Affinage

LIG1

Leucine-rich repeats and immunoglobulin-like domains protein 1 · UniProt Q96JA1

Length
1093 aa
Mass
119.1 kDa
Annotated
2026-06-10
42 papers in source corpus 19 papers cited in narrative 18 extracted findings
Cross-family judge vs UniProt: Affinage preferred faithfulness: 8/8 claims corpus-supported (100%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

LIG1 is the principal ATP-dependent DNA ligase that seals nicks to complete DNA replication and base excision repair, catalyzing phosphodiester bond formation through a multi-step adenylation reaction at single-strand breaks (PMID:35790757, PMID:38522520). It is recruited to nicked DNA via two PCNA-interacting motifs—one in its disordered N-terminus and one in its DNA-binding domain—forming a two-stack ring with PCNA that encircles DNA; once assembled, the N-terminal PIP is released and only the DBD PIP is required for ligation, enabling a toolbelt handoff of substrate from FEN1 on an unoccupied PCNA monomer (PMID:36539424). Its N-terminal domain promotes one-dimensional diffusion along DNA so it becomes enriched at nicks with long binding lifetimes, supporting efficient nick searching (PMID:39404052). Fidelity is governed by an active-site network: residues Phe635 and Phe872 enforce DNA-end rigidity and alignment, and their loss abolishes faithful ligation of all mismatched ends (PMID:39574773), while Asp570 and Arg871 sense the 2'-OH of ribose at the nick, conferring proficient sugar discrimination against 5'-ribonucleotides but not 3'-ribonucleotides (PMID:38522520, PMID:39159820). LIG1 accommodates mismatched and oxidatively damaged termini such as G:T and 8-oxoG, sealing them mutagenically or non-mutagenically depending on base-pairing geometry, with APE1 acting as a compensatory 3'-proofreading exonuclease at the final repair steps (PMID:35790757, PMID:41370201, PMID:40286853). Beyond catalysis, methylated LIG1 K126 is read by the UHRF1 tandem Tudor domain with nanomolar affinity, relieving UHRF1 auto-inhibition and recruiting it to chromatin for DNA methylation maintenance, linking the ligase to epigenetic inheritance (PMID:30639225). Disease-associated variants define its physiological roles: R771W and R641L destabilize a DNA–LIG1 cooperative network that couples substrate engagement to Mg2+ binding, reducing ligation efficiency (LIG1 syndrome) (PMID:33444456), and the K845N variant enhances mismatch discrimination, increases fidelity, and suppresses somatic CAG-repeat expansion in a Huntington's disease mouse model (PMID:41770933, PMID:41346861). LIG1 loss is synthetically lethal with PARP inhibition through accumulation of unsealed nicks, replication stress, and double-strand breaks (PMID:39718835, PMID:39868490).

Mechanistic history

Synthesis pass · year-by-year structured walk · 13 steps
  1. 2018 Medium

    Before this work it was unclear how LIG1 expression is controlled post-transcriptionally; the finding established a translational regulatory input linking LIG1 abundance to proliferation in cancer cells.

    Evidence RIP, mRNA stability assays, and siRNA knockdown with proliferation/apoptosis readouts in NSCLC cells

    PMID:30181552

    Open questions at the time
    • Single-lab study confined to NSCLC
    • Does not address whether SRSF1 regulation operates in normal tissues or other cancers
  2. 2019 High

    It was unknown how LIG1 could connect replication/repair to epigenetic maintenance; structural work showed methylated LIG1 K126 is a high-affinity ligand for the UHRF1 tandem Tudor domain that switches UHRF1 to an open, active conformation.

    Evidence X-ray crystallography of the UHRF1 TTD–LIG1 K126me3 peptide complex with affinity and conformational analysis

    PMID:30639225

    Open questions at the time
    • The writer methyltransferase for LIG1 K126 is not identified here
    • Cellular consequences for global methylation maintenance not directly quantified
  3. 2021 High

    The molecular basis of LIG1 syndrome was unresolved; structures and kinetics of R771W and R641L revealed a cooperative DNA–LIG1 interaction network coupling substrate engagement to productive Mg2+ binding that these mutations disrupt.

    Evidence X-ray crystallography plus steady-state and pre-steady-state kinetics with systematic mutagenesis

    PMID:33444456

    Open questions at the time
    • Does not establish the in vivo immunodeficiency mechanism at the cellular level
    • Patient-derived cell phenotypes not assayed
  4. 2022 High

    How LIG1 engages PCNA and receives substrate from upstream factors was undefined; cryo-EM showed a two-PIP, two-ring toolbelt mechanism enabling FEN1-to-LIG1 handoff on PCNA.

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

    PMID:36539424

    Open questions at the time
    • Dynamics of the handoff in cells not directly visualized
    • Stoichiometry on stalled or damaged forks not addressed
  5. 2022 High

    Whether LIG1 discriminates mismatched ends and how errors are corrected was unclear; structures of mismatch-containing nicks plus APE1 interaction data showed LIG1 can mis-seal certain mismatches while APE1 proofreads them.

    Evidence X-ray crystallography of LIG1/mismatch-nick complexes, ligation/abortive-ligation assays, and Co-IP with APE1

    PMID:35790757

    Open questions at the time
    • APE1 recruitment mechanism at the final BER step not defined
    • In vivo contribution of APE1 proofreading not quantified
  6. 2024 High

    It was unknown whether LIG1 discriminates ribonucleotides at nick ends; paired structural studies showed Asp570/Arg871 sense the 2'-OH but tolerate 3'-ribonucleotides while strongly rejecting 5'-ribonucleotides.

    Evidence X-ray crystallography of LIG1 with 3'- and 5'-ribonucleotide nicks plus in vitro ligation assays and active-site mutagenesis

    PMID:38522520 PMID:39159820

    Open questions at the time
    • Physiological consequences of 3'-ribonucleotide tolerance during RER not measured in cells
    • Coupling to upstream ribonucleotide excision factors not addressed
  7. 2024 High

    How LIG1 locates nicks among bulk DNA was unresolved; single-molecule imaging showed the N-terminal domain enables 1D diffusion and nick enrichment with long dwell times.

    Evidence C-Trap optical tweezers and TIRF single-molecule microscopy comparing full-length vs C-terminal LIG1

    PMID:39404052

    Open questions at the time
    • Behavior in the context of PCNA/chromatin not measured
    • Quantitative search kinetics in cells unknown
  8. 2024 Medium

    Whether LIG1 can mis-seal incomplete repair intermediates was unclear; biochemistry showed LIG1 ligates pol-beta-defective gap intermediates to generate single-nucleotide deletions, with APE1 proofreading 3'-errors.

    Evidence In vitro ligation assays with pol-beta-defective substrates and APE1 substrate-specificity assays

    PMID:38366780

    Open questions at the time
    • Single-lab in vitro reconstitution
    • In vivo frequency of such mutagenic events not established
  9. 2024 High

    Targeting LIG1 therapeutically required a synthetic-lethal rationale; CRISPR screens and xenograft validation showed LIG1 loss with PARP inhibition causes replication stress and apoptosis dependent on its catalytic nick-sealing activity.

    Evidence Genome-wide CRISPR screen, multiple loss-of-function approaches, xenograft models, and catalytic-dead K568A rescue

    PMID:39718835 PMID:39868490

    Open questions at the time
    • Tumor-genotype determinants of sensitivity beyond BRCA1 not fully mapped
    • Resistance mechanisms not characterized
  10. 2025 High

    How LIG1 processes oxidatively damaged 8-oxoG ends was unresolved; pre- and post-catalytic structures explained mutagenic vs non-mutagenic sealing via syn/anti Hoogsteen or Watson-Crick pairing.

    Evidence X-ray crystallography of LIG1 with 3'-8oxodG/8oxorG nicks plus in vitro ligation assays

    PMID:41370201

    Open questions at the time
    • Cellular mutagenic burden from this ligation not quantified
    • Interplay with downstream mismatch repair not addressed
  11. 2025 High

    The mechanistic consequences of the HD-modifier K845N variant were unknown; combined biochemistry, structure, kinetics and a mouse model showed it raises fidelity, reduces ligation of damaged/mismatched/ribonucleotide nicks, and suppresses somatic CAG expansion.

    Evidence In vitro ligase assays, enzyme kinetics, X-ray crystallography, TIRF single-molecule, HD knock-in mouse, and cell-based oxidative stress assays

    PMID:41346861 PMID:41770933

    Open questions at the time
    • Mechanistic link between ligation fidelity and repeat-instability suppression not fully resolved
    • Human relevance of the mouse phenotype not directly tested
  12. 2025 High

    Active-site determinants of fidelity were undefined; structural and biochemical analysis identified Phe635 and Phe872 as residues enforcing end rigidity required for faithful ligation of mismatched ends.

    Evidence X-ray crystallography of F635A/F872A mutants, in vitro ligation assays, mutagenesis, and single-molecule TIRF (preprint)

    PMID:39574773

    Open questions at the time
    • Preprint, single lab
    • In vivo fidelity contribution of these residues not tested
  13. 2025 Medium

    The temporal order of Okazaki fragment maturation factors on PCNA was unclear; cell-based work showed JMJD1B demethylates FEN1 R192 to release FEN1, allowing sequential LIG1 recruitment, with disruption activating a mutagenic PARP1-LIG3 pathway.

    Evidence Cell-based Co-IP/chromatin fractionation with FEN1 R192Q and Jmjd1b-/- mutants and replication intermediate analysis (preprint)

    PMID:bio_10.1101_2025.10.06.680735

    Open questions at the time
    • Preprint, single lab
    • Direct demonstration of LIG1 timing independent of FEN1 release not isolated

Open questions

Synthesis pass · forward-looking unresolved questions
  • How LIG1 nick-sealing fidelity, PCNA toolbelt dynamics, and K126 methylation are coordinately regulated in living cells across replication and the multiple repair pathways remains unresolved.
  • No in vivo measurement integrating search, handoff and catalysis
  • Methyltransferase writing LIG1 K126 not identified in the corpus
  • Pathway-specific regulation of fidelity in cells not established

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0016874 ligase activity 5 GO:0140097 catalytic activity, acting on DNA 3 GO:0003677 DNA binding 2 GO:0140657 ATP-dependent activity 2
Localization
GO:0005634 nucleus 2 GO:0005694 chromosome 1
Pathway
R-HSA-73894 DNA Repair 4 R-HSA-69306 DNA Replication 2 R-HSA-4839726 Chromatin organization 1
Partners
APE1FEN1PCNAPOLBSRSF1UHRF1
Complex memberships
LIG1-PCNA two-ring clamp

Evidence

Reading pass · 18 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 in its DNA binding domain (PIPDBD) — to recruit PCNA to nicked DNA. Cryo-EM structures showed that once LIG1 and PCNA assemble as two-stack rings encircling DNA, PIPN-term is released and only PIPDBD is required for ligation, facilitating substrate handoff from FEN1 via a toolbelt mechanism on an unoccupied PCNA monomer. Cryo-EM structures combined with functional ligation assays and PCNA-interacting motif mutagenesis Nature Communications High 36539424
2022 X-ray structures of LIG1 bound to nick DNA containing G:T (wobble) and A:C mismatches revealed that LIG1 can accommodate a G:T mismatch and transfer AMP to the 5'-phosphate (DNA-AMP intermediate), while with an A:C mismatch the AMP remains on the LIG1-AMP intermediate. APE1 was shown to interact with LIG1 at the final BER steps and remove mismatched bases as a compensatory proofreading enzyme. X-ray crystallography of LIG1/nick-DNA complexes with mismatches; in vitro ligation and abortive ligation assays; Co-IP/interaction assay with APE1 Nature Communications High 35790757
2021 High-resolution X-ray structures and pre-steady-state kinetics of LIG1 disease-associated variants R771W and R641L (LIG1 syndrome) revealed a cooperative network of DNA-LIG1 interactions connecting DNA substrate engagement with productive Mg2+ cofactor binding. These mutations destabilize the network, reduce Mg2+ binding affinity, decrease ligation efficiency, and increase abortive ligation. X-ray crystallography, steady-state and pre-steady-state kinetics, systematic mutagenesis Nucleic Acids Research High 33444456
2019 Crystal structure of the UHRF1 tandem Tudor domain (TTD) bound to a LIG1 K126me3 peptide showed that methylated LIG1 K126 binds the TTD with nanomolar affinity (higher than histone H3K9me2/3). This interaction switches UHRF1 from a closed (auto-inhibited) to a flexible open conformation, relieving auto-inhibition and permitting UHRF1 recruitment to chromatin for DNA methylation maintenance. X-ray crystallography of UHRF1 TTD–LIG1 K126me3 peptide complex; binding affinity measurements; conformational analysis Structure High 30639225
2024 X-ray structures of LIG1 bound to 3'-ribonucleotide-containing nick DNA (3'-rA:T and 3'-rG:C) at pre- and post-step-3 ligation stages revealed that Asp570 and Arg871 side chains interact with the 2'-OH of the ribose at the nick, but these interactions do not prevent ligation. LIG1 was shown to ligate nick substrates with pre-inserted 3'-ribonucleotides as efficiently as Watson-Crick base-paired DNA ends in vitro, demonstrating a lack of sugar discrimination at the 3'-end. X-ray crystallography; in vitro ligation assays Journal of Biological Chemistry High 38522520
2024 X-ray structures of LIG1 bound to a nick with a 5'-ribonucleotide (5'-rG:C) at the initial ligation step uncovered a large conformational change downstream of the nick with a shift in Arg871 in the adenylation domain. Functionally, ligation of nick DNA with a 5'-ribonucleotide was significantly diminished compared with efficient ligation of a nick with a 3'-ribonucleotide, demonstrating proficient sugar discrimination at the 5'-end during ribonucleotide excision repair. X-ray crystallography; in vitro ligation assays; active-site mutagenesis Journal of Biological Chemistry High 39159820
2024 Single-molecule fluorescence (C-Trap and TIRF) measurements showed that full-length LIG1 exhibits 1D diffusion along DNA and becomes enriched at nick sites with longer binding lifetimes, whereas the LIG1 C-terminal mutant (catalytic core + DNA-binding domain) binds non-specifically and for shorter durations throughout DNA. This demonstrated that the N-terminal domain promotes 1D diffusion and efficient nick searching. Single-molecule fluorescence microscopy (C-Trap optical tweezers + TIRF); comparison of full-length vs. C-terminal LIG1 mutant Nucleic Acids Research High 39404052
2024 Biochemical analyses demonstrated that when polβ fails to fill a one-nucleotide gap repair intermediate, LIG1 ligates the resulting gap DNA, generating single-nucleotide deletion products (aberrant/mutagenic nick sealing). APE1 showed distinct substrate specificity for exonuclease removal of 3'-mismatched bases and ribonucleotides from nick repair intermediates, providing a proofreading role. In vitro ligation assays with polβ-defective substrates; biochemical substrate-specificity assays for APE1 Nucleic Acids Research Medium 38366780
2024 X-ray structures of LIG1/nick complexes containing 3'-8oxodG and 3'-8oxorG opposite templating C or A, captured at steps 2 and 3 of the ligation reaction, revealed structural adjustments (differences in distances at +1/+2 nucleotides and template base position shifts depending on 8-oxoG syn/anti conformation) that underlie mutagenic ligation or non-mutagenic end joining. LIG1 wild-type and disease-associated variants seal 3'-8oxodG:A and 3'-8oxorG:A nicks mutagenically in vitro. X-ray crystallography; in vitro ligation assays with oxidatively damaged substrates; comparison with LIG3α and disease variants bioRxiv (preprint)preprint Medium 38766188
2025 X-ray structures of LIG1 with 3'-8oxodG and 3'-8oxorG at pre- and post-catalytic steps demonstrated that 8-oxoG accommodates Hoogsteen or Watson-Crick pairing in syn or anti conformation, leading to mutagenic ligation or non-mutagenic end joining respectively. These structural adjustments explain how LIG1 processes oxidatively damaged nick ends during DNA repair. X-ray crystallography; in vitro ligation assays Nucleic Acids Research High 41370201
2025 The Huntington's disease-associated LIG1 K845N variant (lysine to asparagine) was shown by in vitro ligase assays and enzyme kinetics to enhance mismatch substrate discrimination and increase ligation fidelity. The mouse orthologue (K843N) suppressed somatic CAG repeat expansion in HD knock-in mice. Cell-based assays showed K845N confers protection against oxidative stress. In vitro ligase assays; enzyme kinetics; HD knock-in mouse model; cell-based oxidative stress assays Proceedings of the National Academy of Sciences High 41770933
2025 Biochemical, X-ray crystallographic, and TIRF single-molecule analyses of LIG1 K845N showed reduced ligation efficiency for nicks with mismatches, 8-oxoG, and 3'-ribonucleotides compared to wild-type, with K845N exhibiting a lack of discrimination against 3'-ribonucleotide-containing nicks. Structural comparison showed similar active-site conformation but altered distances between the K/N845 residue and DNA ends. Single-molecule data revealed less frequent and shorter-lived nick binding by K845N. X-ray crystallography; in vitro ligation assays; TIRF single-molecule microscopy NAR Molecular Medicine High 41346861
2025 Active site residues Phe635 and Phe872 of LIG1 are required for faithful ligation: F635A/L and F872A/L substitutions abolished ligation of all 12 non-canonical mismatches. Structures of LIG1 F635A and F872A mutants with mismatched and 8-oxoG-containing nick DNA demonstrated that these residues govern DNA end rigidity and alignment at the active site, and their mutation causes a shift in a flexible loop near the 5'-end of the nick that increases the barrier to adenylate transfer. X-ray crystallography; in vitro ligation assays; active-site mutagenesis; single-molecule TIRF bioRxiv (preprint)preprint High 39574773
2024 CRISPR/Cas9 screening in prostate cancer cell lines identified that LIG1 loss combined with PARP inhibition induces replication stress, DNA double-strand breaks, and apoptosis (synthetic lethality). This synthetic lethal interaction was confirmed in vivo in xenograft models and was shown to depend on LIG1's role in sealing ssDNA nicks, as catalytically dead LIG1 K568A failed to rescue viability in BRCA1 mutant cells. CRISPR/Cas9 genome-wide screen; CRISPRn/CRISPRi/RNAi/protein degradation; xenograft in vivo model; catalytic mutant rescue assay Journal of Clinical Investigation / Molecular Cancer Therapeutics High 39718835 39868490
2025 Single-molecule TIRF measurements comparing LIG1 and LIG3α showed that LIG3α binds less frequently but forms longer-lived complexes than LIG1 for canonical and mismatch-containing nicks. LIG1 can stably bind to and ligate gap DNA substrates (including one-nucleotide and larger gaps), with a higher percentage of LIG1 molecules forming stable long-lived complexes on gap DNA compared to LIG3α. TIRF single-molecule fluorescence microscopy; in vitro ligation assays bioRxiv (preprint)preprint Medium 40666977
2025 In the context of Okazaki fragment maturation, LIG1 is recruited to PCNA only after JMJD1B-mediated demethylation of FEN1 R192 causes FEN1 to dissociate from PCNA. This sequential (not simultaneous) binding of Polδ, FEN1, and LIG1 to PCNA was demonstrated in mammalian cells; disruption leads to unprocessed 5' flaps and induction of a PARP1-LIG3-dependent alternative mutagenic pathway. Cell-based Co-IP/chromatin fractionation; mutant cell lines (FEN1 R192Q, Jmjd1b-/-); replication intermediate analysis bioRxiv (preprint)preprint Medium bio_10.1101_2025.10.06.680735
2018 The RNA-binding protein SRSF1 binds to LIG1 mRNA, increases its stability, and enhances its translation in an mTOR-dependent manner in non-small cell lung cancer cells. siRNA-mediated LIG1 knockdown reduced proliferation and increased apoptosis of NSCLC cells. RIP (RNA immunoprecipitation) for SRSF1-LIG1 mRNA binding; mRNA stability assays; siRNA knockdown with proliferation/apoptosis readout; mTOR inhibitor experiments Laboratory Investigation Medium 30181552
2025 LIG1 seals the nick repair product after polβ mutagenic dATP insertion opposite 8-oxoG, whereas LIG3α cannot ligate the dCTP:8-oxoG polβ insertion product. Ribonucleotide insertions by polβ during 8-oxoG bypass completely diminish coordination with both LIG1 and LIG3α. APE1 proofreads 3'-mismatches and ribonucleotides templating 8-oxoG. In vitro ligation assays with defined polβ insertion products; substrate-specificity analysis comparing LIG1 vs. LIG3α; APE1 exonuclease assays Journal of Biological Chemistry Medium 40286853

Source papers

Stage 0 corpus · 42 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
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 49 38044421
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) 49 30639225
2018 The oncogenic RNA-binding protein SRSF1 regulates LIG1 in non-small cell lung cancer. Laboratory investigation; a journal of technical methods and pathology 37 30181552
2022 Mechanism of human Lig1 regulation by PCNA in Okazaki fragment sealing. Nature communications 28 36539424
2012 Structure and catalytic mechanism of LigI: insight into the amidohydrolase enzymes of cog3618 and lignin degradation. Biochemistry 28 22475079
2022 Structures of LIG1 that engage with mutagenic mismatches inserted by polβ in base excision repair. Nature communications 21 35790757
2021 LIG1 syndrome mutations remodel a cooperative network of ligand binding interactions to compromise ligation efficiency. Nucleic acids research 21 33444456
2016 Association between Single-Nucleotide Polymorphisms of the hOGG1,NEIL1,APEX1, FEN1,LIG1, and LIG3 Genes and Alzheimer's Disease Risk. Neuropsychobiology 20 27010693
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 7 39718835
2024 Probing the mechanism of nick searching by LIG1 at the single-molecule level. Nucleic acids research 6 39404052
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
2025 LIG1 Is a Synthetic Lethal Target in BRCA1 Mutant Cancers. Molecular cancer therapeutics 4 39868490
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
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 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
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 1 41770933
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
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

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