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Showing SSNA1NA14 is a alias.

SSNA1

Microtubule nucleation factor SSNA1 · UniProt O43805

Length
119 aa
Mass
13.6 kDa
Annotated
2026-06-10
52 papers in source corpus 13 papers cited in narrative 14 extracted findings
Cross-family judge vs UniProt: Affinage preferred faithfulness: 5/6 claims corpus-supported (83%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

SSNA1 (NA14/DIP13) is a small coiled-coil protein that self-assembles into fibrillar higher-order structures and functions at microtubule-based and centriolar structures to support cell division and ciliogenesis (PMID:22008182, PMID:25390646, PMID:39803484, PMID:40804232). The protein forms a predominantly coiled-coil fold in which a central self-association region drives oligomerization, and structural work establishes an anti-parallel coiled-coil whose C-terminal residue overhangs dock onto adjacent molecules to form triple-stranded helical junctions; this self-assembly creates the hubs required for effective microtubule interaction, and impairing self-assembly phenocopies loss of the gene (PMID:22008182, PMID:39803484, PMID:40804232). In reconstituted systems SSNA1 binds cooperatively along the microtubule lattice and growing ends and modulates all parameters of dynamic instability—slowing growth, shrinkage, and catastrophe while promoting rescue—and it becomes enriched at microtubule damage sites where it protects against spastin-mediated severing, increases lattice rigidity, and blocks incorporation of new tubulin to reinforce mechanical strength rather than promote repair (PMID:34970964, PMID:41648615). At centrioles SSNA1 occupies a distal luminal ring in a 9-fold symmetric configuration as part of a C2CD3/SAS-1–dependent luminal network, is recruited there upstream by SAS-1/C2CD3 within a C2CD3–SSNA1–LRRCC1 targeting hierarchy, and promotes cilia assembly by facilitating CP110 removal (PMID:41124206). SSNA1 acts as an adaptor for the microtubule-severing AAA-ATPase spastin at the centrosome, and its loss impairs cell division, producing cytokinesis defects and multipolar spindles (PMID:15269182, PMID:25390646, PMID:39803484, PMID:40804232). Across diverse eukaryotes, orthologs localize to basal bodies, flagella, conoid, and cytoplasmic microtubules and their disruption perturbs cell division, indicating a conserved role at microtubule-organizing structures (PMID:12640030, PMID:22363749, PMID:27324377).

Mechanistic history

Synthesis pass · year-by-year structured walk · 12 steps
  1. 1998 Medium

    Established SSNA1/NA14 as a discrete small protein with a coiled-coil-forming architecture, defining the structural basis for all later self-assembly work.

    Evidence cDNA cloning from autoimmune serum, immunoprecipitation, and immunofluorescence of tagged protein in HeLa and 3T3 cells

    PMID:9430706

    Open questions at the time
    • Punctate nuclear localization of tagged protein was later contradicted by KO-validated imaging
    • No microtubule or centriole link yet established
  2. 2003 Medium

    Connected the protein to microtubule-organizing structures and cell division by showing the Chlamydomonas ortholog at basal bodies, axonemes, and microtubules with division defects on knockdown.

    Evidence Antibody immunolocalization, cross-species staining of human cells, and antisense suppression in Chlamydomonas

    PMID:12640030

    Open questions at the time
    • Antisense phenotype not mechanistically dissected
    • Direct microtubule binding not tested biochemically
  3. 2004 Medium

    Identified SSNA1 as a centrosomal adaptor that physically engages the severing enzyme spastin, framing its functional partnership with microtubule remodeling machinery.

    Evidence Co-immunoprecipitation, gamma-tubulin co-fractionation, and deletion-mutant binding analysis

    PMID:15269182

    Open questions at the time
    • Adaptor model inferred from binding/fractionation, not direct recruitment assay
    • Functional consequence of spastin targeting not measured here
  4. 2008 Medium

    Reported a separable microtubule-independent function—binding and plasma-membrane transport of the orphan receptor TPRA40/GPR175—via an N-terminal-deletion mutant that uncouples receptor binding from microtubule binding.

    Evidence Yeast two-hybrid, GST pull-down, co-IP, and translocation assays in HeLa cells and mouse embryos

    PMID:18459117

    Open questions at the time
    • TPRA40 transport role not corroborated by later structural/centriolar studies
    • Single-lab finding without independent replication
  5. 2011 Medium

    Defined the biophysical basis of self-association, mapping the parallel coiled-coil self-association region and candidate residues for spastin/microtubule contacts.

    Evidence CD spectroscopy, NMR, denaturation studies, and site-directed mutagenesis

    PMID:22008182

    Open questions at the time
    • Leu83/Leu93 contribution to spastin/microtubule binding hypothesized but not proven
    • Coiled-coil orientation later revised to anti-parallel
  6. 2012 Medium

    Demonstrated that self-assembly into fibrils is an intrinsic, conserved property of the protein family, here for the T. brucei ortholog co-localizing with acetylated tubulin.

    Evidence In vitro and in vivo self-assembly assays, immunofluorescence, and gene deletion in T. brucei

    PMID:22363749

    Open questions at the time
    • Deletion produced little phenotype, leaving functional role unresolved in this organism
    • Direct microtubule binding not biochemically tested
  7. 2014 Medium

    Localized SSNA1 to centrioles in human cells and neurons and linked its loss to cytokinesis failure while overexpression drives axon outgrowth, establishing cell-type-spanning division/morphogenesis roles.

    Evidence Endogenous immunofluorescence, stable shRNA knockdown, and neuronal overexpression with quantified phenotypes

    PMID:25390646

    Open questions at the time
    • Cytokinesis-essential role later disputed by KO-validated study
    • Mechanism linking centriole localization to neuronal outgrowth unresolved
  8. 2016 Medium

    Extended conserved self-assembly and division-modulating function to the Toxoplasma conoid/basal complex, reinforcing a pan-eukaryotic role at apical microtubule-organizing structures.

    Evidence Fluorescence localization, in vitro/in vivo self-assembly, overexpression, and conditional disruption in T. gondii

    PMID:27324377

    Open questions at the time
    • Protein dispensable for in vitro growth, leaving essential function unclear
    • No structural mechanism for self-association defined here
  9. 2021 High

    Provided definitive in vitro evidence that SSNA1 directly regulates microtubule dynamic instability and protects against spastin severing, resolving its biochemical activity on microtubules.

    Evidence In vitro reconstitution with purified proteins, TIRF microscopy, and severing assays

    PMID:34970964

    Open questions at the time
    • In vitro lattice binding later contested by KO-validated co-pelleting assays in another study
    • Cellular contribution of damage-site enrichment not yet quantified
  10. 2024 High

    Solved the self-assembly architecture by cryo-EM, showing C-terminal overhangs form triple-stranded helical junctions that house the microtubule-binding region, mechanistically coupling self-assembly to function in vivo.

    Evidence Cryo-EM structure (4.55 Å) with C. elegans knockout and self-assembly-deficient mutants scored for viability and spindle phenotypes

    PMID:39803484 PMID:40804232

    Open questions at the time
    • Resolution limits atomic detail of the junction
    • How self-assembly hubs engage centriolar versus cytoplasmic microtubules not separated
  11. 2025 High

    Placed SSNA1 in a defined centriolar targeting hierarchy and luminal ring, showing SAS-1/C2CD3 recruits it upstream of LRRCC1 and that it promotes ciliogenesis via CP110 removal, while challenging earlier microtubule-binding and nuclear/cytokinesis claims.

    Evidence Super-resolution/expansion microscopy, cryo-ET, null-allele epistasis in C. elegans, heterologous recruitment assays, and KO-validated antibody/co-pelleting assays

    PMID:41124206

    Open questions at the time
    • Direct in vitro microtubule binding remains contested between datasets (preprint co-pelleting vs reconstitution)
    • Molecular mechanism by which SSNA1 drives CP110 removal undefined
  12. 2026 Medium

    Refined the microtubule-protection mechanism, showing SSNA1 mechanically reinforces lattices and blocks tubulin re-incorporation at damage sites rather than promoting self-repair.

    Evidence In vitro reconstitution with TIRF, kinesin-gliding, microfluidic-flow mechanics, and damage-site tubulin incorporation assays (preprint)

    PMID:41648615

    Open questions at the time
    • Preprint, single lab
    • In vivo relevance of mechanical reinforcement not established

Open questions

Synthesis pass · forward-looking unresolved questions
  • Whether SSNA1's in vitro microtubule lattice binding and dynamics regulation reflect its principal in-cell function, or whether its dominant cellular role is as a centriolar distal-luminal ring component recruited by C2CD3, remains unresolved.
  • No single study reconciles microtubule-binding and luminal-ring models
  • Substrate/mechanism of CP110 removal unknown
  • Spastin-adaptor role not retested with KO-validated reagents

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0005198 structural molecule activity 2 GO:0008092 cytoskeletal protein binding 2 GO:0060090 molecular adaptor activity 2
Localization
GO:0005815 microtubule organizing center 3 GO:0005856 cytoskeleton 3 GO:0005929 cilium 2
Pathway
R-HSA-1640170 Cell Cycle 2 R-HSA-1852241 Organelle biogenesis and maintenance 2
Complex memberships
centriole distal luminal ring (C2CD3/SFI1/centrin-2/CEP135/NA14)

Evidence

Reading pass · 14 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
1998 NA14 (SSNA1) is a novel 14-kDa protein with an N-terminal acidic domain containing heptad repeats characteristic of alpha-helices forming dimeric coiled-coil structures, and an alkaline C-terminal domain. It localizes to numerous punctate nuclear structures in HeLa and 3T3 cells as determined by immunofluorescence of transiently transfected tagged protein. cDNA library screening with autoimmune serum, immunoprecipitation from cell lysates, recombinant protein antibody generation, confocal immunofluorescence microscopy of tagged transfected protein The Journal of biological chemistry Medium 9430706
2003 DIP13 (Chlamydomonas ortholog of human NA14/SSNA1) localizes to basal bodies, flagellar axonemes, and cytoplasmic microtubules. Anti-DIP13 antibody cross-reacted with human NA14 and stained basal bodies/flagella of human sperm cells and centrosomes of HeLa cells. Antisense suppression of DIP13 in Chlamydomonas produced multinucleate, multiflagellate cells, implicating a role in proper cell division. Specific antibody immunolocalization, cross-species immunofluorescence, antisense knockdown with cellular phenotype readout Journal of cell science Medium 12640030
2004 Spastin (SPG4) physically interacts with the centrosomal protein NA14 (SSNA1). Spastin co-fractionates with gamma-tubulin (a centrosomal marker). Deletion of the spastin region required for binding to NA14 disrupts spastin's interaction with microtubules, suggesting NA14 acts as an adaptor to target spastin activity at the centrosome. Co-immunoprecipitation, subcellular fractionation with gamma-tubulin marker, deletion mutant analysis of binding region and microtubule interaction Human molecular genetics Medium 15269182
2008 NA14 (SSNA1) binds to the C-terminal region of the orphan receptor TPRA40/GPR175, as confirmed by GST pull-down and co-immunoprecipitation. NA14 mediates the transport of TPRA40 from cytosol to the plasma membrane; an N-terminal deletion mutant of NA14 (GFP-NA14ΔN) that cannot bind microtubules but retains TPRA40 binding inhibited TPRA40 membrane translocation. This functional membrane transport of TPRA40 by NA14 regulates cell division of early mouse embryos. Yeast two-hybrid screening, GST pull-down, co-immunoprecipitation, fluorescence microscopy of FLAG-tagged TPRA40 translocation, GFP-NA14 deletion mutant expression in HeLa cells and mouse embryos Journal of cellular physiology Medium 18459117
2011 Human NA14 (SSNA1) forms a highly helical, predominantly coiled-coil structure with its N- and C-termini (residues 1-13 and 105-119) lacking preferred structure. Residues 14-104 participate in NA14 self-association via a parallel coiled-coil. The protein is insoluble and forms fibrils/oligomers. Leu83 and Leu93 are hypothesized (but not fully proven) to mediate interactions with spastin and microtubules. Two conserved Tyr residues may stabilize the structure via Glu-COO⁻ |||HO-Tyr H-bonds. CD spectroscopy, NMR (of quintuple mutant and wild-type in detergent micelles), urea and thermal denaturation, site-directed mutagenesis of Cys and Leu residues Protein engineering, design & selection : PEDS Medium 22008182
2012 The T. brucei orthologue of SSNA1 (TbDIP13) self-assembles into fibril-like structures both in vitro and in vivo, and partially co-localizes with acetylated α-tubulin in procyclic-stage parasites. Deletion of TbDIP13 in bloodstream and procyclic stages had little effect on growth or morphology, indicating functional redundancy or a role in an alternative life-cycle stage. Comparative proteomics for interacting partners, in vitro and in vivo self-assembly assays, immunofluorescence co-localization with acetylated α-tubulin, gene deletion PloS one Medium 22363749
2014 NA14 (SSNA1) localizes specifically to centrioles in HeLa cells and rat cortical neurons. Stable NA14 knockdown dramatically impairs cell division, particularly cytokinesis. Overexpression of NA14 in neurons significantly increases axon outgrowth and branching and enhances neuronal differentiation. NA14 is proposed to act as an adaptor regulating spastin localization to centrosomes. Immunofluorescence of endogenous proteins, stable shRNA knockdown with cytokinesis phenotype readout, neuronal overexpression with axon outgrowth and branching quantification PloS one Medium 25390646
2016 An SSNA1/DIP13 homologue in Toxoplasma gondii localizes to the conoid (apical complex) in mature and dividing cells and to the basal complex in elongating daughter cells during division. The protein self-associates into higher-order structures both in vitro and in vivo; overexpression impairs parasite division. The protein is dispensable for in vitro parasite growth. Fluorescence microscopy localization, in vitro and in vivo self-assembly assays, overexpression with division phenotype readout, conditional gene disruption Scientific reports Medium 27324377
2021 SSNA1 directly modulates all parameters of microtubule dynamic instability in vitro: it slows rates of growth, shrinkage, and catastrophe, and promotes rescue. SSNA1 forms stretches along growing microtubule ends and binds cooperatively to the microtubule lattice. SSNA1 is enriched at microtubule damage sites (both naturally occurring and induced by the severing enzyme spastin), and its binding protects microtubules against spastin-mediated severing. In vitro reconstitution with purified proteins, TIRF microscopy, quantitative analysis of dynamic instability parameters, microtubule severing assays with spastin eLife High 34970964
2024 SSNA1 (C. elegans SSNA-1) forms an anti-parallel coiled-coil whose self-assembly is facilitated by 16 C-terminal residue overhangs that dock on the adjacent coiled-coil to form a triple-stranded helical junction. The microtubule-binding region resides within this triple-stranded junction, indicating that self-assembly creates hubs for effective microtubule interaction. SSNA-1 deletion in C. elegans reduces embryonic viability and causes multipolar spindles during cell division; impairing self-assembly has a comparable effect on viability as knockout. Cryo-EM structure determination (4.55 Å resolution), C. elegans genetic knockout and self-assembly-deficient mutants with embryonic viability and spindle phenotype readouts bioRxiv (preprint); subsequently published in Nature Communications (2025) High 39803484 40804232
2025 SAS-1 (C2CD3 homologue) is essential for SSNA-1 localization to centrioles during oogenesis and to the transition zone during ciliogenesis in C. elegans. SSNA-1 localizes next to the SAS-1 C-terminus in centriole architecture. In a heterologous human cell assay, SAS-1 recruits SSNA-1 to microtubules, establishing a genetic epistasis relationship where SAS-1 acts upstream of SSNA-1 for centriole/cilium localization. U-Ex-STED super-resolution imaging, null allele genetics in C. elegans, molecular epistasis experiments with null alleles of both components, heterologous human cell recruitment assay PLoS genetics High 41124206
2025 SSNA1 localizes to the distal lumen of centrioles and basal bodies in a ring-like 9-fold symmetric configuration, apart from centriolar microtubules. A C2CD3–SSNA1–LRRCC1 hierarchical targeting network operates in the distal lumen. SSNA1 promotes cilia assembly by facilitating CP110 removal. Contrary to previous reports, KO-validated antibody and microtubule co-pelleting assays show SSNA1 does not bind microtubules in vitro, and it does not reside in the nucleus, midbody, or ciliary axoneme. SSNA1 is dispensable for cell division, overall centriole organization, and duplication. KO-validated antibody immunofluorescence, super-resolution imaging with expansion microscopy (ExM), microtubule co-pelleting assays with tag-free SSNA1 and oligomerization-deficient mutants, KO analysis of ciliogenesis and CP110 removal bioRxiv (preprint)preprint Medium
2025 SSNA1 is part of a distal luminal ring network (C2CD3/SFI1/centrin-2/CEP135/NA14) in the centriole. C2CD3 depletion destabilizes this luminal ring network. SSNA1 (NA14) is identified as a component of the ~100 nm luminal ring structure at the distal centriole by U-ExM and cryo-ET structural analysis. Ultrastructure Expansion Microscopy (U-ExM), iterative U-ExM, in situ cryo-electron tomography, C2CD3 depletion and network component analysis bioRxiv (preprint)preprint Medium
2026 SSNA1 binding increases microtubule rigidity and resistance to breakage under kinesin-driven gliding and microfluidic flow forces. SSNA1 localizes to microtubule damage sites and inhibits incorporation of new tubulin dimers at those sites, thereby blocking lattice self-repair. Conversely, SSNA1 does not recognize damage sites that have been repaired by tubulin incorporation. Thus SSNA1 reinforces mechanical strength of microtubules without promoting self-repair. In vitro reconstitution with purified proteins, TIRF microscopy, kinesin-driven gliding assays, microfluidic flow assays for microtubule mechanics, tubulin incorporation assays at damage sites bioRxiv (preprint)preprint Medium 41648615

Source papers

Stage 0 corpus · 52 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2001 Murine notch homologs (N1-4) undergo presenilin-dependent proteolysis. The Journal of biological chemistry 147 11518718
2004 Spastin interacts with the centrosomal protein NA14, and is enriched in the spindle pole, the midbody and the distal axon. Human molecular genetics 108 15269182
2004 High butanol production by Clostridium saccharoperbutylacetonicum N1-4 in fed-batch culture with pH-Stat continuous butyric acid and glucose feeding method. Journal of bioscience and bioengineering 82 16233703
2014 The toll-like receptor family protein RP105/MD1 complex is involved in the immunoregulatory effect of exopolysaccharides from Lactobacillus plantarum N14. Molecular immunology 63 25466614
2017 Genome Editing in Clostridium saccharoperbutylacetonicum N1-4 with the CRISPR-Cas9 System. Applied and environmental microbiology 51 28258147
2003 Chlamydomonas DIP13 and human NA14: a new class of proteins associated with microtubule structures is involved in cell division. Journal of cell science 51 12640030
2007 Characterization of the sol operon in butanol-hyperproducing Clostridium saccharoperbutylacetonicum strain N1-4 and its degeneration mechanism. Bioscience, biotechnology, and biochemistry 37 17213660
2008 Metabolic engineering for solvent productivity by downregulation of the hydrogenase gene cluster hupCBA in Clostridium saccharoperbutylacetonicum strain N1-4. Applied microbiology and biotechnology 35 18188555
1999 Extractive acetone-butanol-ethanol fermentation using methylated crude palm oil as extractant in batch culture of Clostridium saccharoperbutylacetonicum N1-4 (ATCC 13564). Journal of bioscience and bioengineering 35 16232480
1990 Effect of N1,N14-bis(ethyl)homospermine on the growth of U-87 MG and SF-126 human brain tumor cells. Cancer research 31 2334909
1998 NA14 is a novel nuclear autoantigen with a coiled-coil domain. The Journal of biological chemistry 30 9430706
2019 Inhibitory Effect of Volatiles Emitted From Alcaligenes faecalis N1-4 on Aspergillus flavus and Aflatoxins in Storage. Frontiers in microbiology 27 31293550
2018 Enhancement of sucrose metabolism in Clostridium saccharoperbutylacetonicum N1-4 through metabolic engineering for improved acetone-butanol-ethanol (ABE) fermentation. Bioresource technology 26 30245312
2016 An evolutionarily conserved SSNA1/DIP13 homologue is a component of both basal and apical complexes of Toxoplasma gondii. Scientific reports 25 27324377
1991 Effect on N1,N14-bis-(ethyl)-homospermine (BE-4-4-4) on the growth of U-251 MG and SF-188 human brain tumor cells. International journal of cancer 25 1860734
2014 Spastin-interacting protein NA14/SSNA1 functions in cytokinesis and axon development. PloS one 24 25390646
2021 SSNA1 stabilizes dynamic microtubules and detects microtubule damage. eLife 23 34970964
2017 Enhancement of solvent production by overexpressing key genes of the acetone-butanol-ethanol fermentation pathway in Clostridium saccharoperbutylacetonicum N1-4. Bioresource technology 17 28898840
2016 Development of a High-Efficiency Transformation Method and Implementation of Rational Metabolic Engineering for the Industrial Butanol Hyperproducer Clostridium saccharoperbutylacetonicum Strain N1-4. Applied and environmental microbiology 17 27836845
2009 Autoantibody to NA14 is an independent marker primarily for Sjogren's syndrome. Frontiers in bioscience (Landmark edition) 17 19273306
2013 Genome Sequence of the Butanol Hyperproducer Clostridium saccharoperbutylacetonicum N1-4. Genome announcements 16 23516201
2008 TPRA40/GPR175 regulates early mouse embryogenesis through functional membrane transport by Sjögren's syndrome-associated protein NA14. Journal of cellular physiology 15 18459117
2012 The orthologue of Sjögren's syndrome nuclear autoantigen 1 (SSNA1) in Trypanosoma brucei is an immunogenic self-assembling molecule. PloS one 13 22363749
1998 Genetic analysis of extended life span in Drosophila melanogaster. II. Replication of the backcross test and molecular characterization of the N14 locus. Genetica 13 9949700
2023 Production of acetone, butanol, and ethanol by electro-fermentation with Clostridium saccharoperbutylacetonicum N1-4. Bioelectrochemistry (Amsterdam, Netherlands) 12 36940584
2011 Characterization of the structure and self-recognition of the human centrosomal protein NA14: implications for stability and function. Protein engineering, design & selection : PEDS 11 22008182
2020 Investigation of secondary metabolism in the industrial butanol hyper-producer Clostridium saccharoperbutylacetonicum N1-4. Journal of industrial microbiology & biotechnology 9 32103460
2022 Design, Synthesis, and Biological Evaluation of N14-Amino Acid-Substituted Tetrandrine Derivatives as Potential Antitumor Agents against Human Colorectal Cancer. Molecules (Basel, Switzerland) 8 35807286
2016 A re-evaluation of anti-NA-14 antibodies in patients with primary Sjögren's syndrome: Significant role of interferon-γ in the production of autoantibodies against NA-14. Autoimmunity 8 27328271
2013 A novel process for direct production of acetone-butanol-ethanol from native starches using granular starch hydrolyzing enzyme by Clostridium saccharoperbutylacetonicum N1-4. Applied biochemistry and biotechnology 7 24272773
2012 Decreased hydrogen production leads to selective butanol production in co-cultures of Clostridium thermocellum and Clostridium saccharoperbutylacetonicum strain N1-4. Journal of bioscience and bioengineering 7 22999358
2021 Effect of Dietary Supplementation of Immunobiotic Lactiplantibacillusplantarum N14 Fermented Rakkyo (Allium chinense) Pickled Juice on the Immunocompetence and Production Performance of Pigs. Animals : an open access journal from MDPI 6 33803393
2017 HM2-phage resistant solventogenic Clostridium saccharoperbutylacetonicum N1-4 shows increased exopolysaccharide production. FEMS microbiology letters 6 28961718
2024 Structural insights into SSNA1 self-assembly and its microtubule binding for centriole maintenance. bioRxiv : the preprint server for biology 5 39803484
2023 SSNA1 Promotes Hepatocellular Carcinoma Metastasis Via STAT3/EMT Induction. Anticancer research 5 37500134
2021 Identification and Investigation of Autolysin Genes in Clostridium saccharoperbutylacetonicum Strain N1-4 for Enhanced Biobutanol Production. Applied and environmental microbiology 5 33514516
2020 Genome sequence analysis of the temperate bacteriophage TBP2 of the solvent producer Clostridium saccharoperbutylacetonicum N1-4 (HMT, ATCC 27021). FEMS microbiology letters 5 32614389
2016 Autoantibodies against lamin C, NA14 and CK15 in primary vasculitides or autoimmune diseases with secondary vasculitis. Clinical and experimental rheumatology 5 27214601
2025 Structural insights into SSNA1 self-assembly and its microtubule binding for centriole maintenance. Nature communications 4 40804232
2025 C. elegans SAS-1 ensures centriole integrity and ciliary function, and operates with SSNA-1. PLoS genetics 4 41124206
1994 Radiopotentiation of human brain tumor cells by the spermine analog N1,N14-bis(ethyl)homospermine. International journal of radiation oncology, biology, physics 4 8083073
2025 Discovery of a Novel Antimicrobial Peptide from Paenibacillus sp. Na14 with Potent Activity Against Gram-Negative Bacteria and Genomic Insights into Its Biosynthetic Pathway. Antibiotics (Basel, Switzerland) 3 40867999
2022 Polycationic Surfaces Promote Whole-Cell Immobilization and Induce Microgranulation of Clostridium saccharoperbutylacetonicum N1-4 for Enhanced Biobutanol Production. ACS applied materials & interfaces 3 36282625
2017 Adenine Addition Restores Cell Viability and Butanol Production in Clostridium saccharoperbutylacetonicum N1-4 (ATCC 13564) Cultivated at 37°C. Applied and environmental microbiology 3 28130303
2023 Effect of spo0A, sigE, sigG, and sigK disruption on butanol production and spore formation in Clostridium saccharoperbutylacetonicum strain N1-4 (ATCC13564). Journal of bioscience and bioengineering 2 37487916
2000 [Cloning and infectivity analysis of the cDNAs of tobacco mosaic virus (tomato strain) and its attenuated virus(N14) genomes]. Sheng wu gong cheng xue bao = Chinese journal of biotechnology 2 10976328
1993 [Virological studies on the usefulness of anti-HCV ELISA assay using recombinant N-14 fusion protein in various liver diseases]. Fukuoka igaku zasshi = Hukuoka acta medica 1 7686126
2026 SSNA1 mechanically reinforces the damaged microtubule lattice. bioRxiv : the preprint server for biology 0 41648615
2024 Development of a novel N14-substituted antitumor evodiamine derivative with inhibiting heat shock protein 70 in non-small cell lung cancer. Scientific reports 0 39455626
1994 [Changes in C100-3, and N14 antibodies in patients with chronic hepatitis C treated with interferon]. Rinsho byori. The Japanese journal of clinical pathology 0 7511184
1994 Hepatitis C virus RNA and anti-N14 antibody levels during interferon alpha therapy for chronic hepatitis C. Internal medicine (Tokyo, Japan) 0 7530068
1992 [Clinical significance of N-14 antibody (ELISA) in diagnosis of non-A, non-B liver disease]. Fukuoka igaku zasshi = Hukuoka acta medica 0 1318860

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