{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,21]],"date-time":"2026-05-21T04:44:51Z","timestamp":1779338691950,"version":"3.51.4"},"reference-count":51,"publisher":"Oxford University Press (OUP)","issue":"10","license":[{"start":{"date-parts":[[2024,5,14]],"date-time":"2024-05-14T00:00:00Z","timestamp":1715644800000},"content-version":"vor","delay-in-days":30,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"Association Fran\u00e7aise Contre les Myopathies T\u00e9l\u00e9thon","award":["24167"],"award-info":[{"award-number":["24167"]}]},{"name":"Association Fran\u00e7aise Contre les Myopathies T\u00e9l\u00e9thon","award":["25052"],"award-info":[{"award-number":["25052"]}]},{"DOI":"10.13039\/501100004359","name":"Swedish Research Council","doi-asserted-by":"publisher","award":["2021-00932"],"award-info":[{"award-number":["2021-00932"]}],"id":[{"id":"10.13039\/501100004359","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100012538","name":"Swedish Cancer Foundation","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100012538","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100004063","name":"Knut and Alice Wallenberg Foundation","doi-asserted-by":"publisher","award":["2017.0080"],"award-info":[{"award-number":["2017.0080"]}],"id":[{"id":"10.13039\/501100004063","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100004063","name":"Knut and Alice Wallenberg Foundation","doi-asserted-by":"publisher","award":["2018.0204"],"award-info":[{"award-number":["2018.0204"]}],"id":[{"id":"10.13039\/501100004063","id-type":"DOI","asserted-by":"publisher"}]},{"name":"Spanish Ministry of Science","award":["MCIN\/AEI\/10.13039\/501100011033"],"award-info":[{"award-number":["MCIN\/AEI\/10.13039\/501100011033"]}]},{"DOI":"10.13039\/501100008530","name":"European Regional Development Fund","doi-asserted-by":"publisher","award":["PID2021-129038NB-I00"],"award-info":[{"award-number":["PID2021-129038NB-I00"]}],"id":[{"id":"10.13039\/501100008530","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100002809","name":"Generalitat de Catalunya","doi-asserted-by":"publisher","award":["2021_SGR-00425"],"award-info":[{"award-number":["2021_SGR-00425"]}],"id":[{"id":"10.13039\/501100002809","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100011658","name":"French Infrastructure for Integrated Structural Biology","doi-asserted-by":"publisher","award":["ANR-10-INBS-05"],"award-info":[{"award-number":["ANR-10-INBS-05"]}],"id":[{"id":"10.13039\/501100011658","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2024,6,10]]},"abstract":"<jats:title>Abstract<\/jats:title>\n               <jats:p>Mitochondrial single-stranded DNA-binding protein (mtSSB) is essential for mitochondrial DNA (mtDNA) replication. Recently, several mtSSB variants have been associated with autosomal dominant mitochondrial optic atrophy and retinal dystrophy. Here, we have studied at the molecular level the functional consequences of one of the most severe mtSSB variants, R107Q. We first studied the oligomeric state of this variant and observed that the mtSSBR107Q mutant forms stable tetramers in vitro. On the other hand, we showed, using complementary single-molecule approaches, that mtSSBR107Q displays a lower intramolecular ssDNA compaction ability and a higher ssDNA dissociation rate than the WT protein. Real-time competition experiments for ssDNA-binding showed a marked advantage of mtSSBWT over mtSSBR107Q. Combined, these results show that the R107Q mutation significantly impaired the ssDNA-binding and compacting ability of mtSSB, likely by weakening mtSSB ssDNA wrapping efficiency. These features are in line with our molecular modeling of ssDNA on mtSSB showing that the R107Q mutation may destabilize local interactions and results in an electronegative spot that interrupts an ssDNA-interacting-electropositive patch, thus reducing the potential mtSSB-ssDNA interaction sites.<\/jats:p>","DOI":"10.1093\/nar\/gkae354","type":"journal-article","created":{"date-parts":[[2024,5,14]],"date-time":"2024-05-14T10:46:49Z","timestamp":1715683609000},"page":"5912-5927","source":"Crossref","is-referenced-by-count":2,"title":["The mutation R107Q alters mtSSB ssDNA compaction ability and binding dynamics"],"prefix":"10.1093","volume":"52","author":[{"given":"Martial","family":"Martucci","sequence":"first","affiliation":[{"name":"Universit\u00e9 Clermont Auvergne, CNRS, Laboratoire de Physique de Clermont , F-63000 Clermont-Ferrand , France"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-1700-3999","authenticated-orcid":false,"given":"Amandine","family":"Moretton","sequence":"additional","affiliation":[{"name":"Universit\u00e9 Clermont Auvergne, CNRS, Laboratoire de Physique de Clermont , F-63000 Clermont-Ferrand , France"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Aleix","family":"Tarr\u00e9s-Sol\u00e9","sequence":"additional","affiliation":[{"name":"Structural MitoLab, Molecular Biology Institute Barcelona (IBMB-CSIC), Barcelona Science Park , Barcelona 08028 , Spain"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Virginie","family":"Ropars","sequence":"additional","affiliation":[{"name":"Universit\u00e9 Paris-Saclay, CEA, CNRS, Institute for Integrative Biology of the Cell (I2BC) , 91198 Gif-sur-Yvette , France"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Louise","family":"Lambert","sequence":"additional","affiliation":[{"name":"Universit\u00e9 Clermont Auvergne, CNRS, Laboratoire de Physique de Clermont , F-63000 Clermont-Ferrand , France"},{"name":"Department of Medical Biochemistry and Cell Biology, University of Gothenburg , P.O. Box 440 , SE-405 30 Gothenburg , Sweden"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Patrick","family":"Vernet","sequence":"additional","affiliation":[{"name":"Universit\u00e9 Clermont Auvergne, CNRS, Laboratoire de Physique de Clermont , F-63000 Clermont-Ferrand , France"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-8713-173X","authenticated-orcid":false,"given":"Maria","family":"Sol\u00e0","sequence":"additional","affiliation":[{"name":"Structural MitoLab, Molecular Biology Institute Barcelona (IBMB-CSIC), Barcelona Science Park , Barcelona 08028 , Spain"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Maria","family":"Falkenberg","sequence":"additional","affiliation":[{"name":"Department of Medical Biochemistry and Cell Biology, University of Gothenburg , P.O. Box 440 , SE-405 30 Gothenburg , Sweden"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-1054-4274","authenticated-orcid":false,"given":"Geraldine","family":"Farge","sequence":"additional","affiliation":[{"name":"Universit\u00e9 Clermont Auvergne, CNRS, Laboratoire de Physique de Clermont , F-63000 Clermont-Ferrand , France"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Siet","family":"van\u00a0den\u00a0Wildenberg","sequence":"additional","affiliation":[{"name":"Universit\u00e9 Clermont Auvergne, CNRS, Laboratoire de Physique de Clermont , F-63000 Clermont-Ferrand , France"},{"name":"Universit\u00e9 Clermont Auvergne, CNRS, IRD, Universit\u00e9 Jean Monnet Saint Etienne, LMV , F-63000 Clermont-Ferrand , France"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"286","published-online":{"date-parts":[[2024,4,14]]},"reference":[{"key":"2024061000021712900_B1","doi-asserted-by":"crossref","first-page":"17047","DOI":"10.1074\/jbc.M400283200","article-title":"Physiological and biochemical defects in functional interactions of mitochondrial DNA polymerase and DNA-binding mutants of single-stranded DNA-binding protein","volume":"279","author":"Farr","year":"2004","journal-title":"J. Biol. Chem."},{"key":"2024061000021712900_B2","doi-asserted-by":"crossref","first-page":"e1004832","DOI":"10.1371\/journal.pgen.1004832","article-title":"In vivo occupancy of mitochondrial single-stranded DNA binding protein supports the strand displacement mode of DNA replication","volume":"10","author":"Miralles\u00a0Fust\u00e9","year":"2014","journal-title":"PLos Genet."},{"key":"2024061000021712900_B3","doi-asserted-by":"crossref","first-page":"860","DOI":"10.1074\/jbc.270.2.860","article-title":"Stimulation of drosophila mitochondrial DNA polymerase by single-stranded DNA-binding protein","volume":"270","author":"Williams","year":"1995","journal-title":"J. Biol. Chem."},{"key":"2024061000021712900_B4","doi-asserted-by":"crossref","first-page":"48627","DOI":"10.1074\/jbc.M306981200","article-title":"TWINKLE has 5\u2032 \u2192 3\u2032 DNA helicase activity and is specifically stimulated by mitochondrial single-stranded DNA-binding protein","volume":"278","author":"Korhonen","year":"2003","journal-title":"J. Biol. Chem."},{"key":"2024061000021712900_B5","doi-asserted-by":"crossref","first-page":"721864","DOI":"10.3389\/fgene.2021.721864","article-title":"Physical and functional interaction of mitochondrial single-stranded DNA-binding protein and the catalytic subunit of DNA polymerase gamma","volume":"12","author":"Ciesielski","year":"2021","journal-title":"Front. Genet."},{"key":"2024061000021712900_B6","doi-asserted-by":"crossref","first-page":"2423","DOI":"10.1038\/sj.emboj.7600257","article-title":"Reconstitution of a minimal mtDNA replisome in vitro","volume":"23","author":"Korhonen","year":"2004","journal-title":"EMBO J."},{"key":"2024061000021712900_B7","doi-asserted-by":"crossref","first-page":"1750","DOI":"10.1093\/nar\/gkad037","article-title":"Mechanism of strand displacement DNA synthesis by the coordinated activities of human mitochondrial DNA polymerase and SSB","volume":"51","author":"Plaza-G.a","year":"2023","journal-title":"Nucleic Acids Res."},{"key":"2024061000021712900_B8","doi-asserted-by":"crossref","first-page":"eabf8631","DOI":"10.1126\/sciadv.abf8631","article-title":"The mitochondrial single-stranded DNA binding protein is essential for initiation of mtDNA replication","volume":"7","author":"Jiang","year":"2021","journal-title":"Sci. Adv."},{"key":"2024061000021712900_B9","doi-asserted-by":"crossref","first-page":"671","DOI":"10.1093\/abbs\/gmw044","article-title":"Human single-stranded DNA binding proteins: guardians of genome stability","volume":"48","author":"Wu","year":"2016","journal-title":"Acta Biochim. Biophy. Sin."},{"key":"2024061000021712900_B10","doi-asserted-by":"crossref","first-page":"435","DOI":"10.1111\/j.1432-1033.1994.tb18756.x","article-title":"Single-stranded-DNA-binding proteins from human mitochondria and Escherichia coli have analogous physicochemical properties","volume":"221","author":"Curth","year":"1994","journal-title":"Eur. J. Biochem."},{"key":"2024061000021712900_B11","doi-asserted-by":"crossref","first-page":"6652","DOI":"10.1073\/pnas.94.13.6652","article-title":"Crystal structure of the homo-tetrameric DNA binding domain of Escherichia coli single-stranded DNA-binding protein determined by multiwavelength x-ray diffraction on the selenomethionyl protein at 2.9-\u00c5 resolution","volume":"94","author":"Raghunathan","year":"1997","journal-title":"Natl. Acad. Sci."},{"key":"2024061000021712900_B12","doi-asserted-by":"crossref","first-page":"269","DOI":"10.1016\/j.jmb.2012.04.021","article-title":"Plasmodium falciparum SSB tetramer wraps single stranded DNA with similar topology but opposite polarity to E. coli SSB","volume":"420","author":"Antony","year":"2012","journal-title":"J. Mol. Biol."},{"key":"2024061000021712900_B13","first-page":"153","article-title":"Crystal structure of human mitochondrial single-stranded DNA binding protein at 2.4 A resolution","volume":"4","author":"Yang","year":"1997","journal-title":"Nature"},{"key":"2024061000021712900_B14","doi-asserted-by":"crossref","first-page":"143","DOI":"10.1172\/JCI128513","article-title":"Dominant mutations in mtDNA maintenance gene SSBP1 cause optic atrophy and foveopathy","volume":"130","author":"Piro-M\u00e9gy","year":"2020","journal-title":"J. Clin. Invest."},{"key":"2024061000021712900_B15","doi-asserted-by":"crossref","first-page":"13068","DOI":"10.1074\/jbc.M117.791392","article-title":"The human mitochondrial single-stranded DNA-binding protein displays distinct kinetics and thermodynamics of DNA binding and exchange","volume":"292","author":"Qian","year":"2017","journal-title":"J. Biol. Chem."},{"key":"2024061000021712900_B16","doi-asserted-by":"crossref","first-page":"1532","DOI":"10.1093\/nar\/gkaa1267","article-title":"Multiprotein E. coli SSB-ssDNA complex shows both stable binding and rapid dissociation due to interprotein interactions","volume":"49","author":"Naufer","year":"2021","journal-title":"Nucleic Acids Res."},{"key":"2024061000021712900_B17","doi-asserted-by":"crossref","first-page":"3594","DOI":"10.1016\/S0021-9258(19)83663-3","article-title":"Two binding modes in Escherichia coli single strand binding protein-single stranded DNA complexes. Modulation by NaCl concentration","volume":"260","author":"Lohman","year":"1985","journal-title":"J. Biol. Chem."},{"key":"2024061000021712900_B18","doi-asserted-by":"crossref","first-page":"2260","DOI":"10.1021\/bi00407a002","article-title":"Negative cooperativity within individual tetramers of Escherichia coli single strand binding protein is responsible for the transition between the (SSB)35 and (SSB)56 DNA binding modes","volume":"27","author":"Lohman","year":"1988","journal-title":"Biochemistry"},{"key":"2024061000021712900_B19","doi-asserted-by":"crossref","first-page":"1092","DOI":"10.1038\/nature08442","article-title":"SSB protein diffusion on single-stranded DNA stimulates RecA filament formation","volume":"461","author":"Roy","year":"2009","journal-title":"Nature"},{"key":"2024061000021712900_B20","doi-asserted-by":"crossref","first-page":"222","DOI":"10.1016\/j.cell.2011.06.036","article-title":"SSB functions as a sliding platform that migrates on DNA via reptation","volume":"146","author":"Zhou","year":"2011","journal-title":"Cell"},{"key":"2024061000021712900_B21","doi-asserted-by":"crossref","first-page":"102","DOI":"10.1016\/j.semcdb.2018.03.017","article-title":"Dynamics of E. coli single stranded DNA binding (SSB) protein-DNA complexes","volume":"86","author":"Antony","year":"2019","journal-title":"Semin. Cell Dev. Biol."},{"key":"2024061000021712900_B22","doi-asserted-by":"crossref","first-page":"2413","DOI":"10.1016\/j.jmb.2014.04.023","article-title":"Ultrafast redistribution of E. coli SSB along long single-stranded DNA via intersegment transfer","volume":"426","author":"Lee","year":"2014","journal-title":"J. Mol. Biol."},{"key":"2024061000021712900_B23","doi-asserted-by":"crossref","first-page":"6540","DOI":"10.1093\/nar\/gkad485","article-title":"Regulation of T7 gp2. 5 binding dynamics by its C-terminal tail, template conformation and sequence","volume":"51","author":"Xu","year":"2023","journal-title":"Nucleic Acids Res."},{"key":"2024061000021712900_B24","doi-asserted-by":"crossref","first-page":"7237","DOI":"10.1093\/nar\/gkx395","article-title":"DNA synthesis determines the binding mode of the human mitochondrial single-stranded DNA-binding protein","volume":"45","author":"Morin","year":"2017","journal-title":"Nucleic Acids Res."},{"key":"2024061000021712900_B25","doi-asserted-by":"crossref","first-page":"1373","DOI":"10.1073\/pnas.1318001111","article-title":"Structural mechanisms of PriA-mediated DNA replication restart","volume":"111","author":"Bhattacharyya","year":"2014","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"2024061000021712900_B26","doi-asserted-by":"crossref","first-page":"17569","DOI":"10.1074\/jbc.M113.478156","article-title":"PriC-mediated DNA replication restart requires PriC complex formation with the single-stranded DNA-binding protein","volume":"288","author":"Wessel","year":"2013","journal-title":"J. Biol. Chem."},{"key":"2024061000021712900_B27","doi-asserted-by":"crossref","first-page":"11878","DOI":"10.1093\/nar\/gkx939","article-title":"RecQ helicase triggers a binding mode change in the SSB\u2013DNA complex to efficiently initiate DNA unwinding","volume":"45","author":"Mills","year":"2017","journal-title":"Nucleic Acids Res."},{"key":"2024061000021712900_B28","doi-asserted-by":"crossref","first-page":"553","DOI":"10.1101\/SQB.1984.049.01.062","article-title":"Visualization of SSB-ssDNA complexes active in the assembly of stable RecA-DNA filaments","volume":"49","author":"Griffith","year":"1984","journal-title":"Cold Spring Harb. Symp. Quant. Biol."},{"key":"2024061000021712900_B29","doi-asserted-by":"crossref","first-page":"e58","DOI":"10.1093\/nar\/gkm147","article-title":"High-resolution AFM imaging of single-stranded DNA-binding (SSB) protein\u2013DNA complexes","volume":"35","author":"Hamon","year":"2007","journal-title":"Nucleic Acids Res."},{"key":"2024061000021712900_B30","doi-asserted-by":"crossref","first-page":"e08646","DOI":"10.7554\/eLife.08646","article-title":"Imaging and energetics of single SSB-ssDNA molecules reveal intramolecular condensation and insight into RecOR function","volume":"4","author":"Bell","year":"2015","journal-title":"eLife"},{"key":"2024061000021712900_B31","doi-asserted-by":"crossref","first-page":"e08193","DOI":"10.7554\/eLife.08193","article-title":"Structural dynamics of E. Coli singlestranded DNA binding protein reveal DNA wrapping and unwrapping pathways","volume":"4","author":"Suksombat","year":"2015","journal-title":"eLife"},{"key":"2024061000021712900_B32","doi-asserted-by":"crossref","first-page":"108","DOI":"10.1172\/JCI128514","article-title":"SSBP1 mutations cause mtDNA depletion underlying a complex optic atrophy disorder","volume":"130","author":"Del\u00a0Dotto","year":"2020","journal-title":"J. Clin. Invest."},{"key":"2024061000021712900_B33","doi-asserted-by":"crossref","first-page":"368","DOI":"10.1002\/ana.25550","article-title":"SSBP1 mutations in dominant optic atrophy with variable retinal degeneration","volume":"86","author":"Jurkute","year":"2019","journal-title":"Ann. Neurol."},{"key":"2024061000021712900_B34","doi-asserted-by":"crossref","first-page":"12","DOI":"10.1167\/iovs.62.15.12","article-title":"SSBP1-Disease update: expanding the genetic and clinical spectrum, reporting variable penetrance and confirming recessive inheritance","volume":"62","author":"Jurkute","year":"2021","journal-title":"Invest. Ophthalmol. Vis. Sci."},{"key":"2024061000021712900_B35","doi-asserted-by":"crossref","first-page":"e0221829","DOI":"10.1371\/journal.pone.0221829","article-title":"Mitochondrial single-stranded DNA binding protein novel de novo SSBP1 mutation in a child with single large-scale mtDNA deletion (SLSMD) clinically manifesting as Pearson, Kearns-Sayre, and Leigh syndromes","volume":"14","author":"Gustafson","year":"2019","journal-title":"PLoS One"},{"key":"2024061000021712900_B36","doi-asserted-by":"crossref","first-page":"103212","DOI":"10.1016\/j.dnarep.2021.103212","article-title":"Mechanisms of SSBP1 variants in mitochondrial disease: molecular dynamics simulations reveal stable tetramers with altered DNA binding surfaces","volume":"107","author":"Gustafson","year":"2021","journal-title":"DNA Repair (Amst.)"},{"key":"2024061000021712900_B37","doi-asserted-by":"crossref","first-page":"103212","DOI":"10.1016\/j.dnarep.2021.103212","article-title":"Mechanisms of SSBP1 variants in mitochondrial disease: molecular dynamics simulations reveal stable tetramers with altered DNA binding surfaces","volume":"107","author":"Gustafson","year":"2021","journal-title":"DNA Repair (Amst.)"},{"key":"2024061000021712900_B38","doi-asserted-by":"crossref","first-page":"427","DOI":"10.1016\/S0076-6879(10)75017-5","article-title":"Combining optical tweezers, single-molecule fluorescence microscopy, and microfluidics for studies of DNA-protein interactions","volume":"475","author":"Gross","year":"2010","journal-title":"Methods Enzymol."},{"key":"2024061000021712900_B39","doi-asserted-by":"crossref","first-page":"121","DOI":"10.1007\/978-1-0716-2922-2_10","article-title":"How to quantify DNA compaction by TFAM with acoustic force spectroscopy and total internal reflection fluorescence microscopy","volume":"2615","author":"Martucci","year":"2023","journal-title":"Methods Mol. Biol."},{"key":"2024061000021712900_B40","doi-asserted-by":"crossref","first-page":"795","DOI":"10.1126\/science.271.5250.795","article-title":"Overstretching B-DNA: the elastic response of individual double-stranded and single-stranded DNA molecules","volume":"271","author":"Smith","year":"1996","journal-title":"Science"},{"key":"2024061000021712900_B41","doi-asserted-by":"crossref","first-page":"486","DOI":"10.1107\/S0907444910007493","article-title":"Features and development of Coot","volume":"66","author":"Emsley","year":"2010","journal-title":"Acta. Crystallogr. D Biol. Crystallogr."},{"key":"2024061000021712900_B42","doi-asserted-by":"crossref","first-page":"1605","DOI":"10.1002\/jcc.20084","article-title":"UCSF Chimera\u2013a visualization system for exploratory research and analysis","volume":"25","author":"Pettersen","year":"2004","journal-title":"J. Comput. Chem."},{"key":"2024061000021712900_B43","doi-asserted-by":"crossref","first-page":"1832","DOI":"10.1126\/science.1071152","article-title":"Equilibrium information from nonequilibrium measurements in an experimental test of Jarzynski's equality","volume":"296","author":"Liphardt","year":"2002","journal-title":"Science"},{"key":"2024061000021712900_B44","volume-title":"Biological Physics : Energy, Information, Life","author":"Nelson","year":"2004"},{"key":"2024061000021712900_B45","doi-asserted-by":"crossref","first-page":"1594","DOI":"10.1110\/ps.04634604","article-title":"Sequence-structure mapping errors in the PDB: oB-fold domains","volume":"13","author":"Venclovas","year":"2004","journal-title":"Protein Sci."},{"key":"2024061000021712900_B46","doi-asserted-by":"crossref","first-page":"648","DOI":"10.1038\/77943","article-title":"Structure of the DNA binding domain of E. coli SSB bound to ssDNA","volume":"7","author":"Raghunathan","year":"2000","journal-title":"Nat. Struct. Biol."},{"key":"2024061000021712900_B47","doi-asserted-by":"crossref","first-page":"11287","DOI":"10.1093\/nar\/gky875","article-title":"Single-molecule DREEM imaging reveals DNA wrapping around human mitochondrial single-stranded DNA binding protein","volume":"46","author":"Kaur","year":"2018","journal-title":"Nucleic Acids Res."},{"key":"2024061000021712900_B48","doi-asserted-by":"crossref","first-page":"28697","DOI":"10.1074\/jbc.M115.673707","article-title":"Mitochondrial single-stranded DNA-binding proteins stimulate the activity of DNA polymerase \u03b3 by organization of the template DNA","volume":"290","author":"Ciesielski","year":"2015","journal-title":"J. Biol. Chem."},{"key":"2024061000021712900_B49","doi-asserted-by":"crossref","first-page":"8587","DOI":"10.1093\/nar\/gkad595","article-title":"Dynamic structure of T4 gene 32 protein filaments facilitates rapid noncooperative protein dissociation","volume":"51","author":"Cashen","year":"2023","journal-title":"Nucleic Acids Res."},{"key":"2024061000021712900_B50","doi-asserted-by":"crossref","first-page":"5763","DOI":"10.1021\/ma970381+","article-title":"Persistence length of single-stranded DNA","volume":"30","author":"Tinland","year":"1997","journal-title":"Macromolecules"},{"key":"2024061000021712900_B51","doi-asserted-by":"crossref","first-page":"2530","DOI":"10.1016\/S0006-3495(04)74308-8","article-title":"Probing single-stranded DNA conformational flexibility using fluorescence spectroscopy","volume":"86","author":"Murphy","year":"2004","journal-title":"Biophys. J."}],"container-title":["Nucleic Acids Research"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/academic.oup.com\/nar\/article-pdf\/52\/10\/5912\/58173059\/gkae354.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/academic.oup.com\/nar\/article-pdf\/52\/10\/5912\/58173059\/gkae354.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2024,6,10]],"date-time":"2024-06-10T00:03:26Z","timestamp":1717977806000},"score":1,"resource":{"primary":{"URL":"https:\/\/academic.oup.com\/nar\/article\/52\/10\/5912\/7671318"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2024,4,14]]},"references-count":51,"journal-issue":{"issue":"10","published-online":{"date-parts":[[2024,4,14]]},"published-print":{"date-parts":[[2024,6,10]]}},"URL":"https:\/\/doi.org\/10.1093\/nar\/gkae354","relation":{},"ISSN":["0305-1048","1362-4962"],"issn-type":[{"value":"0305-1048","type":"print"},{"value":"1362-4962","type":"electronic"}],"subject":[],"published-other":{"date-parts":[[2024,6,10]]},"published":{"date-parts":[[2024,4,14]]}}}