{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,11,2]],"date-time":"2026-11-02T18:26:34Z","timestamp":1793643994284,"version":"4.5.1"},"reference-count":87,"publisher":"Elsevier BV","issue":"22","license":[{"start":{"date-parts":[[2026,11,1]],"date-time":"2026-11-01T00:00:00Z","timestamp":1793491200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2026,11,1]],"date-time":"2026-11-01T00:00:00Z","timestamp":1793491200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2027,10,1]],"date-time":"2027-10-01T00:00:00Z","timestamp":1822348800000},"content-version":"am","delay-in-days":334,"URL":"http:\/\/www.elsevier.com\/open-access\/userlicense\/1.0\/"},{"start":{"date-parts":[[2026,11,1]],"date-time":"2026-11-01T00:00:00Z","timestamp":1793491200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2026,11,1]],"date-time":"2026-11-01T00:00:00Z","timestamp":1793491200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2026,11,1]],"date-time":"2026-11-01T00:00:00Z","timestamp":1793491200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2026,11,1]],"date-time":"2026-11-01T00:00:00Z","timestamp":1793491200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2026,11,1]],"date-time":"2026-11-01T00:00:00Z","timestamp":1793491200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"funder":[{"DOI":"10.13039\/100000057","name":"National Institute of General Medical Sciences","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100000057","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Journal of Molecular Biology"],"published-print":{"date-parts":[[2026,11]]},"DOI":"10.1016\/j.jmb.2026.170029","type":"journal-article","created":{"date-parts":[[2026,9,21]],"date-time":"2026-09-21T15:18:56Z","timestamp":1790003936000},"page":"170029","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":0,"title":["DNA Polymerase \u03b1 has Cyclobutane Pyrimidine Dimer Translesion Activity that is Suppressed During Normal Replication"],"prefix":"10.1016","volume":"438","author":[{"ORCID":"https:\/\/orcid.org\/0009-0000-8767-9711","authenticated-orcid":false,"given":"Projit","family":"Mukherjee","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0009-0001-1259-9204","authenticated-orcid":false,"given":"Abheerup","family":"Sarker","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-6200-1311","authenticated-orcid":false,"given":"Grant D.","family":"Schauer","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.jmb.2026.170029_b0005","doi-asserted-by":"crossref","first-page":"82","DOI":"10.1038\/nchembio.139","article-title":"DNA damage tolerance: when it\u2019s OK to make mistakes","volume":"5","author":"Chang","year":"2009","journal-title":"Nature Chem. Biol."},{"key":"10.1016\/j.jmb.2026.170029_b0010","doi-asserted-by":"crossref","first-page":"1027","DOI":"10.1534\/genetics.115.186452","article-title":"Chromosome duplication in Saccharomyces cerevisiae","volume":"203","author":"Bell","year":"2016","journal-title":"Genetics"},{"key":"10.1016\/j.jmb.2026.170029_b0015","doi-asserted-by":"crossref","first-page":"417","DOI":"10.1146\/annurev-biochem-061516-044709","article-title":"Eukaryotic DNA replication fork","volume":"86","author":"Burgers","year":"2017","journal-title":"Annu. Rev. Biochem"},{"key":"10.1016\/j.jmb.2026.170029_b0020","doi-asserted-by":"crossref","DOI":"10.1101\/cshperspect.a010363","article-title":"Translesion DNA polymerases","volume":"5","author":"Goodman","year":"2013","journal-title":"Cold Spring Harb. Perspect. Biol."},{"key":"10.1016\/j.jmb.2026.170029_b0025","doi-asserted-by":"crossref","DOI":"10.1146\/annurev-biochem-062917-011921","article-title":"Lesion bypass and the reactivation of stalled replication forks","volume":"87","author":"Marians","year":"2018","journal-title":"Annu. Rev. Biochem."},{"key":"10.1016\/j.jmb.2026.170029_b0030","doi-asserted-by":"crossref","first-page":"127","DOI":"10.1016\/j.dnarep.2018.08.016","article-title":"Eukaryotic translesion synthesis: choosing the right tool for the job","volume":"71","author":"Powers","year":"2018","journal-title":"DNA Repair"},{"key":"10.1016\/j.jmb.2026.170029_b0035","doi-asserted-by":"crossref","first-page":"239","DOI":"10.1146\/annurev-biochem-062917-012405","article-title":"Translesion and repair DNA polymerases: diverse structure and mechanism","volume":"87","author":"Yang","year":"2018","journal-title":"Annu. Rev. Biochem."},{"key":"10.1016\/j.jmb.2026.170029_b0040","doi-asserted-by":"crossref","first-page":"450","DOI":"10.1038\/s41594-020-0418-4","article-title":"Reconstitution of translesion synthesis reveals a mechanism of eukaryotic DNA replication restart","volume":"27","author":"Guilliam","year":"2020","journal-title":"Nature Struct. Mol. Biol."},{"key":"10.1016\/j.jmb.2026.170029_b0045","doi-asserted-by":"crossref","DOI":"10.3389\/fmolb.2021.811540","article-title":"Beyond the lesion: back to high fidelity DNA synthesis","volume":"8","author":"Kaszubowski","year":"2022","journal-title":"Front. Mol. Biosci."},{"key":"10.1016\/j.jmb.2026.170029_b0050","doi-asserted-by":"crossref","first-page":"1067","DOI":"10.1016\/j.molcel.2018.04.022","article-title":"The initial response of a eukaryotic replisome to DNA damage","volume":"70","author":"Taylor","year":"2018","journal-title":"Mol. Cell"},{"key":"10.1016\/j.jmb.2026.170029_b0055","doi-asserted-by":"crossref","first-page":"1001","DOI":"10.1126\/science.283.5404.1001","article-title":"Efficient bypass of a thymine-thymine dimer by yeast DNA polymerase, Pol\u03b7","volume":"283","author":"Johnson","year":"1999","journal-title":"Science"},{"key":"10.1016\/j.jmb.2026.170029_b0060","doi-asserted-by":"crossref","first-page":"274","DOI":"10.1080\/10409238.2017.1291576","article-title":"Translesion DNA polymerases in eukaryotes: what makes them tick?","volume":"52","author":"Vaisman","year":"2017","journal-title":"Crit. Rev. Biochem. Mol. Biol."},{"key":"10.1016\/j.jmb.2026.170029_b0065","doi-asserted-by":"crossref","first-page":"417","DOI":"10.1016\/S1097-2765(01)00306-9","article-title":"Structure of the catalytic core of S. cerevisiae DNA polymerase eta: implications for translesion DNA synthesis","volume":"8","author":"Trincao","year":"2001","journal-title":"Mol. Cell"},{"key":"10.1016\/j.jmb.2026.170029_b0070","doi-asserted-by":"crossref","first-page":"1044","DOI":"10.1038\/nature09196","article-title":"Structure and mechanism of human DNA polymerase \u03b7","volume":"465","author":"Biert\u00fcmpfel","year":"2010","journal-title":"Nature"},{"key":"10.1016\/j.jmb.2026.170029_b0075","doi-asserted-by":"crossref","first-page":"5361","DOI":"10.1073\/pnas.0801310105","article-title":"Regulation of polymerase exchange between Pol\u03b7 and Pol\u03b4 by monoubiquitination of PCNA and the movement of DNA polymerase holoenzyme","volume":"105","author":"Zhuang","year":"2008","journal-title":"PNAS"},{"key":"10.1016\/j.jmb.2026.170029_b0080","doi-asserted-by":"crossref","first-page":"3217","DOI":"10.1021\/bi400194r","article-title":"Regulatory role of ubiquitin in eukaryotic DNA translesion synthesis","volume":"52","author":"Yang","year":"2013","journal-title":"Biochemistry"},{"key":"10.1016\/j.jmb.2026.170029_b0085","doi-asserted-by":"crossref","first-page":"479","DOI":"10.1038\/nsmb.1776","article-title":"Structure of monoubiquitinated PCNA and implications for translesion synthesis and DNA polymerase exchange","volume":"17","author":"Freudenthal","year":"2010","journal-title":"Nature Struct. Mol. Biol."},{"key":"10.1016\/j.jmb.2026.170029_b0090","doi-asserted-by":"crossref","first-page":"4219","DOI":"10.1002\/j.1460-2075.1987.tb02770.x","article-title":"Structural and functional relationships between prokaryotic and eukaryotic DNA polymerases","volume":"6","author":"Bernad","year":"1987","journal-title":"EMBO J."},{"key":"10.1016\/j.jmb.2026.170029_b0095","article-title":"Principles and concepts of DNA Replication in bacteria, archaea, and Eukarya","volume":"5","author":"O\u2019Donnell","year":"2013","journal-title":"Cold Spring Harb. Perspect. Biol."},{"key":"10.1016\/j.jmb.2026.170029_b0100","doi-asserted-by":"crossref","first-page":"5403","DOI":"10.1093\/nar\/20.20.5403","article-title":"PCNA-induced DNA synthesis past cis-syn and trans-syn-I thymine dimers by calf thymus DNA polymerase delta in vitro","volume":"20","author":"O\u2019Day","year":"1992","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.jmb.2026.170029_b0105","doi-asserted-by":"crossref","first-page":"1228","DOI":"10.1111\/j.1365-2443.2010.01457.x","article-title":"Human replicative DNA polymerase \u03b4 can bypass T-T (6-4) ultraviolet photoproducts on template strands","volume":"15","author":"Narita","year":"2010","journal-title":"Genes Cells"},{"key":"10.1016\/j.jmb.2026.170029_b0110","doi-asserted-by":"crossref","first-page":"541","DOI":"10.1016\/j.molcel.2013.09.025","article-title":"PrimPol, an archaic primase\/polymerase operating in human cells","volume":"52","author":"Garc\u00eda-G\u00f3mez","year":"2013","journal-title":"Mol. Cell"},{"key":"10.1016\/j.jmb.2026.170029_b0115","doi-asserted-by":"crossref","first-page":"566","DOI":"10.1016\/j.molcel.2013.10.035","article-title":"PrimPol bypasses UV photoproducts during eukaryotic chromosomal DNA replication","volume":"52","author":"Bianchi","year":"2013","journal-title":"Mol. Cell"},{"key":"10.1016\/j.jmb.2026.170029_b0120","doi-asserted-by":"crossref","DOI":"10.1038\/s41598-021-96692-y","article-title":"Translesion activity of PrimPol on DNA with cisplatin and DNA\u2013protein cross-links","volume":"11","author":"Boldinova","year":"2021","journal-title":"Sci. Rep."},{"key":"10.1016\/j.jmb.2026.170029_b0125","doi-asserted-by":"crossref","first-page":"1383","DOI":"10.1038\/nsmb.2719","article-title":"Repriming of DNA synthesis at stalled replication forks by human PrimPol","volume":"20","author":"Mour\u00f3n","year":"2013","journal-title":"Nature Struct. Mol. Biol."},{"key":"10.1016\/j.jmb.2026.170029_b0130","doi-asserted-by":"crossref","DOI":"10.15252\/embj.2020106355","article-title":"PrimPol-mediated repriming facilitates replication traverse of DNA interstrand crosslinks","volume":"40","author":"Gonz\u00e1lez-Acosta","year":"2021","journal-title":"EMBO J."},{"key":"10.1016\/j.jmb.2026.170029_b0135","doi-asserted-by":"crossref","DOI":"10.1073\/pnas.2517556122","article-title":"DNA polymerase \u03b1-primase can function as a translesion DNA polymerase","volume":"122","author":"Mayle","year":"2025","journal-title":"PNAS"},{"key":"10.1016\/j.jmb.2026.170029_b0140","doi-asserted-by":"crossref","first-page":"3697","DOI":"10.1038\/s41467-023-39441-1","article-title":"Molecular choreography of primer synthesis by the eukaryotic Pol \u03b1-primase","volume":"14","author":"Yuan","year":"2023","journal-title":"Nature Commun."},{"key":"10.1016\/j.jmb.2026.170029_b0145","doi-asserted-by":"crossref","first-page":"2911","DOI":"10.1016\/j.molcel.2023.06.035","article-title":"How Pol \u03b1-primase is targeted to replisomes to prime eukaryotic DNA replication","volume":"83","author":"Jones","year":"2023","journal-title":"Mol. Cell"},{"key":"10.1016\/j.jmb.2026.170029_b0150","doi-asserted-by":"crossref","first-page":"777","DOI":"10.1038\/s41594-024-01227-4","article-title":"A mechanistic model of primer synthesis from catalytic structures of DNA polymerase \u03b1-primase","volume":"31","author":"Mullins","year":"2024","journal-title":"Nature Struct. Mol. Biol."},{"key":"10.1016\/j.jmb.2026.170029_b0155","doi-asserted-by":"crossref","first-page":"774","DOI":"10.1038\/nchembio.424","article-title":"Genome instability due to ribonucleotide incorporation into DNA","volume":"6","author":"McElhinny","year":"2010","journal-title":"Nature Chem. Biol."},{"key":"10.1016\/j.jmb.2026.170029_b0160","doi-asserted-by":"crossref","first-page":"4949","DOI":"10.1073\/pnas.0914857107","article-title":"Abundant ribonucleotide incorporation into DNA by yeast replicative polymerases","volume":"107","author":"Nick McElhinny","year":"2010","journal-title":"PNAS"},{"key":"10.1016\/j.jmb.2026.170029_b0165","doi-asserted-by":"crossref","DOI":"10.21769\/BioProtoc.2548","article-title":"In vitro assays for eukaryotic leading\/lagging strand DNA replication","volume":"7","author":"Schauer","year":"2017","journal-title":"Bio Protoc."},{"key":"10.1016\/j.jmb.2026.170029_b0170","doi-asserted-by":"crossref","first-page":"15390","DOI":"10.1073\/pnas.1418334111","article-title":"CMG helicase and DNA polymerase form a functional 15-subunit holoenzyme for eukaryotic leading-strand DNA replication","volume":"111","author":"Langston","year":"2014","journal-title":"PNAS"},{"key":"10.1016\/j.jmb.2026.170029_b0175","doi-asserted-by":"crossref","first-page":"675","DOI":"10.1073\/pnas.1619748114","article-title":"Quality control mechanisms exclude incorrect polymerases from the eukaryotic replication fork","volume":"114","author":"Schauer","year":"2017","journal-title":"PNAS"},{"key":"10.1016\/j.jmb.2026.170029_b0180","doi-asserted-by":"crossref","first-page":"2040","DOI":"10.1016\/j.jmb.2019.03.011","article-title":"Dynamics of replication fork progression following helicase\u2013polymerase uncoupling in eukaryotes","volume":"431","author":"Taylor","year":"2019","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jmb.2026.170029_b0185","doi-asserted-by":"crossref","first-page":"4665","DOI":"10.1093\/nar\/gkh777","article-title":"Enzymatic switching for efficient and accurate translesion DNA replication","volume":"32","author":"McCulloch","year":"2004","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.jmb.2026.170029_b0190","doi-asserted-by":"crossref","DOI":"10.7554\/eLife.04988","article-title":"Reconstitution of a eukaryotic replisome reveals suppression mechanisms that define leading\/lagging strand operation","volume":"4","author":"Georgescu","year":"2015","journal-title":"eLife"},{"key":"10.1016\/j.jmb.2026.170029_b0195","doi-asserted-by":"crossref","first-page":"1487","DOI":"10.1534\/genetics.105.052480","article-title":"The in vivo characterization of translesion synthesis across UV-induced lesions in Saccharomyces cerevisiae: insights into Pol\u03b6- and Pol\u03b7-dependent frameshift mutagenesis","volume":"172","author":"Abdulovic","year":"2006","journal-title":"Genetics"},{"key":"10.1016\/j.jmb.2026.170029_b0200","doi-asserted-by":"crossref","first-page":"1557","DOI":"10.1093\/genetics\/147.4.1557","article-title":"The Saccharomyces cerevisiae RAD30 gene, a homologue of Escherichia coli dinB and umuC, is DNA damage inducible and functions in a novel error-free postreplication repair mechanism","volume":"147","author":"McDonald","year":"1997","journal-title":"Genetics"},{"key":"10.1016\/j.jmb.2026.170029_b0205","doi-asserted-by":"crossref","first-page":"2992","DOI":"10.1038\/emboj.2009.226","article-title":"A key role for Ctf4 in coupling the MCM2\u20107 helicase to DNA polymerase \u03b1 within the eukaryotic replisome","volume":"28","author":"Gambus","year":"2009","journal-title":"EMBO J."},{"key":"10.1016\/j.jmb.2026.170029_b0210","doi-asserted-by":"crossref","first-page":"293","DOI":"10.1038\/nature13234","article-title":"A Ctf4 trimer couples the CMG helicase to DNA polymerase [agr] in the eukaryotic replisome","volume":"510","author":"Simon","year":"2014","journal-title":"Nature"},{"key":"10.1016\/j.jmb.2026.170029_b0215","doi-asserted-by":"crossref","DOI":"10.7554\/eLife.47405","article-title":"Ctf4 organizes sister replisomes and Pol \u03b1 into a replication factory","volume":"8","author":"Yuan","year":"2019","journal-title":"eLife"},{"key":"10.1016\/j.jmb.2026.170029_b0220","doi-asserted-by":"crossref","first-page":"385","DOI":"10.1016\/j.molcel.2016.06.009","article-title":"Ctf4 is a hub in the eukaryotic replisome that links multiple CIP-box proteins to the CMG helicase","volume":"63","author":"Villa","year":"2016","journal-title":"Mol. Cell"},{"key":"10.1016\/j.jmb.2026.170029_b0225","doi-asserted-by":"crossref","first-page":"277","DOI":"10.1016\/S1016-8478(23)25248-6","article-title":"Yeast replicative DNA polymerases and their role at the replication fork","volume":"12","author":"Kawasaki","year":"2001","journal-title":"Mol. Cells"},{"key":"10.1016\/j.jmb.2026.170029_b0230","doi-asserted-by":"crossref","first-page":"41","DOI":"10.1016\/j.dnarep.2015.04.006","article-title":"Quantifying the contributions of base selectivity, proofreading and mismatch repair to nuclear DNA replication in Saccharomyces cerevisiae","volume":"31","author":"St Charles","year":"2015","journal-title":"DNA Repair (Amst)"},{"key":"10.1016\/j.jmb.2026.170029_b0235","doi-asserted-by":"crossref","first-page":"8443","DOI":"10.1021\/bi970473r","article-title":"Role of protein\u2212protein interactions in the function of replication protein A (RPA): RPA modulates the activity of DNA polymerase \u03b1 by multiple mechanisms","volume":"36","author":"Braun","year":"1997","journal-title":"Biochemistry"},{"key":"10.1016\/j.jmb.2026.170029_b0240","doi-asserted-by":"crossref","first-page":"17","DOI":"10.1016\/j.molcel.2019.10.005","article-title":"Tunability of DNA polymerase stability during eukaryotic DNA replication","volume":"77","author":"Lewis","year":"2020","journal-title":"Mol. Cell"},{"key":"10.1016\/j.jmb.2026.170029_b0245","doi-asserted-by":"crossref","first-page":"600","DOI":"10.1016\/j.cell.2019.06.032","article-title":"Replication fork activation is enabled by a single-stranded DNA gate in CMG helicase","volume":"178","author":"Wasserman","year":"2019","journal-title":"Cell"},{"key":"10.1016\/j.jmb.2026.170029_b0250","doi-asserted-by":"crossref","first-page":"30354","DOI":"10.1073\/pnas.2020189117","article-title":"Replisome bypass of a protein-based R-loop block by Pif1","volume":"117","author":"Schauer","year":"2020","journal-title":"PNAS"},{"key":"10.1016\/j.jmb.2026.170029_b0255","doi-asserted-by":"crossref","first-page":"7199","DOI":"10.1128\/MCB.21.21.7199-7206.2001","article-title":"Physical and functional interactions of human DNA polymerase eta with PCNA","volume":"21","author":"Haracska","year":"2001","journal-title":"Mol. Cell Biol."},{"key":"10.1016\/j.jmb.2026.170029_b0260","doi-asserted-by":"crossref","first-page":"36835","DOI":"10.1074\/jbc.274.52.36835","article-title":"Fidelity and processivity of Saccharomyces cerevisiae DNA polymerase \u03b7*","volume":"274","author":"Washington","year":"1999","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jmb.2026.170029_b0265","doi-asserted-by":"crossref","first-page":"3881","DOI":"10.1093\/emboj\/cdf363","article-title":"Lesion bypass in yeast cells: Pol \u03b7 participates in a multi-DNA polymerase process","volume":"21","author":"Bresson","year":"2002","journal-title":"EMBO J."},{"key":"10.1016\/j.jmb.2026.170029_b0270","doi-asserted-by":"crossref","first-page":"685","DOI":"10.1146\/annurev.bi.62.070193.003345","article-title":"Conformational coupling in DNA polymerase fidelity","volume":"62","author":"Johnson","year":"1993","journal-title":"Annu. Rev. Biochem."},{"key":"10.1016\/j.jmb.2026.170029_b0275","doi-asserted-by":"crossref","first-page":"5660","DOI":"10.1093\/nar\/gkn555","article-title":"Evidence for lesion bypass by yeast replicative DNA polymerases during DNA damage","volume":"36","author":"Sabouri","year":"2008","journal-title":"Nucl. Acids Res."},{"key":"10.1016\/j.jmb.2026.170029_b0280","doi-asserted-by":"crossref","first-page":"2830","DOI":"10.1093\/nar\/gkp103","article-title":"The efficiency and fidelity of 8-oxo-guanine bypass by DNA polymerases delta and eta","volume":"37","author":"McCulloch","year":"2009","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.jmb.2026.170029_b0285","doi-asserted-by":"crossref","DOI":"10.15252\/embj.2020107037","article-title":"The eukaryotic replisome tolerates leading\u2010strand base damage by replicase switching","volume":"40","author":"Guilliam","year":"2021","journal-title":"EMBO J."},{"key":"10.1016\/j.jmb.2026.170029_b0290","doi-asserted-by":"crossref","first-page":"31555","DOI":"10.1074\/jbc.M109.043927","article-title":"Translesion synthesis of abasic sites by yeast DNA polymerase \u220a","volume":"284","author":"Sabouri","year":"2009","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jmb.2026.170029_b0295","doi-asserted-by":"crossref","first-page":"737","DOI":"10.1038\/nature02046","article-title":"Global analysis of protein expression in yeast","volume":"425","author":"Ghaemmaghami","year":"2003","journal-title":"Nature"},{"key":"10.1016\/j.jmb.2026.170029_b0300","doi-asserted-by":"crossref","first-page":"319","DOI":"10.1038\/nmeth.2834","article-title":"Minimal, encapsulated proteomic-sample processing applied to copy-number estimation in eukaryotic cells","volume":"11","author":"Kulak","year":"2014","journal-title":"Nature Methods"},{"key":"10.1016\/j.jmb.2026.170029_b0305","doi-asserted-by":"crossref","first-page":"913","DOI":"10.1038\/s41594-020-0476-7","article-title":"Structure and mechanism of B-family DNA polymerase \u03b6 specialized for translesion DNA synthesis","volume":"27","author":"Malik","year":"2020","journal-title":"Nature Struct. Mol. Biol."},{"key":"10.1016\/j.jmb.2026.170029_b0310","doi-asserted-by":"crossref","first-page":"967","DOI":"10.1126\/science.1148242","article-title":"Bypass of DNA lesions generated during anticancer treatment with cisplatin by DNA polymerase \u03b7","volume":"318","author":"Alt","year":"2007","journal-title":"Science"},{"key":"10.1016\/j.jmb.2026.170029_b0315","doi-asserted-by":"crossref","first-page":"20720","DOI":"10.1073\/pnas.1008894107","article-title":"Mechanism of replication blocking and bypass of Y-family polymerase eta by bulky acetylaminofluorene DNA adducts","volume":"107","author":"Schorr","year":"2010","journal-title":"PNAS"},{"key":"10.1016\/j.jmb.2026.170029_b0320","doi-asserted-by":"crossref","first-page":"5113","DOI":"10.1073\/pnas.0837578100","article-title":"Yeast DNA polymerase eta makes functional contacts with the DNA minor groove only at the incoming nucleoside triphosphate","volume":"100","author":"Washington","year":"2003","journal-title":"PNAS"},{"key":"10.1016\/j.jmb.2026.170029_b0325","doi-asserted-by":"crossref","first-page":"627","DOI":"10.1016\/j.jmb.2011.11.038","article-title":"Human DNA polymerase \u03b7 is pre-aligned for dNTP binding and catalysis","volume":"415","author":"Ummat","year":"2012","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jmb.2026.170029_b0330","doi-asserted-by":"crossref","first-page":"6824","DOI":"10.1074\/jbc.RA117.001074","article-title":"Activity and fidelity of human DNA polymerase \u03b1 depend on primer structure","volume":"293","author":"Baranovskiy","year":"2018","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jmb.2026.170029_b0335","doi-asserted-by":"crossref","first-page":"502","DOI":"10.1038\/nature14183","article-title":"Lagging-strand replication shapes the mutational landscape of the genome","volume":"518","author":"Reijns","year":"2015","journal-title":"Nature"},{"key":"10.1016\/j.jmb.2026.170029_b0340","doi-asserted-by":"crossref","first-page":"249","DOI":"10.1016\/S0092-8674(85)80120-3","article-title":"CDC17: an essential gene that prevents telomere elongation in yeast","volume":"42","author":"Carson","year":"1985","journal-title":"Cell"},{"key":"10.1016\/j.jmb.2026.170029_b0345","doi-asserted-by":"crossref","first-page":"2107","DOI":"10.1091\/mbc.9.8.2107","article-title":"Mutational effect of fission yeast polalpha on cell cycle events","volume":"9","author":"Bhaumik","year":"1998","journal-title":"Mol. Biol. Cell"},{"key":"10.1016\/j.jmb.2026.170029_b0350","doi-asserted-by":"crossref","first-page":"1088","DOI":"10.1016\/j.cell.2013.10.043","article-title":"ATR prohibits replication catastrophe by preventing global exhaustion of RPA","volume":"155","author":"Toledo","year":"2013","journal-title":"Cell"},{"key":"10.1016\/j.jmb.2026.170029_b0355","doi-asserted-by":"crossref","first-page":"735","DOI":"10.1016\/j.molcel.2017.05.001","article-title":"Replication catastrophe: when a checkpoint fails because of exhaustion","volume":"66","author":"Toledo","year":"2017","journal-title":"Mol. Cell"},{"key":"10.1016\/j.jmb.2026.170029_b0360","doi-asserted-by":"crossref","first-page":"622","DOI":"10.1038\/nrm.2017.67","article-title":"The essential kinase ATR: ensuring faithful duplication of a challenging genome","volume":"18","author":"Saldivar","year":"2017","journal-title":"Nature Rev. Mol. Cell Biol."},{"key":"10.1016\/j.jmb.2026.170029_b0365","doi-asserted-by":"crossref","first-page":"2416","DOI":"10.1016\/j.celrep.2020.01.067","article-title":"Physiological tolerance to ssDNA enables strand uncoupling during DNA replication","volume":"30","author":"Ercilla","year":"2020","journal-title":"Cell Rep."},{"key":"10.1016\/j.jmb.2026.170029_b0370","doi-asserted-by":"crossref","first-page":"4243","DOI":"10.1016\/j.molcel.2021.08.009","article-title":"A basal-level activity of ATR links replication fork surveillance and stress response","volume":"81","author":"Yin","year":"2021","journal-title":"Mol. Cell"},{"key":"10.1016\/j.jmb.2026.170029_b0375","doi-asserted-by":"crossref","first-page":"2474","DOI":"10.1016\/j.molcel.2025.06.002","article-title":"The DNA replication checkpoint prevents PCNA\/RFC depletion to protect forks from HLTF-induced collapse in human cells","volume":"85","author":"Bertolin","year":"2025","journal-title":"Mol. Cell"},{"key":"10.1016\/j.jmb.2026.170029_b0380","doi-asserted-by":"crossref","first-page":"664","DOI":"10.1038\/nsmb.2851","article-title":"Mechanism of asymmetric polymerase assembly at the eukaryotic replication fork","volume":"21","author":"Georgescu","year":"2014","journal-title":"Nature Struct. Mol. Biol."},{"key":"10.1016\/j.jmb.2026.170029_b0385","doi-asserted-by":"crossref","first-page":"280","DOI":"10.1038\/nprot.2006.43","article-title":"Site-specific protein labeling by Sfp phosphopantetheinyl transferase","volume":"1","author":"Yin","year":"2006","journal-title":"Nature Protoc."},{"key":"10.1016\/j.jmb.2026.170029_b0390","doi-asserted-by":"crossref","first-page":"337","DOI":"10.1021\/cb700054k","article-title":"Genetically encoded short peptide tags for orthogonal protein labeling by Sfp and AcpS phosphopantetheinyl transferases","volume":"2","author":"Zhou","year":"2007","journal-title":"ACS Chem. Biol."},{"key":"10.1016\/j.jmb.2026.170029_b0395","doi-asserted-by":"crossref","DOI":"10.1073\/pnas.2404470121","article-title":"Revised mechanism of hydroxyurea-induced cell cycle arrest and an improved alternative","volume":"121","author":"Shaw","year":"2024","journal-title":"PNAS"},{"key":"10.1016\/j.jmb.2026.170029_b0400","series-title":"Methods in Molecular Biology","article-title":"Simplified bypass assays to quantify DNA translesion synthesis","author":"Mukherjee","year":"2026"},{"key":"10.1016\/j.jmb.2026.170029_b0405","doi-asserted-by":"crossref","first-page":"857","DOI":"10.1002\/1097-0061(20000630)16:9<857::AID-YEA561>3.0.CO;2-B","article-title":"Rapid and reliable protein extraction from yeast","volume":"16","author":"Kushnirov","year":"2000","journal-title":"Yeast"},{"key":"10.1016\/j.jmb.2026.170029_b0410","doi-asserted-by":"crossref","DOI":"10.3791\/50549","article-title":"Surface passivation for single-molecule protein studies","author":"Chandradoss","year":"2014","journal-title":"J. Visual. Exp. (JoVE)"},{"key":"10.1016\/j.jmb.2026.170029_b0415","doi-asserted-by":"crossref","first-page":"1826","DOI":"10.1529\/biophysj.107.117689","article-title":"An oxygen scavenging system for improvement of dye stability in single-molecule fluorescence experiments","volume":"94","author":"Aitken","year":"2008","journal-title":"Biophys. J."},{"key":"10.1016\/j.jmb.2026.170029_b0420","doi-asserted-by":"crossref","first-page":"341","DOI":"10.1038\/nmeth.3769","article-title":"Single-molecule imaging of non-equilibrium molecular ensembles on the millisecond timescale","volume":"13","author":"Juette","year":"2016","journal-title":"Nature Methods"},{"key":"10.1016\/j.jmb.2026.170029_b0425","doi-asserted-by":"crossref","first-page":"593","DOI":"10.1038\/nmeth.3435","article-title":"iSMS: single-molecule FRET microscopy software","volume":"12","author":"Preus","year":"2015","journal-title":"Nature Methods"},{"key":"10.1016\/j.jmb.2026.170029_b0430","doi-asserted-by":"crossref","unstructured":"CASTpFold: Computed Atlas of Surface Topography of the universe of protein Folds, Nucleic Acids Research, Oxford Academic, n.d. https:\/\/academic.oup.com\/nar\/article\/52\/W1\/W194\/7680624 (accessed August 20, 2026).","DOI":"10.1093\/nar\/gkae415"},{"key":"10.1016\/j.jmb.2026.170029_b0435","doi-asserted-by":"crossref","first-page":"417","DOI":"10.1016\/S1097-2765(01)00306-9","article-title":"Structure of the catalytic core of S. cerevisiae DNA polymerase \u03b7: implications for translesion DNA synthesis","volume":"8","author":"Trincao","year":"2001","journal-title":"Mol. Cell"}],"container-title":["Journal of Molecular Biology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S002228362600402X?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S002228362600402X?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2026,11,2]],"date-time":"2026-11-02T17:30:33Z","timestamp":1793640633000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S002228362600402X"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,11]]},"references-count":87,"journal-issue":{"issue":"22","published-print":{"date-parts":[[2026,11]]}},"alternative-id":["S002228362600402X"],"URL":"https:\/\/doi.org\/10.1016\/j.jmb.2026.170029","relation":{},"ISSN":["0022-2836"],"issn-type":[{"value":"0022-2836","type":"print"}],"subject":[],"published":{"date-parts":[[2026,11]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"DNA Polymerase \u03b1 has Cyclobutane Pyrimidine Dimer Translesion Activity that is Suppressed During Normal Replication","name":"articletitle","label":"Article Title"},{"value":"Journal of Molecular Biology","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.jmb.2026.170029","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2026 Elsevier Ltd. All rights are reserved, including those for text and data mining, AI training, and similar technologies.","name":"copyright","label":"Copyright"}],"article-number":"170029"}}