Affinage

TFIP11

Tuftelin-interacting protein 11 · UniProt Q9UBB9

Length
837 aa
Mass
96.8 kDa
Annotated
2026-06-10
34 papers in source corpus 18 papers cited in narrative 18 extracted findings
Cross-family judge vs UniProt: Affinage preferred faithfulness: 6/6 claims corpus-supported (100%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

TFIP11 (human ortholog of yeast Ntr1/Spp382) is a G-patch splicing factor that governs the final, disassembly stage of the spliceosome cycle and additionally supports replication-fork stability (PMID:19103666, PMID:38925148). Through its N-terminal G-patch domain, TFIP11 directly engages and activates the DEAH-box RNA helicase DHX15/hPrp43, recruiting the otherwise diffusely distributed helicase to nuclear speckles and to the post-catalytic intron-lariat spliceosome (PMID:19165350, PMID:19103666). In the human and nematode terminal intron-lariat spliceosome, TFIP11 together with C19L1, SYF1, SYF2 and SDE2 docks onto and activates DHX15 on the catalytic U6 snRNA to detect release of ligated mRNA and trigger disassembly, debranching of the excised intron, and recycling of snRNPs (PMID:38925148, PMID:19103666). A separate, DHX15-independent function localizes TFIP11 to nucleoli and Cajal bodies, where it promotes fibrillarin/snoRNA-dependent 2'-O-methylation of U6 snRNA required for proper U4/U6.U5 tri-snRNP assembly and splicing fidelity (PMID:34789764). Beyond RNA metabolism, TFIP11 forms a complex with the BLM helicase, binds stalled-replication-fork-mimicking DNA, and is required for RAD51-mediated fork reversal and genome stability (PMID:38341452). The conserved yeast ortholog establishes the underlying disassembly machinery: Ntr1/Spp382 binds Prp43 and acts as its spliceosome-targeting factor for intron release and snRNP recycling, defining a turnover/discard pathway for defective spliceosomes (PMID:16880513, PMID:16945917, PMID:17893323).

Mechanistic history

Synthesis pass · year-by-year structured walk · 15 steps
  1. 2005 Medium

    Established that human TFIP11 is a bona fide splicing factor with dynamic, RNA-dependent subnuclear organization, rather than its originally inferred transcription-factor role.

    Evidence GFP live-cell imaging with RNase A and Pol II inhibitor treatment plus an in vivo splicing assay in human cells

    PMID:15868102

    Open questions at the time
    • Does not define the molecular step of splicing TFIP11 acts at
    • No interacting partners identified
  2. 2006 High

    Defined the core disassembly function in yeast: the ortholog Ntr1/Spp382 targets Prp43 to the post-splicing intron complex to drive intron release and snRNP recycling, and a discard pathway for defective spliceosomes.

    Evidence Metabolic depletion, in vitro splicing/snRNP analysis, co-IP, genetic suppressor screen and TAP in budding yeast

    PMID:16880513 PMID:16945917

    Open questions at the time
    • Whether human TFIP11 performs the identical step was not yet shown
    • Role of the G-patch domain not resolved
  3. 2007 High

    Resolved how the disassembly factor is delivered to the spliceosome: Ntr1 partners with Ntr2 (which contacts U5/Brr2) to recruit Prp43 dynamically, with spliceosome binding ATP-independent but disassembly requiring ATP hydrolysis.

    Evidence Co-IP, in vitro binding, ATP-hydrolysis-deficient mutants and genetic interaction analysis in yeast

    PMID:17893323

    Open questions at the time
    • Human counterpart of the Ntr1-Ntr2 module not established
    • Mechanism of helicase activation not defined
  4. 2007 Medium

    Uncovered a non-splicing role: NTR1/Ntr1 binds XRCC4/Lif1 and PinX1, occupying DNA ligase IV sites to restrain NHEJ and localizing to telomeres and nucleoli.

    Evidence Yeast two-hybrid, plasmid ligation and chromosomal DSB repair assays, subcellular localization in yeast and human cells

    PMID:17389648

    Open questions at the time
    • Physiological significance of NHEJ inhibition in human cells unclear
    • Relationship between RNA and DNA-repair functions undefined
  5. 2008 High

    Connected human TFIP11 directly to the disassembly machinery, showing it occupies the post-splicing IL complex and cooperates with hPrp43 to drive the IL-to-IS transition enabling debranching.

    Evidence Two-tag affinity purification of lariat-intron complexes, glycerol gradient sedimentation, and in vitro splicing with an interaction-domain deletion mutant

    PMID:19103666

    Open questions at the time
    • Structural basis of the TFIP11-hPrp43 interaction not resolved
    • Full IL complex composition incomplete
  6. 2008 Medium

    Localized the helicase-recruiting activity to a defined domain and identified additional speckle partners, showing the G-patch mediates DHX15 recruitment and that TFIP11 co-localizes with CCNL1 and EWSR1.

    Evidence GFP co-transfection and confocal co-localization, yeast two-hybrid, sequence homology analysis in mammalian cells

    PMID:19122807 PMID:19165350

    Open questions at the time
    • CCNL1/EWSR1 interactions shown only by co-localization, no biochemical confirmation
    • Functional consequence of these partnerships untested
  7. 2009 Medium

    Mapped the targeting determinants of TFIP11 and expanded the yeast cofactor network, defining a novel NLS and speckle-targeting sequence and implicating Cwc23/Sqs1 chaperone-helicase coordination.

    Evidence C-terminal deletion/mutagenesis with fluorescence imaging in mouse TFIP11; dosage interference, copurification and two-hybrid in yeast

    PMID:19581443 PMID:19857462

    Open questions at the time
    • Human counterparts of Sqs1/Cwc23 modulation not addressed
    • Hsp70 chaperone role inferred only genetically
  8. 2010 Medium

    Implicated an Hsp70-coupled chaperone in TFIP11-orchestrated disassembly by showing a Cwc23 mutant with reduced Ntr1 binding accumulates lariat intron and unspliced pre-mRNA.

    Evidence Genetic interaction analysis, co-IP and J-domain mutagenesis with in vivo splicing assays in yeast

    PMID:19822657

    Open questions at the time
    • J-domain mechanistic contribution remains genetic, not biochemical
    • Conservation in human disassembly untested
  9. 2013 Medium

    Extended the human post-splicing IL complex composition by identifying C2ORF3 as a functional component required for in vitro splicing.

    Evidence Reciprocal IP with TFIP11 and hPrp43, mass spectrometry, and depletion-rescue in vitro splicing in human extracts

    PMID:24304693

    Open questions at the time
    • Direct binding partner of C2ORF3 within the complex undefined
    • Structural placement not resolved
  10. 2015 Medium

    Demonstrated that the G-patch is not merely a Prp43 tether but specifies pathway-selective helicase activity, since G-patches of different cofactors are not interchangeable.

    Evidence Yeast two-hybrid, domain-swap and mutagenesis with in vivo splicing/rRNA processing assays

    PMID:25808954

    Open questions at the time
    • Molecular basis of G-patch specificity unresolved
    • Human G-patch specificity not directly tested
  11. 2017 High

    Provided structural context for disassembly by visualizing the Ntr1 C-terminal domain on Snu114 and Prp43 bound to Syf1 near the U6 3' end in the intron-lariat spliceosome.

    Evidence 3.5 Å cryo-EM of the yeast intron-lariat spliceosome

    PMID:28919079

    Open questions at the time
    • Human ILS architecture not resolved in this study
    • Dynamics of helicase activation not captured
  12. 2021 High

    Revealed a second, helicase-independent TFIP11 function in U6 snRNA modification, showing it is required for fibrillarin/snoRNA-dependent 2'-O-methylation that ensures tri-snRNP assembly and splicing fidelity.

    Evidence siRNA knockdown, snRNA methylation analysis, co-IP, tri-snRNP assembly assays and RNA-seq in human cells

    PMID:34789764

    Open questions at the time
    • Direct snoRNA/fibrillarin binding interface on TFIP11 undefined
    • How nucleolar/Cajal-body and speckle functions are partitioned unclear
  13. 2024 High

    Established the activated human disassembly machine, showing TFIP11 with C19L1, SYF1, SYF2 and SDE2 docks onto and activates DHX15 on catalytic U6 snRNA to sense ligated-mRNA release.

    Evidence Cryo-EM of human and nematode terminal ILS complexes with biochemical and genetic validation

    PMID:38925148

    Open questions at the time
    • Sequence of conformational events during activation not fully resolved
    • Regulation of disassembly timing unaddressed
  14. 2024 High

    Defined a direct genome-stability role, showing TFIP11 complexes with BLM, binds stalled-fork DNA, and is required for RAD51-mediated fork reversal and chromosomal stability.

    Evidence Co-IP, DNA-substrate binding, replication-fork and RAD51 foci assays, survival and chromosomal instability analysis with siRNA/knockout in human cells

    PMID:38341452

    Open questions at the time
    • Whether the G-patch/RNA functions are required for fork protection unknown
    • Mechanistic link to BLM regulation at the fork incomplete
  15. 2024 Medium

    Characterized the biophysical nature of the functional N-terminal region as an intrinsically disordered polyampholyte with salt-dependent structural duality affecting the G-patch.

    Evidence Disorder prediction, molecular dynamics and spectroscopy on recombinant TFIP11 N-terminal domain

    PMID:39089542

    Open questions at the time
    • Phase-separation behavior inferred, not demonstrated in cells
    • No functional mutagenesis linking disorder to activity

Open questions

Synthesis pass · forward-looking unresolved questions
  • How TFIP11's distinct activities — spliceosome disassembly, U6 methylation, and replication-fork protection — are coordinated, partitioned among subnuclear compartments, and regulated remains unresolved.
  • No unified model linking RNA and DNA functions
  • Regulation/post-translational control of compartment switching unknown
  • No disease association established in the corpus

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0003723 RNA binding 3 GO:0098772 molecular function regulator activity 3 GO:0060090 molecular adaptor activity 2 GO:0003677 DNA binding 1
Localization
GO:0005634 nucleus 2 GO:0005654 nucleoplasm 2 GO:0005730 nucleolus 2
Pathway
R-HSA-8953854 Metabolism of RNA 3 R-HSA-73894 DNA Repair 2
Partners
BLMC19L1CCNL1DHX15EWSR1SDE2SYF1SYF2
Complex memberships
Ntr1-Ntr2 (NTR) complexTFIP11-BLM complexintron lariat spliceosome (ILS)post-splicing Intron Large (IL) complex

Evidence

Reading pass · 18 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2005 TFIP11 localizes to a novel subnuclear structure termed the 'TFIP body', distinct from but proximal to SC35 nuclear speckles. This localization is RNA-dependent (TFIP body disperses after RNase A treatment), and RNA polymerase II inhibition causes enlargement and reduced number of TFIP bodies. An in vivo splicing assay demonstrated TFIP11 functions as a splicing factor. GFP-tagging and live-cell fluorescence microscopy, RNase A treatment, RNA Pol II inhibitor treatment (α-amanitin, actinomycin D), in vivo splicing assay Cellular and molecular life sciences : CMLS Medium 15868102
2008 TFIP11 (human homolog of yeast Ntr1) is present in the post-splicing Intron Large (IL) complex containing U2, U5, and U6 snRNAs. A TFIP11 mutant lacking the interaction domain with hPrp43 caused accumulation of the IL complex and reduction of Intron Small (IS) complex formation in vitro, indicating TFIP11 cooperates with hPrp43 to mediate the IL-to-IS transition, enabling debranching and intron turnover. Two-tag affinity purification of lariat intron RNA-protein complexes, glycerol gradient sedimentation, in vitro splicing assay with TFIP11 interaction-domain mutant Nucleic acids research High 19103666
2008 TFIP11 directly interacts with mDEAH9/DHX15 (the mammalian homolog of yeast Prp43). When co-expressed, TFIP11 recruits mDEAH9 to distinct nuclear speckles, whereas mDEAH9 alone shows diffuse nuclear distribution. The G-patch domain in the N-terminal region of TFIP11 is responsible for this interaction. Co-transfection of GFP-tagged proteins, confocal microscopy co-localization, sequence homology analysis International journal of molecular sciences Medium 19165350
2008 TFIP11 interacts with cyclin L1 (CCNL1) and Ewing sarcoma breakpoint region 1 protein (EWSR1), both spliceosome-related proteins, and all three co-localize to speckled nuclear domains, suggesting participation in a common RNA splicing activity. Yeast two-hybrid assay (initial identification), fluorescently-tagged protein co-expression and confocal microscopy co-localization International journal of molecular sciences Low 19122807
2009 TFIP11 contains a novel atypical nuclear localization signal (NLS) at amino acids 701-706 (VKDKFN) and a distinct speckle-targeting sequence (STS) within amino acids 711-735, identified by sequential C-terminal deletions and mutational analyses of mouse TFIP11. Sequential C-terminal deletions and site-directed mutagenesis of GFP-tagged TFIP11, fluorescence microscopy Biochemical and biophysical research communications Medium 19857462
2007 Yeast Ntr1/Spp382 (ortholog of human TFIP11) and Ntr2 form a stable complex that recruits the DExD/H-box helicase Prp43 dynamically to the spliceosome to catalyze disassembly. Ntr1-Ntr2 can bind the spliceosome prior to Prp43 recruitment; spliceosome binding does not require ATP but disassembly requires ATP hydrolysis. Ntr2 interacts with U5 component Brr2 and is essential for NTR-U5 and NTR-spliceosome interactions. Co-immunoprecipitation, in vitro binding assays, ATP hydrolysis-deficient mutants, genetic interaction analysis, metabolic depletion Molecular and cellular biology High 17893323
2006 Yeast Ntr1/Spp382 (ortholog of TFIP11) associates with a post-splicing complex containing the excised intron and U2, U5, U6 snRNAs. Depletion of Ntr1 reduces splicing activity, causes intron accumulation, decreases free U5 and U6 snRNPs, and disrupts Prp43 association with the excised intron. Ntr1 acts as a spliceosome receptor/RNA-targeting factor for Prp43 to promote intron release and snRNP recycling. Metabolic depletion of Ntr1, in vitro splicing assays, snRNA/snRNP analysis, co-immunoprecipitation Molecular and cellular biology High 16880513
2006 Yeast Spp382/Ntr1 (ortholog of TFIP11) is required for cellular splicing and intron turnover. Weak spp382 alleles suppress splicing defects caused by mutations in Prp38 and Prp8, defining a Spp382-dependent turnover/discard pathway for defective spliceosomes. Spp382 binds Prp43, and Prp43 requires Spp382 for intron release. Spp382 also interacts with the DnaJ-like protein Cwc23. Defective splicing complexes lacking the 5' exon cleavage intermediate are recovered with tagged Spp382. Genetic suppressor screen, tandem affinity purification, two-hybrid assay, proteomic analysis, in vivo splicing assays Proceedings of the National Academy of Sciences of the United States of America High 16945917
2007 Human TFIP11 (NTR1) and its yeast ortholog Ntr1/Spp382 interact with the DNA ligase IV-associated proteins XRCC4 (human) and Lif1p (yeast), occupying the DNA ligase IV-binding sites and thereby preventing formation of an active NHEJ ligation complex. Excess Ntr1p in yeast reduces NHEJ efficiency in plasmid ligation and chromosomal DSB repair assays. Both yeast and human NTR1 also interact with the G-patch protein PinX1. TFIP11/Ntr1 localizes to telomeres and nucleoli. Yeast two-hybrid assay, plasmid ligation assay, chromosomal DSB repair assay, subcellular localization (yeast and human cells) Nucleic acids research Medium 17389648
2009 Yeast Spp382/Ntr1 interacts with multiple splicing factors (Prp8, Prp9, Prp11, Prp39, Yhc1) and with Sqs1 and Cwc23. Sqs1 copurifies with Prp43, binds both Prp43 and Spp382, and overexpression of Sqs1 blocks pre-mRNA splicing; increased Prp43 levels buffer Sqs1 cytotoxicity, identifying Prp43 as a target of Sqs1. CWC23 activity is critical for splicing and intron metabolism but the DnaJ motif is dispensable, though genetic interactions between the CWC23 J domain and Ntr1/Prp43 suggest an auxiliary Hsp70 chaperone role in disassembly. Dosage interference assay, copurification, yeast two-hybrid, overexpression epistasis, in vivo splicing assays Genetics Medium 19581443
2013 C2ORF3 was identified as a novel component of the post-splicing IL (Intron Large) complex via immunoprecipitation with hPrp43 and TFIP11 followed by mass spectrometry. Depletion of C2ORF3 from nuclear extracts significantly represses pre-mRNA splicing in vitro, suggesting its role in intron turnover. Immunoprecipitation with TFIP11 and hPrp43, mass spectrometry, in vitro splicing with C2ORF3-depleted nuclear extract Genes to cells : devoted to molecular & cellular mechanisms Medium 24304693
2017 Cryo-EM structure of the yeast intron lariat spliceosome (ILS) at 3.5 Å resolution shows the C-terminal domain of Ntr1/Spp382 (yeast ortholog of TFIP11) associates with the GTPase Snu114, while Ntr2 is anchored to Prp8 and interacts with the superhelical domain of Ntr1. The DEAH helicase Prp43 binds Syf1 at the spliceosome periphery with its RNA-binding site close to the 3' end of U6 snRNA, providing structural basis for ILS disassembly. Cryo-electron microscopy structure determination at 3.5 Å resolution Cell High 28919079
2021 TFIP11 localizes to nucleoli and Cajal Bodies and is essential for 2'-O-methylation of U6 snRNA. TFIP11 knockdown reduces association of U6 snRNA with fibrillarin and associated snoRNAs, thereby impairing U6 2'-O-methylation. U6 hypomethylation impairs U4/U6.U5 tri-snRNP assembly, leading to spliceosome assembly defects and altered splicing fidelity. This function of TFIP11 is independent of DHX15. siRNA knockdown, snRNA methylation analysis, co-immunoprecipitation (U6 with fibrillarin/snoRNAs), tri-snRNP assembly assay, RNA-seq splicing analysis, fluorescence microscopy Nature communications High 34789764
2024 Cryo-EM structures of nematode and human terminal intron lariat spliceosomes reveal that TFIP11 and C19L1, together with SYF1, SYF2, and SDE2, dock onto and activate DHX15 on the catalytic U6 snRNA to initiate spliceosome disassembly. TFIP11 and C19L1 probe inner and outer spliceosome surfaces to detect the release of ligated mRNA. U6 snRNA thus controls both the start and end of pre-mRNA splicing. Cryo-electron microscopy structure determination of nematode and human terminal ILS complexes, biochemical and genetic validation Nature High 38925148
2024 TFIP11 forms a complex with the BLM helicase and preferentially binds DNA substrates mimicking stalled replication fork structures. Loss of TFIP11 causes abnormal accumulation of BLM at stalled forks, impairs RAD51-mediated fork reversal and fork slowing, sensitizes cells to replication stress-inducing agents, and enhances chromosomal instability. Co-immunoprecipitation, DNA substrate binding assays, replication fork assays, RAD51 foci analysis, cell survival assays, chromosomal instability analysis, siRNA/genetic knockout Nature communications High 38341452
2024 The N-terminal region of TFIP11 is an intrinsically disordered polyampholytic protein that exhibits structural duality with coexisting ordered and disordered assemblies in a salt-dependent manner. Increasing ionic strength enhances conformational flexibility, promoting a more globule-like shape that may favor liquid-liquid phase separation and protein-RNA interaction. The G-patch domain, essential for TFIP11 function, is among the most conformationally impacted regions. Disorder prediction, molecular dynamics simulation, spectroscopy (CD, NMR-type methods implied), recombinant protein characterization International journal of biological macromolecules Medium 39089542
2010 A partial loss-of-function CWC23 mutant shows reduced interaction with Ntr1/Spp382 (yeast ortholog of TFIP11) and causes accumulation of excised lariat intron and unspliced pre-mRNA, implicating Cwc23 in the spliceosome disassembly pathway coordinated by Ntr1. Genetic interactions between the CWC23 J domain and Ntr1 or Prp43 suggest an auxiliary Hsp70-based chaperone role. Genetic interaction analysis, co-immunoprecipitation (Cwc23-Ntr1), in vivo splicing assays, site-directed mutagenesis of J domain Molecular and cellular biology Medium 19822657
2015 The G-patch domain of Spp382/Ntr1 (yeast ortholog of TFIP11) is required for Spp382 function and differs from the G-patches of Sqs1 and Pxr1 in Prp43 two-hybrid response and ability to reconstitute RNA processing factors. G-patch domains are not freely interchangeable between Prp43 cofactors, suggesting G-patch identity specifies pathway-selective DExD/H-box helicase activity beyond simply tethering Prp43. Yeast two-hybrid, domain-swap experiments, site-directed mutagenesis, in vivo splicing/rRNA processing assays Genetics Medium 25808954

Source papers

Stage 0 corpus · 34 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2013 Genes expressed in dental enamel development are associated with molar-incisor hypomineralization. Archives of oral biology 121 23790503
2017 Structure of an Intron Lariat Spliceosome from Saccharomyces cerevisiae. Cell 82 28919079
2008 Isolation and characterization of post-splicing lariat-intron complexes. Nucleic acids research 81 19103666
2018 A novel role in skeletal segment regeneration of extracellular vesicles released from periodontal-ligament stem cells. International journal of nanomedicine 78 29988728
2007 Dynamic interactions of Ntr1-Ntr2 with Prp43 and with U5 govern the recruitment of Prp43 to mediate spliceosome disassembly. Molecular and cellular biology 69 17893323
2006 Yeast ntr1/spp382 mediates prp43 function in postspliceosomes. Molecular and cellular biology 58 16880513
2006 Inhibition of a spliceosome turnover pathway suppresses splicing defects. Proceedings of the National Academy of Sciences of the United States of America 56 16945917
2010 Cwc23, an essential J protein critical for pre-mRNA splicing with a dispensable J domain. Molecular and cellular biology 38 19822657
2014 Effects of enamel matrix genes on dental caries are moderated by fluoride exposures. Human genetics 30 25373699
2005 Structural organization and cellular localization of tuftelin-interacting protein 11 (TFIP11). Cellular and molecular life sciences : CMLS 28 15868102
2019 De novo single-nucleotide and copy number variation in discordant monozygotic twins reveals disease-related genes. European journal of human genetics : EJHG 26 30886340
2008 TFIP11 interacts with mDEAH9, an RNA helicase involved in spliceosome disassembly. International journal of molecular sciences 26 19165350
2017 Polymorphisms in Nonamelogenin Enamel Matrix Genes Are Associated with Dental Fluorosis. Caries research 25 29207377
2009 Spp382p interacts with multiple yeast splicing factors, including possible regulators of Prp43 DExD/H-Box protein function. Genetics 23 19581443
2009 Identification of a novel nuclear localization signal and speckle-targeting sequence of tuftelin-interacting protein 11, a splicing factor involved in spliceosome disassembly. Biochemical and biophysical research communications 23 19857462
2016 Genetic variation may explain why females are less susceptible to dental erosion. European journal of oral sciences 22 27666331
2021 DHX15-independent roles for TFIP11 in U6 snRNA modification, U4/U6.U5 tri-snRNP assembly and pre-mRNA splicing fidelity. Nature communications 20 34789764
2013 Identification of a novel component C2ORF3 in the lariat-intron complex: lack of C2ORF3 interferes with pre-mRNA splicing via intron turnover pathway. Genes to cells : devoted to molecular & cellular mechanisms 19 24304693
2020 Genes in the pathway of tooth mineral tissues and dental caries risk: a systematic review and meta-analysis. Clinical oral investigations 18 32945961
2024 Mechanism for the initiation of spliceosome disassembly. Nature 17 38925148
2007 Conserved interactions of the splicing factor Ntr1/Spp382 with proteins involved in DNA double-strand break repair and telomere metabolism. Nucleic acids research 17 17389648
2019 Dental caries: Genetic and protein interactions. Archives of oral biology 16 31476523
2015 Limited portability of G-patch domains in regulators of the Prp43 RNA helicase required for pre-mRNA splicing and ribosomal RNA maturation in Saccharomyces cerevisiae. Genetics 14 25808954
2008 TFIP11, CCNL1 and EWSR1 Protein-protein Interactions, and Their Nuclear Localization. International journal of molecular sciences 11 19122807
2024 TFIP11 promotes replication fork reversal to preserve genome stability. Nature communications 8 38341452
2022 Polymorphisms in genes expressed during amelogenesis and their association with dental caries: a case-control study. Clinical oral investigations 8 36422720
2006 Using the yeast two-hybrid assay to discover protein partners for the leucine-rich amelogenin peptide and for tuftelin-interacting protein 11. European journal of oral sciences 8 16674698
2017 Variation in Enamel Formation Genes Influences Enamel Demineralization In Vitro in a Streptococcus mutans Biofilm Model. Frontiers in physiology 7 29163197
2023 Impact of tooth mineral tissues genes on dental caries: A birth-cohort study. Journal of dentistry 6 37031884
2022 Single Nucleotide Polymorphisms and Dental Fluorosis: A Systematic Review. Dentistry journal 6 36354656
2020 Biomarkers for Lifetime Caries-Free Status. Journal of personalized medicine 6 33396693
2007 Restricting the ligation step of non-homologous end-joining. DNA repair 3 17977804
2021 Comparisons among rainbow trout, Oncorhynchus mykiss, populations of maternal transcript profile associated with egg viability. BMC genomics 2 34130620
2024 Intrinsic disorder and salt-dependent conformational changes of the N-terminal region of TFIP11 splicing factor. International journal of biological macromolecules 0 39089542

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