Affinage

LIG1

DNA ligase 1 · UniProt P18858

Length
919 aa
Mass
101.7 kDa
Annotated
2026-04-28
43 papers in source corpus 18 papers cited in narrative 17 extracted findings

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

LIG1 is the principal replicative DNA ligase in human cells, sealing Okazaki fragments during lagging-strand synthesis and completing nick ligation in base excision repair (BER) and ribonucleotide excision repair pathways. It catalyzes phosphodiester bond formation through a three-step AMP-dependent mechanism, using two PCNA-interacting motifs to assemble a toolbelt complex with PCNA and FEN1 on nicked DNA—where PIPN-term mediates initial recruitment and PIPDBD sustains ligation, enabling substrate handoff from FEN1 (PMID:36539424)—while its N-terminal non-catalytic domain drives one-dimensional diffusion along DNA to locate nick sites (PMID:39404052). LIG1 discriminates against aberrant substrates through active-site residues F635 and F872 that enforce DNA end rigidity to block mismatch ligation (PMID:39574773), a cooperative network coupling DNA engagement to Mg²⁺ cofactor binding (PMID:33444456), and asymmetric sugar selectivity that permits 3′-ribonucleotide but rejects 5′-ribonucleotide nick sealing (PMID:38522520, PMID:39159820); APE1 acts as a compensatory proofreader removing mismatched or damaged 3′-ends that escape this fidelity checkpoint (PMID:35790757, PMID:38366780). LIG1 catalytic activity is selectively essential in BRCA1-deficient cells, where its loss causes accumulation of single-strand breaks, replication stress, and synthetic lethality both in vitro and in vivo (PMID:39868490, PMID:39718835), and the Huntington's disease-modifier variant K845N enhances mismatch discrimination and suppresses somatic CAG repeat expansion in HD knock-in mice (PMID:41770933).

Mechanistic history

Synthesis pass · year-by-year structured walk · 11 steps
  1. 2018 Medium

    How LIG1 protein levels are controlled post-transcriptionally was unknown; SRSF1 was shown to bind and stabilize LIG1 mRNA while promoting its mTOR-dependent translation, linking LIG1 abundance to growth signaling in cancer cells.

    Evidence RNA immunoprecipitation, mRNA stability assays, and mTOR inhibition in NSCLC cells

    PMID:30181552

    Open questions at the time
    • Limited mechanistic depth on SRSF1-LIG1 mRNA binding specificity
    • No direct in vivo validation of mTOR-dependent LIG1 regulation
    • Other post-transcriptional regulators of LIG1 not explored
  2. 2019 High

    The mechanism by which LIG1 connects to chromatin maintenance machinery was unclear; structural and biophysical studies revealed that UHRF1's tandem Tudor domain binds LIG1-K126me2/me3 with nanomolar affinity, switching UHRF1 from an auto-inhibited to an open conformation and thereby recruiting UHRF1 to chromatin.

    Evidence X-ray crystallography of UHRF1-TTD/LIG1-K126me3 peptide complex with binding affinity measurements

    PMID:30639225

    Open questions at the time
    • Functional consequence of this interaction for DNA methylation maintenance in cells not fully established
    • Writers/erasers of K126 methylation not identified in this study
  3. 2021 High

    How disease-causing LIG1 mutations impair catalysis was unknown; structural and kinetic analysis of the LIG1 syndrome variants R771W and R641L revealed they disrupt a cooperative network coupling DNA engagement to productive Mg²⁺ binding, increasing abortive ligation.

    Evidence X-ray crystallography combined with pre-steady-state and steady-state kinetics of active-site mutants

    PMID:33444456

    Open questions at the time
    • Whether compensatory repair pathways mitigate these defects in patient cells not addressed
    • Structural basis for other LIG1 syndrome mutations not yet determined
  4. 2022 High

    How LIG1 coordinates with PCNA and FEN1 during Okazaki fragment maturation was structurally undefined; cryo-EM structures showed LIG1 uses two PIP motifs to recruit PCNA to nicked DNA as stacked rings, with PIPN-term released after assembly so that PCNA forms a toolbelt with FEN1 to hand off the nick substrate to LIG1.

    Evidence Cryo-EM structures with PIP-motif mutagenesis and functional ligation assays

    PMID:36539424

    Open questions at the time
    • Dynamics of the handoff in the cellular context not captured
    • Role of post-translational modifications on PIP motifs not explored
  5. 2022 High

    Whether LIG1 has intrinsic mismatch discrimination and how APE1 compensates was unclear; X-ray structures showed LIG1 accommodates a G:T wobble mismatch (reaching DNA-AMP) but stalls on A:C mismatches (remaining at LIG1-AMP), and APE1 was shown to interact with LIG1 and proofread mismatched nick ends.

    Evidence X-ray crystallography of LIG1/mismatch-nick complexes, biochemical assays, and APE1 co-immunoprecipitation

    PMID:35790757

    Open questions at the time
    • Structural basis of the APE1-LIG1 physical interface not resolved
    • Contribution of mismatch discrimination in vivo not quantified
  6. 2024 High

    How LIG1 handles ribonucleotide-containing nicks during ribonucleotide excision repair was unknown; structural and biochemical studies established that LIG1 efficiently seals 3′-ribonucleotide nicks (Asp570/Arg871 contact the 2′-OH) but discriminates against 5′-ribonucleotide nicks via conformational rearrangements at Arg871, defining an asymmetric sugar-selectivity mechanism.

    Evidence X-ray crystallography of LIG1 with 3′- and 5′-RNA-DNA hybrid nick substrates, in vitro nick-sealing assays with active-site mutants

    PMID:38522520 PMID:39159820

    Open questions at the time
    • In vivo relevance of asymmetric sugar discrimination for genome stability not tested
    • Whether LIG3α shares this asymmetry not determined
  7. 2024 High

    The specific active-site determinants of LIG1 mismatch fidelity were undefined; mutagenesis and structures of F635A and F872A mutants demonstrated these residues enforce DNA end rigidity and 5′-end alignment at the nick, creating a barrier to adenylate transfer on all 12 non-canonical mismatches.

    Evidence X-ray crystallography of LIG1 F635/F872 mutants with mismatched nick DNA, comprehensive biochemical ligation panel

    PMID:39574773

    Open questions at the time
    • Preprint at time of discovery; awaits formal peer review
    • Whether these residues also govern discrimination against damaged bases not fully explored
  8. 2024 High

    How LIG1 locates nick sites along DNA was unknown; single-molecule imaging revealed that the N-terminal non-catalytic domain enables one-dimensional diffusion along DNA before forming long-lived complexes at nicks, whereas the catalytic core alone binds non-specifically and transiently.

    Evidence Single-molecule TIRF and C-Trap fluorescence microscopy with full-length versus C-terminal truncation constructs

    PMID:39404052

    Open questions at the time
    • Whether PCNA or other replication factors modulate 1D diffusion not tested
    • In vivo diffusion parameters not measured
  9. 2024 High

    How LIG1 handles oxidative lesions inserted by pol β during BER was structurally unresolved; crystal structures captured LIG1 at pre- and post-catalytic steps with 3′-8-oxodG/8-oxorG nicks, revealing that Hoogsteen versus Watson-Crick pairing of 8-oxoG determines mutagenic or non-mutagenic ligation outcomes, and that APE1 can excise oxidatively damaged ends to limit mutagenic sealing.

    Evidence X-ray crystallography of LIG1 with 8-oxoG-containing nick substrates, in vitro ligation assays

    PMID:38766188 PMID:41370201

    Open questions at the time
    • Cellular frequency of mutagenic versus non-mutagenic ligation of 8-oxoG nicks not quantified
    • Contribution of LIG3α to 8-oxoG nick ligation in BER not compared
  10. 2024 High

    Whether LIG1 is a therapeutic vulnerability in homologous recombination-deficient cancers was untested; multiple orthogonal depletion strategies demonstrated that LIG1 loss causes selective lethality in BRCA1-mutant cells through accumulation of single-strand breaks and replication stress, establishing LIG1 as a synthetic lethal target.

    Evidence CRISPR screens, CRISPRi, RNAi, targeted protein degradation, catalytic-dead rescue (K568A), PAR staining, xenograft models

    PMID:39718835 PMID:39868490

    Open questions at the time
    • Whether LIG1 inhibition synergizes with PARP inhibitors in clinical contexts not established
    • Mechanism of synthetic lethality beyond nick accumulation not fully dissected
  11. 2025 High

    The functional impact of the Huntington's disease-associated LIG1 K845N variant was unknown; structural, kinetic, and in vivo studies showed K845N reduces nick affinity and enhances mismatch discrimination, conferring protection against oxidative stress in cells and suppressing somatic CAG repeat expansion in HD knock-in mice.

    Evidence X-ray crystallography, pre-steady-state kinetics, TIRF single-molecule microscopy, cell-based oxidative stress assays, HD knock-in mouse model

    PMID:41346861 PMID:41770933

    Open questions at the time
    • Whether K845N affects replicative ligation efficiency in vivo not fully addressed
    • Mechanism by which enhanced fidelity suppresses repeat expansion at the molecular level not fully defined

Open questions

Synthesis pass · forward-looking unresolved questions
  • Key unresolved questions include: the structural basis of the APE1-LIG1 physical interaction; how post-translational modifications (beyond K126 methylation) regulate LIG1 activity and recruitment in vivo; and whether LIG1's 1D diffusion mechanism operates in the chromatin context and is modulated by replication/repair factors.
  • No structure of an APE1-LIG1 complex
  • In vivo regulation of LIG1 by PTMs beyond K126me largely unexplored
  • Chromatin-context single-molecule studies of LIG1 not performed

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0016874 ligase activity 10 GO:0003677 DNA binding 6
Localization
GO:0005634 nucleus 2 GO:0005694 chromosome 1
Pathway
R-HSA-73894 DNA Repair 9 R-HSA-1643685 Disease 4 R-HSA-69306 DNA Replication 2
Partners
APE1FEN1PCNAPOLBSRSF1UHRF1
Complex memberships
PCNA-FEN1-LIG1 toolbelt

Evidence

Reading pass · 17 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2022 Human LIG1 uses two PCNA-interacting motifs (PIPs) — one at its disordered N-terminus (PIPN-term) and one at its DNA-binding domain (PIPDBD) — to recruit PCNA to nicked DNA. Cryo-EM structures show LIG1 and PCNA assemble as two-stack rings encircling DNA; once assembled, PIPN-term is released and only PIPDBD is required for ligation, facilitating substrate handoff from FEN1. PCNA forms a toolbelt with FEN1 and nicked DNA and recruits LIG1 to an unoccupied monomer to drive the transfer of DNA to LIG1 during Okazaki fragment sealing. Cryo-EM structures combined with functional ligation assays and PIP-motif mutagenesis Nature Communications High 36539424
2022 X-ray structures of LIG1 bound to nick DNA containing G:T and A:C mismatches show that the LIG1 active site can accommodate a G:T wobble mismatch and transfer AMP to the 5'-phosphate (DNA-AMP intermediate), whereas an A:C mismatch stalls the reaction at the LIG1-AMP intermediate. APE1 interacts with LIG1 at the final BER steps and acts as a compensatory proofreading enzyme by removing mismatched bases. X-ray crystallography of LIG1/nick-DNA complexes, biochemical ligation assays, Co-IP/pull-down with APE1 Nature Communications High 35790757
2021 LIG1 syndrome mutations R771W and R641L disrupt a cooperative network of DNA-LIG1 interactions that couple DNA substrate engagement with productive Mg2+ cofactor binding required for catalysis. High-resolution X-ray structures and pre-steady-state kinetics show these mutations destabilize Mg2+ binding affinity and increase abortive ligation. X-ray crystallography, steady-state and pre-steady-state kinetics, active-site mutant characterization Nucleic Acids Research High 33444456
2019 The UHRF1 tandem Tudor domain (TTD) binds the methylated histone-like region of DNA Ligase 1 (LIG1 K126me2/me3) with nanomolar affinity, permitting UHRF1 recruitment to chromatin; crystal structure of the UHRF1 TTD bound to a LIG1-K126me3 peptide reveals the structural basis for high-affinity binding and shows that phosphorylation can regulate this interaction. LIG1-K126me3 binding switches UHRF1 from a closed (auto-inhibited) to an open/flexible conformation. X-ray crystallography of UHRF1-TTD/LIG1-K126me3 peptide complex, binding affinity measurements, structural analysis of auto-inhibition relief Structure High 30639225
2024 X-ray structures of LIG1 bound to 3'-RNA-DNA hybrid nicks (3'-rA:T and 3'-rG:C) reveal that residues Asp570 and Arg871 contact the 2'-OH of the ribose at the nick, and LIG1 forms a final phosphodiester bond with 3'-ribonucleotides as efficiently as with canonical deoxyribonucleotides in vitro, indicating a lack of sugar discrimination at the 3'-terminus. X-ray crystallography, in vitro nick-sealing assays Journal of Biological Chemistry High 38522520
2024 X-ray structures of LIG1 bound to 5'-rG:C nick DNA at the initial ligation step reveal a large conformational change downstream of the nick and a shift at Arg871 in the adenylation domain; LIG1 discriminates against 5'-ribonucleotide-containing nicks (diminished ligation) compared to 3'-ribonucleotide-containing nicks (efficient ligation), establishing a sugar-discrimination mechanism specific to the 5'-end during ribonucleotide excision repair. X-ray crystallography, in vitro ligation assays with wild-type and active-site mutants Journal of Biological Chemistry High 39159820
2024 Single-molecule fluorescence (C-Trap and TIRF) shows LIG1 full-length binds enriched at nick sites and exhibits 1D diffusion along DNA before forming a long-lived nick complex, whereas the C-terminal catalytic fragment binds non-specifically and more transiently; the N-terminal non-catalytic domain drives 1D diffusion and nick-site enrichment. Single-molecule fluorescence microscopy (C-Trap, TIRF), nick-binding assays with full-length and C-terminal truncation Nucleic Acids Research High 39404052
2024 Active-site residues F635 and F872 of LIG1 are required for mismatch discrimination: Ala/Leu substitutions at these positions abolish ligation of all 12 non-canonical mismatched nick substrates. Structures of F635A and F872A mutants reveal that these residues govern DNA end rigidity and the alignment of the 5'-end of the nick, creating a barrier to adenylate transfer in the presence of mismatches. X-ray crystallography of LIG1 active-site mutants with mismatch-containing nick DNA, biochemical ligation assays bioRxiv (preprint, later published)preprint High 39574773
2024 LIG1 forms X-ray crystal structure complexes with 3'-8-oxodG and 3'-8-oxorG nicks opposite C or A, capturing pre- and post-catalytic ligation steps. The ligase active site accommodates oxidative lesions via shifts in template base position depending on 8-oxoG Hoogsteen vs. Watson-Crick conformation, leading to mutagenic or non-mutagenic ligation. LIG1 and LIG3α seal nicks after polβ insertion of 8-oxorGTP:A, and APE1 can clean oxidatively damaged ends. X-ray crystallography, in vitro ligation assays with wild-type and variant enzymes bioRxiv (preprint)preprint High 38766188
2024 Unfilled gaps by polβ result in gap ligation by LIG1, forming single-nucleotide deletion products. LIG1 cannot discriminate against nick DNA containing a 3'-ribonucleotide regardless of base-pairing potential; APE1 has distinct exonuclease specificity for removing 3'-mismatched bases and ribonucleotides at the nick. In vitro gap-filling and nick-sealing assays with polβ and LIG1, ribonucleotide substitution experiments, APE1 exonuclease assays Nucleic Acids Research High 38366780
2025 The HD-associated LIG1 K845N variant shows reduced ligation efficiency for nicks with mismatches, 8-oxoG, and damaged ends; crystal structures show differences in distances between the K/N845 side chain and DNA ends; single-molecule TIRF reveals K845N binds less frequently to nick sites, indicating diminished nick affinity, consistent with impaired nick recognition. X-ray crystallography, pre-steady-state kinetics, TIRF single-molecule microscopy NAR Molecular Medicine High 41346861
2025 In vitro ligase assays demonstrate that the K845N HD-modifier variant of LIG1 enhances discrimination toward mismatched substrates and increases ligation fidelity. In cell-based assays, K845N confers protection against oxidative stress. In vivo, the mouse ortholog (K843N) suppresses somatic CAG repeat expansion in HD knock-in mice. In vitro ligation kinetics, cell-based oxidative stress assays, HD knock-in mouse model Proceedings of the National Academy of Sciences High 41770933
2025 X-ray structures of LIG1 with 3'-8-oxodG and 3'-8-oxorG nick substrates templating A or C show structural adjustments at the +1 and +2 nucleotide positions and template base shifts depending on the dual coding potential (Hoogsteen vs. Watson-Crick) of 8-oxoG. These differences lead to mutagenic or non-mutagenic nick sealing by LIG1. X-ray crystallography, in vitro ligation assays Nucleic Acids Research High 41370201
2025 LIG1 inactivation (via CRISPRn, CRISPRi, RNAi, and targeted protein degradation) causes viability loss selectively in BRCA1-mutant cells in vitro and in vivo. This synthetic lethality requires LIG1 catalytic activity (catalytically dead K568A does not rescue), and LIG1 perturbation increases PAR staining consistent with accumulation of ssDNA nicks. CRISPR/Cas9 screens also identified LIG1 loss as a PARP inhibitor sensitizer, causing replication stress and DNA double-strand breaks. CRISPR/Cas9 genetic screens, multiple LIG1 depletion strategies with catalytic mutant rescue, PAR staining, xenograft in vivo model Molecular Cancer Therapeutics / Journal of Clinical Investigation High 39718835 39868490
2018 SRSF1 binds to LIG1 mRNA and stabilizes it while also enhancing its translation in an mTOR-dependent manner, thereby increasing LIG1 protein levels in NSCLC cells. siRNA-mediated LIG1 knockdown reduces NSCLC cell proliferation and increases apoptosis. RNA-binding protein immunoprecipitation, mRNA stability assays, mTOR inhibition, siRNA knockdown with phenotypic readout Laboratory Investigation Medium 30181552
2025 During Okazaki fragment maturation, Polδ, FEN1, and LIG1 sequentially but not simultaneously bind PCNA. FEN1 R192 methylation mediates its PCNA association and prevents premature LIG1 loading; JMJD1B-mediated demethylation of FEN1 R192 promotes FEN1 dissociation from PCNA and enables LIG1 recruitment for nick ligation. Cell-based co-immunoprecipitation, methylation mutant analysis, JMJD1B knockout cells, replication intermediate analysis bioRxiv (preprint)preprint Medium bio_10.1101_2025.10.06.680735
2025 Single-molecule TIRF shows LIG3α binds less frequently but forms longer-lived complexes than LIG1 on nick DNA; both ligases can bind gap DNA as efficiently as nick DNA, but LIG1 forms more stable long-lived complexes on gap DNA compared to LIG3α, revealing distinct nick vs. gap substrate recognition dynamics between the two ligases. Single-molecule TIRF microscopy, in vitro ligation assays comparing LIG1 and LIG3α bioRxiv (preprint)preprint Medium 40666977

Source papers

Stage 0 corpus · 43 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2001 Cloning, characterization, and expression of human LIG1. Biochemical and biophysical research communications 119 11414704
2002 Targeted disruption of LIG-1 gene results in psoriasiform epidermal hyperplasia. FEBS letters 96 12067728
1996 cDNA cloning of a novel membrane glycoprotein that is expressed specifically in glial cells in the mouse brain. LIG-1, a protein with leucine-rich repeats and immunoglobulin-like domains. The Journal of biological chemistry 72 8798419
2019 Structure of the UHRF1 Tandem Tudor Domain Bound to a Methylated Non-histone Protein, LIG1, Reveals Rules for Binding and Regulation. Structure (London, England : 1993) 48 30639225
2023 hsa_circ_0007919 induces LIG1 transcription by binding to FOXA1/TET1 to enhance the DNA damage response and promote gemcitabine resistance in pancreatic ductal adenocarcinoma. Molecular cancer 44 38044421
2011 Arabidopsis ARP endonuclease functions in a branched base excision DNA repair pathway completed by LIG1. The Plant journal : for cell and molecular biology 44 21781197
2018 The oncogenic RNA-binding protein SRSF1 regulates LIG1 in non-small cell lung cancer. Laboratory investigation; a journal of technical methods and pathology 36 30181552
2022 Mechanism of human Lig1 regulation by PCNA in Okazaki fragment sealing. Nature communications 27 36539424
2012 Structure and catalytic mechanism of LigI: insight into the amidohydrolase enzymes of cog3618 and lignin degradation. Biochemistry 26 22475079
2022 Structures of LIG1 that engage with mutagenic mismatches inserted by polβ in base excision repair. Nature communications 20 35790757
2016 Association between Single-Nucleotide Polymorphisms of the hOGG1,NEIL1,APEX1, FEN1,LIG1, and LIG3 Genes and Alzheimer's Disease Risk. Neuropsychobiology 20 27010693
2021 LIG1 syndrome mutations remodel a cooperative network of ligand binding interactions to compromise ligation efficiency. Nucleic acids research 19 33444456
2020 Evaluation of the influence of chronic low-dose radiation on DNA repair gene polymorphisms [XRCC1, XRCC3, PRKDC (XRCC7), LIG1, NEIL1] in individuals from normal and high level natural radiation areas of Kerala Coast. International journal of radiation biology 14 32149571
1999 Phytochrome-induced expression of lig1, a homologue of the fission yeast cell-cycle checkpoint gene hus1, is associated with the developmental switch in Physarum polycephalum plasmodia. Current genetics 14 10447599
2024 Structures of LIG1 provide a mechanistic basis for understanding a lack of sugar discrimination against a ribonucleotide at the 3'-end of nick DNA. The Journal of biological chemistry 12 38522520
2024 Unfilled gaps by polβ lead to aberrant ligation by LIG1 at the downstream steps of base excision repair pathway. Nucleic acids research 11 38366780
2015 Association Between the LIG1 Polymorphisms and Lung Cancer Risk: A Meta-analysis of Case-Control Studies. Cell biochemistry and biophysics 9 27352326
2014 Single-nucleotide polymorphisms of LIG1 associated with risk of lung cancer. Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine 9 24929328
1998 Polymorphisms in the human DNA ligase I gene (LIG1) including a complex GT repeat. Mutation research 9 9920050
2024 CRISPR/Cas9 screens identify LIG1 as a sensitizer of PARP inhibitors in castration-resistant prostate cancer. The Journal of clinical investigation 6 39718835
2024 Structures of LIG1 uncover the mechanism of sugar discrimination against 5'-RNA-DNA junctions during ribonucleotide excision repair. The Journal of biological chemistry 5 39159820
2024 Structural and biochemical characterization of LIG1 during mutagenic nick sealing of oxidatively damaged ends at the final step of DNA repair. bioRxiv : the preprint server for biology 4 38766188
2024 Probing the mechanism of nick searching by LIG1 at the single-molecule level. Nucleic acids research 4 39404052
2015 Theoretical study of the hydrolysis mechanism of 2-pyrone-4,6-dicarboxylate (PDC) catalyzed by LigI. Journal of molecular graphics & modelling 4 26188792
2025 LIG1 Is a Synthetic Lethal Target in BRCA1 Mutant Cancers. Molecular cancer therapeutics 3 39868490
2025 Repair pathway coordination from gap filling by polβ and subsequent nick sealing by LIG1 or LIG3α governs BER efficiency at the downstream steps. DNA repair 3 40081282
2025 Nick sealing of polβ mismatch insertion products by LIG1 and LIG3α during 8-oxoG bypass leads to mutagenic or error-free base excision repair. The Journal of biological chemistry 2 40286853
2021 Histidine protonation states are key in the LigI catalytic reaction mechanism. Proteins 2 34318530
2013 Human DNA ligase i (ligi) gene and risk of cervical cancer in North Indian women. Experimental oncology 2 24084463
2026 TMEM106C, BSG, COPE, CDCA8, KPNA2, LIG1, UQCRH, and CCT5: Predictive of Survival and Immunotherapy Resistance in Hepatocellular Carcinoma. Human mutation 1 41674779
2025 Development of a Synthetic Lethality-Based Combination Therapy Using LIG1 and PARP Inhibitors for Prostate Cancer. Cancer science 1 40957713
2024 miR-325 Supresses Cell Proliferation and Migration in Non-Small Cell Lung Cancer via Targeting DNA Ligase 1 (LIG1). Folia biologica 1 39231317
2024 Mutagenic ligation of polβ mismatch insertion products during 8-oxoG bypass by LIG1 and LIG3α at the downstream steps of base excision repair pathway. bioRxiv : the preprint server for biology 1 39484546
2014 LIG1 polymorphisms: the Indian scenario. Journal of genetics 1 25189241
2026 Huntington's disease LIG1 modifier variant increases ligase fidelity and suppresses somatic CAG repeat expansion. Proceedings of the National Academy of Sciences of the United States of America 0 41770933
2025 Single-molecule analysis of gap and nick binding by LIG1 and LIG3α at the final step of DNA repair. bioRxiv : the preprint server for biology 0 40666977
2025 Huntington's disease LIG1 modifier variant increases ligase fidelity and suppresses somatic CAG repeat expansion. bioRxiv : the preprint server for biology 0 40791503
2025 Impaired nick recognition and ligation efficiency by LIG1 K845N variant linked to Huntington's disease. NAR molecular medicine 0 41346861
2025 Processing of DNA single-strand breaks with oxidatively damaged ends by LIG1. Nucleic acids research 0 41370201
2024 Uncovering nick DNA binding by LIG1 at the single-molecule level. bioRxiv : the preprint server for biology 0 38586032
2024 Biochemical, structural, and single-molecule characterization of LIG1 active site mutants demonstrate role of F635 and F872 residues for faithful ligation. bioRxiv : the preprint server for biology 0 39574773
2023 Structures of LIG1 active site mutants reveal the importance of DNA end rigidity for mismatch discrimination. bioRxiv : the preprint server for biology 0 36993234
2023 Structures of LIG1 active site mutants reveal the importance of DNA end rigidity for mismatch discrimination. Research square 0 37090517