{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,12]],"date-time":"2025-10-12T04:45:16Z","timestamp":1760244316804,"version":"build-2065373602"},"reference-count":42,"publisher":"Springer Science and Business Media LLC","issue":"2","license":[{"start":{"date-parts":[[2025,8,9]],"date-time":"2025-08-09T00:00:00Z","timestamp":1754697600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0"},{"start":{"date-parts":[[2025,8,9]],"date-time":"2025-08-09T00:00:00Z","timestamp":1754697600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0"}],"funder":[{"DOI":"10.13039\/100000865","name":"Bill & Melinda Gates Foundation","doi-asserted-by":"crossref","award":["INV-040070"],"award-info":[{"award-number":["INV-040070"]}],"id":[{"id":"10.13039\/100000865","id-type":"DOI","asserted-by":"crossref"}]},{"DOI":"10.13039\/501100000268","name":"Biotechnology and Biological Sciences Research Council","doi-asserted-by":"publisher","award":["BB\/S007965\/1"],"award-info":[{"award-number":["BB\/S007965\/1"]}],"id":[{"id":"10.13039\/501100000268","id-type":"DOI","asserted-by":"publisher"}]},{"name":"Florey Institute AMR Research Capital Funding","award":["NIHR200636"],"award-info":[{"award-number":["NIHR200636"]}]}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["Biomol NMR Assign"],"published-print":{"date-parts":[[2025,12]]},"abstract":"<jats:title>Abstract<\/jats:title>\n          <jats:p>Flap endonuclease (FEN) enzymes are a group of metallonucleases that have essential roles in DNA repair and the maintenance of genomic resilience. They catalyse hydrolytic cleavage of a phosphodiester bond to remove 5\u2032-flaps present on double-stranded DNA molecules formed during DNA replication. FEN locates a target scissile bond through the structural recognition of a pronounced bend in the double-stranded DNA substrate along with the presence of both a 5\u2032-flap and a 1-nucleotide 3\u2032-flap. FEN enzymes share a common structural architecture and are functionally conserved across all living organisms. In this work, we report the <jats:sup>1<\/jats:sup>H, <jats:sup>15<\/jats:sup>N and <jats:sup>13<\/jats:sup>C backbone resonance assignments of residues 2\u2013349 of FEN from <jats:italic>Plasmodium falciparum<\/jats:italic> (<jats:italic>Pf<\/jats:italic>FEN349) in its substrate-free state. Using heteronuclear multidimensional NMR spectroscopy, 90% of all backbone resonances of <jats:italic>Pf<\/jats:italic>FEN349 were assigned, with 298 backbone amide resonances out of 337 theoretically-detectible resonances (which exclude 10 prolines and the N-terminal glycine) identified in the <jats:sup>1<\/jats:sup>H\u2013<jats:sup>15<\/jats:sup>\u00a0N TROSY spectrum. Prediction of solution secondary structure content from a chemical shift analysis using the TALOS-N webserver is mostly in good agreement with an AlphaFold model of <jats:italic>Pf<\/jats:italic>FEN349. The reported assignments provide a pathway for drug discovery as <jats:italic>Pf<\/jats:italic>FEN349 is a potential target for the development of new inhibitors that could be utilised to control the incidence of malaria across the globe.<\/jats:p>","DOI":"10.1007\/s12104-025-10241-6","type":"journal-article","created":{"date-parts":[[2025,8,9]],"date-time":"2025-08-09T01:26:47Z","timestamp":1754702807000},"page":"235-243","update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["1H, 15N and 13C backbone resonance assignments of flap endonuclease from Plasmodium falciparum"],"prefix":"10.1007","volume":"19","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-6331-4216","authenticated-orcid":false,"given":"Rodolpho","family":"do Aido-Machado","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0009-0000-8292-7800","authenticated-orcid":false,"given":"Nicola J.","family":"Baxter","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-9237-1540","authenticated-orcid":false,"given":"Michelle L.","family":"Rowe","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-2272-9946","authenticated-orcid":false,"given":"Manoj B.","family":"Pohare","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-6738-6647","authenticated-orcid":false,"given":"Srdjan","family":"Vitovski","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-5082-1443","authenticated-orcid":false,"given":"Jon R.","family":"Sayers","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-7402-5492","authenticated-orcid":false,"given":"Jonathan P.","family":"Waltho","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"297","published-online":{"date-parts":[[2025,8,9]]},"reference":[{"key":"10241_CR1","doi-asserted-by":"publisher","first-page":"285","DOI":"10.1042\/BJ20081637","volume":"418","author":"LM Allen","year":"2009","unstructured":"Allen LM, Hodskinson MRG, Sayers JR (2009) Active site substitutions delineate distinct classes of eubacterial flap endonuclease. Biochem J 418:285\u2013292. https:\/\/doi.org\/10.1042\/BJ20081637","journal-title":"Biochem J"},{"key":"10241_CR2","doi-asserted-by":"publisher","first-page":"640","DOI":"10.1038\/nsmb.3241","volume":"23","author":"FA AlMalki","year":"2016","unstructured":"AlMalki FA, Flemming CS, Zhang J, Feng M, Sedelnikova SE, Ceska T, Rafferty JB, Sayers JR, Artymiuk PJ (2016) Direct observation of DNA Threading in flap endonuclease complexes. Nat Struct Mol Biol 23:640\u2013646. https:\/\/doi.org\/10.1038\/nsmb.3241","journal-title":"Nat Struct Mol Biol"},{"key":"10241_CR3","doi-asserted-by":"publisher","first-page":"8357","DOI":"10.1093\/nar\/gkt591","volume":"41","author":"CS Anstey-Gilbert","year":"2013","unstructured":"Anstey-Gilbert CS, Hemsworth GR, Flemming CS, Hodskinson MR, Zhang J, Sedelnikova SE, Stillman TJ, Sayers JR, Artymiuk PJ (2013) The structure of Escherichia coli ExoIX\u2013implications for DNA binding and catalysis in flap endonucleases. Nucleic Acids Res 41:8357\u20138367. https:\/\/doi.org\/10.1093\/nar\/gkt591","journal-title":"Nucleic Acids Res"},{"key":"10241_CR4","doi-asserted-by":"publisher","first-page":"119","DOI":"10.1146\/annurev-biochem-072511-122603","volume":"82","author":"L Balakrishnan","year":"2013","unstructured":"Balakrishnan L, Bambara RA (2013) Flap endonuclease 1. Annu Rev Biochem 82:119\u2013138. https:\/\/doi.org\/10.1146\/annurev-biochem-072511-122603","journal-title":"Annu Rev Biochem"},{"key":"10241_CR5","doi-asserted-by":"publisher","first-page":"400","DOI":"10.1093\/nar\/gki180","volume":"33","author":"CD Bayliss","year":"2005","unstructured":"Bayliss CD, Sweetman WA, Moxon ER (2005) Destabilization of tetranucleotide repeats in Haemophilus influenzae mutants lacking RnaseHI or the Klenow domain of poll. Nucleic Acids Res 33:400\u2013408. https:\/\/doi.org\/10.1093\/nar\/gki180","journal-title":"Nucleic Acids Res"},{"key":"10241_CR6","doi-asserted-by":"publisher","first-page":"5634","DOI":"10.1093\/nar\/gky313","volume":"46","author":"JR Becker","year":"2018","unstructured":"Becker JR, Gallo D, Leung W, Croissant T, Thu YM, Nguyen HD, Starr TK, Brown GW, Bielinsky AK (2018) Flap endonuclease overexpression drives genome instability and DNA damage hypersensitivity in a PCNA-dependent manner. Nucleic Acids Res 46:5634\u20135650. https:\/\/doi.org\/10.1093\/nar\/gky313","journal-title":"Nucleic Acids Res"},{"key":"10241_CR7","doi-asserted-by":"publisher","first-page":"5618","DOI":"10.1093\/nar\/gky293","volume":"46","author":"IA Bennet","year":"2018","unstructured":"Bennet IA, Finger DL, Baxter NJ, Ambrose B, Hounslow AM, Thompson MJ, Exell JC, Nur Nazihah NNB, Craggs TD, Waltho JP, Grasby JA (2018) Regional conformational flexibility couples substrate specificity and scissile phosphate diester selectivity in human flap endonuclease 1. Nucleic Acids Res 46:5618\u20135633. https:\/\/doi.org\/10.1093\/nar\/gky293","journal-title":"Nucleic Acids Res"},{"key":"10241_CR8","doi-asserted-by":"publisher","first-page":"1638","DOI":"10.1126\/science.1130258","volume":"313","author":"DD Boehr","year":"2006","unstructured":"Boehr DD, McElheny D, Dyson HJ, Wright PE (2006) The dynamic energy landscape of dihydrofolate reductase catalysis. Science 313:1638\u20131642. https:\/\/doi.org\/10.1126\/science.1130258","journal-title":"Science"},{"key":"10241_CR9","doi-asserted-by":"publisher","first-page":"669","DOI":"10.1042\/BCJ20240019","volume":"481","author":"EM Brudenell","year":"2024","unstructured":"Brudenell EM, Pohare MB, Zafred D, Phipps J, Hornsby HR, Darby JF, Dai J, Liggett L, Cain KM, Barran PE, de Silva TI, Sayers JR (2024) Efficient overexpression and purification of severe acute respiratory syndrome coronavirus 2 nucleocapsid proteins in Escherichia coli. Biochem J 481:669\u2013682. https:\/\/doi.org\/10.1042\/BCJ20240019","journal-title":"Biochem J"},{"key":"10241_CR10","doi-asserted-by":"publisher","first-page":"4041","DOI":"10.1074\/jbc.R800062200","volume":"284","author":"PMJ Burgers","year":"2009","unstructured":"Burgers PMJ (2009) Polymerase dynamics at the eukaryotic DNA replication fork. J Biol Chem 284:4041\u20134045. https:\/\/doi.org\/10.1074\/jbc.R800062200","journal-title":"J Biol Chem"},{"key":"10241_CR11","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1016\/j.molbiopara.2007.08.008","volume":"157","author":"LJ Casta","year":"2008","unstructured":"Casta LJ, Buguliskis JS, Matsumoto Y, Taraschi TF (2008) Expression and biochemical characterization of the Plasmodium falciparum DNA repair enzyme, flap endonuclease-1 (PfFEN-1). Mol Biochem Parasitol 157:1\u201312. https:\/\/doi.org\/10.1016\/j.molbiopara.2007.08.008","journal-title":"Mol Biochem Parasitol"},{"key":"10241_CR12","doi-asserted-by":"publisher","first-page":"90","DOI":"10.1038\/382090a0","volume":"382","author":"TA Ceska","year":"1996","unstructured":"Ceska TA, Sayers JR, Stier G, Suck D (1996) A helical arch allowing single-stranded DNA to thread through T5 5\u2032-exonuclease. Nature 382:90\u201393. https:\/\/doi.org\/10.1038\/382090a0","journal-title":"Nature"},{"key":"10241_CR13","doi-asserted-by":"publisher","first-page":"8542","DOI":"10.1073\/pnas.082241699","volume":"99","author":"JJ Dervan","year":"2002","unstructured":"Dervan JJ, Feng M, Patel D, Grasby JA, Artymiuk PJ, Ceska TA, Sayers JR (2002) Interactions of mutant and wild-type flap endonucleases with oligonucleotide substrates suggest an alternative model of DNA binding. Proc Natl Acad Sci USA 99:8542\u20138547. https:\/\/doi.org\/10.1073\/pnas.082241699","journal-title":"Proc Natl Acad Sci USA"},{"key":"10241_CR14","doi-asserted-by":"publisher","first-page":"3009","DOI":"10.1111\/j.1365-2958.1992.tb01759.x","volume":"6","author":"A D\u00edaz","year":"1992","unstructured":"D\u00edaz A, Lacks SA, L\u00f3pez P (1992) The 5\u2032 to 3\u2032 exonuclease activity of DNA polymerase I is essential for Streptococcus pneumoniae. Mol Microbiol 6:3009\u20133019. https:\/\/doi.org\/10.1111\/j.1365-2958.1992.tb01759.x","journal-title":"Mol Microbiol"},{"key":"10241_CR15","doi-asserted-by":"publisher","first-page":"450","DOI":"10.1038\/nsmb754","volume":"11","author":"M Feng","year":"2004","unstructured":"Feng M, Patel D, Dervan JJ, Ceska T, Suck D, Haq I, Sayers JR (2004) Roles of divalent metal ions in flap endonuclease-substrate interactions. Nat Struct Mol Biol 11:450\u2013456. https:\/\/doi.org\/10.1038\/nsmb754","journal-title":"Nat Struct Mol Biol"},{"key":"10241_CR16","doi-asserted-by":"publisher","first-page":"256","DOI":"10.1016\/j.molbiopara.2006.08.011","volume":"150","author":"ZP Feng","year":"2006","unstructured":"Feng ZP, Zhang X, Han P, Arora N, Anders RF, Norton RS (2006) Abundance of intrinsically unstructured proteins in P. falciparum and other apicomplexan parasite proteomes. Mol Biochem Parasitol 150:256\u2013267. https:\/\/doi.org\/10.1016\/j.molbiopara.2006.08.011","journal-title":"Mol Biochem Parasitol"},{"key":"10241_CR17","doi-asserted-by":"publisher","first-page":"8575","DOI":"10.1128\/JB.00653-07","volume":"189","author":"S Fukushima","year":"2007","unstructured":"Fukushima S, Itaya M, Kato H, Ogasawara N, Yoshikawa H (2007) Reassessment of the in vivo functions of DNA polymerase I and RNase H in bacterial cell growth. J Bacteriol 189:8575\u20138583. https:\/\/doi.org\/10.1128\/JB.00653-07","journal-title":"J Bacteriol"},{"key":"10241_CR18","doi-asserted-by":"publisher","first-page":"357","DOI":"10.1146\/annurev.biophys.27.1.357","volume":"27","author":"KH Gardner","year":"1998","unstructured":"Gardner KH, Kay LE (1998) The use of 2H, 13C, 15N multidimensional NMR to study the structure and dynamics of proteins. Annu Rev Biophys Biomol Struct 27:357\u2013406. https:\/\/doi.org\/10.1146\/annurev.biophys.27.1.357","journal-title":"Annu Rev Biophys Biomol Struct"},{"key":"10241_CR19","doi-asserted-by":"publisher","first-page":"38","DOI":"10.1073\/pnas.96.1.38","volume":"96","author":"SJ Garforth","year":"1999","unstructured":"Garforth SJ, Ceska TA, Suck D, Sayers JR (1999) Mutagenesis of conserved lysine residues in bacteriophage T5 5\u2032-3\u2032 exonuclease suggests separate mechanisms of endo- and exonucleolytic cleavage. Proc Natl Acad Sci USA 96:38\u201343. https:\/\/doi.org\/10.1073\/pnas.96.1.38","journal-title":"Proc Natl Acad Sci USA"},{"key":"10241_CR20","doi-asserted-by":"publisher","first-page":"2772","DOI":"10.1093\/nar\/29.13.2772","volume":"29","author":"SJ Garforth","year":"2001","unstructured":"Garforth SJ, Patel D, Feng M, Sayers JR (2001) Unusually wide co-factor tolerance in a metalloenzyme; divalent metal ions modulate endo-exonuclease activity in T5 exonuclease. Nucleic Acids Res 29:2772\u20132779. https:\/\/doi.org\/10.1093\/nar\/29.13.2772","journal-title":"Nucleic Acids Res"},{"key":"10241_CR21","doi-asserted-by":"publisher","first-page":"3165","DOI":"10.1093\/nar\/gkaa075","volume":"48","author":"S Ghosh","year":"2020","unstructured":"Ghosh S, Goldgur Y, Shuman S (2020) Mycobacterial DNA polymerase I: activities and crystal structures of the POL domain as apoenzyme and in complex with a DNA primer-template and of the full-length FEN\/EXO\u2013POL enzyme. Nucleic Acids Res 48:3165\u20133180. https:\/\/doi.org\/10.1093\/nar\/gkaa075","journal-title":"Nucleic Acids Res"},{"key":"10241_CR22","doi-asserted-by":"publisher","first-page":"763","DOI":"10.1021\/bi9923151","volume":"39","author":"BM Haltiwanger","year":"2000","unstructured":"Haltiwanger BM, Matsumoto Y, Nicolas E, Dianov GL, Bohr VA, Taraschi TF (2000) DNA base excision repair in human malaria parasites is predominantly by a long-patch pathway. Biochem 39:763\u2013772. https:\/\/doi.org\/10.1021\/bi9923151","journal-title":"Biochem"},{"key":"10241_CR23","doi-asserted-by":"publisher","first-page":"315","DOI":"10.1007\/s10858-012-9611-z","volume":"52","author":"SG Hyberts","year":"2012","unstructured":"Hyberts SG, Milbradt AG, Wagner AB, Arthanari H, Wagner G (2012) Application of iterative soft thresholding for fast reconstruction of NMR data non-uniformly sampled with multidimensional Poisson gap scheduling. J Biomol NMR 52:315\u2013327. https:\/\/doi.org\/10.1007\/s10858-012-9611-z","journal-title":"J Biomol NMR"},{"key":"10241_CR24","doi-asserted-by":"publisher","first-page":"167","DOI":"10.1007\/s10858-012-9698-2","volume":"55","author":"SG Hyberts","year":"2013","unstructured":"Hyberts SG, Robson SA, Wagner G (2013) Exploring signal-to-noise ratio and sensitivity in non-uniformly sampled multi-dimensional NMR spectra. J Biomol NMR 55:167\u2013178. https:\/\/doi.org\/10.1007\/s10858-012-9698-2","journal-title":"J Biomol NMR"},{"key":"10241_CR25","doi-asserted-by":"publisher","first-page":"3341","DOI":"10.1093\/emboj\/16.11.3341","volume":"16","author":"A Klungland","year":"1997","unstructured":"Klungland A, Lindahl T (1997) Second pathway for completion of human DNA base excision-repair: reconstitution with purified proteins and requirement for DNase IV (FEN1). EMBO J 16:3341\u20133348. https:\/\/doi.org\/10.1093\/emboj\/16.11.3341","journal-title":"EMBO J"},{"key":"10241_CR26","doi-asserted-by":"publisher","first-page":"9924","DOI":"10.1073\/pnas.152321699","volume":"99","author":"M Kucherlapati","year":"2002","unstructured":"Kucherlapati M, Yang K, Kuraguchi M, Zhao J, Lia M, Heyer J, Kane MF, Fan K, Russell R, Brown AMC, Kneitz B, Edelmann W, Kolodner RD, Lipkin M, Kucherlapati R (2002) Haploinsufficiency of flap endonuclease (Fen1) leads to rapid tumor progression. Proc Natl Acad Sci USA 99:9924\u20139929. https:\/\/doi.org\/10.1073\/pnas.152321699","journal-title":"Proc Natl Acad Sci USA"},{"key":"10241_CR27","doi-asserted-by":"publisher","first-page":"5346","DOI":"10.1128\/MCB.23.15.5346-5353.2003","volume":"23","author":"E Larsen","year":"2003","unstructured":"Larsen E, Gran C, S\u00e6ther BE, Seeberg E, Klungland A (2003) Proliferation failure and gamma radiation sensitivity of Fen1 null mutant mice at the blastocyst stage. Mol Cell Biol 23:5346\u20135353. https:\/\/doi.org\/10.1128\/MCB.23.15.5346-5353.2003","journal-title":"Mol Cell Biol"},{"key":"10241_CR28","doi-asserted-by":"publisher","first-page":"e1010585","DOI":"10.1371\/journal.pgen.1010585","volume":"19","author":"FC Lowder","year":"2023","unstructured":"Lowder FC, Simmons LA (2023) Bacillus subtilis encodes a discrete flap endonuclease that cleaves RNA-DNA hybrids. PLoS Genet 19:e1010585. https:\/\/doi.org\/10.1371\/journal.pgen.1010585","journal-title":"PLoS Genet"},{"key":"10241_CR30","doi-asserted-by":"publisher","first-page":"1101","DOI":"10.1016\/S0092-8674(00)81310-0","volume":"85","author":"TC Mueser","year":"1996","unstructured":"Mueser TC, Nossal NG, Hyde CC (1996) Structure of bacteriophage T4 RNase H, a 5\u2019 to 3\u2019 RNA-DNA and DNA-DNA exonuclease with sequence similarity to the RAD2 family of eukaryotic proteins. Cell 85:1101\u20131112. https:\/\/doi.org\/10.1016\/S0092-8674(00)81310-0","journal-title":"Cell"},{"key":"10241_CR29","doi-asserted-by":"publisher","first-page":"1191","DOI":"10.1016\/s0021-9258(17)42241-1","volume":"269","author":"RS Murante","year":"1994","unstructured":"Murante RS, Huang L, Turchi JJ, Bambara RA (1994) The calf 5\u2032- to 3\u2032-exonuclease is also an endonuclease with both activities dependent on primers annealed upstream of the point of cleavage. J Biol Chem 269:1191\u20131196. https:\/\/doi.org\/10.1016\/s0021-9258(17)42241-1","journal-title":"J Biol Chem"},{"key":"10241_CR31","doi-asserted-by":"publisher","first-page":"1025","DOI":"10.1016\/S0022-2836(02)00547-8","volume":"320","author":"D Patel","year":"2002","unstructured":"Patel D, Tock MR, Frary E, Feng M, Pickering TJ, Grasby JA, Sayers JR (2002) A conserved tyrosine residue aids ternary complex formation, but not catalysis, in phage T5 flap endonuclease. J Mol Biol 320:1025\u20131035. https:\/\/doi.org\/10.1016\/S0022-2836(02)00547-8","journal-title":"J Mol Biol"},{"key":"10241_CR32","doi-asserted-by":"publisher","first-page":"1189","DOI":"10.1016\/S0022-2836(03)00625-9","volume":"330","author":"MAC Reed","year":"2003","unstructured":"Reed MAC, Hounslow AM, Sze KH, Barsukov IG, Hosszu LLP, Clarke AR, Craven CJ, Waltho JP (2003) Effects of domain dissection on the folding and stability of the 43\u00a0kda protein PGK probed by NMR. J Mol Biol 330:1189\u20131201. https:\/\/doi.org\/10.1016\/S0022-2836(03)00625-9","journal-title":"J Mol Biol"},{"key":"10241_CR33","doi-asserted-by":"publisher","first-page":"227","DOI":"10.1007\/s10858-013-9741-y","volume":"56","author":"Y Shen","year":"2013","unstructured":"Shen Y, Bax A (2013) Protein backbone and sidechain torsion angles predicted from NMR chemical shifts using artificial neural networks. J Biomol NMR 56:227\u2013241. https:\/\/doi.org\/10.1007\/s10858-013-9741-y","journal-title":"J Biomol NMR"},{"key":"10241_CR34","doi-asserted-by":"publisher","first-page":"171","DOI":"10.1016\/S0968-0004(98)01199-2","volume":"23","author":"B Shen","year":"1998","unstructured":"Shen B, Qiu J, Hosfield D, Tainer JA (1998) Flap endonuclease homologs in archaebacteria exist as independent proteins. Trends Biochem Sci 23:171\u2013173. https:\/\/doi.org\/10.1016\/S0968-0004(98)01199-2","journal-title":"Trends Biochem Sci"},{"key":"10241_CR35","doi-asserted-by":"publisher","first-page":"28741","DOI":"10.1074\/jbc.M801264200","volume":"283","author":"K Syson","year":"2008","unstructured":"Syson K, Tomlinson C, Chapados BR, Sayers JR, Tainer JA, Williams NH, Grasby JA (2008) Three metal ions participate in the reaction catalyzed by T5 flap endonuclease. J Biol Chem 283:28741\u201328746. https:\/\/doi.org\/10.1074\/jbc.M801264200","journal-title":"J Biol Chem"},{"key":"10241_CR36","doi-asserted-by":"publisher","first-page":"198","DOI":"10.1016\/j.cell.2011.03.004","volume":"145","author":"SE Tsutakawa","year":"2011","unstructured":"Tsutakawa SE, Classen S, Chapados BR, Arvai AS, Finger LD, Guenther G, Tomlinson CG, Thompson P, Sarker AH, Shen B, Cooper PK, Grasby JA, Tainer JA (2011) Human flap endonuclease structures, DNA double-base flipping, and a unified Understanding of the FEN1 superfamily. Cell 145:198\u2013211. https:\/\/doi.org\/10.1016\/j.cell.2011.03.004","journal-title":"Cell"},{"key":"10241_CR37","doi-asserted-by":"publisher","first-page":"D439","DOI":"10.1093\/nar\/gkab1061","volume":"50","author":"M Varadi","year":"2022","unstructured":"Varadi M, Anyango S, Deshpande M, Nair S, Natassia C, Yordanova G, Yuan D, Stroe O, Wood G, Laydon A, Z\u00eddek A, Green T, Tunyasuvunakool K, Petersen S, Jumper J, Clancy E, Green R, Vora A, Lutfi M, Velankar S (2022) AlphaFold protein structure database: massively expanding the structural coverage of protein-sequence space with high-accuracy models. Nucleic Acids Res 50:D439\u2013D444. https:\/\/doi.org\/10.1093\/nar\/gkab1061","journal-title":"Nucleic Acids Res"},{"key":"10241_CR38","doi-asserted-by":"publisher","first-page":"D368","DOI":"10.1093\/nar\/gkad1011","volume":"52","author":"M Varadi","year":"2024","unstructured":"Varadi M, Bertoni D, Magana P, Paramval U, Pidruchna I, Radhakrishnan M, Tsenkov M, Nair S, Mirdita M, Yeo J, Kovalevskiy O, Tunyasuvunakool K, Laydon A, \u017d\u00eddek A, Tomlinson H, Hariharan D, Abrahamson J, Green T, Jumper J, Velankar S (2024) AlphaFold protein structure database in 2024: providing structure coverage for over 214 million protein sequences. Nucleic Acids Res 52:D368\u2013D375. https:\/\/doi.org\/10.1093\/nar\/gkad1011","journal-title":"Nucleic Acids Res"},{"key":"10241_CR39","doi-asserted-by":"publisher","first-page":"34","DOI":"10.1016\/j.jmb.2007.04.063","volume":"371","author":"R Williams","year":"2007","unstructured":"Williams R, Sengerov\u00e1 B, Osborne S, Syson K, Ault S, Kilgour A, Chapados BR, Tainer JA, Sayers JR, Grasby JA (2007) Comparison of the catalytic parameters and reaction specificities of a phage and an archaeal flap endonuclease. J Mol Biol 371:34\u201348. https:\/\/doi.org\/10.1016\/j.jmb.2007.04.063","journal-title":"J Mol Biol"},{"key":"10241_CR40","doi-asserted-by":"publisher","first-page":"11315","DOI":"10.1093\/nar\/gky911","volume":"46","author":"H Xu","year":"2018","unstructured":"Xu H, Shi R, Han W, Cheng J, Xu X, Cheng K, Wang L, Tian B, Zheng L, Shen B, Hua Y (2018) Structural basis of 5\u2032 flap recognition and protein\u2013protein interactions of human flap endonuclease 1. Nucleic Acids Res 46:11315\u201311325. https:\/\/doi.org\/10.1093\/nar\/gky911","journal-title":"Nucleic Acids Res"},{"key":"10241_CR41","doi-asserted-by":"publisher","first-page":"83","DOI":"10.1038\/sj.embor.7400313","volume":"6","author":"L Zheng","year":"2005","unstructured":"Zheng L, Zhou M, Chai Q, Parrish J, Xue D, Patrick SM, Turchi JJ, Yannone SM, Chen D, Shen B (2005) Novel function of the flap endonuclease 1 complex in processing stalled DNA replication forks. EMBO Rep 6:83\u201389. https:\/\/doi.org\/10.1038\/sj.embor.7400313","journal-title":"EMBO Rep"},{"key":"10241_CR42","doi-asserted-by":"publisher","first-page":"781","DOI":"10.1093\/nar\/gkq884","volume":"39","author":"L Zheng","year":"2011","unstructured":"Zheng L, Jia J, Finger LD, Guo Z, Zer C, Shen B (2011) Functional regulation of FEN1 nuclease and its link to cancer. Nucleic Acids Res 39:781\u2013794. https:\/\/doi.org\/10.1093\/nar\/gkq884","journal-title":"Nucleic Acids Res"}],"container-title":["Biomolecular NMR Assignments"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1007\/s12104-025-10241-6.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/link.springer.com\/article\/10.1007\/s12104-025-10241-6\/fulltext.html","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1007\/s12104-025-10241-6.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,11]],"date-time":"2025-10-11T01:18:58Z","timestamp":1760145538000},"score":1,"resource":{"primary":{"URL":"https:\/\/link.springer.com\/10.1007\/s12104-025-10241-6"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2025,8,9]]},"references-count":42,"journal-issue":{"issue":"2","published-print":{"date-parts":[[2025,12]]}},"alternative-id":["10241"],"URL":"https:\/\/doi.org\/10.1007\/s12104-025-10241-6","relation":{},"ISSN":["1874-2718","1874-270X"],"issn-type":[{"type":"print","value":"1874-2718"},{"type":"electronic","value":"1874-270X"}],"subject":[],"published":{"date-parts":[[2025,8,9]]},"assertion":[{"value":"27 May 2025","order":1,"name":"received","label":"Received","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"9 July 2025","order":2,"name":"accepted","label":"Accepted","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"9 August 2025","order":3,"name":"first_online","label":"First Online","group":{"name":"ArticleHistory","label":"Article History"}},{"order":1,"name":"Ethics","group":{"name":"EthicsHeading","label":"Declarations"}},{"value":"The authors declare no competing interests.","order":2,"name":"Ethics","group":{"name":"EthicsHeading","label":"Competing interests"}}]}}