{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,8]],"date-time":"2026-10-08T01:34:58Z","timestamp":1791423298903,"version":"4.3.3"},"reference-count":30,"publisher":"Springer Science and Business Media LLC","issue":"7112","license":[{"start":{"date-parts":[[2006,9,10]],"date-time":"2006-09-10T00:00:00Z","timestamp":1157846400000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/www.springer.com\/tdm"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Nature"],"published-print":{"date-parts":[[2006,10]]},"DOI":"10.1038\/nature05164","type":"journal-article","created":{"date-parts":[[2006,9,10]],"date-time":"2006-09-10T13:12:27Z","timestamp":1157893947000},"page":"713-716","source":"Crossref","is-referenced-by-count":358,"title":["The neurodegenerative disease protein aprataxin resolves abortive DNA ligation intermediates"],"prefix":"10.1038","volume":"443","author":[{"given":"Ivan","family":"Ahel","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ulrich","family":"Rass","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sherif F.","family":"El-Khamisy","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sachin","family":"Katyal","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Paula M.","family":"Clements","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Peter J.","family":"McKinnon","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Keith W.","family":"Caldecott","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Stephen C.","family":"West","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2006,9,10]]},"reference":[{"key":"BFnature05164_CR1","doi-asserted-by":"publisher","first-page":"184","DOI":"10.1038\/ng1001-184","volume":"29","author":"H Date","year":"2001","unstructured":"Date, H. et al. Early-onset ataxia with ocular motor apraxia and hypoalbuminemia is caused by mutations in a new HIT superfamily gene. Nature Genet. 29, 184\u2013188 (2001)","journal-title":"Nature Genet."},{"key":"BFnature05164_CR2","doi-asserted-by":"publisher","first-page":"189","DOI":"10.1038\/ng1001-189","volume":"29","author":"MC Moreira","year":"2001","unstructured":"Moreira, M. C. et al. The gene mutated in ataxia-ocular apraxia 1 encodes the new HIT\/Zn-finger protein aprataxin. Nature Genet. 29, 189\u2013193 (2001)","journal-title":"Nature Genet."},{"key":"BFnature05164_CR3","doi-asserted-by":"publisher","first-page":"9003","DOI":"10.1021\/bi025942q","volume":"41","author":"C Brenner","year":"2002","unstructured":"Brenner, C. Hint, Fhit, and GalT: Function, structure, evolution and mechanism of three branches of the histidine triad superfamily of nucleotide hydrolases and transferases. Biochemistry 41, 9003\u20139014 (2002)","journal-title":"Biochemistry"},{"key":"BFnature05164_CR4","doi-asserted-by":"publisher","first-page":"1493","DOI":"10.1016\/j.dnarep.2004.06.017","volume":"3","author":"PM Clements","year":"2004","unstructured":"Clements, P. M. et al. The ataxia-oculomotor apraxia 1 gene product has a role distinct from ATM and interacts with the DNA strand break repair proteins XRCC1 and XRCC4. DNA Repair (Amst.) 3, 1493\u20131502 (2004)","journal-title":"DNA Repair (Amst.)"},{"key":"BFnature05164_CR5","doi-asserted-by":"publisher","first-page":"1081","DOI":"10.1093\/hmg\/ddh122","volume":"13","author":"N Gueven","year":"2004","unstructured":"Gueven, N. et al. Aprataxin, a novel protein that protects against genotoxic stress. Hum. Mol. Genet. 13, 1081\u20131093 (2004)","journal-title":"Hum. Mol. Genet."},{"key":"BFnature05164_CR6","doi-asserted-by":"publisher","first-page":"241","DOI":"10.1002\/ana.10808","volume":"55","author":"Y Sano","year":"2004","unstructured":"Sano, Y. et al. Aprataxin, the causative protein for EAOH is a nuclear protein with a potential role as a DNA repair protein. Ann. Neurol. 55, 241\u2013249 (2004)","journal-title":"Ann. Neurol."},{"key":"BFnature05164_CR7","doi-asserted-by":"publisher","first-page":"8356","DOI":"10.1128\/MCB.24.19.8356-8365.2004","volume":"24","author":"H Luo","year":"2004","unstructured":"Luo, H. et al. A new XRCC1-containing complex and its role in cellular survival of methyl methanesulfonate treatment. Mol. Cell. Biol. 24, 8356\u20138365 (2004)","journal-title":"Mol. Cell. Biol."},{"key":"BFnature05164_CR8","doi-asserted-by":"publisher","first-page":"485","DOI":"10.1007\/s00018-004-4441-0","volume":"62","author":"P Mosesso","year":"2005","unstructured":"Mosesso, P. et al. The novel human gene aprataxin is directly involved in DNA single-strand break repair. Cell. Mol. Life Sci. 62, 485\u2013491 (2005)","journal-title":"Cell. Mol. Life Sci."},{"key":"BFnature05164_CR9","doi-asserted-by":"publisher","first-page":"687","DOI":"10.1021\/cr040498d","volume":"106","author":"AE Tomkinson","year":"2006","unstructured":"Tomkinson, A. E., Vijayakumar, S., Pascal, J. M. & Ellenberger, T. DNA ligases: structure, reaction mechanism and function. Chem. Rev. 106, 687\u2013699 (2006)","journal-title":"Chem. Rev."},{"key":"BFnature05164_CR10","doi-asserted-by":"publisher","first-page":"13939","DOI":"10.1074\/jbc.M507946200","volume":"281","author":"AW Kijas","year":"2006","unstructured":"Kijas, A. W., Harris, J. L., Harris, J. M. & Lavin, M. F. Aprataxin forms a discrete branch in the HIT (histidine triad) superfamily of proteins with both DNA\/RNA binding and nucleotide hydrolase activities. J. Biol. Chem. 281, 13939\u201313948 (2006)","journal-title":"J. Biol. Chem."},{"key":"BFnature05164_CR11","doi-asserted-by":"publisher","first-page":"10852","DOI":"10.1074\/jbc.M111480200","volume":"277","author":"P Bieganowski","year":"2002","unstructured":"Bieganowski, P. et al. Adenosine monophosphoramidase activity of Hint and Hnt1 supports function of Kin28, Ccl1, and Tfb3. J. Biol. Chem. 277, 10852\u201310860 (2002)","journal-title":"J. Biol. Chem."},{"key":"BFnature05164_CR12","doi-asserted-by":"publisher","first-page":"231","DOI":"10.1038\/nsb0397-231","volume":"4","author":"C Brenner","year":"1997","unstructured":"Brenner, C. et al. Crystal structures of Hint demonstrate that histidine triad proteins are GalT-related nucleotide-binding proteins. Nature Struct. Biol. 4, 231\u2013238 (1997)","journal-title":"Nature Struct. Biol."},{"key":"BFnature05164_CR13","doi-asserted-by":"publisher","first-page":"18711","DOI":"10.1074\/jbc.M314271200","volume":"279","author":"A Krakowiak","year":"2004","unstructured":"Krakowiak, A. et al. Biochemical, crystallographic, and mutagenic characterization of Hint, the AMP-lysine hydrolase, with novel substrates and inhibitors. J. Biol. Chem. 279, 18711\u201318716 (2004)","journal-title":"J. Biol. Chem."},{"key":"BFnature05164_CR14","doi-asserted-by":"publisher","first-page":"11529","DOI":"10.1021\/bi961415t","volume":"35","author":"LD Barnes","year":"1996","unstructured":"Barnes, L. D. et al. Fhit, a putative tumor suppressor in humans, is a dinucleoside 5\u2032,5\u2034-P1,P3-triphosphate hydrolase. Biochemistry 35, 11529\u201311535 (1996)","journal-title":"Biochemistry"},{"key":"BFnature05164_CR15","doi-asserted-by":"publisher","first-page":"286","DOI":"10.1126\/science.278.5336.286","volume":"278","author":"CD Lima","year":"1997","unstructured":"Lima, C. D., Klein, M. G. & Hendrickson, W. A. Structure-based analysis of catalysis and substrate definition in the HIT protein family. Science 278, 286\u2013290 (1997)","journal-title":"Science"},{"key":"BFnature05164_CR16","doi-asserted-by":"publisher","first-page":"4555","DOI":"10.1074\/jbc.275.7.4555","volume":"275","author":"A Draganescu","year":"2000","unstructured":"Draganescu, A., Hodawadekar, S. C., Gee, K. R. & Brenner, C. Fhit-nucleotide specificity probed with novel fluorescent and fluorogenic substrates. J. Biol. Chem. 275, 4555\u20134560 (2000)","journal-title":"J. Biol. Chem."},{"key":"BFnature05164_CR17","doi-asserted-by":"publisher","first-page":"737","DOI":"10.1038\/nature02046","volume":"425","author":"S Ghaemmaghami","year":"2003","unstructured":"Ghaemmaghami, S. et al. Global analysis of protein expression in yeast. Nature 425, 737\u2013741 (2003)","journal-title":"Nature"},{"key":"BFnature05164_CR18","doi-asserted-by":"publisher","first-page":"6437","DOI":"10.1128\/jb.171.12.6437-6445.1989","volume":"171","author":"P Plateau","year":"1989","unstructured":"Plateau, P., Fromant, M., Schmitter, J. M., Buhler, J. M. & Blanquet, S. Isolation, characterization, and inactivation of the Apa1 gene encoding yeast diadenosine 5\u2032,5\u2034-P1,P4-tetraphosphate phosphorylase. J. Bacteriol. 171, 6437\u20136445 (1989)","journal-title":"J. Bacteriol."},{"key":"BFnature05164_CR19","doi-asserted-by":"publisher","first-page":"19095","DOI":"10.1074\/jbc.272.31.19095","volume":"272","author":"ES Henle","year":"1997","unstructured":"Henle, E. S. & Linn, S. Formation, prevention, and repair of DNA damage by iron\/hydrogen peroxide. J. Biol. Chem. 272, 19095\u201319098 (1997)","journal-title":"J. Biol. Chem."},{"key":"BFnature05164_CR20","doi-asserted-by":"publisher","first-page":"1089","DOI":"10.1021\/cr960437i","volume":"98","author":"WK Pogozelski","year":"1998","unstructured":"Pogozelski, W. K. & Tullius, T. D. Oxidative strand scission of nucleic acids: routes initiated by hydrogen abstraction from the sugar moiety. Chem. Rev. 98, 1089\u20131108 (1998)","journal-title":"Chem. Rev."},{"key":"BFnature05164_CR21","first-page":"65","volume-title":"DNA Damage and Repair","author":"JF Ward","year":"1998","unstructured":"Ward, J. F. in DNA Damage and Repair Vol. 2 (eds Nicoloff, J. A. & Hoekstra, M. F.) 65\u201385 (Humana, Totowa, New Jersey, 1998)"},{"key":"BFnature05164_CR22","doi-asserted-by":"publisher","first-page":"17","DOI":"10.1016\/S0092-8674(04)00206-5","volume":"117","author":"JI Loizou","year":"2004","unstructured":"Loizou, J. I. et al. The protein kinase CK2 facilitates repair of chromosomal DNA single-strand breaks. Cell 117, 17\u201328 (2004)","journal-title":"Cell"},{"key":"BFnature05164_CR23","doi-asserted-by":"publisher","first-page":"107","DOI":"10.1016\/S0092-8674(01)00195-7","volume":"104","author":"CJ Whitehouse","year":"2001","unstructured":"Whitehouse, C. J. et al. XRCC1 stimulates human polynucleotide kinase activity at damaged DNA termini and accelerates DNA single-strand break repair. Cell 104, 107\u2013117 (2001)","journal-title":"Cell"},{"key":"BFnature05164_CR24","doi-asserted-by":"publisher","first-page":"7","DOI":"10.1016\/S0092-8674(02)01247-3","volume":"112","author":"KW Caldecott","year":"2003","unstructured":"Caldecott, K. W. DNA single-strand break repair and spinocerebellar ataxia. Cell 112, 7\u201310 (2003)","journal-title":"Cell"},{"key":"BFnature05164_CR25","doi-asserted-by":"publisher","first-page":"20927","DOI":"10.1074\/jbc.M502889200","volume":"280","author":"HF Seidle","year":"2005","unstructured":"Seidle, H. F., Bieganowski, P. & Brenner, C. Disease-associated mutations inactivate AMP-lysine hydrolase activity of Aprataxin. J. Biol. Chem. 280, 20927\u201320931 (2005)","journal-title":"J. Biol. Chem."},{"key":"BFnature05164_CR26","doi-asserted-by":"publisher","first-page":"R262","DOI":"10.1016\/S0960-9822(02)00788-1","volume":"12","author":"DE Barnes","year":"2002","unstructured":"Barnes, D. E. DNA damage: Air-breaks? Curr. Biol. 12, R262\u2013R264 (2002)","journal-title":"Curr. Biol."},{"key":"BFnature05164_CR27","doi-asserted-by":"publisher","first-page":"1395","DOI":"10.1016\/S0960-9822(98)00021-9","volume":"8","author":"DE Barnes","year":"1998","unstructured":"Barnes, D. E., Stamp, G., Rosewell, I., Denzel, A. & Lindahl, T. Targeted disruption of the gene encoding DNA ligase IV leads to lethality in embryonic mice. Curr. Biol. 8, 1395\u20131398 (1998)","journal-title":"Curr. Biol."},{"key":"BFnature05164_CR28","doi-asserted-by":"publisher","first-page":"891","DOI":"10.1016\/S0092-8674(00)81714-6","volume":"95","author":"Y Gao","year":"1998","unstructured":"Gao, Y. et al. A critical role for DNA end-joining proteins in both lymphogenesis and neurogenesis. Cell 95, 891\u2013902 (1998)","journal-title":"Cell"},{"key":"BFnature05164_CR29","doi-asserted-by":"publisher","first-page":"1141","DOI":"10.1016\/j.dnarep.2004.03.009","volume":"3","author":"CW Abner","year":"2004","unstructured":"Abner, C. W. & McKinnon, P. J. The DNA double-strand break response in the nervous system. DNA Repair (Amst.) 3, 1141\u20131147 (2004)","journal-title":"DNA Repair (Amst.)"},{"key":"BFnature05164_CR30","doi-asserted-by":"publisher","first-page":"108","DOI":"10.1038\/nature03314","volume":"434","author":"SF El Khamisy","year":"2005","unstructured":"El Khamisy, S. F. et al. Defective DNA single-strand break repair in spinocerebellar ataxia with axonal neuropathy-1. Nature 434, 108\u2013113 (2005)","journal-title":"Nature"}],"container-title":["Nature"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/www.nature.com\/articles\/nature05164.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"http:\/\/www.nature.com\/articles\/nature05164","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"http:\/\/www.nature.com\/articles\/nature05164.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2023,5,18]],"date-time":"2023-05-18T13:59:05Z","timestamp":1684418345000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.nature.com\/articles\/nature05164"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2006,9,10]]},"references-count":30,"journal-issue":{"issue":"7112","published-print":{"date-parts":[[2006,10]]}},"alternative-id":["BFnature05164"],"URL":"https:\/\/doi.org\/10.1038\/nature05164","relation":{"has-review":[{"id-type":"doi","id":"10.3410\/f.1047303.497241","asserted-by":"object"},{"id-type":"doi","id":"10.3410\/f.1047303.496420","asserted-by":"object"},{"id-type":"doi","id":"10.3410\/f.1047303.516637","asserted-by":"object"}]},"ISSN":["0028-0836","1476-4687"],"issn-type":[{"value":"0028-0836","type":"print"},{"value":"1476-4687","type":"electronic"}],"subject":[],"published":{"date-parts":[[2006,9,10]]}}}