{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,27]],"date-time":"2026-09-27T08:44:45Z","timestamp":1790498685910,"version":"4.1.0"},"reference-count":69,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2018,4,1]],"date-time":"2018-04-01T00:00:00Z","timestamp":1522540800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2018,3,29]],"date-time":"2018-03-29T00:00:00Z","timestamp":1522281600000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by-nc-nd\/4.0\/"}],"funder":[{"DOI":"10.13039\/100004440","name":"Wellcome Trust","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100004440","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100000288","name":"Royal Society","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100000288","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["bmn.com","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Current Opinion in Structural Biology"],"published-print":{"date-parts":[[2018,4]]},"DOI":"10.1016\/j.sbi.2018.03.010","type":"journal-article","created":{"date-parts":[[2018,4,3]],"date-time":"2018-04-03T19:26:31Z","timestamp":1522783591000},"page":"177-189","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":61,"special_numbering":"C","title":["Architecture and activation of phosphatidylinositol 3-kinase related kinases"],"prefix":"10.1016","volume":"49","author":[{"given":"Stefan","family":"Imseng","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Christopher HS","family":"Aylett","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Timm","family":"Maier","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.sbi.2018.03.010_bib0350","doi-asserted-by":"crossref","first-page":"50","DOI":"10.1126\/science.270.5233.50","article-title":"PIK-related kinases: DNA repair, recombination, and cell cycle checkpoints","volume":"270","author":"Keith","year":"1995","journal-title":"Science"},{"key":"10.1016\/j.sbi.2018.03.010_bib0355","doi-asserted-by":"crossref","first-page":"225","DOI":"10.1016\/S0968-0004(00)01563-2","article-title":"FAT: a novel domain in PIK-related kinases","volume":"25","author":"Bosotti","year":"2000","journal-title":"Trends Biochem Sci"},{"key":"10.1016\/j.sbi.2018.03.010_sbref0360","doi-asserted-by":"crossref","first-page":"520","DOI":"10.1126\/science.aak9654","article-title":"DNA-PKcs structure suggests an allosteric mechanism modulating DNA double-strand break repair","volume":"355","author":"Sibanda","year":"2017","journal-title":"Science"},{"key":"10.1016\/j.sbi.2018.03.010_bib0365","doi-asserted-by":"crossref","first-page":"217","DOI":"10.1038\/nature12122","article-title":"mTOR kinase structure, mechanism and regulation","volume":"497","author":"Yang","year":"2013","journal-title":"Nature"},{"key":"10.1016\/j.sbi.2018.03.010_bib0370","doi-asserted-by":"crossref","first-page":"905","DOI":"10.1126\/science.1715094","article-title":"Targets for cell cycle arrest by the immunosuppressant rapamycin in yeast","volume":"253","author":"Heitman","year":"1991","journal-title":"Science"},{"key":"10.1016\/j.sbi.2018.03.010_bib0375","doi-asserted-by":"crossref","first-page":"585","DOI":"10.1016\/0092-8674(93)90144-F","article-title":"Target of rapamycin in yeast, TOR2, is an essential phosphatidylinositol kinase homolog required for G1 progression","volume":"73","author":"Kunz","year":"1993","journal-title":"Cell"},{"key":"10.1016\/j.sbi.2018.03.010_bib0380","doi-asserted-by":"crossref","first-page":"163","DOI":"10.1016\/S0092-8674(02)00808-5","article-title":"mTOR interacts with raptor to form a nutrient-sensitive complex that signals to the cell growth machinery","volume":"110","author":"Kim","year":"2002","journal-title":"Cell"},{"key":"10.1016\/j.sbi.2018.03.010_bib0385","doi-asserted-by":"crossref","first-page":"960","DOI":"10.1016\/j.cell.2017.02.004","article-title":"mTOR signaling in growth, metabolism, and disease","volume":"168","author":"Saxton","year":"2017","journal-title":"Cell"},{"key":"10.1016\/j.sbi.2018.03.010_bib0390","doi-asserted-by":"crossref","first-page":"274","DOI":"10.1016\/j.cell.2012.03.017","article-title":"mTOR signaling in growth control and disease","volume":"149","author":"Saxton","year":"2012","journal-title":"Cell"},{"key":"10.1016\/j.sbi.2018.03.010_bib0395","doi-asserted-by":"crossref","first-page":"1177","DOI":"10.1534\/genetics.111.133363","article-title":"Target of rapamycin (TOR) in nutrient signaling and growth control","volume":"189","author":"Loewith","year":"2011","journal-title":"Genetics"},{"key":"10.1016\/j.sbi.2018.03.010_bib0400","doi-asserted-by":"crossref","first-page":"744","DOI":"10.1016\/j.ceb.2011.09.003","article-title":"mTOR signaling in disease","volume":"23","author":"Dazert","year":"2011","journal-title":"Curr Opin Cell Biol"},{"key":"10.1016\/j.sbi.2018.03.010_bib0405","doi-asserted-by":"crossref","first-page":"758","DOI":"10.1038\/341758a0","article-title":"A receptor for the immuno-suppressant FK506 is a cis\u2013trans peptidyl\u2013prolyl isomerase","volume":"341","author":"Harding","year":"1989","journal-title":"Nature"},{"key":"10.1016\/j.sbi.2018.03.010_bib0410","doi-asserted-by":"crossref","first-page":"755","DOI":"10.1038\/341755a0","article-title":"A cytosolic binding protein for the immunosuppressant FK506 has peptidyl\u2013prolyl isomerase activity but is distinct from cyclophilin","volume":"341","author":"Siekierka","year":"1989","journal-title":"Nature"},{"key":"10.1016\/j.sbi.2018.03.010_bib0415","doi-asserted-by":"crossref","first-page":"4715","DOI":"10.1021\/ja043277y","article-title":"Characterization of the FKBP-rapamycin-FRB ternary complex","volume":"127","author":"Banaszynski","year":"2005","journal-title":"J Am Chem Soc"},{"key":"10.1016\/j.sbi.2018.03.010_bib0420","doi-asserted-by":"crossref","first-page":"9622","DOI":"10.1021\/acs.jmedchem.6b00411","article-title":"Peptidyl-proline isomerases (PPIases): targets for natural products and natural product-inspired compounds","volume":"59","author":"Dunyak","year":"2016","journal-title":"J Med Chem"},{"key":"10.1016\/j.sbi.2018.03.010_bib0425","doi-asserted-by":"crossref","first-page":"30697","DOI":"10.1074\/jbc.M505553200","article-title":"Molecular organization of target of rapamycin complex 2","volume":"280","author":"Wullschleger","year":"2005","journal-title":"J Biol Chem"},{"key":"10.1016\/j.sbi.2018.03.010_bib0430","doi-asserted-by":"crossref","first-page":"768","DOI":"10.1016\/j.molcel.2010.05.017","article-title":"Structure of the human mTOR complex I and its implications for rapamycin inhibition","volume":"38","author":"Yip","year":"2010","journal-title":"Mol Cell"},{"key":"10.1016\/j.sbi.2018.03.010_bib0435","doi-asserted-by":"crossref","first-page":"977","DOI":"10.1016\/j.molcel.2015.04.031","article-title":"Molecular basis of the rapamycin insensitivity of target of rapamycin complex 2","volume":"58","author":"Gaubitz","year":"2015","journal-title":"Mol Cell"},{"key":"10.1016\/j.sbi.2018.03.010_bib0440","doi-asserted-by":"crossref","first-page":"895","DOI":"10.1016\/S1097-2765(03)00114-X","article-title":"GbetaL, a positive regulator of the rapamycin-sensitive pathway required for the nutrient-sensitive interaction between raptor and mTOR","volume":"11","author":"Kim","year":"2003","journal-title":"Mol Cell"},{"key":"10.1016\/j.sbi.2018.03.010_sbref0445","doi-asserted-by":"crossref","first-page":"48","DOI":"10.1126\/science.aaa3870","article-title":"Architecture of human mTOR complex 1","volume":"351","author":"Aylett","year":"2016","journal-title":"Science"},{"key":"10.1016\/j.sbi.2018.03.010_sbref0450","doi-asserted-by":"crossref","first-page":"11016","DOI":"10.1038\/ncomms11016","article-title":"Tor forms a dimer through an N-terminal helical solenoid with a complex topology","volume":"7","author":"Baretic","year":"2016","journal-title":"Nat Commun"},{"key":"10.1016\/j.sbi.2018.03.010_bib0455","doi-asserted-by":"crossref","first-page":"878","DOI":"10.1007\/s13238-016-0346-6","article-title":"4.4\u00c5 resolution cryo-EM structure of human mTOR complex 1","volume":"7","author":"Yang","year":"2016","journal-title":"Protein Cell"},{"key":"10.1016\/j.sbi.2018.03.010_sbref0460","doi-asserted-by":"crossref","first-page":"368","DOI":"10.1038\/nature25023","article-title":"Mechanisms of mTORC1 activation by RHEB and inhibition by PRAS40","volume":"552","author":"Yang","year":"2017","journal-title":"Nature"},{"key":"10.1016\/j.sbi.2018.03.010_bib0465","doi-asserted-by":"crossref","first-page":"457","DOI":"10.1016\/S1097-2765(02)00636-6","article-title":"Two TOR complexes, only one of which is rapamycin sensitive, have distinct roles in cell growth control","volume":"10","author":"Loewith","year":"2002","journal-title":"Mol Cell"},{"key":"10.1016\/j.sbi.2018.03.010_bib0470","doi-asserted-by":"crossref","first-page":"532","DOI":"10.1016\/j.tibs.2016.04.001","article-title":"TORC2 structure and function","volume":"41","author":"Gaubitz","year":"2016","journal-title":"Trends Biochem Sci"},{"key":"10.1016\/j.sbi.2018.03.010_bib0475","doi-asserted-by":"crossref","first-page":"177","DOI":"10.1016\/S0092-8674(02)00833-4","article-title":"Raptor, a binding partner of target of rapamycin (TOR), mediates TOR action","volume":"110","author":"Hara","year":"2002","journal-title":"Cell"},{"key":"10.1016\/j.sbi.2018.03.010_bib0480","doi-asserted-by":"crossref","first-page":"1496","DOI":"10.1126\/science.1157535","article-title":"The Rag GTPases bind raptor and mediate amino acid signaling to mTORC1","volume":"320","author":"Sancak","year":"2008","journal-title":"Science"},{"key":"10.1016\/j.sbi.2018.03.010_bib0485","doi-asserted-by":"crossref","first-page":"797","DOI":"10.1016\/S0960-9822(03)00329-4","article-title":"TOS motif-mediated raptor binding regulates 4E-BP1 multisite phosphorylation and function","volume":"13","author":"Schalm","year":"2003","journal-title":"Curr Biol"},{"key":"10.1016\/j.sbi.2018.03.010_bib0490","doi-asserted-by":"crossref","first-page":"15461","DOI":"10.1074\/jbc.C200665200","article-title":"The mammalian target of rapamycin (mTOR) partner, raptor, binds the mTOR substrates p70 S6 kinase and 4E-BP1 through their TOR signaling (TOS) motif","volume":"278","author":"Nojima","year":"2003","journal-title":"J Biol Chem"},{"key":"10.1016\/j.sbi.2018.03.010_bib0495","doi-asserted-by":"crossref","first-page":"1296","DOI":"10.1016\/j.cub.2004.06.054","article-title":"Rictor, a novel binding partner of mTOR, defines a rapamycin-insensitive and raptor-independent pathway that regulates the cytoskeleton","volume":"14","author":"Dos","year":"2004","journal-title":"Curr Biol"},{"key":"10.1016\/j.sbi.2018.03.010_bib0500","doi-asserted-by":"crossref","first-page":"1865","DOI":"10.1016\/j.cub.2006.08.001","article-title":"mSin1 is necessary for Akt\/PKB phosphorylation, and its isoforms define three distinct mTORC2s","volume":"16","author":"Frias","year":"2006","journal-title":"Curr Biol"},{"key":"10.1016\/j.sbi.2018.03.010_bib0505","doi-asserted-by":"crossref","first-page":"125","DOI":"10.1016\/j.cell.2006.08.033","article-title":"SIN1\/MIP1 maintains rictor-mTOR complex integrity and regulates Akt phosphorylation and substrate specificity","volume":"127","author":"Jacinto","year":"2006","journal-title":"Cell"},{"key":"10.1016\/j.sbi.2018.03.010_bib0510","doi-asserted-by":"crossref","first-page":"2820","DOI":"10.1101\/gad.1461206","article-title":"Identification of Sin1 as an essential TORC2 component required for complex formation and kinase activity","volume":"20","author":"Yang","year":"2006","journal-title":"Genes Dev"},{"key":"10.1016\/j.sbi.2018.03.010_bib0515","doi-asserted-by":"crossref","first-page":"1340","DOI":"10.1038\/ncb2860","article-title":"Sin1 phosphorylation impairs mTORC2 complex integrity and inhibits downstream Akt signalling to suppress tumorigenesis","volume":"15","author":"Liu","year":"2013","journal-title":"Nat Cell Biol"},{"key":"10.1016\/j.sbi.2018.03.010_bib0520","doi-asserted-by":"crossref","first-page":"e19594","DOI":"10.7554\/eLife.19594","article-title":"Substrate specificity of tor complex 2 is determined by a ubiquitin-fold domain of the sin1 subunit","volume":"6","author":"Tatebe","year":"2017","journal-title":"Elife"},{"key":"10.1016\/j.sbi.2018.03.010_bib0525","doi-asserted-by":"crossref","first-page":"513","DOI":"10.1042\/BJ20070540","article-title":"Identification of Protor as a novel Rictor-binding component of mTOR complex-2","volume":"405","author":"Pearce","year":"2007","journal-title":"Biochem J"},{"key":"10.1016\/j.sbi.2018.03.010_sbref0530","doi-asserted-by":"crossref","first-page":"1729","DOI":"10.1038\/s41467-017-01862-0","article-title":"Cryo-EM structure of Saccharomyces cerevisiae target of rapamycin complex 2","volume":"8","author":"Karuppasamy","year":"2017","journal-title":"Nat Commun"},{"key":"10.1016\/j.sbi.2018.03.010_sbref0535","doi-asserted-by":"crossref","DOI":"10.7554\/eLife.33101","article-title":"Architecture of the human mTORC2 core complex","volume":"7","author":"Stuttfeld","year":"2018","journal-title":"Elife"},{"key":"10.1016\/j.sbi.2018.03.010_bib0540","doi-asserted-by":"crossref","first-page":"386","DOI":"10.1107\/S1744309112007178","article-title":"Structures of the pleckstrin homology domain of Saccharomyces cerevisiae Avo1 and its human orthologue Sin1, an essential subunit of TOR complex 2","volume":"68","author":"Pan","year":"2012","journal-title":"Acta Crystallogr Sect F Struct Biol Cryst Commun"},{"key":"10.1016\/j.sbi.2018.03.010_sbref0545","doi-asserted-by":"crossref","first-page":"265","DOI":"10.1038\/nature24021","article-title":"TORC1 organized in inhibited domains (TOROIDs) regulate TORC1 activity","volume":"550","author":"Prouteau","year":"2017","journal-title":"Nature"},{"key":"10.1016\/j.sbi.2018.03.010_bib0550","doi-asserted-by":"crossref","first-page":"a012716","DOI":"10.1101\/cshperspect.a012716","article-title":"DNA damage sensing by the ATM and ATR kinases","volume":"5","author":"Mar\u00e9chal","year":"2013","journal-title":"Cold Spring Harb Perspect Biol"},{"key":"10.1016\/j.sbi.2018.03.010_bib0555","doi-asserted-by":"crossref","first-page":"801","DOI":"10.1016\/j.molcel.2017.05.015","article-title":"ATM, ATR, and DNA-PK: the trinity at the heart of the DNA damage response","volume":"66","author":"Blackford","year":"2017","journal-title":"Mol Cell"},{"key":"10.1016\/j.sbi.2018.03.010_bib0560","doi-asserted-by":"crossref","first-page":"1160","DOI":"10.1126\/science.1140321","article-title":"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage","volume":"316","author":"Matsuoka","year":"2007","journal-title":"Science"},{"key":"10.1016\/j.sbi.2018.03.010_bib0565","doi-asserted-by":"crossref","first-page":"93","DOI":"10.1126\/science.1091496","article-title":"Direct activation of the ATM protein kinase by the Mre11\/Rad50\/Nbs1 complex","volume":"304","author":"Lee","year":"2004","journal-title":"Science"},{"key":"10.1016\/j.sbi.2018.03.010_bib0570","doi-asserted-by":"crossref","first-page":"499","DOI":"10.1038\/nature01368","article-title":"DNA damage activates ATM through intermolecular autophosphorylation and dimer dissociation","volume":"421","author":"Bakkenist","year":"2003","journal-title":"Nature"},{"key":"10.1016\/j.sbi.2018.03.010_sbref0575","doi-asserted-by":"crossref","first-page":"e1700933","DOI":"10.1126\/sciadv.1700933","article-title":"Structures of closed and open conformations of dimeric human ATM","volume":"3","author":"Bareti\u0107","year":"2017","journal-title":"Sci Adv"},{"key":"10.1016\/j.sbi.2018.03.010_bib0580","doi-asserted-by":"crossref","first-page":"1117","DOI":"10.1080\/15384101.2016.1158362","article-title":"Structure of the human dimeric ATM kinase","volume":"15","author":"Lau","year":"2016","journal-title":"Cell Cycle"},{"key":"10.1016\/j.sbi.2018.03.010_sbref0585","doi-asserted-by":"crossref","first-page":"11655","DOI":"10.1038\/ncomms11655","article-title":"Structure of the intact ATM\/Tel1 kinase","volume":"7","author":"Wang","year":"2016","journal-title":"Nat Commun"},{"key":"10.1016\/j.sbi.2018.03.010_bib0590","doi-asserted-by":"crossref","first-page":"13436","DOI":"10.1074\/jbc.M115.708263","article-title":"The dimeric architecture of checkpoint kinases Mec1ATR and Tel1ATM reveal a common structural organization","volume":"291","author":"Sawicka","year":"2016","journal-title":"J Biol Chem"},{"key":"10.1016\/j.sbi.2018.03.010_bib0595","doi-asserted-by":"crossref","first-page":"5363","DOI":"10.1128\/MCB.25.13.5363-5379.2005","article-title":"ATM activation and its recruitment to damaged DNA require binding to the C terminus of Nbs1","volume":"25","author":"You","year":"2005","journal-title":"Mol Cell Biol"},{"key":"10.1016\/j.sbi.2018.03.010_bib0600","doi-asserted-by":"crossref","first-page":"15158","DOI":"10.1074\/jbc.M412065200","article-title":"DNA damage-induced association of ATM with its target proteins requires a protein interaction domain in the N terminus of ATM","volume":"280","author":"Fernandes","year":"2005","journal-title":"J Biol Chem"},{"key":"10.1016\/j.sbi.2018.03.010_bib0605","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.sbi.2018.03.010_bib0610","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.sbi.2018.03.010_bib0615","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.sbi.2018.03.010_sbref0620","doi-asserted-by":"crossref","first-page":"1206","DOI":"10.1126\/science.aan8414","article-title":"3.9\u00c5 structure of the yeast Mec1-Ddc2 complex, a homolog of human ATR-ATRIP","volume":"358","author":"Wang","year":"2017","journal-title":"Science"},{"key":"10.1016\/j.sbi.2018.03.010_bib0625","doi-asserted-by":"crossref","first-page":"143","DOI":"10.1038\/cr.2017.158","article-title":"Cryo-EM structure of human ATR-ATRIP complex","volume":"28","author":"Rao","year":"2017","journal-title":"Cell Res"},{"key":"10.1016\/j.sbi.2018.03.010_bib0630","doi-asserted-by":"crossref","first-page":"181","DOI":"10.1146\/annurev.biochem.052308.093131","article-title":"The mechanism of double-strand DNA break repair by the nonhomologous DNA end-joining pathway","volume":"79","author":"Lieber","year":"2010","journal-title":"Annu Rev Biochem"},{"key":"10.1016\/j.sbi.2018.03.010_bib0635","doi-asserted-by":"crossref","first-page":"320","DOI":"10.1016\/j.molcel.2012.05.052","article-title":"Quantitative live cell imaging reveals a gradual shift between DNA repair mechanisms and a maximal use of HR in mid S phase","volume":"47","author":"Karanam","year":"2012","journal-title":"Mol Cell"},{"key":"10.1016\/j.sbi.2018.03.010_bib0640","doi-asserted-by":"crossref","first-page":"194","DOI":"10.1016\/j.pbiomolbio.2014.12.003","article-title":"The DNA-dependent protein kinase: a multifunctional protein kinase with roles in DNA double strand break repair and mitosis","volume":"117","author":"Jette","year":"2015","journal-title":"Prog Biophys Mol Biol"},{"key":"10.1016\/j.sbi.2018.03.010_bib0645","doi-asserted-by":"crossref","first-page":"3881","DOI":"10.1128\/MCB.02366-06","article-title":"trans Autophosphorylation at DNA-dependent protein kinase's two major autophosphorylation site clusters facilitates end processing but not end joining","volume":"27","author":"Meek","year":"2007","journal-title":"Mol Cell Biol"},{"key":"10.1016\/j.sbi.2018.03.010_bib0650","doi-asserted-by":"crossref","first-page":"1414","DOI":"10.1074\/jbc.M109.065615","article-title":"Ku and DNA-dependent protein kinase dynamic conformations and assembly regulate DNA binding and the initial non-homologous end joining complex","volume":"285","author":"Hammel","year":"2010","journal-title":"J Biol Chem"},{"key":"10.1016\/j.sbi.2018.03.010_bib0655","doi-asserted-by":"crossref","first-page":"1341","DOI":"10.1038\/cr.2017.110","article-title":"Cryo-EM structure of human DNA-PK holoenzyme","volume":"27","author":"Yin","year":"2017","journal-title":"Cell Res"},{"key":"10.1016\/j.sbi.2018.03.010_sbref0660","doi-asserted-by":"crossref","first-page":"7367","DOI":"10.1073\/pnas.1707386114","article-title":"Cryo-EM structure of the DNA-PK holoenzyme","volume":"114","author":"Sharif","year":"2017","journal-title":"Proc Natl Acad Sci U S A"},{"key":"10.1016\/j.sbi.2018.03.010_bib0665","doi-asserted-by":"crossref","first-page":"607","DOI":"10.1038\/35088000","article-title":"Structure of the Ku heterodimer bound to DNA and its implications for double-strand break repair","volume":"412","author":"Walker","year":"2001","journal-title":"Nature"},{"key":"10.1016\/j.sbi.2018.03.010_bib0670","doi-asserted-by":"crossref","first-page":"850","DOI":"10.1016\/j.tibs.2017.09.001","article-title":"Sharing the SAGA","volume":"42","author":"Helmlinger","year":"2017","journal-title":"Trends Biochem Sci"},{"key":"10.1016\/j.sbi.2018.03.010_sbref0675","doi-asserted-by":"crossref","first-page":"e28384","DOI":"10.7554\/eLife.28384","article-title":"Cryo-EM structure of the SAGA and NuA4 coactivator subunit Tra1 at 3.7 angstrom resolution","volume":"6","author":"D\u00edaz-Sant\u00edn","year":"2017","journal-title":"Elife"},{"key":"10.1016\/j.sbi.2018.03.010_sbref0680","doi-asserted-by":"crossref","first-page":"1556","DOI":"10.1038\/s41467-017-01564-7","article-title":"Structure of the transcription activator target Tra1 within the chromatin modifying complex SAGA","volume":"8","author":"Sharov","year":"2017","journal-title":"Nat Commun"},{"key":"10.1016\/j.sbi.2018.03.010_bib0685","doi-asserted-by":"crossref","first-page":"2809","DOI":"10.4161\/cc.7.18.6689","article-title":"Activation of ATR and related PIKKs","volume":"7","author":"Mordes","year":"2008","journal-title":"Cell Cycle"},{"key":"10.1016\/j.sbi.2018.03.010_bib0690","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"}],"container-title":["Current Opinion in Structural Biology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0959440X18300186?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0959440X18300186?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2019,8,8]],"date-time":"2019-08-08T22:37:53Z","timestamp":1565303873000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0959440X18300186"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2018,4]]},"references-count":69,"alternative-id":["S0959440X18300186"],"URL":"https:\/\/doi.org\/10.1016\/j.sbi.2018.03.010","relation":{"has-review":[{"id-type":"doi","id":"10.3410\/f.732994786.793554251","asserted-by":"object"}]},"ISSN":["0959-440X"],"issn-type":[{"value":"0959-440X","type":"print"}],"subject":[],"published":{"date-parts":[[2018,4]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Architecture and activation of phosphatidylinositol 3-kinase related kinases","name":"articletitle","label":"Article Title"},{"value":"Current Opinion in Structural Biology","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.sbi.2018.03.010","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2018 The Authors. Published by Elsevier Ltd.","name":"copyright","label":"Copyright"}]}}