{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,20]],"date-time":"2026-10-20T15:12:47Z","timestamp":1792509167769,"version":"4.5.0"},"reference-count":76,"publisher":"American Chemical Society (ACS)","issue":"19","license":[{"start":{"date-parts":[[2026,9,8]],"date-time":"2026-09-08T00:00:00Z","timestamp":1788825600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100001659","name":"Deutsche Forschungsgemeinschaft","doi-asserted-by":"publisher","award":["192904750"],"award-info":[{"award-number":["192904750"]}],"id":[{"id":"10.13039\/501100001659","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001659","name":"Deutsche Forschungsgemeinschaft","doi-asserted-by":"publisher","award":["Ju295\/181"],"award-info":[{"award-number":["Ju295\/181"]}],"id":[{"id":"10.13039\/501100001659","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001659","name":"Deutsche Forschungsgemeinschaft","doi-asserted-by":"publisher","award":["Si868\/271"],"award-info":[{"award-number":["Si868\/271"]}],"id":[{"id":"10.13039\/501100001659","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001824","name":"Grantov? Agentura Cesk? Republiky","doi-asserted-by":"publisher","award":["24-12155S"],"award-info":[{"award-number":["24-12155S"]}],"id":[{"id":"10.13039\/501100001824","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100004240","name":"Akademie Ved Cesk? Republiky","doi-asserted-by":"publisher","award":["86652036"],"award-info":[{"award-number":["86652036"]}],"id":[{"id":"10.13039\/501100004240","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2026,10,6]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>Posttranslational lysine acetylation and methylation are generally considered mutually exclusive modifications of the \u03b5-amino group. The recent discovery of N-acetyl-N-methyl lysine (KAcMe) on histone H4 showed that both marks can coexist on the same lysine side chain, raising the question of whether this dual modification is enzymatically reversible. Here, we synthesized model peptides containing N-acyl lysine or N-acyl-N-methyl lysine residues and tested their processing by Zn2+-dependent HDACs and NAD+-dependent sirtuins. While the corresponding unmethylated substrates were deacylated by the expected enzymes, KAcMe-containing peptides were not detectably deacetylated by either enzyme family. N-methylation also blocked HDAC8\/11-mediated demyristoylation and SIRT5-mediated desuccinylation, whereas SIRT2 and SIRT6 retained weak demyristoylase activity toward N-myristoyl-N-methyl lysine. X-ray crystal structures of sirtuin\u2013peptide complexes, supported by inhibition studies and molecular docking, reveal that N-methylation disrupts productive substrate positioning and misaligns the scissile amide bond for catalysis. These findings suggest that KAcMe is resistant to canonical lysine deacetylases and may represent a persistent chromatin-associated modification.<\/jats:p>","DOI":"10.1021\/acs.biochem.6c00508","type":"journal-article","created":{"date-parts":[[2026,9,8]],"date-time":"2026-09-08T10:01:47Z","timestamp":1788861707000},"page":"3092-3105","source":"Crossref","is-referenced-by-count":1,"title":["Structural and\nEnzymatic Basis for Impaired Deacylation\nof\n                    <i>N<\/i>\n                    -Acyl-\n                    <i>N<\/i>\n                    -Methyl\nLysine Residues"],"prefix":"10.1021","volume":"65","author":[{"ORCID":"https:\/\/orcid.org\/0009-0003-0611-7365","authenticated-orcid":true,"given":"Sebastian","family":"Hilscher","sequence":"first","affiliation":[{"name":"Martin-Luther-University Halle-Wittenberg , , Kurt-Mothes-Str. 3 , ,","place":["Halle\/Saale, Germany, 06120"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Paul Horst","family":"Bo\u0308ttcher","sequence":"additional","affiliation":[{"name":"Martin-Luther-University Halle-Wittenberg , , Kurt-Mothes-Str. 3a , ,","place":["Halle\/Saale, Germany, 06120"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-5420-6184","authenticated-orcid":true,"given":"Florian","family":"Friedrich","sequence":"additional","affiliation":[{"name":"University of Freiburg , , Albertstr. 25 , ,","place":["Freiburg, Germany, 79104"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Martin","family":"Pannek","sequence":"additional","affiliation":[{"name":"University of Bayreuth , , Universitaetsstr. 30 , ,","place":["Bayreuth, Germany, 95447"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Fady","family":"Baselious","sequence":"additional","affiliation":[{"name":"Martin-Luther-University Halle-Wittenberg , , Kurt-Mothes-Str. 3 , ,","place":["Halle\/Saale, Germany, 06120"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Marat","family":"Meleshin","sequence":"additional","affiliation":[{"name":"Martin-Luther-University Halle-Wittenberg , , Kurt-Mothes-Str. 3a , ,","place":["Halle\/Saale, Germany, 06120"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Oliver","family":"Einsle","sequence":"additional","affiliation":[{"name":"University of Freiburg , , Albertstr. 21 , ,","place":["Freiburg, Germany, 79104"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-2751-3060","authenticated-orcid":true,"given":"Cyril","family":"Barinka","sequence":"additional","affiliation":[{"name":"Institute of Biotechnology of the Czech Academy of Sciences, BIOCEV , Prumyslova 595 , ,","place":["Vestec, Czech Republic, 252 50"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-0913-1467","authenticated-orcid":true,"given":"Clemens","family":"Steegborn","sequence":"additional","affiliation":[{"name":"University of Bayreuth , , Universitaetsstr. 30 , ,","place":["Bayreuth, Germany, 95447"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-5985-9261","authenticated-orcid":true,"given":"Wolfgang","family":"Sippl","sequence":"additional","affiliation":[{"name":"Martin-Luther-University Halle-Wittenberg , , Kurt-Mothes-Str. 3 , ,","place":["Halle\/Saale, Germany, 06120"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-6361-7716","authenticated-orcid":true,"given":"Manfred","family":"Jung","sequence":"additional","affiliation":[{"name":"University of Freiburg , , Albertstr. 25 , ,","place":["Freiburg, Germany, 79104"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-0919-7076","authenticated-orcid":true,"given":"Mike","family":"Schutkowski","sequence":"additional","affiliation":[{"name":"Martin-Luther-University Halle-Wittenberg , , Kurt-Mothes-Str. 3a , ,","place":["Halle\/Saale, Germany, 06120"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0009-0006-5807-9315","authenticated-orcid":true,"given":"Cordelia","family":"Schiene-Fischer","sequence":"additional","affiliation":[{"name":"Martin-Luther-University Halle-Wittenberg , , Kurt-Mothes-Str. 3a , ,","place":["Halle\/Saale, Germany, 06120"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"316","published-online":{"date-parts":[[2026,9,8]]},"reference":[{"issue":"45","key":"2026100608064199500_cit1","doi-asserted-by":"publisher","first-page":"7342","DOI":"10.1002\/anie.200501023","article-title":"Protein posttranslational modifications:\nthe chemistry of proteome diversifications","volume":"44","author":"Walsh","year":"2005","journal-title":"Angew. Chem., Int. Ed."},{"issue":"8","key":"2026100608064199500_cit2","doi-asserted-by":"publisher","first-page":"953","DOI":"10.1016\/j.chembiol.2020.07.002","article-title":"The Chemical Biology\nof Reversible Lysine Post-translational\nModifications","volume":"27","author":"Wang","year":"2020","journal-title":"Cell Chem. Biol."},{"issue":"6765","key":"2026100608064199500_cit3","doi-asserted-by":"publisher","first-page":"41","DOI":"10.1038\/47412","article-title":"The language of\ncovalent histone modifications","volume":"403","author":"Strahl","year":"2000","journal-title":"Nature"},{"issue":"5532","key":"2026100608064199500_cit4","doi-asserted-by":"publisher","first-page":"1074","DOI":"10.1126\/science.1063127","article-title":"Translating the\nhistone code","volume":"293","author":"Jenuwein","year":"2001","journal-title":"Science"},{"issue":"4","key":"2026100608064199500_cit5","doi-asserted-by":"publisher","first-page":"194990","DOI":"10.1016\/j.bbagrm.2023.194990","article-title":"Unraveling the battle\nfor lysine: A review of the competition among post-translational modifications","volume":"1866","author":"Shukri","year":"2023","journal-title":"Biochim. Biophys. Acta, Gene Regul. Mech."},{"issue":"7981","key":"2026100608064199500_cit6","doi-asserted-by":"publisher","first-page":"173","DOI":"10.1038\/s41586-023-06565-9","article-title":"Acetyl-methyllysine\nmarks chromatin at active transcription\nstart sites","volume":"622","author":"Lu-Culligan","year":"2023","journal-title":"Nature"},{"issue":"4","key":"2026100608064199500_cit7","doi-asserted-by":"publisher","first-page":"F842","DOI":"10.1152\/ajprenal.00313.2017","article-title":"Dynamic regulation\nof lysine acetylation: the balance\nbetween acetyltransferase and deacetylase activities","volume":"313","author":"Hyndman","year":"2017","journal-title":"Am. J. Physiol. Renal Phys."},{"issue":"3","key":"2026100608064199500_cit8","doi-asserted-by":"publisher","first-page":"340","DOI":"10.1021\/acs.chemrev.7b00181","article-title":"Lysine Acetylation\nGoes Global: From Epigenetics to Metabolism and Therapeutics","volume":"118","author":"Ali","year":"2018","journal-title":"Chem. Rev."},{"key":"2026100608064199500_cit9","doi-asserted-by":"publisher","first-page":"9","DOI":"10.1016\/j.sbi.2019.01.004","article-title":"Structure, mechanism, and inhibition\nof the zinc-dependent\nhistone deacetylases","volume":"59","author":"Porter","year":"2019","journal-title":"Curr. Opin. Struct. Biol."},{"key":"2026100608064199500_cit10","doi-asserted-by":"publisher","first-page":"25","DOI":"10.1016\/bs.pmbts.2017.11.003","article-title":"Targeting Sirtuins:\nSubstrate Specificity and Inhibitor Design","volume":"154","author":"Rajabi","year":"2018","journal-title":"Prog. Mol. Biol. Transl. Sci."},{"issue":"1","key":"2026100608064199500_cit11","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1016\/j.molcel.2006.12.010","article-title":"Dynamic regulation of histone lysine methylation by\ndemethylases","volume":"25","author":"Shi","year":"2007","journal-title":"Mol. Cell"},{"issue":"5","key":"2026100608064199500_cit12","doi-asserted-by":"publisher","first-page":"340","DOI":"10.1080\/15592294.2017.1290032","article-title":"Structural insight\ninto inhibitors of flavin adenine\ndinucleotide-dependent lysine demethylases","volume":"12","author":"Niwa","year":"2017","journal-title":"Epigenetics"},{"issue":"7078","key":"2026100608064199500_cit13","doi-asserted-by":"publisher","first-page":"811","DOI":"10.1038\/nature04433","article-title":"Histone demethylation\nby a family\nof JmjC domain-containing proteins","volume":"439","author":"Tsukada","year":"2006","journal-title":"Nature"},{"issue":"9","key":"2026100608064199500_cit14","doi-asserted-by":"publisher","first-page":"715","DOI":"10.1038\/nrg1945","article-title":"JmjC-domain-containing proteins and\nhistone demethylation","volume":"7","author":"Klose","year":"2006","journal-title":"Nat. Rev. Genet"},{"issue":"48","key":"2026100608064199500_cit15","doi-asserted-by":"publisher","first-page":"4777","DOI":"10.1021\/acs.biochem.9b00786","article-title":"One-Atom Substitution\nEnables Direct\nand Continuous Monitoring of Histone Deacylase Activity","volume":"58","author":"Zessin","year":"2019","journal-title":"Biochemistry"},{"key":"2026100608064199500_cit16","doi-asserted-by":"publisher","first-page":"22643","DOI":"10.1038\/srep22643","article-title":"A continuous\nsirtuin activity assay without any coupling to enzymatic or chemical\nreactions","volume":"6","author":"Schuster","year":"2016","journal-title":"Sci. Rep."},{"issue":"3","key":"2026100608064199500_cit17","doi-asserted-by":"publisher","first-page":"685","DOI":"10.1021\/acschembio.7b00942","article-title":"Histone Deacetylase\n11 Is a Fatty-Acid Deacylase","volume":"13","author":"Kutil","year":"2018","journal-title":"ACS Chem. Biol."},{"key":"2026100608064199500_cit18","doi-asserted-by":"publisher","first-page":"105425","DOI":"10.1016\/j.bioorg.2021.105425","article-title":"Continuous\nSirtuin\/HDAC (histone deacetylase) activity assay using thioamides\nas PET (Photoinduced Electron Transfer)-based fluorescence quencher","volume":"117","author":"Zessin","year":"2021","journal-title":"Bioorg. Chem."},{"key":"2026100608064199500_cit19","doi-asserted-by":"publisher","first-page":"201","DOI":"10.1016\/j.jare.2023.07.005","article-title":"Novel hydroxamic acid derivative\ninduces apoptosis and constrains autophagy in leukemic cells","volume":"60","author":"Fischer","year":"2024","journal-title":"J. Adv. Res."},{"issue":"40","key":"2026100608064199500_cit20","doi-asserted-by":"publisher","first-page":"10728","DOI":"10.1002\/anie.201402679","article-title":"Chemical probing of the human sirtuin\n5 active site\nreveals its substrate acyl specificity and peptide-based inhibitors","volume":"53","author":"Roessler","year":"2014","journal-title":"Angew. Chem., Int. Ed."},{"issue":"22","key":"2026100608064199500_cit21","doi-asserted-by":"publisher","first-page":"19895","DOI":"10.1021\/acsomega.9b02808","article-title":"Continuous\nActivity Assay for HDAC11 Enabling Reevaluation\nof HDAC Inhibitors","volume":"4","author":"Kutil","year":"2019","journal-title":"ACS Omega"},{"issue":"10","key":"2026100608064199500_cit22","doi-asserted-by":"publisher","DOI":"10.1002\/ardp.202400486","article-title":"Utilization of an optimized AlphaFold\nprotein model for structure-based design of a selective HDAC11 inhibitor\nwith anti-neuroblastoma activity","volume":"357","author":"Baselious","year":"2024","journal-title":"Arch. Pharm."},{"issue":"7","key":"2026100608064199500_cit23","doi-asserted-by":"crossref","first-page":"141","DOI":"10.1140\/epjp\/i2015-15141-2","article-title":"The macromolecular\ncrystallography\nbeamlines at BESSY II of the Helmholtz-Zentrum Berlin: Current status\nand perspectives","volume":"130","author":"Mueller","year":"2015","journal-title":"Eur. Phys. J. Plus"},{"issue":"Pt 2","key":"2026100608064199500_cit24","doi-asserted-by":"publisher","first-page":"125","DOI":"10.1107\/S0907444909047337","article-title":"Biol Crystallogr\n66 (Pt 2)Xds","volume":"66","author":"Kabsch","year":"2010","journal-title":"Acta Crystallogr., Sect. D"},{"key":"2026100608064199500_cit25","doi-asserted-by":"publisher","first-page":"1022","DOI":"10.1107\/S0021889897006766","article-title":"MOLREP: an\nautomated program for molecular replacement","volume":"30","author":"Vagin","year":"1997","journal-title":"J. Appl. Crystallogr."},{"key":"2026100608064199500_cit26","doi-asserted-by":"publisher","first-page":"240","DOI":"10.1107\/S0907444996012255","article-title":"Refinement of macromolecular\nstructures\nby the maximum-likelihood method","volume":"53","author":"Murshudov","year":"1997","journal-title":"Acta Crystallogr.\nD"},{"key":"2026100608064199500_cit27","doi-asserted-by":"publisher","first-page":"300","DOI":"10.1016\/S0076-6879(03)74014-2","article-title":"Macromolecular TLS refinement in\nREFMAC at moderate resolutions","volume":"374","author":"Winn","year":"2003","journal-title":"Method. Enzymol."},{"issue":"Pt 4","key":"2026100608064199500_cit28","doi-asserted-by":"publisher","first-page":"486","DOI":"10.1107\/S0907444910007493","article-title":"Features and development\nof Coot","volume":"66","author":"Emsley","year":"2010","journal-title":"Acta Crystallogr., Sect. D"},{"issue":"8","key":"2026100608064199500_cit29","doi-asserted-by":"publisher","first-page":"1355","DOI":"10.1107\/S0907444904011679","article-title":"PRODRG:\na tool for high-throughput crystallography\nof protein-ligand complexes","volume":"60","author":"Schuttelkopf","year":"2004","journal-title":"Acta Crystallogr.,\nSect. D"},{"key":"2026100608064199500_cit30","doi-asserted-by":"publisher","first-page":"6263","DOI":"10.1038\/ncomms7263","article-title":"Selective Sirt2 inhibition\nby ligand-induced rearrangement of the active site","volume":"6","author":"Rumpf","year":"2015","journal-title":"Nat. Commun."},{"issue":"Pt 4","key":"2026100608064199500_cit31","doi-asserted-by":"publisher","first-page":"293","DOI":"10.1107\/S0907444911007773","article-title":"Data processing and\nanalysis with the autoPROC toolbox","volume":"67","author":"Vonrhein","year":"2011","journal-title":"Acta Crystallogr.,\nSect. D"},{"issue":"4","key":"2026100608064199500_cit32","doi-asserted-by":"publisher","first-page":"235","DOI":"10.1107\/S0907444910045749","article-title":"Overview\nof the CCP4 suite and current developments","volume":"67","author":"Winn","year":"2011","journal-title":"Acta Crystallogr., Sect. D"},{"issue":"Pt 4","key":"2026100608064199500_cit33","doi-asserted-by":"publisher","first-page":"658","DOI":"10.1107\/S0021889807021206","article-title":"Phaser crystallographic software","volume":"40","author":"McCoy","year":"2007","journal-title":"J. Appl. Crystallogr."},{"issue":"11","key":"2026100608064199500_cit34","doi-asserted-by":"publisher","first-page":"10771","DOI":"10.1021\/acs.jmedchem.4c02896","article-title":"Efficient\nCrystallization\nof Apo Sirt2 for Small-Molecule Soaking and Structural Analysis of\nLigand Interactions","volume":"68","author":"Friedrich","year":"2025","journal-title":"J. Med. Chem."},{"issue":"19","key":"2026100608064199500_cit35","doi-asserted-by":"publisher","first-page":"3037","DOI":"10.1021\/acs.biochem.5b00150","article-title":"Kinetic and Structural Basis for\nAcyl-Group Selectivity and NAD(+) Dependence in Sirtuin-Catalyzed\nDeacylation","volume":"54","author":"Feldman","year":"2015","journal-title":"Biochemistry"},{"issue":"Pt 4","key":"2026100608064199500_cit36","doi-asserted-by":"publisher","first-page":"355","DOI":"10.1107\/S0907444911001314","article-title":"REFMAC5\nfor the refinement of macromolecular crystal structures","volume":"67","author":"Murshudov","year":"2011","journal-title":"Acta Crystallogr., Sect. D"},{"issue":"Pt 2","key":"2026100608064199500_cit37","doi-asserted-by":"publisher","first-page":"213","DOI":"10.1107\/S0907444909052925","article-title":"PHENIX: a comprehensive\nPython-based\nsystem for macromolecular structure solution","volume":"66","author":"Adams","year":"2010","journal-title":"Acta Crystallogr., Sect. D"},{"issue":"Pt 1","key":"2026100608064199500_cit38","doi-asserted-by":"publisher","first-page":"12","DOI":"10.1107\/S0907444909042073","article-title":"MolProbity: all-atom structure validation for macromolecular\ncrystallography","volume":"66","author":"Chen","year":"2010","journal-title":"Acta Crystallogr., Sect. D"},{"key":"2026100608064199500_cit39","volume-title":"Schro\u0308dinger\nRelease 2025\u20132:\nLigPrep","author":"Schro\u0308dinger.","year":"2025"},{"issue":"1","key":"2026100608064199500_cit40","doi-asserted-by":"publisher","first-page":"281","DOI":"10.1021\/acs.jctc.5b00864","article-title":"OPLS3:\nA Force Field\nProviding Broad Coverage of Drug-like Small Molecules and Proteins","volume":"12","author":"Harder","year":"2016","journal-title":"J. Chem. Theory Comput."},{"issue":"45","key":"2026100608064199500_cit41","doi-asserted-by":"publisher","first-page":"11225","DOI":"10.1021\/ja9621760","article-title":"Development\nand testing of the OPLS\nall-atom force field on conformational energetics and properties of\norganic liquids","volume":"118","author":"Jorgensen","year":"1996","journal-title":"J. Am. Chem. Soc."},{"issue":"6","key":"2026100608064199500_cit42","doi-asserted-by":"publisher","first-page":"1657","DOI":"10.1021\/ja00214a001","article-title":"The OPLS [optimized\npotentials for liquid simulations]\npotential functions for proteins, energy minimizations for crystals\nof cyclic peptides and crambin","volume":"110","author":"Jorgensen","year":"1988","journal-title":"J. Am. Chem.\nSoc."},{"issue":"5","key":"2026100608064199500_cit43","doi-asserted-by":"publisher","first-page":"1509","DOI":"10.1021\/ct900587b","article-title":"Prediction of Absolute Solvation Free Energies using\nMolecular Dynamics Free Energy Perturbation and the OPLS Force Field","volume":"6","author":"Shivakumar","year":"2010","journal-title":"J. Chem. Theory Comput."},{"issue":"3","key":"2026100608064199500_cit44","doi-asserted-by":"publisher","first-page":"1863","DOI":"10.1021\/acs.jctc.8b01026","article-title":"OPLS3e: Extending\nForce Field Coverage for Drug-Like Small Molecules","volume":"15","author":"Roos","year":"2019","journal-title":"J. Chem. Theory Comput."},{"issue":"7","key":"2026100608064199500_cit45","doi-asserted-by":"publisher","first-page":"4291","DOI":"10.1021\/acs.jctc.1c00302","article-title":"OPLS4: Improving\nForce Field Accuracy on Challenging Regimes of Chemical Space","volume":"17","author":"Lu","year":"2021","journal-title":"J. Chem. Theory Comput."},{"key":"2026100608064199500_cit46","volume-title":"Schro\u0308dinger\nRelease 2025\u20132,\nForce Fields","author":"Schro\u0308dinger.","year":"2025"},{"key":"2026100608064199500_cit47","doi-asserted-by":"publisher","first-page":"107700","DOI":"10.1016\/j.compbiomed.2023.107700","article-title":"Utilization\nof AlphaFold models for\ndrug discovery: Feasibility and challenges. Histone deacetylase 11\nas a case study","volume":"167","author":"Baselious","year":"2023","journal-title":"Comput. Biol. Med."},{"issue":"9","key":"2026100608064199500_cit48","doi-asserted-by":"publisher","first-page":"879","DOI":"10.1038\/sj.embor.7401047","article-title":"Substrate binding to histone deacetylases\nas shown\nby the crystal structure of the HDAC8-substrate complex","volume":"8","author":"Vannini","year":"2007","journal-title":"EMBO Rep."},{"issue":"21","key":"2026100608064199500_cit49","doi-asserted-by":"publisher","first-page":"6177","DOI":"10.1021\/jm051256o","article-title":"Extra precision\nglide: docking and scoring incorporating a model of hydrophobic enclosure\nfor protein-ligand complexes","volume":"49","author":"Friesner","year":"2006","journal-title":"J. Med. Chem."},{"issue":"7","key":"2026100608064199500_cit50","doi-asserted-by":"publisher","first-page":"1750","DOI":"10.1021\/jm030644s","article-title":"Glide: a new approach for rapid,\naccurate docking and scoring. 2. 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