germline stem cells, compound heterozygous mice

    PMID:32624547

    Open questions at the time
    • Direct binding site on Nanos3 mRNA not mapped
    • single lab
  12. 2020 Medium

    Showed NANOS3 supports oncogenic stemness phenotypes outside the germline in glioblastoma.

    Evidence CRISPR/Cas9 knockout with proliferation, invasion, chemoresistance and xenograft assays

    PMID:32508533

    Open questions at the time
    • Direct mRNA targets in tumor cells not defined
    • mechanism linking NANOS3 to stemness proteins unresolved
  13. 2015 Medium

    Demonstrated a cancer-relevant post-transcriptional mechanism, with NANOS3 binding vimentin mRNA, regulating its poly(A) tail and protecting it from miRNA repression to drive EMT.

    Evidence Overexpression/silencing in NSCLC lines, RIP, poly(A) tail assay, invasion assay

    PMID:25904364

    Open questions at the time
    • E-cadherin transcriptional repression mechanism unclear
    • single lab
  14. 2021 High

    Explained the non-redundancy between NANOS2 and NANOS3, attributing it to zinc-finger structural differences that weaken NANOS3's CNOT1 and DND1 binding.

    Evidence Conditional Nanos2/Nanos3 double KO, chimeric NANOS proteins, in vitro/in vivo binding assays

    PMID:33199444

    Open questions at the time
    • Structural basis described functionally but without atomic resolution at this stage
    • context shaping partner choice not fully defined
  15. 2022 Medium

    Identified FOXM1 as a NANOS3-PUM1 target and assigned NANOS3 a specific role at the G2/M cell-cycle transition in human PGC models.

    Evidence RNA-seq on NANOS1/NANOS3 overexpression, FOXM1 3'UTR reporter assays, cell cycle analysis in TCam-2 cells

    PMID:35743036

    Open questions at the time
    • Endogenous regulation of FOXM1 by NANOS3 in vivo not tested
    • single lab
  16. 2022 Medium

    Established that NANOS3 sustains spermatogonial progenitors postnatally by blocking retinoic acid signaling and preventing premature differentiation.

    Evidence Late-embryonic conditional Nanos3 KO with histology, spermatogenic staging and RA pathway markers

    PMID:35394008

    Open questions at the time
    • Direct RA-pathway mRNA targets of NANOS3 not identified
    • single lab
  17. 2025 High

    Provided the definitive structural and biochemical mechanism: NANOS3 lacks intrinsic RNA specificity but, with DND1, forms a continuous RNA-binding surface recognizing the AUGAAUU N3-DRE motif to repress targets including Cdk1 in vivo.

    Evidence Tandem PAR-CLIP, 1.7-Å crystal structure of DND1-NANOS3-CDK1 N3-DRE RNA, genome editing of N3-DRE in mouse PGCs (preprint)

    PMID:41040373

    Open questions at the time
    • Preprint, peer review pending
    • full target repertoire beyond CDK1 not exhaustively validated in vivo
    • link to deadenylation/decay machinery at the structural level not addressed
  18. 2025 High

    Defined the human PGC-specific output of the DND1-NANOS3 complex, showing it represses SOX4 translation in P-bodies and that NANOS3 bridges DND1 to the repressor 4E-T.

    Evidence Reciprocal co-IP, mRNA binding analysis, P-body localization and SOX4 translational repression in hPGCLCs

    PMID:40410171

    Open questions at the time
    • Generality of 4E-T bridging across other targets untested
    • interplay with CCR4-NOT not resolved here
  19. 2025 Medium

    Revealed context-dependent translational ACTIVATION by NANOS3, where the zebrafish Nanos3-Dnd1 complex promotes translation via eIF3 to maintain germ cell identity, contrasting its repressive role.

    Evidence Transcriptomics, in vivo imaging, interaction-disruption and translational activation assays in zebrafish PGCs

    PMID:42026270

    Open questions at the time
    • Molecular switch between activation and repression unknown
    • eIF3 subunit and binding interface not mapped
    • zebrafish-specific generality unclear

Open questions

Synthesis pass · forward-looking unresolved questions
  • How NANOS3 switches between translational repression (via CCR4-NOT/4E-T and P-bodies) and translational activation (via eIF3), and what determines target and partner choice across germline and cancer contexts, remains unresolved.
  • No unified model reconciling repressor vs activator activity
  • no structural data on the activating eIF3-bound state
  • context-dependent partner selection mechanism undefined

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0003723 RNA binding 3 GO:0045182 translation regulator activity 3 GO:0098772 molecular function regulator activity 2
Localization
GO:0005829 cytosol 2 GO:0005634 nucleus 1
Pathway
R-HSA-8953854 Metabolism of RNA 3 R-HSA-1474165 Reproduction 2 R-HSA-1640170 Cell Cycle 2 R-HSA-5357801 Programmed Cell Death 2
Partners
CNOT8DND1EIF4ENIF1FBFPTBP1PUM1PUM2
Complex memberships
CCR4-NOTDND1-NANOS3 ribonucleoprotein complex

Evidence

Reading pass · 20 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
1999 C. elegans NANOS-3 (NOS-3) physically interacts with FBF RNA-binding protein, as demonstrated by yeast two-hybrid and in vitro binding assays. This complex is proposed to repress fem-3 mRNA to control the sperm-oocyte switch. Loss of nos-3 (deletion mutant) causes defects in the hermaphrodite sperm-oocyte switch and germ-line death that does not require the apoptotic protease CED-3. Yeast two-hybrid, in vitro binding assay, deletion mutant analysis, RNA-mediated interference Current biology : CB High 10508609
2007 Mouse NANOS3 interacts with the RNA-binding protein Pumilio2, forming a conserved translational repressor complex. In prepuberal testis, NANOS3 upregulation causes accumulation of spermatogonial cells in G1 phase, indicating it delays cell cycle progression. Expression is downregulated by retinoic acid (a differentiation factor), consistent with a role in maintaining undifferentiated spermatogonia. Co-immunoprecipitation/interaction assay with Pumilio2, cell cycle analysis (G1 accumulation upon NANOS3 upregulation), retinoic acid treatment with expression analysis Developmental biology Medium 18089289
2008 NANOS3 maintains the germ cell lineage in mouse embryos by suppressing both Bax-dependent and Bax-independent apoptotic pathways. In Nanos3-null embryos, migrating primordial germ cells (PGCs) undergo apoptosis. Double knockout of Nanos3 and Bax only partially rescued PGC apoptosis, demonstrating that NANOS3 suppresses a Bax-independent apoptotic pathway in addition to the Bax-dependent pathway. Double knockout mouse (Nanos3/Bax), lineage analysis using Nanos3-Cre-pA transgenic line, apoptosis quantification Developmental biology High 18436203
2009 NANOS3-EGFP fusion protein co-localizes predominantly with TIAL1 (TIAR) and phosphorylated eIF2α (markers of stress granules) in primordial germ cells, while a fraction co-localizes with DCP1A (a processing body marker). NANOS3-EGFP does not co-localize with Tudor domain-containing protein 1 (intermitochondrial cement marker) in spermatogenic cells. The transgene fully rescues the sterile phenotype of Nanos3 homozygous mutants, confirming functional equivalency. Transgenic NANOS3-EGFP reporter mice, confocal co-localization with stress granule and P-body markers, phenotypic rescue of Nanos3 null mutants Reproduction (Cambridge, England) High 19861488
2010 The Nanos3 3'UTR is required for germ cell-specific expression of NANOS3 in mouse embryos. Although Nanos3 is transcribed in both germ cells and somatic cells, the 3'UTR mediates mRNA destabilization in somatic cells, restricting protein expression to the germline. Even under strong ubiquitous CAG promoter-driven transcription, addition of the Nanos3 3'UTR sequence to an exogenous gene was sufficient to restrict protein expression to germ cells. Transgenic mouse reporter constructs with wild-type and truncated Nanos3-3'UTR, mRNA stability assays in germ vs. somatic cells PloS one High 20174582
2011 NANOS3 is expressed in human germ cell nuclei where it co-localizes with chromosomal DNA during mitosis/meiosis. Reduced NANOS3 expression (via morpholinos or shRNA) in human embryonic stem cell-derived germ cells causes a reduction in germ cell numbers and decreased expression of germ cell-intrinsic genes required for maintenance of pluripotency and meiotic initiation and progression. Morpholino knockdown, shRNA knockdown, immunofluorescence co-localization, gene expression analysis in hESC-derived germ cells Human molecular genetics Medium 21421998
2013 A NANOS3 missense mutation (p.Arg153Trp) identified in a POI patient decreases the stability of the NANOS3 protein, creating a hypomorph. Mouse model analysis showed that PGC population size is controlled by NANOS3 protein dosage. Patient mutation screening, protein stability assay (Western blot of mutant vs. wild-type), mouse dosage analysis Cell death & disease Medium 24091668
2014 A homozygous p.Glu120Lys mutation in NANOS3, located within the second C2HC motif of the zinc finger domain, impairs NANOS3's capacity to prevent apoptosis as shown by in vitro flow cytometry and confocal microscopy apoptosis assays. In silico modelling suggests this mutation destabilizes protein-RNA interaction. In vitro apoptosis assay (flow cytometry, confocal microscopy), in silico molecular modelling of mutant protein BioMed research international Medium 25054146
2014 NANOS3 associates with the CCR4-NOT deadenylation complex via a direct interaction with CNOT8, in contrast to NANOS2 which interacts with CNOT1. This differential interaction with CCR4-NOT components underlies the molecular basis for functional redundancy and differences between NANOS2 and NANOS3 in male germ cells. Co-immunoprecipitation in mouse germ cells, transgenic mouse expressing NANOS2 zinc-finger mutant, phenotypic analysis of double mutants Biology open Medium 25416063
2015 Human NANOS3 promotes epithelial-mesenchymal transition (EMT) in lung cancer cells by repressing E-cadherin at the transcriptional level and upregulating vimentin post-transcriptionally. NANOS3 binds vimentin mRNAs and regulates the length of their poly(A) tail. NANOS3 also protects vimentin mRNA from microRNA-mediated repression. NANOS3 overexpression and silencing in NSCLC cell lines, EMT marker analysis (E-cadherin, vimentin), RNA immunoprecipitation (NANOS3 binds vimentin mRNA), poly(A) tail length assay, invasion assay The Journal of pathology Medium 25904364
2020 DND1 interacts with NANOS2 or NANOS3, and these complexes play a vital role in male embryonic germ cells. Double mutants for Dnd1 and Nanos2 or Nanos3 show synergistic increases in testicular teratoma incidence, placing DND1 in the same pathway as NANOS3 for suppression of teratoma formation from PGCs in the 129 genetic background. Conventional Dnd1 knockout mouse line, double mutant analysis (Dnd1/Nanos2 and Dnd1/Nanos3), teratoma incidence quantification, protein interaction previously established PloS one Medium 32339196
2020 NANOS3 knockdown in glioblastoma cells (by CRISPR-Cas9) reduces proliferation, migration, invasion, and chemoresistance, and inhibits subcutaneous xenograft tumor growth in vivo. NANOS3 deletion decreases levels of stemness/germline proteins CD133, Oct4, Ki67, and Dazl in glioblastoma cells. CRISPR/Cas9 knockout in glioblastoma cell lines, CCK8 proliferation assay, transwell migration/invasion assay, drug sensitivity assay, xenograft mouse model Cancer cell international Medium 32508533
2021 NANOS3 fails to bind CNOT1 (an N-terminal interactor of NANOS2), and its ability to recruit DND1 is poor due to differences in the zinc-finger structure compared to NANOS2. Conditional double knockout of Nanos2 and Nanos3 leads to rapid loss of germ cells. These molecular differences explain why NANOS3 cannot rescue NANOS2 function despite being upregulated in Nanos2-null conditions. Conditional knockout mice (Nanos3/Nanos2), chimeric mice expressing chimeric NANOS proteins, in vitro and in vivo binding assays, protein interaction analysis Development (Cambridge, England) High 33199444
2020 PTBP1 protein binds Nanos3 mRNA in spermatogonia and stabilizes it; loss of Ptbp1 significantly decreases Nanos3 mRNA expression. Mice heterozygous for both Nanos3 and Ptbp1 (Nanos3+/-;Ptbp1+/-) show abnormal spermatogenesis resembling germ cell-specific Ptbp1 KO, while single heterozygotes are normal, demonstrating a genetic interaction between PTBP1 and NANOS3 in spermatogonium homeostasis. RNA immunoprecipitation (PTBP1 binding Nanos3 mRNA), RNA-seq in Ptbp1-KO germline stem cells, compound heterozygous mouse analysis The Journal of reproduction and development Medium 32624547
2022 NANOS3 in complex with PUM1 causes 3'UTR-mediated post-transcriptional repression of FOXM1 mRNA, which encodes a transcription factor critical for G2/M phase transition. NANOS3 specifically influences the G2/M cell cycle phase transition (distinct from NANOS1 which affects G1/S), identified in a human primordial germ cell model (TCam-2 cells). RNA-seq upon NANOS1 and NANOS3 overexpression in TCam-2 cells, 3'UTR reporter assays for FOXM1 repression, cell cycle phase analysis International journal of molecular sciences Medium 35743036
2022 Conditional deletion of Nanos3 at a later embryonic stage (after PGC specification) results in reduction of spermatogonial progenitors postnatally due to premature differentiation. This premature differentiation causes seminiferous stage disagreement and disrupts the spermatogenic epithelial cycle. NANOS3 blocks the retinoic acid (RA) signaling pathway to suppress premature spermatogonial differentiation. Conditional Nanos3 knockout mice (late embryonic deletion), histological analysis, spermatogenic staging analysis, RA pathway marker analysis Biology open Medium 35394008
2012 Medaka Ol4E-T (eIF4E-transporter homolog) can interact with medaka Nanos3 and Vasa proteins in vitro, as shown by yeast two-hybrid assay, suggesting a role for Ol4E-T in translational regulation together with Nanos3 in germ cells. Yeast two-hybrid assay Journal of experimental zoology. Part B, Molecular and developmental evolution Low 22951962
2025 DND1 and NANOS3 form a ribonucleoprotein complex that specifically recognizes an AUGAAUU heptanucleotide motif (N3-DRE) in 3'UTRs of target mRNAs including CDK1. mRNAs with N3-DREs are aberrantly upregulated in DND1- or NANOS3-deficient germ cells. The N3-DRE is essential for Cdk1 repression in mouse PGCs in vivo. A 1.7-Å crystal structure of the ternary DND1-NANOS3-CDK1 N3-DRE RNA complex reveals a continuous RNA-binding surface conferring high-affinity sequence-specific recognition. NANOS3 has no intrinsic sequence-specificity alone but jointly with DND1 builds a high-information-content recognition motif. Tandem PAR-CLIP, X-ray crystallography (1.7 Å), genome editing of N3-DRE in mouse PGCs, transcriptome analysis of DND1/NANOS3 deficient germ cells bioRxivpreprint High 41040373
2025 DND1 and NANOS3 form a complex in human PGC-like cells (hPGCLCs) that restricts PGC specification. DND1 facilitates the binding of NANOS3 to hPGCLC-related mRNAs. SOX4 mRNA is a key downstream target of the DND1-NANOS3 complex; the complex functions in processing bodies (P-bodies) to repress SOX4 mRNA translation. NANOS3 mediates the interaction between DND1 and the translational repressor 4E-T. Co-immunoprecipitation, mRNA binding analysis, P-body localization studies, SOX4 translational repression assay, hPGCLC differentiation system Nature communications High 40410171
2025 In zebrafish, Nanos3 and Dead end1 (Dnd1) form a complex that activates translation of both nanos3 and dead end1 RNAs, establishing a positive feedback loop. Nanos3 acts as a translational activator (not repressor) in this context by interacting with an eIF3 complex protein, promoting translation and maintaining specific RNAs at the periphery of phase-separated germ granules. Disrupting the physical interaction between Nanos3 and Dead end1 leads to transdifferentiation of germ cells into somatic lineages. Transcriptomics, in vivo imaging-based analyses, interaction disruption experiments, translational activation assays in zebrafish PGCs EMBO reports Medium 42026270

Source papers

Stage 0 corpus · 45 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
1999 NANOS-3 and FBF proteins physically interact to control the sperm-oocyte switch in Caenorhabditis elegans. Current biology : CB 227 10508609
2009 The heterogeneity of spermatogonia is revealed by their topology and expression of marker proteins including the germ cell-specific proteins Nanos2 and Nanos3. Developmental biology 151 19818747
2008 Nanos3 maintains the germ cell lineage in the mouse by suppressing both Bax-dependent and -independent apoptotic pathways. Developmental biology 106 18436203
2012 nanos3 maintains germline stem cells and expression of the conserved germline stem cell gene nanos2 in the zebrafish ovary. Developmental biology 104 23228893
2011 NANOS3 function in human germ cell development. Human molecular genetics 82 21421998
2007 Potential role of Nanos3 in maintaining the undifferentiated spermatogonia population. Developmental biology 60 18089289
2013 A NANOS3 mutation linked to protein degradation causes premature ovarian insufficiency. Cell death & disease 47 24091668
2014 Homozygous inactivating mutation in NANOS3 in two sisters with primary ovarian insufficiency. BioMed research international 37 25054146
2012 Expression of vasa and nanos3 during primordial germ cell formation and migration in Atlantic cod (Gadus morhua L.). Theriogenology 31 22898013
2014 Interaction of NANOS2 and NANOS3 with different components of the CNOT complex may contribute to the functional differences in mouse male germ cells. Biology open 26 25416063
2009 Functional reconstruction of NANOS3 expression in the germ cell lineage by a novel transgenic reporter reveals distinct subcellular localizations of NANOS3. Reproduction (Cambridge, England) 26 19861488
2016 Generation of exogenous germ cells in the ovaries of sterile NANOS3-null beef cattle. Scientific reports 20 27117862
2007 Mutation analysis of NANOS3 in 80 Chinese and 88 Caucasian women with premature ovarian failure. Fertility and sterility 20 17418157
2015 A new pattern of primordial germ cell migration in olive flounder (Paralichthys olivaceus) identified using nanos3. Development genes and evolution 19 26025098
2013 Conserved mechanisms for germ cell-specific localization of nanos3 transcripts in teleost species with aquaculture significance. Marine biotechnology (New York, N.Y.) 19 24091820
2010 The Nanos3-3'UTR is required for germ cell specific NANOS3 expression in mouse embryos. PloS one 19 20174582
2016 Over Expression of NANOS3 and DAZL in Human Embryonic Stem Cells. PloS one 18 27768780
2021 Generation of chimeric mice with spermatozoa fully derived from embryonic stem cells using a triple-target CRISPR method for Nanos3†. Biology of reproduction 17 32965494
2015 The human NANOS3 gene contributes to lung tumour invasion by inducing epithelial-mesenchymal transition. The Journal of pathology 16 25904364
2020 Mouse dead end1 acts with Nanos2 and Nanos3 to regulate testicular teratoma incidence. PloS one 14 32339196
2018 Nanos3 not nanos1 and nanos2 is a germ cell marker gene in large yellow croaker during embryogenesis. Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology 14 29331522
2022 Distinct Roles of NANOS1 and NANOS3 in the Cell Cycle and NANOS3-PUM1-FOXM1 Axis to Control G2/M Phase in a Human Primordial Germ Cell Model. International journal of molecular sciences 10 35743036
2021 Genetic and structural analysis of the in vivo functional redundancy between murine NANOS2 and NANOS3. Development (Cambridge, England) 10 33199444
2020 Nanos3, a cancer-germline gene, promotes cell proliferation, migration, chemoresistance, and invasion of human glioblastoma. Cancer cell international 10 32508533
2019 Visualizing primordial germ cell migration in embryos of rice field eel (Monopterus albus) using fluorescent protein tagged 3' untranslated regions of nanos3, dead end and vasa. Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology 9 31176867
2023 Germline ablation achieved via CRISPR/Cas9 targeting of NANOS3 in bovine zygotes. Frontiers in genome editing 7 38089499
2020 Expression pattern and potential role of Nanos3 in regulating testosterone biosynthesis in Leydig cells of sheep. Theriogenology 6 32474303
2020 RNA-binding protein Ptbp1 regulates alternative splicing and transcriptome in spermatogonia and maintains spermatogenesis in concert with Nanos3. The Journal of reproduction and development 6 32624547
2016 Mutation analysis of NANOS3 in Brazilian women with primary ovarian failure. Clinics (Sao Paulo, Brazil) 6 28076512
2012 Ol4E-T, a eukaryotic translation initiation factor 4E-binding protein of medaka fish (Oryzias latipes), can interact with nanos3 and vasa in vitro. Journal of experimental zoology. Part B, Molecular and developmental evolution 6 22951962
2025 RNA-binding proteins DND1 and NANOS3 cooperatively suppress the entry of germ cell lineage. Nature communications 5 40410171
2022 Generation of germ cell-deficient pigs by NANOS3 knockout. The Journal of reproduction and development 5 36273893
2019 Visualization of Turbot (Scophthalmus maximus) Primordial Germ Cells in vivo Using Fluorescent Protein Mediated by the 3' Untranslated Region of nanos3 or vasa Gene. Marine biotechnology (New York, N.Y.) 5 31502176
2016 Conserved elements in the nanos3 3'UTR of olive flounder are responsible for the selective retention of RNA in germ cells. Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology 4 27085583
2013 Nanos3 gene targeting in medaka ES cells. International journal of biological sciences 4 23678294
2022 NANOS3 suppresses premature spermatogonial differentiation to expand progenitors and fine-tunes spermatogenesis in mice. Biology open 3 35394008
2018 Nanos3 of the frog Rana rugosa: Molecular cloning and characterization. Development, growth & differentiation 3 29405266
2025 Generation of primordial germ cell-like cells by two germ plasm components, dnd1 and nanos3, in medaka (Oryzias latipes). iScience 2 40060892
2025 The DND1-NANOS3 complex shapes the primordial germ cell transcriptome via a heptanucleotide sequence in mRNA 3' UTRs. bioRxiv : the preprint server for biology 2 41040373
2021 NANOS3 downregulation in Down syndrome hiPSCs during primordial germ cell-like cell differentiation. Histochemistry and cell biology 2 34652540
2023 Generation of NANOS3-mCherry reporter human embryonic stem cell line SYSUe-009-A using CRISPR/Cas9. Stem cell research 1 36630838
2022 Zygotic nanos3 Mutant Medaka (Oryzias latipes) Displays Gradual Loss of Germ Cells and Precocious Spermatogenesis During Gonadal Development. Zoological science 1 35699932
2019 A new mouse model to study the role of ectopic Nanos3 expression in cancer. BMC cancer 1 31208373
2026 A Nanos3-containing protein complex can activate RNA translation in primordial germ cells in vivo. EMBO reports 0 42026270
2021 Gene Alterations and Expression Spectrum of NANOS3 in Nonobstructive Azoospermia. Reproductive sciences (Thousand Oaks, Calif.) 0 34417763

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