{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2024,10,20]],"date-time":"2024-10-20T14:40:28Z","timestamp":1729435228888,"version":"3.27.0"},"reference-count":88,"publisher":"Elsevier BV","issue":"6","license":[{"start":{"date-parts":[[2023,8,1]],"date-time":"2023-08-01T00:00:00Z","timestamp":1690848000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2023,8,1]],"date-time":"2023-08-01T00:00:00Z","timestamp":1690848000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2024,8,1]],"date-time":"2024-08-01T00:00:00Z","timestamp":1722470400000},"content-version":"vor","delay-in-days":366,"URL":"http:\/\/www.elsevier.com\/open-access\/userlicense\/1.0\/"},{"start":{"date-parts":[[2023,8,1]],"date-time":"2023-08-01T00:00:00Z","timestamp":1690848000000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2023,8,1]],"date-time":"2023-08-01T00:00:00Z","timestamp":1690848000000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2023,8,1]],"date-time":"2023-08-01T00:00:00Z","timestamp":1690848000000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2023,8,1]],"date-time":"2023-08-01T00:00:00Z","timestamp":1690848000000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2023,8,1]],"date-time":"2023-08-01T00:00:00Z","timestamp":1690848000000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Biochimica et Biophysica Acta (BBA) - Molecular Cell Research"],"published-print":{"date-parts":[[2023,8]]},"DOI":"10.1016\/j.bbamcr.2023.119484","type":"journal-article","created":{"date-parts":[[2023,5,17]],"date-time":"2023-05-17T02:15:15Z","timestamp":1684289715000},"page":"119484","update-policy":"http:\/\/dx.doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":0,"title":["p130RB2 positively contributes to ATR activation in response to replication stress via the RPA32-ETAA1 axis"],"prefix":"10.1016","volume":"1870","author":[{"given":"Chiharu","family":"Uchida","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Hiroyuki","family":"Niida","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Satoshi","family":"Sakai","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Kenta","family":"Iijima","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Kyoko","family":"Kitagawa","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Tatsuya","family":"Ohhata","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Bunsyo","family":"Shiotani","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Masatoshi","family":"Kitagawa","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1016\/j.bbamcr.2023.119484_bb0005","doi-asserted-by":"crossref","first-page":"1542","DOI":"10.1126\/science.1083430","article-title":"Sensing DNA damage through ATRIP recognition of RPA-ssDNA complexes","volume":"300","author":"Zou","year":"2003","journal-title":"Science"},{"key":"10.1016\/j.bbamcr.2023.119484_bb0010","doi-asserted-by":"crossref","first-page":"4126","DOI":"10.1093\/nar\/gkl550","article-title":"A dynamic model for replication protein a (RPA) function in DNA processing pathways","volume":"34","author":"Fanning","year":"2006","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.bbamcr.2023.119484_bb0015","doi-asserted-by":"crossref","first-page":"301","DOI":"10.1242\/jcs.035105","article-title":"ATR signaling at a glance","volume":"122","author":"Shiotani","year":"2009","journal-title":"J. Cell Sci."},{"key":"10.1016\/j.bbamcr.2023.119484_bb0020","doi-asserted-by":"crossref","first-page":"665","DOI":"10.1093\/abbs\/gmw041","article-title":"Replication protein a and more: single-stranded DNA-binding proteins in eukaryotic cells","volume":"48","author":"Liu","year":"2016","journal-title":"Acta Biochim. Biophys. Sin. Shanghai"},{"key":"10.1016\/j.bbamcr.2023.119484_bb0025","doi-asserted-by":"crossref","first-page":"943","DOI":"10.1111\/j.1742-4658.2008.06841.x","article-title":"The multi-replication protein a (RPA) system - a new perspective","volume":"276","author":"Sakaguchi","year":"2009","journal-title":"FEBS J."},{"key":"10.1016\/j.bbamcr.2023.119484_bb0030","doi-asserted-by":"crossref","first-page":"9","DOI":"10.1038\/cr.2014.147","article-title":"RPA-coated single-stranded DNA as a platform for post-translational modifications in the DNA damage response","volume":"25","author":"Mar\u00e9chal","year":"2015","journal-title":"Cell Res."},{"key":"10.1016\/j.bbamcr.2023.119484_bb0035","doi-asserted-by":"crossref","first-page":"192","DOI":"10.1016\/j.molcel.2011.06.019","article-title":"ATR autophosphorylation as a molecular switch for checkpoint activation","volume":"43","author":"Liu","year":"2011","journal-title":"Mol. Cell"},{"key":"10.1016\/j.bbamcr.2023.119484_bb0040","doi-asserted-by":"crossref","first-page":"26762","DOI":"10.1074\/jbc.M312353200","article-title":"DNA stimulates Mec1-mediated phosphorylation of replication protein a","volume":"279","author":"Bartrand","year":"2004","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbamcr.2023.119484_bb0045","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pgen.1008294","article-title":"Ddc2ATRIP promotes Mec1ATR activation at RPA-ssDNA tracts","volume":"15","author":"Biswas","year":"2019","journal-title":"PLoS Genet."},{"key":"10.1016\/j.bbamcr.2023.119484_bb0050","doi-asserted-by":"crossref","first-page":"327","DOI":"10.1007\/s00294-019-01039-w","article-title":"Activation of ATR-related protein kinase upon DNA damage recognition","volume":"66","author":"Ma","year":"2020","journal-title":"Curr. Genet."},{"key":"10.1016\/j.bbamcr.2023.119484_bb0055","doi-asserted-by":"crossref","first-page":"1227","DOI":"10.1016\/j.dnarep.2005.04.001","article-title":"Identification and functional analysis of TopBP1 and its homologs","volume":"4","author":"Garcia","year":"2005","journal-title":"DNA Repair"},{"key":"10.1016\/j.bbamcr.2023.119484_bb0060","doi-asserted-by":"crossref","first-page":"943","DOI":"10.1016\/j.cell.2005.12.041","article-title":"TopBP1 activates the ATR-ATRIP complex","volume":"124","author":"Kumagai","year":"2006","journal-title":"Cell"},{"key":"10.1016\/j.bbamcr.2023.119484_bb0065","doi-asserted-by":"crossref","first-page":"1478","DOI":"10.1101\/gad.1666208","article-title":"TopBP1 activates ATR through ATRIP and a PIKK regulatory domain","volume":"22","author":"Mordes","year":"2008","journal-title":"Genes Dev."},{"key":"10.1016\/j.bbamcr.2023.119484_bb0070","doi-asserted-by":"crossref","first-page":"13124","DOI":"10.1074\/jbc.M116.729194","article-title":"Direct binding to replication protein a (RPA)-coated single-stranded DNA allows recruitment of the ATR activator TopBP1 to sites of DNA damage","volume":"291","author":"Acevedo","year":"2016","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbamcr.2023.119484_bb0075","doi-asserted-by":"crossref","first-page":"21956","DOI":"10.1074\/jbc.C116.747758","article-title":"Ewing tumor-associated antigen 1 interacts with replication protein a to promote restart of stalled replication forks","volume":"291","author":"Feng","year":"2016","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbamcr.2023.119484_bb0080","doi-asserted-by":"crossref","first-page":"3257","DOI":"10.1016\/j.cub.2016.10.030","article-title":"RPA-binding protein ETAA1 is an ATR activator involved in DNA replication stress response","volume":"26","author":"Lee","year":"2016","journal-title":"Curr. Biol."},{"key":"10.1016\/j.bbamcr.2023.119484_bb0085","doi-asserted-by":"crossref","first-page":"898","DOI":"10.1080\/15384101.2019.1598728","article-title":"RPA-coated single-stranded DNA promotes the ETAA1-dependent activation of ATR","volume":"18","author":"Lyu","year":"2019","journal-title":"Cell Cycle"},{"key":"10.1016\/j.bbamcr.2023.119484_bb0090","doi-asserted-by":"crossref","first-page":"1185","DOI":"10.1038\/ncb3415","article-title":"ETAA1 acts at stalled replication forks to maintain genome integrity","volume":"18","author":"Bass","year":"2016","journal-title":"Nat. Cell Biol."},{"key":"10.1016\/j.bbamcr.2023.119484_bb0095","doi-asserted-by":"crossref","first-page":"1196","DOI":"10.1038\/ncb3422","article-title":"Activation of the ATR kinase by the RPA-binding protein ETAA1","volume":"18","author":"Haahr","year":"2016","journal-title":"Nat. Cell Biol."},{"key":"10.1016\/j.bbamcr.2023.119484_bb0100","doi-asserted-by":"crossref","first-page":"3943","DOI":"10.1083\/jcb.201905064","article-title":"Regulation of ETAA1-mediated ATR activation couples DNA replication fidelity and genome stability","volume":"218","author":"Achuthankutty","year":"2019","journal-title":"J. Cell Biol."},{"key":"10.1016\/j.bbamcr.2023.119484_bb0105","doi-asserted-by":"crossref","first-page":"39517","DOI":"10.1074\/jbc.M605121200","article-title":"RPA2 is a direct downstream target for ATR to regulate the S-phase checkpoint","volume":"281","author":"Olson","year":"2006","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbamcr.2023.119484_bb0110","doi-asserted-by":"crossref","DOI":"10.3390\/genes8020074","article-title":"The intra-S checkpoint responses to DNA damage","volume":"8","author":"Iyer","year":"2017","journal-title":"Genes (Basel)"},{"key":"10.1016\/j.bbamcr.2023.119484_bb0115","doi-asserted-by":"crossref","first-page":"155","DOI":"10.1146\/annurev-genet-121415-121658","article-title":"Functions, regulation, and therapeutic implications of the ATR checkpoint pathway","volume":"50","author":"Yazinski","year":"2016","journal-title":"Annu. Rev. Genet."},{"issue":"622\u2013636","key":"10.1016\/j.bbamcr.2023.119484_bb0120","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":"Nat. Rev. Mol. Cell Biol."},{"key":"10.1016\/j.bbamcr.2023.119484_bb0125","doi-asserted-by":"crossref","first-page":"3257","DOI":"10.1016\/j.cub.2016.10.030","article-title":"RPA-binding protein ETAA1 is an ATR activator involved in DNA replication stress response","volume":"26","author":"Lee","year":"2016","journal-title":"Curr. Biol."},{"key":"10.1016\/j.bbamcr.2023.119484_bb0130","doi-asserted-by":"crossref","first-page":"297","DOI":"10.1038\/nrm3567","article-title":"Molecular mechanisms underlying RB protein function","volume":"14","author":"Dick","year":"2013","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"10.1016\/j.bbamcr.2023.119484_bb0135","doi-asserted-by":"crossref","first-page":"864","DOI":"10.1007\/s13238-011-1117-z","article-title":"Conserved RB functions in development and tumor suppression","volume":"2","author":"Gordon","year":"2011","journal-title":"Protein Cell"},{"key":"10.1016\/j.bbamcr.2023.119484_bb0140","doi-asserted-by":"crossref","DOI":"10.3390\/ijms18081776","article-title":"The retinoblastoma (RB) tumor suppressor: pushing back against genome instability on multiple fronts","volume":"18","author":"V\u00e9lez-Cruz","year":"2017","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.bbamcr.2023.119484_bb0145","doi-asserted-by":"crossref","first-page":"54","DOI":"10.1016\/j.bbrc.2005.11.148","article-title":"Mdm2-mediated pRB downregulation is involved in carcinogenesis in a p53-independent manner","volume":"340","author":"Miwa","year":"2006","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.bbamcr.2023.119484_bb0150","doi-asserted-by":"crossref","first-page":"160","DOI":"10.1038\/sj.emboj.7600486","article-title":"Enhanced Mdm2 activity inhibits pRB function via ubiquitin-dependent degradation","volume":"24","author":"Uchida","year":"2005","journal-title":"EMBO J."},{"key":"10.1016\/j.bbamcr.2023.119484_bb0155","doi-asserted-by":"crossref","first-page":"1622","DOI":"10.2174\/138945012803529938","article-title":"The retinoblastoma protein: functions beyond the G1-S regulator","volume":"13","author":"Uchida","year":"2012","journal-title":"Curr. Drug Targets"},{"key":"10.1016\/j.bbamcr.2023.119484_bb0160","doi-asserted-by":"crossref","first-page":"442","DOI":"10.1038\/s41568-018-0008-5","article-title":"Non-canonical functions of the RB protein in cancer","volume":"18","author":"Dick","year":"2018","journal-title":"Nat. Rev. Cancer"},{"key":"10.1016\/j.bbamcr.2023.119484_bb0165","doi-asserted-by":"crossref","first-page":"714","DOI":"10.1038\/nrc2401","article-title":"Tailoring to RB: tumour suppressor status and therapeutic response","volume":"8","author":"Knudsen","year":"2008","journal-title":"Nat. Rev. Cancer"},{"key":"10.1016\/j.bbamcr.2023.119484_bb0170","doi-asserted-by":"crossref","DOI":"10.3390\/ijms18081776","article-title":"The retinoblastoma (RB) tumor suppressor: pushing back against genome instability on multiple fronts","volume":"18","author":"V\u00e9lez-Cruz","year":"2017","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.bbamcr.2023.119484_bb0175","doi-asserted-by":"crossref","first-page":"323","DOI":"10.1016\/0092-8674(95)90385-2","article-title":"The retinoblastoma protein and cell cycle control","volume":"81","author":"Weinberg","year":"1995","journal-title":"Cell"},{"key":"10.1016\/j.bbamcr.2023.119484_bb0180","doi-asserted-by":"crossref","first-page":"2245","DOI":"10.1101\/gad.12.15.2245","article-title":"The regulation of E2F by pRB-family proteins","volume":"12","author":"Dyson","year":"1998","journal-title":"Genes Dev."},{"key":"10.1016\/j.bbamcr.2023.119484_bb0185","doi-asserted-by":"crossref","first-page":"11","DOI":"10.1038\/nrm714","article-title":"Sibling rivalry in the E2F family","volume":"3","author":"Trimarchi","year":"2002","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"10.1016\/j.bbamcr.2023.119484_bb0190","first-page":"739","article-title":"Distinct and overlapping roles for E2F family members in transcription, proliferation and apoptosis","volume":"6","author":"DeGregori","year":"2012","journal-title":"Curr. Mol. Med."},{"key":"10.1016\/j.bbamcr.2023.119484_bb0195","doi-asserted-by":"crossref","first-page":"539","DOI":"10.1016\/j.molcel.2007.04.015","article-title":"Evolutionarily conserved multisubunit RBL2\/p130 and E2F4 protein complex represses human cell cycle-dependent genes in quiescence","volume":"26","author":"Litovchick","year":"2007","journal-title":"Mol. Cell"},{"key":"10.1016\/j.bbamcr.2023.119484_bb0200","doi-asserted-by":"crossref","first-page":"89","DOI":"10.1111\/gtc.12119","article-title":"Interaction between RB protein and NuMA is required for proper alignment of spindle microtubules","volume":"19","author":"Uchida","year":"2014","journal-title":"Genes Cells"},{"key":"10.1016\/j.bbamcr.2023.119484_bb0205","doi-asserted-by":"crossref","DOI":"10.1155\/2014\/549719","article-title":"The Mcm2-7 replicative helicase: a promising chemotherapeutic target","author":"Simon","year":"2014","journal-title":"Biomed. Res."},{"key":"10.1016\/j.bbamcr.2023.119484_bb0210","article-title":"Chromatin regulators in retinoblastoma: biological roles and therapeutic applications","author":"Lee","year":"2020","journal-title":"J. Cell. Physiol."},{"key":"10.1016\/j.bbamcr.2023.119484_bb0215","doi-asserted-by":"crossref","first-page":"638","DOI":"10.1080\/10409238.2017.1360836","article-title":"Cell cycle transcription control: DREAM\/MuvB and RB-E2F complexes","volume":"52","author":"Fischer","year":"2017","journal-title":"Crit. Rev. Biochem. Mol. Biol."},{"key":"10.1016\/j.bbamcr.2023.119484_bb0220","doi-asserted-by":"crossref","first-page":"585","DOI":"10.1038\/nrc3556","article-title":"The DREAM complex: master coordinator of cell cycle-dependent gene expression","volume":"13","author":"Sadasivam","year":"2013","journal-title":"Nat. Rev. Cancer"},{"key":"10.1016\/j.bbamcr.2023.119484_bb0225","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0013720","article-title":"Interaction of the retinoblastoma protein with orc1 and its recruitment to human origins of DNA replication","volume":"5","author":"Mendoza-Maldonado","year":"2010","journal-title":"PLoS One"},{"key":"10.1016\/j.bbamcr.2023.119484_bb0230","doi-asserted-by":"crossref","first-page":"840","DOI":"10.1158\/2159-8290.CD-14-0215","article-title":"Haploinsufficiency of an RB-E2F1-Condensin II complex leads to aberrant replication and aneuploidy","volume":"4","author":"Coschi","year":"2014","journal-title":"Cancer Discov."},{"key":"10.1016\/j.bbamcr.2023.119484_bb0235","article-title":"An RB-Condensin II complex mediates long-range chromosome interactions and influences expression at divergently paired genes","volume":"40","author":"Marshall","year":"2019","journal-title":"Mol. Cell. Biol."},{"key":"10.1016\/j.bbamcr.2023.119484_bb0240","doi-asserted-by":"crossref","first-page":"2006","DOI":"10.1016\/j.celrep.2015.02.059","article-title":"Direct involvement of retinoblastoma family proteins in DNA repair by non-homologous end-joining","volume":"10","author":"Cook","year":"2015","journal-title":"Cell Rep."},{"key":"10.1016\/j.bbamcr.2023.119484_bb0245","doi-asserted-by":"crossref","first-page":"2748","DOI":"10.1128\/MCB.18.5.2748","article-title":"Negative regulation of DNA replication by the retinoblastoma protein is mediated by its association with MCM7","volume":"18","author":"Sterner","year":"1998","journal-title":"Mol. Cell. Biol."},{"key":"10.1016\/j.bbamcr.2023.119484_bb0250","doi-asserted-by":"crossref","first-page":"539","DOI":"10.1093\/jb\/mvq085","article-title":"Identification of proteins that may directly interact with human RPA","volume":"148","author":"Nakaya","year":"2010","journal-title":"J. Biochem."},{"key":"10.1016\/j.bbamcr.2023.119484_bb0255","doi-asserted-by":"crossref","first-page":"10780","DOI":"10.1093\/nar\/gks849","article-title":"Distinct roles for DNA-PK, ATM and ATR in RPA phosphorylation and checkpoint activation in response to replication stress","volume":"40","author":"Liu","year":"2012","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.bbamcr.2023.119484_bb0260","doi-asserted-by":"crossref","first-page":"4129","DOI":"10.1128\/MCB.21.13.4129-4139.2001","article-title":"ATR-mediated checkpoint pathways regulate phosphorylation and activation of human Chk1","volume":"21","author":"Zhao","year":"2001","journal-title":"Mol. Cell. Biol."},{"key":"10.1016\/j.bbamcr.2023.119484_bb0265","doi-asserted-by":"crossref","unstructured":"Lai, Y., Zhu, M., Wu, W., Rokutanda, N., Togashi, Y., Liang, W. & Ohta, T. HERC2 regulates RPA2 by mediating ATR-induced Ser33 phosphorylation and ubiquitin- dependent degradation. Sci. Rep. 9, 1\u201312 (2019). doi.org\/https:\/\/doi.org\/10.1038\/s41598-019-50812.","DOI":"10.1038\/s41598-019-50812-x"},{"key":"10.1016\/j.bbamcr.2023.119484_bb0270","doi-asserted-by":"crossref","first-page":"622","DOI":"10.1016\/j.molcel.2017.04.022","article-title":"RFWD3-mediated ubiquitination promotes timely removal of both RPA and RAD51 from DNA damage sites to facilitate homologous recombination","volume":"66","author":"Inano","year":"2017","journal-title":"Mol. Cell"},{"key":"10.1016\/j.bbamcr.2023.119484_bb0275","doi-asserted-by":"crossref","first-page":"473","DOI":"10.1038\/nbt0502-473","article-title":"Protein detection using proximity-dependent DNA ligation assays","volume":"20","author":"Fredriksson","year":"2002","journal-title":"Nat. Biotechnol."},{"key":"10.1016\/j.bbamcr.2023.119484_bb0280","doi-asserted-by":"crossref","DOI":"10.1002\/cpim.58","article-title":"Proximity ligation assay (PLA)","volume":"123","author":"Alam","year":"2018","journal-title":"Curr. Protoc. Immunol."},{"key":"10.1016\/j.bbamcr.2023.119484_bb0285","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1093\/narcan\/zcaa022","article-title":"Replication protein A: a multifunctional protein with roles in DNA replication, repair and beyond","volume":"2","author":"Dueva","year":"2020","journal-title":"NAR Cancer"},{"key":"10.1016\/j.bbamcr.2023.119484_bb0290","doi-asserted-by":"crossref","first-page":"237","DOI":"10.1016\/j.ceb.2009.01.017","article-title":"ATR\/Mec1: coordinating fork stability and repair","volume":"21","author":"Friedel","year":"2009","journal-title":"Curr. Opin. Chem. Biol."},{"key":"10.1016\/j.bbamcr.2023.119484_bb0295","doi-asserted-by":"crossref","first-page":"149","DOI":"10.1016\/j.dnarep.2015.04.026","article-title":"Preventing replication fork collapse to maintain genome integrity","volume":"32","author":"Cortez","year":"2015","journal-title":"DNA Repair (Amst)"},{"key":"10.1016\/j.bbamcr.2023.119484_bb0300","doi-asserted-by":"crossref","DOI":"10.15252\/embr.201846263","article-title":"Mechanisms for stalled replication fork stabilization: new targets for synthetic lethality strategies in cancer treatments","volume":"19","author":"Liao","year":"2018","journal-title":"EMBO Rep."},{"key":"10.1016\/j.bbamcr.2023.119484_bb0305","doi-asserted-by":"crossref","first-page":"735","DOI":"10.1007\/s00018-019-03206-1","article-title":"Acute hydroxyurea-induced replication blockade results in replisome components disengagement from nascent DNA without causing fork collapse","volume":"77","author":"Ercilla","year":"2020","journal-title":"Cell. Mol. Life Sci."},{"key":"10.1016\/j.bbamcr.2023.119484_bb0310","doi-asserted-by":"crossref","first-page":"806","DOI":"10.1126\/science.aap9346","article-title":"An intrinsic S\/G2 checkpoint enforced by ATR","volume":"361","author":"Saldivar","year":"2018","journal-title":"Science"},{"key":"10.1016\/j.bbamcr.2023.119484_bb0315","doi-asserted-by":"crossref","first-page":"3883","DOI":"10.1083\/jcb.201910157","article-title":"ETAA1 ensures proper chromosome segregation: a matter of S phase or mitosis?","volume":"218","author":"Gonz\u00e1lez Besteiro","year":"2019","journal-title":"J. Cell Biol."},{"key":"10.1016\/j.bbamcr.2023.119484_bb0320","doi-asserted-by":"crossref","first-page":"1713","DOI":"10.1126\/science.1065521","article-title":"ATR and ATRIP: partners in checkpoint signaling","volume":"294","author":"Cortez","year":"2001","journal-title":"Science"},{"key":"10.1016\/j.bbamcr.2023.119484_bb0325","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":"Nat. Rev. Mol. Cell Biol."},{"key":"10.1016\/j.bbamcr.2023.119484_bb0330","doi-asserted-by":"crossref","first-page":"11236","DOI":"10.1073\/pnas.201373498","article-title":"Purification and characterization of human DNA damage checkpoint rad complexes","volume":"98","author":"Lindsey-Boltz","year":"2001","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbamcr.2023.119484_bb0335","doi-asserted-by":"crossref","first-page":"926","DOI":"10.1091\/mbc.e09-11-0958","article-title":"Rad17 plays a central role in establishment of the interaction between TopBP1 and the Rad9-Hus1-Rad1 complex at stalled replication forks","volume":"21","author":"Lee","year":"2010","journal-title":"Mol. Biol. Cell"},{"key":"10.1016\/j.bbamcr.2023.119484_bb0340","doi-asserted-by":"crossref","first-page":"1313","DOI":"10.1126\/science.1203430","article-title":"A DNA damage response screen identifies RHINO, a 9-1-1 and TopBP1 interacting protein required for ATR signaling","volume":"1","author":"Cotta-ramusino","year":"2011","journal-title":"Science"},{"key":"10.1016\/j.bbamcr.2023.119484_bb0345","doi-asserted-by":"crossref","first-page":"116","DOI":"10.1016\/j.molcel.2013.03.006","article-title":"A role for the MRN complex in ATR activation via TOPBP1 recruitment","volume":"50","author":"Duursma","year":"2013","journal-title":"Mol. Cell"},{"key":"10.1016\/j.bbamcr.2023.119484_bb0350","doi-asserted-by":"crossref","first-page":"1651","DOI":"10.1016\/j.celrep.2013.04.018","article-title":"Two distinct modes of ATR activation orchestrated by Rad17 and Nbs1","volume":"3","author":"Shiotani","year":"2013","journal-title":"Cell Rep."},{"key":"10.1016\/j.bbamcr.2023.119484_bb0355","doi-asserted-by":"crossref","first-page":"29767","DOI":"10.1074\/jbc.M005782200","article-title":"The human checkpoint protein hRad17 interacts with the PCNA-like proteins hRad1, hHus1, and hRad9","volume":"275","author":"Rauen","year":"2000","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbamcr.2023.119484_bb0360","doi-asserted-by":"crossref","first-page":"793","DOI":"10.1083\/jcb.200810185","article-title":"TopBP1 and DNA polymerase-\u03b1 directly recruit the 9-1-1 complex to stalled DNA replication forks","volume":"184","author":"Yan","year":"2009","journal-title":"J. Cell Biol."},{"key":"10.1016\/j.bbamcr.2023.119484_bb0365","doi-asserted-by":"crossref","first-page":"479","DOI":"10.1016\/S0960-9822(00)00447-4","article-title":"Targeted disruption of the cell-cycle checkpoint gene ATR leads to early embryonic lethality in mice","volume":"10","author":"De Klein","year":"2000","journal-title":"Curr. Biol."},{"key":"10.1016\/j.bbamcr.2023.119484_bb0370","doi-asserted-by":"crossref","first-page":"2500","DOI":"10.1101\/gad.288282.116","article-title":"RB localizes to DNA double-strand breaks and promotes DNA end resection and homologous recombination through the recruitment of BRG1","volume":"30","author":"V\u00e9lez-Cruz","year":"2016","journal-title":"Genes Dev."},{"key":"10.1016\/j.bbamcr.2023.119484_bb0375","first-page":"20746","volume":"6","author":"Huang","year":"2015","journal-title":"RB in DNA repair. Oncotarget"},{"key":"10.1016\/j.bbamcr.2023.119484_bb0380","doi-asserted-by":"crossref","first-page":"638","DOI":"10.1080\/10409238.2017.1360836","article-title":"Cell cycle transcription control: DREAM\/MuvB and RB-E2F complexes","volume":"52","author":"Fischer","year":"2017","journal-title":"Crit. Rev. Biochem. Mol. Biol."},{"key":"10.1016\/j.bbamcr.2023.119484_bb0385","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1073\/pnas.2011278118","article-title":"SETD2-mediated H3K14 trimethylation promotes ATR activation and stalled replication fork restart in response to DNA replication stress","volume":"118","author":"Zhu","year":"2021","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbamcr.2023.119484_bb0390","doi-asserted-by":"crossref","DOI":"10.1155\/2016\/5959721","article-title":"Roles of pRB in the regulation of nucleosome and chromatin structures","author":"Uchida","year":"2016","journal-title":"Biomed. Res. Int."},{"key":"10.1016\/j.bbamcr.2023.119484_bb0395","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.bbamcr.2023.119484_bb0400","doi-asserted-by":"crossref","first-page":"4070","DOI":"10.1242\/jcs.053702","article-title":"Human RPA phosphorylation by ATR stimulates DNA synthesis and prevents ssDNA accumulation during DNA-replication stress","volume":"122","author":"Vassin","year":"2009","journal-title":"J. Cell Sci."},{"key":"10.1016\/j.bbamcr.2023.119484_bb0405","doi-asserted-by":"crossref","first-page":"493","DOI":"10.1083\/jcb.201404111","article-title":"Phosphorylated RPA recruits PALB2 to stalled DNA replication forks to facilitate fork recovery","volume":"206","author":"Murphy","year":"2014","journal-title":"J. Cell Biol."},{"key":"10.1016\/j.bbamcr.2023.119484_bb0410","doi-asserted-by":"crossref","first-page":"1013","DOI":"10.1002\/ijc.28226","article-title":"Roles of Chk1 in cell biology and cancer therapy","volume":"134","author":"Zhang","year":"2014","journal-title":"Int. J. Cancer"},{"key":"10.1016\/j.bbamcr.2023.119484_bb0415","doi-asserted-by":"crossref","first-page":"13374","DOI":"10.1073\/pnas.1903418116","article-title":"An ATR and CHK1 kinase signaling mechanism that limits origin firing during unperturbed DNA replication","volume":"116","author":"Moiseeva","year":"2019","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbamcr.2023.119484_bb0420","doi-asserted-by":"crossref","first-page":"323","DOI":"10.1016\/j.molcel.2015.02.031","article-title":"ATR-mediated phosphorylation of FANCI regulates dormant origin firing in response to replication stress","volume":"58","author":"Chen","year":"2015","journal-title":"Mol. Cell"},{"key":"10.1016\/j.bbamcr.2023.119484_bb0425","doi-asserted-by":"crossref","first-page":"1610","DOI":"10.1101\/gad.214080.113","article-title":"ATR phosphorylates SMARCAL1 to prevent replication fork collapse","volume":"27","author":"Couch","year":"2013","journal-title":"Genes Dev."},{"key":"10.1016\/j.bbamcr.2023.119484_bb0430","doi-asserted-by":"crossref","first-page":"3475","DOI":"10.1093\/nar\/gkp244","article-title":"Replication fork reversal and the maintenance of genome stability","volume":"37","author":"Atkinson","year":"2009","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.bbamcr.2023.119484_bb0435","doi-asserted-by":"crossref","first-page":"830","DOI":"10.1016\/j.molcel.2017.11.022","article-title":"Replication fork reversal: players and guardians","volume":"68","author":"Quinet","year":"2017","journal-title":"Mol. Cell"},{"key":"10.1016\/j.bbamcr.2023.119484_bb0440","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1038\/s41467-020-17324-z","article-title":"Sequential role of RAD51 paralog complexes in replication fork remodeling and restart","volume":"11","author":"Berti","year":"2020","journal-title":"Nat. Commun."}],"container-title":["Biochimica et Biophysica Acta (BBA) - Molecular Cell Research"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0167488923000563?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0167488923000563?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2024,10,20]],"date-time":"2024-10-20T14:26:57Z","timestamp":1729434417000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0167488923000563"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2023,8]]},"references-count":88,"journal-issue":{"issue":"6","published-print":{"date-parts":[[2023,8]]}},"alternative-id":["S0167488923000563"],"URL":"https:\/\/doi.org\/10.1016\/j.bbamcr.2023.119484","relation":{},"ISSN":["0167-4889"],"issn-type":[{"type":"print","value":"0167-4889"}],"subject":[],"published":{"date-parts":[[2023,8]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"p130RB2 positively contributes to ATR activation in response to replication stress via the RPA32-ETAA1 axis","name":"articletitle","label":"Article Title"},{"value":"Biochimica et Biophysica Acta (BBA) - Molecular Cell Research","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.bbamcr.2023.119484","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2023 Elsevier B.V.","name":"copyright","label":"Copyright"}],"article-number":"119484"}}