{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,10]],"date-time":"2026-06-10T15:34:16Z","timestamp":1781105656597,"version":"3.54.1"},"reference-count":76,"publisher":"National Academy of Sciences","issue":"30","license":[{"start":{"date-parts":[[2019,1,11]],"date-time":"2019-01-11T00:00:00Z","timestamp":1547164800000},"content-version":"vor","delay-in-days":184,"URL":"http:\/\/www.pnas.org\/site\/aboutpnas\/licenses.xhtml"}],"funder":[{"name":"KU Leuven IDO","award":["IDO\/12\/008-3E130241"],"award-info":[{"award-number":["IDO\/12\/008-3E130241"]}]},{"DOI":"10.13039\/501100001824","name":"Grantov\u00e1 Agentura \u010cesk\u00e9 Republiky","doi-asserted-by":"publisher","award":["16-06357S"],"award-info":[{"award-number":["16-06357S"]}],"id":[{"id":"10.13039\/501100001824","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003130","name":"Fonds Wetenschappelijk Onderzoek","doi-asserted-by":"publisher","award":["G.0595.13"],"award-info":[{"award-number":["G.0595.13"]}],"id":[{"id":"10.13039\/501100003130","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001823","name":"MEYS CR","doi-asserted-by":"crossref","award":["LO1304"],"award-info":[{"award-number":["LO1304"]}],"id":[{"id":"10.13039\/501100001823","id-type":"DOI","asserted-by":"crossref"}]},{"DOI":"10.13039\/501100008530","name":"EC | European Regional Development Fund","doi-asserted-by":"publisher","award":["CZ.02.1.01\/0.0\/0.0\/16_019\/0000729"],"award-info":[{"award-number":["CZ.02.1.01\/0.0\/0.0\/16_019\/0000729"]}],"id":[{"id":"10.13039\/501100008530","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003132","name":"Agentschap voor Innovatie door Wetenschap en Technologie","doi-asserted-by":"publisher","award":["140038"],"award-info":[{"award-number":["140038"]}],"id":[{"id":"10.13039\/501100003132","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["www.pnas.org"],"crossmark-restriction":true},"short-container-title":["Proc. Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[2018,7,24]]},"abstract":"<jats:title>Significance<\/jats:title>\n                  <jats:p>The transcription coactivator LEDGF\/p75 contributes to regulation of gene expression by tethering other factors to actively transcribed genes on chromatin. Its chromatin-tethering activity is hijacked in two important disease settings, HIV and mixed-lineage leukemia; however, the basis for the biological regulation of LEDGF\/p75\u2019s interaction to binding partners has remained unknown. This has represented a gap in our understanding of LEDGF\/p75\u2019s fundamental biological function and a major limitation for development of therapeutic targeting of LEDGF\/p75 in human disease. Our work provides a mechanistic understanding of how the lens epithelium-derived growth factor interaction network is regulated at the molecular level.<\/jats:p>","DOI":"10.1073\/pnas.1803909115","type":"journal-article","created":{"date-parts":[[2018,7,11]],"date-time":"2018-07-11T16:25:44Z","timestamp":1531326344000},"update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":42,"title":["Affinity switching of the LEDGF\/p75 IBD interactome is governed by kinase-dependent phosphorylation"],"prefix":"10.1073","volume":"115","author":[{"given":"Subhalakshmi","family":"Sharma","sequence":"first","affiliation":[{"name":"Molecular Virology and Gene Therapy, KU Leuven, 3000 Leuven, Belgium;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kate\u0159ina","family":"\u010cerm\u00e1kov\u00e1","sequence":"additional","affiliation":[{"name":"Institute of Organic Chemistry and Biochemistry of the Czech Academy of Sciences, 166 10 Prague 6, Czech Republic;"},{"name":"Department of Molecular &amp; Cellular Biology, Baylor College of Medicine, Houston, TX 77030;"},{"name":"Center for Precision Environmental Health, Baylor College of Medicine, Houston, TX 77030;"},{"name":"Dan L Duncan Comprehensive Cancer Center, Baylor College of Medicine, Houston, TX 77030;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jan","family":"De Rijck","sequence":"additional","affiliation":[{"name":"Molecular Virology and Gene Therapy, KU Leuven, 3000 Leuven, Belgium;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jonas","family":"Demeulemeester","sequence":"additional","affiliation":[{"name":"Molecular Virology and Gene Therapy, KU Leuven, 3000 Leuven, Belgium;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Milan","family":"F\u00e1bry","sequence":"additional","affiliation":[{"name":"Institute of Molecular Genetics of the Czech Academy of Sciences, 142 20 Prague 4, Czech Republic;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-9410-5687","authenticated-orcid":false,"given":"Sara","family":"El Ashkar","sequence":"additional","affiliation":[{"name":"Molecular Virology and Gene Therapy, KU Leuven, 3000 Leuven, Belgium;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Siska","family":"Van Belle","sequence":"additional","affiliation":[{"name":"Molecular Virology and Gene Therapy, KU Leuven, 3000 Leuven, Belgium;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Martin","family":"Lep\u0161\u00edk","sequence":"additional","affiliation":[{"name":"Institute of Organic Chemistry and Biochemistry of the Czech Academy of Sciences, 166 10 Prague 6, Czech Republic;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Petr","family":"Tesina","sequence":"additional","affiliation":[{"name":"Institute of Organic Chemistry and Biochemistry of the Czech Academy of Sciences, 166 10 Prague 6, Czech Republic;"},{"name":"Institute of Molecular Genetics of the Czech Academy of Sciences, 142 20 Prague 4, Czech Republic;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Vojt\u011bch","family":"Duchoslav","sequence":"additional","affiliation":[{"name":"Institute of Organic Chemistry and Biochemistry of the Czech Academy of Sciences, 166 10 Prague 6, Czech Republic;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Petr","family":"Nov\u00e1k","sequence":"additional","affiliation":[{"name":"Institute of Microbiology of the Czech Academy of Sciences, 142 20 Prague 4, Czech Republic;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Martin","family":"Hub\u00e1lek","sequence":"additional","affiliation":[{"name":"Institute of Organic Chemistry and Biochemistry of the Czech Academy of Sciences, 166 10 Prague 6, Czech Republic;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Pavel","family":"Srb","sequence":"additional","affiliation":[{"name":"Institute of Organic Chemistry and Biochemistry of the Czech Academy of Sciences, 166 10 Prague 6, Czech Republic;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Frauke","family":"Christ","sequence":"additional","affiliation":[{"name":"Molecular Virology and Gene Therapy, KU Leuven, 3000 Leuven, Belgium;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Pavl\u00edna","family":"\u0158ez\u00e1\u010dov\u00e1","sequence":"additional","affiliation":[{"name":"Institute of Organic Chemistry and Biochemistry of the Czech Academy of Sciences, 166 10 Prague 6, Czech Republic;"},{"name":"Institute of Molecular Genetics of the Czech Academy of Sciences, 142 20 Prague 4, Czech Republic;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-4441-497X","authenticated-orcid":false,"given":"H. Courtney","family":"Hodges","sequence":"additional","affiliation":[{"name":"Department of Molecular &amp; Cellular Biology, Baylor College of Medicine, Houston, TX 77030;"},{"name":"Center for Precision Environmental Health, Baylor College of Medicine, Houston, TX 77030;"},{"name":"Dan L Duncan Comprehensive Cancer Center, Baylor College of Medicine, Houston, TX 77030;"},{"name":"Center for Cancer Epigenetics, The University of Texas MD Anderson Cancer Center, Houston, TX 77030;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Zeger","family":"Debyser","sequence":"additional","affiliation":[{"name":"Molecular Virology and Gene Therapy, KU Leuven, 3000 Leuven, Belgium;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"V\u00e1clav","family":"Veverka","sequence":"additional","affiliation":[{"name":"Institute of Organic Chemistry and Biochemistry of the Czech Academy of Sciences, 166 10 Prague 6, Czech Republic;"},{"name":"Department of Cell Biology, Faculty of Science, Charles University, 116 36 Prague 1, Czech Republic"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"341","published-online":{"date-parts":[[2018,7,11]]},"reference":[{"key":"e_1_3_4_1_2","doi-asserted-by":"crossref","first-page":"26114","DOI":"10.1074\/jbc.M109.089433","article-title":"The Dnmt3a PWWP domain reads histone 3 lysine 36 trimethylation and guides DNA methylation","volume":"285","author":"Dhayalan A","year":"2010","unstructured":"A Dhayalan, , The Dnmt3a PWWP domain reads histone 3 lysine 36 trimethylation and guides DNA methylation. J Biol Chem 285, 26114\u201326120 (2010).","journal-title":"J Biol Chem"},{"key":"e_1_3_4_2_2","doi-asserted-by":"crossref","first-page":"3924","DOI":"10.1093\/nar\/gkt074","article-title":"Structural basis for high-affinity binding of LEDGF PWWP to mononucleosomes","volume":"41","author":"Eidahl JO","year":"2013","unstructured":"JO Eidahl, , Structural basis for high-affinity binding of LEDGF PWWP to mononucleosomes. Nucleic Acids Res 41, 3924\u20133936 (2013).","journal-title":"Nucleic Acids Res"},{"key":"e_1_3_4_3_2","doi-asserted-by":"crossref","first-page":"4241","DOI":"10.1093\/nar\/gkt1394","article-title":"MLL fusion proteins link transcriptional coactivators to previously active CpG-rich promoters","volume":"42","author":"Okuda H","year":"2014","unstructured":"H Okuda, , MLL fusion proteins link transcriptional coactivators to previously active CpG-rich promoters. Nucleic Acids Res 42, 4241\u20134256 (2014).","journal-title":"Nucleic Acids Res"},{"key":"e_1_3_4_4_2","doi-asserted-by":"crossref","first-page":"e1002717","DOI":"10.1371\/journal.pgen.1002717","article-title":"Psip1\/Ledgf p52 binds methylated histone H3K36 and splicing factors and contributes to the regulation of alternative splicing","volume":"8","author":"Pradeepa MM","year":"2012","unstructured":"MM Pradeepa, HG Sutherland, J Ule, GR Grimes, WA Bickmore, Psip1\/Ledgf p52 binds methylated histone H3K36 and splicing factors and contributes to the regulation of alternative splicing. PLoS Genet 8, e1002717 (2012).","journal-title":"PLoS Genet"},{"key":"e_1_3_4_5_2","doi-asserted-by":"crossref","first-page":"48883","DOI":"10.1074\/jbc.M406307200","article-title":"Identification of an evolutionarily conserved domain in human lens epithelium-derived growth factor\/transcriptional co-activator p75 (LEDGF\/p75) that binds HIV-1 integrase","volume":"279","author":"Cherepanov P","year":"2004","unstructured":"P Cherepanov, E Devroe, PA Silver, A Engelman, Identification of an evolutionarily conserved domain in human lens epithelium-derived growth factor\/transcriptional co-activator p75 (LEDGF\/p75) that binds HIV-1 integrase. J Biol Chem 279, 48883\u201348892 (2004).","journal-title":"J Biol Chem"},{"key":"e_1_3_4_6_2","doi-asserted-by":"crossref","first-page":"1287","DOI":"10.1038\/nm1329","article-title":"A role for LEDGF\/p75 in targeting HIV DNA integration","volume":"11","author":"Ciuffi A","year":"2005","unstructured":"A Ciuffi, , A role for LEDGF\/p75 in targeting HIV DNA integration. Nat Med 11, 1287\u20131289 (2005).","journal-title":"Nat Med"},{"key":"e_1_3_4_7_2","doi-asserted-by":"crossref","first-page":"33528","DOI":"10.1074\/jbc.M303594200","article-title":"LEDGF\/p75 is essential for nuclear and chromosomal targeting of HIV-1 integrase in human cells","volume":"278","author":"Maertens G","year":"2003","unstructured":"G Maertens, , LEDGF\/p75 is essential for nuclear and chromosomal targeting of HIV-1 integrase in human cells. J Biol Chem 278, 33528\u201333539 (2003).","journal-title":"J Biol Chem"},{"key":"e_1_3_4_8_2","doi-asserted-by":"crossref","first-page":"e1002558","DOI":"10.1371\/journal.ppat.1002558","article-title":"LEDGF\/p75-independent HIV-1 replication demonstrates a role for HRP-2 and remains sensitive to inhibition by LEDGINs","volume":"8","author":"Schrijvers R","year":"2012","unstructured":"R Schrijvers, , LEDGF\/p75-independent HIV-1 replication demonstrates a role for HRP-2 and remains sensitive to inhibition by LEDGINs. PLoS Pathog 8, e1002558 (2012).","journal-title":"PLoS Pathog"},{"key":"e_1_3_4_9_2","doi-asserted-by":"crossref","first-page":"1767","DOI":"10.1101\/gad.1565107","article-title":"LEDGF\/p75 functions downstream from preintegration complex formation to effect gene-specific HIV-1 integration","volume":"21","author":"Shun MC","year":"2007","unstructured":"MC Shun, , LEDGF\/p75 functions downstream from preintegration complex formation to effect gene-specific HIV-1 integration. Genes Dev 21, 1767\u20131778 (2007).","journal-title":"Genes Dev"},{"key":"e_1_3_4_10_2","doi-asserted-by":"crossref","first-page":"442","DOI":"10.1038\/nchembio.370","article-title":"Rational design of small-molecule inhibitors of the LEDGF\/p75-integrase interaction and HIV replication","volume":"6","author":"Christ F","year":"2010","unstructured":"F Christ, , Rational design of small-molecule inhibitors of the LEDGF\/p75-integrase interaction and HIV replication. Nat Chem Biol 6, 442\u2013448 (2010).","journal-title":"Nat Chem Biol"},{"key":"e_1_3_4_11_2","doi-asserted-by":"crossref","first-page":"407","DOI":"10.1016\/j.jmb.2007.06.090","article-title":"Differential interaction of HIV-1 integrase and JPO2 with the C terminus of LEDGF\/p75","volume":"372","author":"Bartholomeeusen K","year":"2007","unstructured":"K Bartholomeeusen, , Differential interaction of HIV-1 integrase and JPO2 with the C terminus of LEDGF\/p75. J Mol Biol 372, 407\u2013421 (2007).","journal-title":"J Mol Biol"},{"key":"e_1_3_4_12_2","doi-asserted-by":"crossref","first-page":"2563","DOI":"10.1242\/jcs.02995","article-title":"Transcriptional co-activator p75 binds and tethers the Myc-interacting protein JPO2 to chromatin","volume":"119","author":"Maertens GN","year":"2006","unstructured":"GN Maertens, P Cherepanov, A Engelman, Transcriptional co-activator p75 binds and tethers the Myc-interacting protein JPO2 to chromatin. J Cell Sci 119, 2563\u20132571 (2006).","journal-title":"J Cell Sci"},{"key":"e_1_3_4_13_2","doi-asserted-by":"crossref","first-page":"2802","DOI":"10.1158\/0008-5472.CAN-15-2194","article-title":"JPO2\/CDCA7L and LEDGF\/p75 are novel mediators of PI3K\/AKT signaling and aggressive phenotypes in medulloblastoma","volume":"76","author":"Chan TS","year":"2016","unstructured":"TS Chan, C Hawkins, JR Krieger, CJ McGlade, A Huang, JPO2\/CDCA7L and LEDGF\/p75 are novel mediators of PI3K\/AKT signaling and aggressive phenotypes in medulloblastoma. Cancer Res 76, 2802\u20132812 (2016).","journal-title":"Cancer Res"},{"key":"e_1_3_4_14_2","doi-asserted-by":"crossref","first-page":"11467","DOI":"10.1074\/jbc.M807781200","article-title":"Lens epithelium-derived growth factor\/p75 interacts with the transposase-derived DDE domain of PogZ","volume":"284","author":"Bartholomeeusen K","year":"2009","unstructured":"K Bartholomeeusen, , Lens epithelium-derived growth factor\/p75 interacts with the transposase-derived DDE domain of PogZ. J Biol Chem 284, 11467\u201311477 (2009).","journal-title":"J Biol Chem"},{"key":"e_1_3_4_15_2","doi-asserted-by":"crossref","first-page":"541","DOI":"10.1074\/jbc.M109.036491","article-title":"Transcriptional co-activator LEDGF interacts with Cdc7-activator of S-phase kinase (ASK) and stimulates its enzymatic activity","volume":"285","author":"Hughes S","year":"2010","unstructured":"S Hughes, V Jenkins, MJ Dar, A Engelman, P Cherepanov, Transcriptional co-activator LEDGF interacts with Cdc7-activator of S-phase kinase (ASK) and stimulates its enzymatic activity. J Biol Chem 285, 541\u2013554 (2010).","journal-title":"J Biol Chem"},{"key":"e_1_3_4_16_2","doi-asserted-by":"crossref","first-page":"36","DOI":"10.1016\/j.ccr.2008.05.003","article-title":"Menin critically links MLL proteins with LEDGF on cancer-associated target genes","volume":"14","author":"Yokoyama A","year":"2008","unstructured":"A Yokoyama, ML Cleary, Menin critically links MLL proteins with LEDGF on cancer-associated target genes. Cancer Cell 14, 36\u201346 (2008).","journal-title":"Cancer Cell"},{"key":"e_1_3_4_17_2","doi-asserted-by":"crossref","first-page":"7968","DOI":"10.1038\/ncomms8968","article-title":"Multiple cellular proteins interact with LEDGF\/p75 through a conserved unstructured consensus motif","volume":"6","author":"Tesina P","year":"2015","unstructured":"P Tesina, , Multiple cellular proteins interact with LEDGF\/p75 through a conserved unstructured consensus motif. Nat Commun 6, 7968 (2015).","journal-title":"Nat Commun"},{"key":"e_1_3_4_18_2","doi-asserted-by":"crossref","first-page":"5139","DOI":"10.1158\/0008-5472.CAN-13-3602","article-title":"Validation and structural characterization of the LEDGF\/p75-MLL interface as a new target for the treatment of MLL-dependent leukemia","volume":"74","author":"Cerm\u00e1kov\u00e1 K","year":"2014","unstructured":"K Cerm\u00e1kov\u00e1, , Validation and structural characterization of the LEDGF\/p75-MLL interface as a new target for the treatment of MLL-dependent leukemia. Cancer Res 74, 5139\u20135151 (2014).","journal-title":"Cancer Res"},{"key":"e_1_3_4_19_2","doi-asserted-by":"crossref","first-page":"541","DOI":"10.1016\/j.ajhg.2016.02.004","article-title":"Disruption of POGZ is associated with intellectual disability and autism spectrum disorders","volume":"98","author":"Stessman HAF","year":"2016","unstructured":"HAF Stessman, , Disruption of POGZ is associated with intellectual disability and autism spectrum disorders. Am J Hum Genet 98, 541\u2013552 (2016).","journal-title":"Am J Hum Genet"},{"key":"e_1_3_4_20_2","doi-asserted-by":"crossref","first-page":"1262","DOI":"10.1126\/science.aac9396","article-title":"De novo mutations in congenital heart disease with neurodevelopmental and other congenital anomalies","volume":"350","author":"Homsy J","year":"2015","unstructured":"J Homsy, , De novo mutations in congenital heart disease with neurodevelopmental and other congenital anomalies. Science 350, 1262\u20131266 (2015).","journal-title":"Science"},{"key":"e_1_3_4_21_2","doi-asserted-by":"crossref","first-page":"5607","DOI":"10.1158\/0008-5472.CAN-05-0500","article-title":"Identification of a novel c-Myc protein interactor, JPO2, with transforming activity in medulloblastoma cells","volume":"65","author":"Huang A","year":"2005","unstructured":"A Huang, , Identification of a novel c-Myc protein interactor, JPO2, with transforming activity in medulloblastoma cells. Cancer Res 65, 5607\u20135619 (2005).","journal-title":"Cancer Res"},{"key":"e_1_3_4_22_2","doi-asserted-by":"crossref","first-page":"691","DOI":"10.1016\/0092-8674(92)90602-9","article-title":"Involvement of a homolog of Drosophila trithorax by 11q23 chromosomal translocations in acute leukemias","volume":"71","author":"Tkachuk DC","year":"1992","unstructured":"DC Tkachuk, S Kohler, ML Cleary, Involvement of a homolog of Drosophila trithorax by 11q23 chromosomal translocations in acute leukemias. Cell 71, 691\u2013700 (1992).","journal-title":"Cell"},{"key":"e_1_3_4_23_2","first-page":"774","article-title":"MLL tandem duplication and multiple splicing in adult acute myeloid leukemia with normal karyotype","volume":"10","author":"Yu M","year":"1996","unstructured":"M Yu, , MLL tandem duplication and multiple splicing in adult acute myeloid leukemia with normal karyotype. Leukemia 10, 774\u2013780 (1996).","journal-title":"Leukemia"},{"key":"e_1_3_4_24_2","doi-asserted-by":"crossref","first-page":"823","DOI":"10.1038\/nrc2253","article-title":"MLL translocations, histone modifications and leukaemia stem-cell development","volume":"7","author":"Krivtsov AV","year":"2007","unstructured":"AV Krivtsov, SA Armstrong, MLL translocations, histone modifications and leukaemia stem-cell development. Nat Rev Cancer 7, 823\u2013833 (2007).","journal-title":"Nat Rev Cancer"},{"key":"e_1_3_4_25_2","doi-asserted-by":"crossref","first-page":"617","DOI":"10.1128\/MCB.24.2.617-628.2004","article-title":"Hoxa9 and Meis1 are key targets for MLL-ENL-mediated cellular immortalization","volume":"24","author":"Zeisig BB","year":"2004","unstructured":"BB Zeisig, , Hoxa9 and Meis1 are key targets for MLL-ENL-mediated cellular immortalization. Mol Cell Biol 24, 617\u2013628 (2004).","journal-title":"Mol Cell Biol"},{"key":"e_1_3_4_26_2","doi-asserted-by":"crossref","first-page":"1245","DOI":"10.1038\/leu.2013.10","article-title":"Impairing MLL-fusion gene-mediated transformation by dissecting critical interactions with the lens epithelium-derived growth factor (LEDGF\/p75)","volume":"27","author":"M\u00e9reau H","year":"2013","unstructured":"H M\u00e9reau, , Impairing MLL-fusion gene-mediated transformation by dissecting critical interactions with the lens epithelium-derived growth factor (LEDGF\/p75). Leukemia 27, 1245\u20131253 (2013).","journal-title":"Leukemia"},{"key":"e_1_3_4_27_2","doi-asserted-by":"crossref","first-page":"526","DOI":"10.1038\/nsmb937","article-title":"Solution structure of the HIV-1 integrase-binding domain in LEDGF\/p75","volume":"12","author":"Cherepanov P","year":"2005","unstructured":"P Cherepanov, , Solution structure of the HIV-1 integrase-binding domain in LEDGF\/p75. Nat Struct Mol Biol 12, 526\u2013532 (2005).","journal-title":"Nat Struct Mol Biol"},{"key":"e_1_3_4_28_2","doi-asserted-by":"crossref","first-page":"31266","DOI":"10.1074\/jbc.M002595200","article-title":"Structure of a conserved domain common to the transcription factors TFIIS, elongin A, and CRSP70","volume":"275","author":"Booth V","year":"2000","unstructured":"V Booth, CM Koth, AM Edwards, CH Arrowsmith, Structure of a conserved domain common to the transcription factors TFIIS, elongin A, and CRSP70. J Biol Chem 275, 31266\u201331268 (2000).","journal-title":"J Biol Chem"},{"key":"e_1_3_4_29_2","doi-asserted-by":"crossref","first-page":"542","DOI":"10.1038\/nature10806","article-title":"The same pocket in menin binds both MLL and JUND but has opposite effects on transcription","volume":"482","author":"Huang J","year":"2012","unstructured":"J Huang, , The same pocket in menin binds both MLL and JUND but has opposite effects on transcription. Nature 482, 542\u2013546 (2012).","journal-title":"Nature"},{"key":"e_1_3_4_30_2","first-page":"ra83","article-title":"The SH2 domain-containing proteins in 21 species establish the provenance and scope of phosphotyrosine signaling in eukaryotes","volume":"4","author":"Liu BA","year":"2011","unstructured":"BA Liu, , The SH2 domain-containing proteins in 21 species establish the provenance and scope of phosphotyrosine signaling in eukaryotes. Sci Signal 4, ra83 (2011).","journal-title":"Sci Signal"},{"key":"e_1_3_4_31_2","doi-asserted-by":"crossref","first-page":"668","DOI":"10.1126\/science.1708916","article-title":"SH2 and SH3 domains: Elements that control interactions of cytoplasmic signaling proteins","volume":"252","author":"Koch CA","year":"1991","unstructured":"CA Koch, D Anderson, MF Moran, C Ellis, T Pawson, SH2 and SH3 domains: Elements that control interactions of cytoplasmic signaling proteins. Science 252, 668\u2013674 (1991).","journal-title":"Science"},{"key":"e_1_3_4_32_2","first-page":"35","article-title":"Threonine phosphorylation of the MMAC1\/PTEN PDZ binding domain both inhibits and stimulates PDZ binding","volume":"60","author":"Adey NB","year":"2000","unstructured":"NB Adey, , Threonine phosphorylation of the MMAC1\/PTEN PDZ binding domain both inhibits and stimulates PDZ binding. Cancer Res 60, 35\u201337 (2000).","journal-title":"Cancer Res"},{"key":"e_1_3_4_33_2","doi-asserted-by":"crossref","first-page":"3061","DOI":"10.1074\/jbc.R100059200","article-title":"14-3-3 proteins: Active cofactors in cellular regulation by serine\/threonine phosphorylation","volume":"277","author":"Tzivion G","year":"2002","unstructured":"G Tzivion, J Avruch, 14-3-3 proteins: Active cofactors in cellular regulation by serine\/threonine phosphorylation. J Biol Chem 277, 3061\u20133064 (2002).","journal-title":"J Biol Chem"},{"key":"e_1_3_4_34_2","doi-asserted-by":"crossref","first-page":"3979","DOI":"10.1038\/emboj.2010.272","article-title":"The structure of an Iws1\/Spt6 complex reveals an interaction domain conserved in TFIIS, Elongin A and Med26","volume":"29","author":"Diebold M-L","year":"2010","unstructured":"M-L Diebold, , The structure of an Iws1\/Spt6 complex reveals an interaction domain conserved in TFIIS, Elongin A and Med26. EMBO J 29, 3979\u20133991 (2010).","journal-title":"EMBO J"},{"key":"e_1_3_4_35_2","doi-asserted-by":"crossref","first-page":"725","DOI":"10.1016\/j.molcel.2010.11.014","article-title":"Structure and biological importance of the Spn1-Spt6 interaction, and its regulatory role in nucleosome binding","volume":"40","author":"McDonald SM","year":"2010","unstructured":"SM McDonald, D Close, H Xin, T Formosa, CP Hill, Structure and biological importance of the Spn1-Spt6 interaction, and its regulatory role in nucleosome binding. Mol Cell 40, 725\u2013735 (2010).","journal-title":"Mol Cell"},{"key":"e_1_3_4_36_2","doi-asserted-by":"crossref","first-page":"D261","DOI":"10.1093\/nar\/gkr1122","article-title":"PhosphoSitePlus: A comprehensive resource for investigating the structure and function of experimentally determined post-translational modifications in man and mouse","volume":"40","author":"Hornbeck PV","year":"2012","unstructured":"PV Hornbeck, , PhosphoSitePlus: A comprehensive resource for investigating the structure and function of experimentally determined post-translational modifications in man and mouse. Nucleic Acids Res 40, D261\u2013D270 (2012).","journal-title":"Nucleic Acids Res"},{"key":"e_1_3_4_37_2","doi-asserted-by":"crossref","first-page":"634","DOI":"10.1038\/nmeth.2518","article-title":"Integrated proteomic analysis of post-translational modifications by serial enrichment","volume":"10","author":"Mertins P","year":"2013","unstructured":"P Mertins, , Integrated proteomic analysis of post-translational modifications by serial enrichment. Nat Methods 10, 634\u2013637 (2013).","journal-title":"Nat Methods"},{"key":"e_1_3_4_38_2","doi-asserted-by":"crossref","first-page":"10762","DOI":"10.1073\/pnas.0805139105","article-title":"A quantitative atlas of mitotic phosphorylation","volume":"105","author":"Dephoure N","year":"2008","unstructured":"N Dephoure, , A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci USA 105, 10762\u201310767 (2008).","journal-title":"Proc Natl Acad Sci USA"},{"key":"e_1_3_4_39_2","doi-asserted-by":"crossref","first-page":"55","DOI":"10.1038\/nature18003","article-title":"Proteogenomics connects somatic mutations to signalling in breast cancer","volume":"534","author":"Mertins P","year":"2016","unstructured":"P Mertins, , Proteogenomics connects somatic mutations to signalling in breast cancer. Nature; NCI CPTAC 534, 55\u201362 (2016).","journal-title":"Nature"},{"key":"e_1_3_4_40_2","doi-asserted-by":"crossref","first-page":"2513","DOI":"10.1098\/rstb.2012.0013","article-title":"Why nature chose phosphate to modify proteins","volume":"367","author":"Hunter T","year":"2012","unstructured":"T Hunter, Why nature chose phosphate to modify proteins. Philos Trans R Soc Lond B Biol Sci 367, 2513\u20132516 (2012).","journal-title":"Philos Trans R Soc Lond B Biol Sci"},{"key":"e_1_3_4_41_2","doi-asserted-by":"crossref","first-page":"235","DOI":"10.1016\/j.tibs.2005.03.011","article-title":"Mediator and the mechanism of transcriptional activation","volume":"30","author":"Kornberg RD","year":"2005","unstructured":"RD Kornberg, Mediator and the mechanism of transcriptional activation. Trends Biochem Sci 30, 235\u2013239 (2005).","journal-title":"Trends Biochem Sci"},{"key":"e_1_3_4_42_2","doi-asserted-by":"crossref","first-page":"17330","DOI":"10.1074\/jbc.C700079200","article-title":"A proteomic analysis of ataxia telangiectasia-mutated (ATM)\/ATM-Rad3-related (ATR) substrates identifies the ubiquitin-proteasome system as a regulator for DNA damage checkpoints","volume":"282","author":"Mu JJ","year":"2007","unstructured":"JJ Mu, , A proteomic analysis of ataxia telangiectasia-mutated (ATM)\/ATM-Rad3-related (ATR) substrates identifies the ubiquitin-proteasome system as a regulator for DNA damage checkpoints. J Biol Chem 282, 17330\u201317334 (2007).","journal-title":"J Biol Chem"},{"key":"e_1_3_4_43_2","doi-asserted-by":"crossref","first-page":"3873","DOI":"10.1242\/jcs.00074","article-title":"Protein kinase CK2: A challenge to canons","volume":"115","author":"Pinna LA","year":"2002","unstructured":"LA Pinna, Protein kinase CK2: A challenge to canons. J Cell Sci 115, 3873\u20133878 (2002).","journal-title":"J Cell Sci"},{"key":"e_1_3_4_44_2","doi-asserted-by":"crossref","first-page":"44","DOI":"10.1016\/S0014-5793(01)02404-8","article-title":"Selectivity of 4,5,6,7-tetrabromobenzotriazole, an ATP site-directed inhibitor of protein kinase CK2 (\u2018casein kinase-2\u2019)","volume":"496","author":"Sarno S","year":"2001","unstructured":"S Sarno, , Selectivity of 4,5,6,7-tetrabromobenzotriazole, an ATP site-directed inhibitor of protein kinase CK2 (\u2018casein kinase-2\u2019). FEBS Lett 496, 44\u201348 (2001).","journal-title":"FEBS Lett"},{"key":"e_1_3_4_45_2","doi-asserted-by":"crossref","first-page":"6135","DOI":"10.1093\/nar\/gkq410","article-title":"High-resolution profiling of the LEDGF\/p75 chromatin interaction in the ENCODE region","volume":"38","author":"De Rijck J","year":"2010","unstructured":"J De Rijck, K Bartholomeeusen, H Ceulemans, Z Debyser, R Gijsbers, High-resolution profiling of the LEDGF\/p75 chromatin interaction in the ENCODE region. Nucleic Acids Res 38, 6135\u20136147 (2010).","journal-title":"Nucleic Acids Res"},{"key":"e_1_3_4_46_2","doi-asserted-by":"crossref","first-page":"765","DOI":"10.1016\/j.tcb.2017.07.001","article-title":"The mediator complex: At the nexus of RNA polymerase II transcription","volume":"27","author":"Jeronimo C","year":"2017","unstructured":"C Jeronimo, F Robert, The mediator complex: At the nexus of RNA polymerase II transcription. Trends Cell Biol 27, 765\u2013783 (2017).","journal-title":"Trends Cell Biol"},{"key":"e_1_3_4_47_2","doi-asserted-by":"crossref","first-page":"17308","DOI":"10.1073\/pnas.0506924102","article-title":"Structural basis for the recognition between HIV-1 integrase and transcriptional coactivator p75","volume":"102","author":"Cherepanov P","year":"2005","unstructured":"P Cherepanov, AL Ambrosio, S Rahman, T Ellenberger, A Engelman, Structural basis for the recognition between HIV-1 integrase and transcriptional coactivator p75. Proc Natl Acad Sci USA 102, 17308\u201317313 (2005).","journal-title":"Proc Natl Acad Sci USA"},{"key":"e_1_3_4_48_2","doi-asserted-by":"crossref","first-page":"e115609","DOI":"10.1371\/journal.pone.0115609","article-title":"Mining CK2 in cancer","volume":"9","author":"Ortega CE","year":"2014","unstructured":"CE Ortega, Y Seidner, I Dominguez, Mining CK2 in cancer. PLoS One 9, e115609 (2014).","journal-title":"PLoS One"},{"key":"e_1_3_4_49_2","doi-asserted-by":"crossref","first-page":"803","DOI":"10.1038\/nsmb.2314","article-title":"LEDGF (p75) promotes DNA-end resection and homologous recombination","volume":"19","author":"Daugaard M","year":"2012","unstructured":"M Daugaard, , LEDGF (p75) promotes DNA-end resection and homologous recombination. Nat Struct Mol Biol 19, 803\u2013810 (2012).","journal-title":"Nat Struct Mol Biol"},{"key":"e_1_3_4_50_2","doi-asserted-by":"crossref","first-page":"37112","DOI":"10.1074\/jbc.M113.514398","article-title":"DNA-dependent protein kinase regulates DNA end resection in concert with Mre11-Rad50-Nbs1 (MRN) and ataxia telangiectasia-mutated (ATM)","volume":"288","author":"Zhou Y","year":"2013","unstructured":"Y Zhou, TT Paull, DNA-dependent protein kinase regulates DNA end resection in concert with Mre11-Rad50-Nbs1 (MRN) and ataxia telangiectasia-mutated (ATM). J Biol Chem 288, 37112\u201337125 (2013).","journal-title":"J Biol Chem"},{"key":"e_1_3_4_51_2","doi-asserted-by":"crossref","first-page":"1719","DOI":"10.1128\/MCB.01298-10","article-title":"Inhibition of homologous recombination by DNA-dependent protein kinase requires kinase activity, is titratable, and is modulated by autophosphorylation","volume":"31","author":"Neal JA","year":"2011","unstructured":"JA Neal, , Inhibition of homologous recombination by DNA-dependent protein kinase requires kinase activity, is titratable, and is modulated by autophosphorylation. Mol Cell Biol 31, 1719\u20131733 (2011).","journal-title":"Mol Cell Biol"},{"key":"e_1_3_4_52_2","doi-asserted-by":"crossref","first-page":"1345","DOI":"10.1073\/pnas.0406466102","article-title":"Inhibition of homologous recombination by variants of the catalytic subunit of the DNA-dependent protein kinase (DNA-PKcs)","volume":"102","author":"Convery E","year":"2005","unstructured":"E Convery, , Inhibition of homologous recombination by variants of the catalytic subunit of the DNA-dependent protein kinase (DNA-PKcs). Proc Natl Acad Sci USA 102, 1345\u20131350 (2005).","journal-title":"Proc Natl Acad Sci USA"},{"key":"e_1_3_4_53_2","doi-asserted-by":"crossref","first-page":"63","DOI":"10.1007\/s11010-005-3078-0","article-title":"CK2 as a positive regulator of Wnt signalling and tumourigenesis","volume":"274","author":"Seldin DC","year":"2005","unstructured":"DC Seldin, , CK2 as a positive regulator of Wnt signalling and tumourigenesis. Mol Cell Biochem 274, 63\u201367 (2005).","journal-title":"Mol Cell Biochem"},{"key":"e_1_3_4_54_2","doi-asserted-by":"crossref","first-page":"1850","DOI":"10.1007\/s00018-009-9153-z","article-title":"Protein kinase CK2 in health and disease: CK2 and its role in Wnt and NF-kappaB signaling: Linking development and cancer","volume":"66","author":"Dominguez I","year":"2009","unstructured":"I Dominguez, GE Sonenshein, DC Seldin, Protein kinase CK2 in health and disease: CK2 and its role in Wnt and NF-kappaB signaling: Linking development and cancer. Cell Mol Life Sci 66, 1850\u20131857 (2009).","journal-title":"Cell Mol Life Sci"},{"key":"e_1_3_4_55_2","doi-asserted-by":"crossref","first-page":"1858","DOI":"10.1007\/s00018-009-9154-y","article-title":"Protein kinase CK2 in health and disease: CK2: A key player in cancer biology","volume":"66","author":"Trembley JH","year":"2009","unstructured":"JH Trembley, G Wang, G Unger, J Slaton, K Ahmed, Protein kinase CK2 in health and disease: CK2: A key player in cancer biology. Cell Mol Life Sci 66, 1858\u20131867 (2009).","journal-title":"Cell Mol Life Sci"},{"key":"e_1_3_4_56_2","doi-asserted-by":"crossref","first-page":"499","DOI":"10.1016\/j.bbapap.2009.07.018","article-title":"Addiction to protein kinase CK2: A common denominator of diverse cancer cells?","volume":"1804","author":"Ruzzene M","year":"2010","unstructured":"M Ruzzene, LA Pinna, Addiction to protein kinase CK2: A common denominator of diverse cancer cells? Biochim Biophys Acta 1804, 499\u2013504 (2010).","journal-title":"Biochim Biophys Acta"},{"key":"e_1_3_4_57_2","doi-asserted-by":"crossref","first-page":"153","DOI":"10.17219\/acem\/37040","article-title":"Protein kinase CK2 and angiogenesis","volume":"23","author":"Montenarh M","year":"2014","unstructured":"M Montenarh, Protein kinase CK2 and angiogenesis. Adv Clin Exp Med 23, 153\u2013158 (2014).","journal-title":"Adv Clin Exp Med"},{"key":"e_1_3_4_58_2","doi-asserted-by":"crossref","first-page":"243","DOI":"10.1007\/s10456-012-9256-2","article-title":"Protein kinase CK2 is a regulator of angiogenesis in endometriotic lesions","volume":"15","author":"Feng D","year":"2012","unstructured":"D Feng, , Protein kinase CK2 is a regulator of angiogenesis in endometriotic lesions. Angiogenesis 15, 243\u2013252 (2012).","journal-title":"Angiogenesis"},{"key":"e_1_3_4_59_2","doi-asserted-by":"crossref","first-page":"177","DOI":"10.1007\/s11010-008-9831-4","article-title":"Inhibition of protein kinase CK2 suppresses angiogenesis and hematopoietic stem cell recruitment to retinal neovascularization sites","volume":"316","author":"Kramerov AA","year":"2008","unstructured":"AA Kramerov, , Inhibition of protein kinase CK2 suppresses angiogenesis and hematopoietic stem cell recruitment to retinal neovascularization sites. Mol Cell Biochem 316, 177\u2013186 (2008).","journal-title":"Mol Cell Biochem"},{"key":"e_1_3_4_60_2","doi-asserted-by":"crossref","first-page":"708","DOI":"10.1038\/leu.2008.27","article-title":"Targeting survival cascades induced by activation of Ras\/Raf\/MEK\/ERK, PI3K\/PTEN\/Akt\/mTOR and Jak\/STAT pathways for effective leukemia therapy","volume":"22","author":"McCubrey JA","year":"2008","unstructured":"JA McCubrey, , Targeting survival cascades induced by activation of Ras\/Raf\/MEK\/ERK, PI3K\/PTEN\/Akt\/mTOR and Jak\/STAT pathways for effective leukemia therapy. Leukemia 22, 708\u2013722 (2008).","journal-title":"Leukemia"},{"key":"e_1_3_4_61_2","doi-asserted-by":"crossref","first-page":"686","DOI":"10.1038\/leu.2008.26","article-title":"Contributions of the Raf\/MEK\/ERK, PI3K\/PTEN\/Akt\/mTOR and Jak\/STAT pathways to leukemia","volume":"22","author":"Steelman LS","year":"2008","unstructured":"LS Steelman, , Contributions of the Raf\/MEK\/ERK, PI3K\/PTEN\/Akt\/mTOR and Jak\/STAT pathways to leukemia. Leukemia 22, 686\u2013707 (2008).","journal-title":"Leukemia"},{"key":"e_1_3_4_62_2","doi-asserted-by":"crossref","first-page":"6484","DOI":"10.18632\/oncotarget.2248","article-title":"Therapeutic CK2 inhibition attenuates diverse prosurvival signaling cascades and decreases cell viability in human breast cancer cells","volume":"5","author":"Gray GK","year":"2014","unstructured":"GK Gray, BC McFarland, AL Rowse, SA Gibson, EN Benveniste, Therapeutic CK2 inhibition attenuates diverse prosurvival signaling cascades and decreases cell viability in human breast cancer cells. Oncotarget 5, 6484\u20136496 (2014).","journal-title":"Oncotarget"},{"key":"e_1_3_4_63_2","doi-asserted-by":"crossref","first-page":"6484","DOI":"10.1158\/1078-0432.CCR-13-0265","article-title":"Targeting protein kinase CK2 suppresses prosurvival signaling pathways and growth of glioblastoma","volume":"19","author":"Zheng Y","year":"2013","unstructured":"Y Zheng, , Targeting protein kinase CK2 suppresses prosurvival signaling pathways and growth of glioblastoma. Clinical Cancer Res 19, 6484\u20136494 (2013).","journal-title":"Clinical Cancer Res"},{"key":"e_1_3_4_64_2","doi-asserted-by":"crossref","first-page":"156","DOI":"10.1182\/blood-2010-01-266320","article-title":"A CK2-dependent mechanism for activation of the JAK-STAT signaling pathway","volume":"118","author":"Zheng Y","year":"2011","unstructured":"Y Zheng, , A CK2-dependent mechanism for activation of the JAK-STAT signaling pathway. Blood 118, 156\u2013166 (2011).","journal-title":"Blood"},{"key":"e_1_3_4_65_2","doi-asserted-by":"crossref","first-page":"2475","DOI":"10.1091\/mbc.E14-10-1453","article-title":"Regulation of cell proliferation by ERK and signal-dependent nuclear translocation of ERK is dependent on Tm5NM1-containing actin filaments","volume":"26","author":"Schevzov G","year":"2015","unstructured":"G Schevzov, , Regulation of cell proliferation by ERK and signal-dependent nuclear translocation of ERK is dependent on Tm5NM1-containing actin filaments. Mol Biol Cell 26, 2475\u20132490 (2015).","journal-title":"Mol Biol Cell"},{"key":"e_1_3_4_66_2","doi-asserted-by":"crossref","first-page":"ra30","DOI":"10.1126\/scisignal.2001682","article-title":"A peptide-based target screen implicates the protein kinase CK2 in the global regulation of caspase signaling","volume":"4","author":"Duncan JS","year":"2011","unstructured":"JS Duncan, , A peptide-based target screen implicates the protein kinase CK2 in the global regulation of caspase signaling. Sci Signal 4, ra30 (2011).","journal-title":"Sci Signal"},{"key":"e_1_3_4_67_2","doi-asserted-by":"crossref","first-page":"10288","DOI":"10.1158\/0008-5472.CAN-10-1893","article-title":"CX-4945, an orally bioavailable selective inhibitor of protein kinase CK2, inhibits prosurvival and angiogenic signaling and exhibits antitumor efficacy","volume":"70","author":"Siddiqui-Jain A","year":"2010","unstructured":"A Siddiqui-Jain, , CX-4945, an orally bioavailable selective inhibitor of protein kinase CK2, inhibits prosurvival and angiogenic signaling and exhibits antitumor efficacy. Cancer Res 70, 10288\u201310298 (2010).","journal-title":"Cancer Res"},{"key":"e_1_3_4_68_2","doi-asserted-by":"crossref","first-page":"163","DOI":"10.1007\/s11010-008-9814-5","article-title":"CIGB-300, a novel proapoptotic peptide that impairs the CK2 phosphorylation and exhibits anticancer properties both in vitro and in vivo","volume":"316","author":"Perea SE","year":"2008","unstructured":"SE Perea, , CIGB-300, a novel proapoptotic peptide that impairs the CK2 phosphorylation and exhibits anticancer properties both in vitro and in vivo. Mol Cell Biochem 316, 163\u2013167 (2008).","journal-title":"Mol Cell Biochem"},{"key":"e_1_3_4_69_2","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1038\/leu.2017.301","article-title":"Therapeutic targeting of CK2 in acute and chronic leukemias","volume":"32","author":"Buontempo F","year":"2018","unstructured":"F Buontempo, , Therapeutic targeting of CK2 in acute and chronic leukemias. Leukemia 32, 1\u201310 (2018).","journal-title":"Leukemia"},{"key":"e_1_3_4_70_2","doi-asserted-by":"crossref","first-page":"267","DOI":"10.1038\/nature13736","article-title":"Tyrosine phosphorylation of histone H2A by CK2 regulates transcriptional elongation","volume":"516","author":"Basnet H","year":"2014","unstructured":"H Basnet, , Tyrosine phosphorylation of histone H2A by CK2 regulates transcriptional elongation. Nature 516, 267\u2013271 (2014).","journal-title":"Nature"},{"key":"e_1_3_4_71_2","doi-asserted-by":"crossref","first-page":"225","DOI":"10.1023\/B:JNMR.0000048852.40853.5c","article-title":"Sequence-specific assignment and secondary structure determination of the 195-residue complex formed by the Mycobacterium tuberculosis proteins CFP-10 and ESAT-6","volume":"30","author":"Renshaw PS","year":"2004","unstructured":"PS Renshaw, , Sequence-specific assignment and secondary structure determination of the 195-residue complex formed by the Mycobacterium tuberculosis proteins CFP-10 and ESAT-6. J Biomol NMR 30, 225\u2013226 (2004).","journal-title":"J Biomol NMR"},{"key":"e_1_3_4_72_2","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1007\/s10858-005-4324-1","article-title":"NMR assignment of the mTOR domain responsible for rapamycin binding","volume":"36","author":"Veverka V","year":"2006","unstructured":"V Veverka, , NMR assignment of the mTOR domain responsible for rapamycin binding. J Biomol NMR 36, 3 (2006).","journal-title":"J Biomol NMR"},{"key":"e_1_3_4_73_2","doi-asserted-by":"crossref","first-page":"209","DOI":"10.1016\/S0022-2836(02)00241-3","article-title":"Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA","volume":"319","author":"Herrmann T","year":"2002","unstructured":"T Herrmann, P G\u00fcntert, K W\u00fcthrich, Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA. J Mol Biol 319, 209\u2013227 (2002).","journal-title":"J Mol Biol"},{"key":"e_1_3_4_74_2","doi-asserted-by":"crossref","first-page":"585","DOI":"10.1038\/sj.onc.1210693","article-title":"Structural characterization of the interaction of mTOR with phosphatidic acid and a novel class of inhibitor: Compelling evidence for a central role of the FRB domain in small molecule-mediated regulation of mTOR","volume":"27","author":"Veverka V","year":"2008","unstructured":"V Veverka, , Structural characterization of the interaction of mTOR with phosphatidic acid and a novel class of inhibitor: Compelling evidence for a central role of the FRB domain in small molecule-mediated regulation of mTOR. Oncogene 27, 585\u2013595 (2008).","journal-title":"Oncogene"},{"key":"e_1_3_4_75_2","unstructured":"DA Case Amber 14 reference manual. Available at ambermd.org\/doc12\/Amber14.pdf. (2014)."},{"key":"e_1_3_4_76_2","doi-asserted-by":"crossref","first-page":"3084","DOI":"10.1021\/ct400341p","article-title":"PTRAJ and CPPTRAJ: Software for processing and analysis of molecular dynamics trajectory data","volume":"9","author":"Roe DR","year":"2013","unstructured":"DR Roe, 3rd TE Cheatham, PTRAJ and CPPTRAJ: Software for processing and analysis of molecular dynamics trajectory data. J Chem Theory Comput 9, 3084\u20133095 (2013).","journal-title":"J Chem Theory Comput"}],"container-title":["Proceedings of the National Academy of Sciences"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/www.pnas.org\/syndication\/doi\/10.1073\/pnas.1803909115","content-type":"unspecified","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/pnas.org\/doi\/pdf\/10.1073\/pnas.1803909115","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2022,6,7]],"date-time":"2022-06-07T13:41:16Z","timestamp":1654609276000},"score":1,"resource":{"primary":{"URL":"https:\/\/pnas.org\/doi\/full\/10.1073\/pnas.1803909115"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2018,7,11]]},"references-count":76,"journal-issue":{"issue":"30","published-print":{"date-parts":[[2018,7,24]]}},"alternative-id":["10.1073\/pnas.1803909115"],"URL":"https:\/\/doi.org\/10.1073\/pnas.1803909115","relation":{},"ISSN":["0027-8424","1091-6490"],"issn-type":[{"value":"0027-8424","type":"print"},{"value":"1091-6490","type":"electronic"}],"subject":[],"published":{"date-parts":[[2018,7,11]]},"assertion":[{"value":"2018-07-11","order":2,"name":"published","label":"Published","group":{"name":"publication_history","label":"Publication History"}}]}}