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Data show that shade avoidance 6 (SAV6; At5g26680), encodes flap endonuclease-1 (FEN1), assures proper root development through maintenance of genome integrity.
These results reveal an important role of FEN1 phosphorylation to counteract oxygen-induced stress in the heart during the fetal-to-neonatal transition.
WDR4 (show WDR4 Proteins) regulates FEN1's potential DNA cleavage threat near the site of replication.
The FEN1 E359K germline mutation disrupts the FEN1-WRN interaction and FEN1 GEN activity, causing aneuploidy-associated cancers.
PARP1 (show PARP1 Proteins) is required for FEN1 recruitment to DNA repair intermediates in base excision repair.
FFAA Fen1 mutation causes defective Pcna (show PCNA Proteins) -coordinated Okazaki fragment maturation.
A point mutation in the base excision repair gene flap endonuclease 1 causes a functional deficiency in repairing base damage, such that individuals carrying the mutation or similar mutations are predisposed to chemical-induced cancer development.
FEN1 localization within the mitochondrial compartment of mouse brain tissue
Distinct roles for two Mg2 (show MCOLN1 Proteins)+ binding sites in the regulation of FEN-1 nuclease (show DCLRE1C Proteins) activities include enhancement of DNA substrate binding ability and modulation of conformational changes.
FEN1 has roles in DNA repair, as well as in DNA replication
Fen1 is induced independently in mouse embryonic fibroblasts by ultraviolet (UV-C)light
Notably, non-small cell lung cancer patients with FEN1-overexpressed cancers were prone to have poor differentiation and poor prognosis. Furthermore, knockdown of FEN1 resulted in G1/S or G2/M phase cell cycle arrest and suppressed in vitro cellular proliferation in NSCLC cancer cells.
Overexpression of human XPG (show ERCC5 Proteins) and FEN1 increases genome instability in U2OS cells
Data indicate that human cancer-associated genetic alterations in the FEN1 gene can contribute substantially to cancer development.
WRN or the Bloom syndrome helicase (BLM) stimulates DNA polymerase delta (show POLD1 Proteins) progression across telomeric G-rich repeats, only WRN promotes sequential strand displacement synthesis and FEN1 cleavage.
The FEN1 rs174538 A allele is a protective biomarker for childhood ALL and this association is more significant in males and in patients at onset age of 3.5 years or older.
Data indicate that Flap endonuclease 1 (FEN1) single nucleotide polymorphisms and haplotypes are associated with gallbladder cancer risk.
the aim of the present study was to determine the role of FEN1 in the chemosensitivity of SGC7901 cells.
Binding of DNA to human FEN1 in a bent conformation occurred independently of 5'-flap (show ALOX5AP Proteins) accommodation and did not require active site metal ions or the presence of conserved active site residues.
In this study, we found that cohesion establishment factors, like CHlR1 (show DDX11 Proteins), cooperatively stimulate endonuclease activity of hFen1 in in vivo mimic condition, including replication protein-A (show GPR153 Proteins)-coated DNA and high salt.
Under DNA repair conditions, FEN1 efficiently repaired the 5'-phoshotyrosyl bond-containing SSB substrates in the presence of DNA ligase and DNA polymerase (show POLB Proteins).
The protein encoded by this gene removes 5' overhanging flaps in DNA repair and processes the 5' ends of Okazaki fragments in lagging strand DNA synthesis. Direct physical interaction between this protein and AP endonuclease 1 during long-patch base excision repair provides coordinated loading of the proteins onto the substrate, thus passing the substrate from one enzyme to another. The protein is a member of the XPG/RAD2 endonuclease family and is one of ten proteins essential for cell-free DNA replication. DNA secondary structure can inhibit flap processing at certain trinucleotide repeats in a length-dependent manner by concealing the 5' end of the flap that is necessary for both binding and cleavage by the protein encoded by this gene. Therefore, secondary structure can deter the protective function of this protein, leading to site-specific trinucleotide expansions.
flap endonuclease 1
, Flap structure-specific endonuclease 1
, flap structure-specific endonuclease 1
, DNase IV
, maturation factor 1
, maturation factor-1
, 5' nuclease xFEN1a
, flap endonuclease 1-A
, flap structure-specific endonuclease 1-A