{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,29]],"date-time":"2026-07-29T12:20:47Z","timestamp":1785327647189,"version":"3.55.0"},"reference-count":73,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2016,7,1]],"date-time":"2016-07-01T00:00:00Z","timestamp":1467331200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2016,6,6]],"date-time":"2016-06-06T00:00:00Z","timestamp":1465171200000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by-nc-nd\/4.0\/"}],"funder":[{"name":"Ministry of Health, Labor and Welfare of Japan"},{"name":"Research Committee of Molecular Pathogenesis and Therapies for Prion Disease and Slow Virus Infection"},{"DOI":"10.13039\/100009619","name":"Japan Agency for Medical Research and Development","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100009619","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100007449","name":"Takeda Science Foundation","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100007449","id-type":"DOI","asserted-by":"publisher"}]},{"name":"Japan Intractable Disease Research Foundation"},{"DOI":"10.13039\/100011313","name":"Tokyo Biochemical Research Foundation","doi-asserted-by":"crossref","id":[{"id":"10.13039\/100011313","id-type":"DOI","asserted-by":"crossref"}]},{"name":"YOKOYAMA Foundation for Clinical Pharmacology","award":["YRY1502"],"award-info":[{"award-number":["YRY1502"]}]}],"content-domain":{"domain":["ebiomedicine.com","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["EBioMedicine"],"published-print":{"date-parts":[[2016,7]]},"DOI":"10.1016\/j.ebiom.2016.06.010","type":"journal-article","created":{"date-parts":[[2016,6,11]],"date-time":"2016-06-11T11:56:40Z","timestamp":1465646200000},"page":"238-249","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":40,"special_numbering":"C","title":["Structure-Based Drug Discovery for Prion Disease Using a Novel Binding Simulation"],"prefix":"10.1016","volume":"9","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-9844-5109","authenticated-orcid":false,"given":"Daisuke","family":"Ishibashi","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Takehiro","family":"Nakagaki","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Takeshi","family":"Ishikawa","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ryuichiro","family":"Atarashi","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ken","family":"Watanabe","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Felipe A.","family":"Cruz","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tsuyoshi","family":"Hamada","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Noriyuki","family":"Nishida","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.ebiom.2016.06.010_bb0005","doi-asserted-by":"crossref","first-page":"2595","DOI":"10.1099\/vir.0.19073-0","article-title":"A novel generation of heparan sulfate mimetics for the treatment of prion diseases","volume":"84","author":"Adjou","year":"2003","journal-title":"J. Gen. Virol."},{"key":"10.1016\/j.ebiom.2016.06.010_bb0010","doi-asserted-by":"crossref","first-page":"361","DOI":"10.4161\/auto.5.3.7662","article-title":"Autophagy induction by trehalose counteracts cellular prion infection","volume":"5","author":"Aguib","year":"2009","journal-title":"Autophagy"},{"key":"10.1016\/j.ebiom.2016.06.010_bb0015","doi-asserted-by":"crossref","first-page":"1105","DOI":"10.1152\/physrev.00006.2009","article-title":"Prions: protein aggregation and infectious diseases","volume":"89","author":"Aguzzi","year":"2009","journal-title":"Physiol. Rev."},{"key":"10.1016\/j.ebiom.2016.06.010_bb0020","doi-asserted-by":"crossref","first-page":"175","DOI":"10.1038\/nm.2294","article-title":"Ultrasensitive human prion detection in cerebrospinal fluid by real-time quaking-induced conversion","volume":"17","author":"Atarashi","year":"2011","journal-title":"Nat. Med."},{"key":"10.1016\/j.ebiom.2016.06.010_bb0025","doi-asserted-by":"crossref","first-page":"243","DOI":"10.1042\/BJ20111940","article-title":"Structural basis for the protective effect of the human prion protein carrying the dominant-negative E219K polymorphism","volume":"446","author":"Biljan","year":"2012","journal-title":"Biochem. J."},{"key":"10.1016\/j.ebiom.2016.06.010_bb0030","doi-asserted-by":"crossref","first-page":"603","DOI":"10.1083\/jcb.200507002","article-title":"p62\/SQSTM1 forms protein aggregates degraded by autophagy and has a protective effect on Huntingtin-induced cell death","volume":"171","author":"Bjorkoy","year":"2005","journal-title":"J. Cell Biol."},{"key":"10.1016\/j.ebiom.2016.06.010_bb0035","doi-asserted-by":"crossref","first-page":"310","DOI":"10.1038\/nn.2483","article-title":"Axonal prion protein is required for peripheral myelin maintenance","volume":"13","author":"Bremer","year":"2010","journal-title":"Nat. Neurosci."},{"key":"10.1016\/j.ebiom.2016.06.010_bb0040","series-title":"AMBER 10","author":"Case","year":"2008"},{"key":"10.1016\/j.ebiom.2016.06.010_bb0045","doi-asserted-by":"crossref","first-page":"768","DOI":"10.1111\/j.1471-4159.1992.tb09437.x","article-title":"Potent inhibition of scrapie-associated PrP accumulation by congo red","volume":"59","author":"Caughey","year":"1992","journal-title":"J. Neurochem."},{"key":"10.1016\/j.ebiom.2016.06.010_bb0050","doi-asserted-by":"crossref","first-page":"643","DOI":"10.1128\/JVI.67.2.643-650.1993","article-title":"Sulfated polyanion inhibition of scrapie-associated PrP accumulation in cultured cells","volume":"67","author":"Caughey","year":"1993","journal-title":"J. Virol."},{"key":"10.1016\/j.ebiom.2016.06.010_bb0055","doi-asserted-by":"crossref","first-page":"32303","DOI":"10.1074\/jbc.M110.114504","article-title":"Probing the conformation of a prion protein fibril with hydrogen exchange","volume":"285","author":"Damo","year":"2010","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.ebiom.2016.06.010_bb0060","doi-asserted-by":"crossref","first-page":"4999","DOI":"10.1128\/JVI.78.10.4999-5006.2004","article-title":"Treatment of transmissible spongiform encephalopathy by intraventricular drug infusion in animal models","volume":"78","author":"Doh-ura","year":"2004","journal-title":"J. Virol."},{"key":"10.1016\/j.ebiom.2016.06.010_bb0065","doi-asserted-by":"crossref","first-page":"7710","DOI":"10.1523\/JNEUROSCI.3021-12.2013","article-title":"p62\/SQSTM1 differentially removes the toxic mutant androgen receptor via autophagy and inclusion formation in a spinal and bulbar muscular atrophy mouse model","volume":"33","author":"Doi","year":"2013","journal-title":"J. Neurosci."},{"key":"10.1016\/j.ebiom.2016.06.010_bb0070","doi-asserted-by":"crossref","first-page":"1007","DOI":"10.1063\/1.456153","article-title":"Gaussian basis sets for use in correlated molecular calculations. I. The atoms boron through neon and hydrogen","volume":"90","author":"Dunning","year":"1989","journal-title":"J. Chem. Phys."},{"key":"10.1016\/j.ebiom.2016.06.010_bb0075","doi-asserted-by":"crossref","first-page":"9295","DOI":"10.1073\/pnas.151242598","article-title":"Scrapie prion protein accumulation by scrapie-infected neuroblastoma cells abrogated by exposure to a prion protein antibody","volume":"98","author":"Enari","year":"2001","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.ebiom.2016.06.010_bb0080","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0084531","article-title":"Anti-prion activity of a panel of aromatic chemical compounds: in vitro and in silico approaches","volume":"9","author":"Ferreira","year":"2014","journal-title":"PLoS One"},{"key":"10.1016\/j.ebiom.2016.06.010_bb0085","doi-asserted-by":"crossref","first-page":"3957","DOI":"10.1093\/emboj\/20.15.3957","article-title":"Intracellular re-routing of prion protein prevents propagation of PrP(Sc) and delays onset of prion disease","volume":"20","author":"Gilch","year":"2001","journal-title":"EMBO J."},{"key":"10.1016\/j.ebiom.2016.06.010_bb0090","doi-asserted-by":"crossref","first-page":"24129","DOI":"10.1074\/jbc.M114.578344","article-title":"Parallel in-register intermolecular beta-sheet architectures for prion-seeded prion protein (PrP) amyloids","volume":"289","author":"Groveman","year":"2014","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.ebiom.2016.06.010_bb0095","doi-asserted-by":"crossref","first-page":"150","DOI":"10.1016\/S1474-4422(13)70307-7","article-title":"Doxycycline in Creutzfeldt\u2013Jakob disease: a phase 2, randomised, double-blind, placebo-controlled trial","volume":"13","author":"Haik","year":"2014","journal-title":"Lancet Neurol."},{"key":"10.1016\/j.ebiom.2016.06.010_bb0100","doi-asserted-by":"crossref","first-page":"25","DOI":"10.1111\/j.1471-4159.2009.05906.x","article-title":"Lithium induces clearance of protease resistant prion protein in prion-infected cells by induction of autophagy","volume":"109","author":"Heiseke","year":"2009","journal-title":"J. Neurochem."},{"key":"10.1016\/j.ebiom.2016.06.010_bb0105","doi-asserted-by":"crossref","first-page":"6284","DOI":"10.1073\/pnas.0711716105","article-title":"Molecular conformation and dynamics of the Y145Stop variant of human prion protein in amyloid fibrils","volume":"105","author":"Helmus","year":"2008","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.ebiom.2016.06.010_bb0110","doi-asserted-by":"crossref","DOI":"10.1126\/scitranslmed.aab1923","article-title":"). Structure-based drug design identifies polythiophenes as antiprion compounds","volume":"7","author":"Herrmann","year":"2015","journal-title":"Sci. Transl. Med."},{"key":"10.1016\/j.ebiom.2016.06.010_bb0115","first-page":"7","article-title":"New anti-HIV drugs in development","volume":"12","author":"Highleyman","year":"1999","journal-title":"Beta"},{"key":"10.1016\/j.ebiom.2016.06.010_bb0120","doi-asserted-by":"crossref","first-page":"6006","DOI":"10.1038\/srep06006","article-title":"Persistent prion infection disturbs the function of Oct-1, resulting in the down-regulation of murine interferon regulatory factor-3","volume":"4","author":"Homma","year":"2014","journal-title":"Sci. Rep."},{"key":"10.1016\/j.ebiom.2016.06.010_bb0125","doi-asserted-by":"crossref","first-page":"4504","DOI":"10.1038\/srep04504","article-title":"Increased expression of p62\/SQSTM1 in prion diseases and its association with pathogenic prion protein","volume":"4","author":"Homma","year":"2014","journal-title":"Sci. Rep."},{"key":"10.1016\/j.ebiom.2016.06.010_bb0130","doi-asserted-by":"crossref","first-page":"11028","DOI":"10.1038\/srep11028","article-title":"Ubiquitin-specific protease 14 modulates degradation of cellular prion protein","volume":"5","author":"Homma","year":"2015","journal-title":"Sci. Rep."},{"key":"10.1016\/j.ebiom.2016.06.010_bb0135","doi-asserted-by":"crossref","first-page":"712","DOI":"10.1002\/prot.21123","article-title":"Comparison of multiple amber force fields and development of improved protein backbone parameters","volume":"65","author":"Hornak","year":"2006","journal-title":"Proteins"},{"key":"10.1016\/j.ebiom.2016.06.010_bb0140","doi-asserted-by":"crossref","first-page":"14944","DOI":"10.1038\/srep14944","article-title":"Discovery of novel anti-prion compounds using in silico and in vitro approaches","volume":"5","author":"Hyeon","year":"2015","journal-title":"Sci. Rep."},{"key":"10.1016\/j.ebiom.2016.06.010_bb0145","doi-asserted-by":"crossref","first-page":"22847","DOI":"10.1074\/jbc.M802182200","article-title":"Structural basis for sorting mechanism of p62 in selective autophagy","volume":"283","author":"Ichimura","year":"2008","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.ebiom.2016.06.010_bb0150","doi-asserted-by":"crossref","first-page":"9321","DOI":"10.1016\/j.vaccine.2011.10.017","article-title":"Antigenic mimicry-mediated anti-prion effects induced by bacterial enzyme succinylarginine dihydrolase in mice","volume":"29","author":"Ishibashi","year":"2011","journal-title":"Vaccine"},{"key":"10.1016\/j.ebiom.2016.06.010_bb0155","doi-asserted-by":"crossref","first-page":"4947","DOI":"10.1128\/JVI.06326-11","article-title":"Protective role of interferon regulatory factor 3-mediated signaling against prion infection","volume":"86","author":"Ishibashi","year":"2012","journal-title":"J. Virol."},{"key":"10.1016\/j.ebiom.2016.06.010_bb0160","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0137958","article-title":"Strain-dependent effect of macroautophagy on abnormally folded prion protein degradation in infected neuronal cells","volume":"10","author":"Ishibashi","year":"2015","journal-title":"PLoS One"},{"key":"10.1016\/j.ebiom.2016.06.010_bb0165","doi-asserted-by":"crossref","first-page":"195","DOI":"10.1016\/j.cplett.2009.04.045","article-title":"Fragment molecular orbital calculation using the RI-MP2 method","volume":"474","author":"Ishikawa","year":"2009","journal-title":"Chem. Phys. Lett."},{"key":"10.1016\/j.ebiom.2016.06.010_bb0170","doi-asserted-by":"crossref","first-page":"2594","DOI":"10.1002\/jcc.21265","article-title":"Theoretical study of the prion protein based on the fragment molecular orbital method","volume":"30","author":"Ishikawa","year":"2009","journal-title":"J. Comput. Chem."},{"key":"10.1016\/j.ebiom.2016.06.010_bb0175","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/S0169-328X(98)00040-0","article-title":"Microglia-specific localisation of a novel calcium binding protein, Iba1","volume":"57","author":"Ito","year":"1998","journal-title":"Brain Res. Mol. Brain Res."},{"key":"10.1016\/j.ebiom.2016.06.010_bb0180","doi-asserted-by":"crossref","first-page":"532","DOI":"10.1002\/ana.22615","article-title":"Pathogenic protein seeding in Alzheimer disease and other neurodegenerative disorders","volume":"70","author":"Jucker","year":"2011","journal-title":"Ann. Neurol."},{"key":"10.1016\/j.ebiom.2016.06.010_bb0185","doi-asserted-by":"crossref","first-page":"3979","DOI":"10.1021\/jm9704098","article-title":"Viracept (nelfinavir mesylate, AG1343): a potent, orally bioavailable inhibitor of HIV-1 protease","volume":"40","author":"Kaldor","year":"1997","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.ebiom.2016.06.010_bb0190","doi-asserted-by":"crossref","first-page":"12889","DOI":"10.1128\/JVI.01563-07","article-title":"Orally administered amyloidophilic compound is effective in prolonging the incubation periods of animals cerebrally infected with prion diseases in a prion strain-dependent manner","volume":"81","author":"Kawasaki","year":"2007","journal-title":"J. Virol."},{"key":"10.1016\/j.ebiom.2016.06.010_bb0195","doi-asserted-by":"crossref","first-page":"319","DOI":"10.1016\/S0009-2614(99)00937-9","article-title":"Pair interaction molecular orbital method: an approximate computational method for molecular interactions","volume":"312","author":"Kitaura","year":"1999","journal-title":"Chem. Phys. Lett."},{"key":"10.1016\/j.ebiom.2016.06.010_bb0200","doi-asserted-by":"crossref","first-page":"1149","DOI":"10.1016\/j.cell.2007.10.035","article-title":"Homeostatic levels of p62 control cytoplasmic inclusion body formation in autophagy-deficient mice","volume":"131","author":"Komatsu","year":"2007","journal-title":"Cell"},{"key":"10.1016\/j.ebiom.2016.06.010_bb0205","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0043505","article-title":"Quantitative analysis of alpha-synuclein solubility in living cells using split GFP complementation","volume":"7","author":"Kothawala","year":"2012","journal-title":"PLoS One"},{"key":"10.1016\/j.ebiom.2016.06.010_bb0210","doi-asserted-by":"crossref","first-page":"12277","DOI":"10.1021\/bi026129y","article-title":"Locally disordered conformer of the hamster prion protein: a crucial intermediate to PrPSc?","volume":"41","author":"Kuwata","year":"2002","journal-title":"Biochemistry"},{"key":"10.1016\/j.ebiom.2016.06.010_bb0215","doi-asserted-by":"crossref","first-page":"11921","DOI":"10.1073\/pnas.0702671104","article-title":"Hot spots in prion protein for pathogenic conversion","volume":"104","author":"Kuwata","year":"2007","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.ebiom.2016.06.010_bb0220","doi-asserted-by":"crossref","first-page":"11686","DOI":"10.1073\/pnas.201404298","article-title":"Solid-state NMR studies of the secondary structure of a mutant prion protein fragment of 55 residues that induces neurodegeneration","volume":"98","author":"Laws","year":"2001","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.ebiom.2016.06.010_bb0225","doi-asserted-by":"crossref","first-page":"3135","DOI":"10.1128\/JVI.74.7.3135-3140.2000","article-title":"Amphotericin B inhibits the generation of the scrapie isoform of the prion protein in infected cultures","volume":"74","author":"Mange","year":"2000","journal-title":"J. Virol."},{"key":"10.1016\/j.ebiom.2016.06.010_bb0230","first-page":"30","article-title":"Selective inhibitors of cyclooxygenase-2: a growing class of anti-inflammatory drugs","volume":"1","author":"Mardini","year":"2001","journal-title":"Mol. Interv."},{"key":"10.1016\/j.ebiom.2016.06.010_bb0235","doi-asserted-by":"crossref","first-page":"25457","DOI":"10.1074\/jbc.M203248200","article-title":"Filipin prevents pathological prion protein accumulation by reducing endocytosis and inducing cellular PrP release","volume":"277","author":"Marella","year":"2002","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.ebiom.2016.06.010_bb0240","doi-asserted-by":"crossref","first-page":"1345","DOI":"10.1242\/jcs.114801","article-title":"4-Hydroxytamoxifen leads to PrPSc clearance by conveying both PrPC and PrPSc to lysosomes independently of autophagy","volume":"126","author":"Marzo","year":"2013","journal-title":"J. Cell Sci."},{"key":"10.1016\/j.ebiom.2016.06.010_bb0245","doi-asserted-by":"crossref","first-page":"279","DOI":"10.1016\/j.molcel.2011.07.039","article-title":"Serine 403 phosphorylation of p62\/SQSTM1 regulates selective autophagic clearance of ubiquitinated proteins","volume":"44","author":"Matsumoto","year":"2011","journal-title":"Mol. Cell"},{"key":"10.1016\/j.ebiom.2016.06.010_bb0250","doi-asserted-by":"crossref","first-page":"R796","DOI":"10.1016\/S0960-9822(99)80491-6","article-title":"Relenza","volume":"9","author":"McCauley","year":"1999","journal-title":"Curr. Biol."},{"key":"10.1016\/j.ebiom.2016.06.010_bb0255","doi-asserted-by":"crossref","first-page":"1386","DOI":"10.4161\/auto.25381","article-title":"FK506 reduces abnormal prion protein through the activation of autolysosomal degradation and prolongs survival in prion-infected mice","volume":"9","author":"Nakagaki","year":"2013","journal-title":"Autophagy"},{"key":"10.1016\/j.ebiom.2016.06.010_bb0260","doi-asserted-by":"crossref","first-page":"320","DOI":"10.1128\/JVI.74.1.320-325.2000","article-title":"Successful transmission of three mouse-adapted scrapie strains to murine neuroblastoma cell lines overexpressing wild-type mouse prion protein","volume":"74","author":"Nishida","year":"2000","journal-title":"J. Virol."},{"key":"10.1016\/j.ebiom.2016.06.010_bb0265","doi-asserted-by":"crossref","first-page":"33","DOI":"10.1186\/1758-2946-3-33","article-title":"Open babel: an open chemical toolbox","volume":"3","author":"O'Boyle","year":"2011","journal-title":"J. Cheminform"},{"key":"10.1016\/j.ebiom.2016.06.010_bb0270","doi-asserted-by":"crossref","first-page":"24131","DOI":"10.1074\/jbc.M702824200","article-title":"p62\/SQSTM1 binds directly to Atg8\/LC3 to facilitate degradation of ubiquitinated protein aggregates by autophagy","volume":"282","author":"Pankiv","year":"2007","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.ebiom.2016.06.010_bb0275","doi-asserted-by":"crossref","first-page":"739","DOI":"10.1038\/35089090","article-title":"Antibodies inhibit prion propagation and clear cell cultures of prion infectivity","volume":"412","author":"Peretz","year":"2001","journal-title":"Nature"},{"key":"10.1016\/j.ebiom.2016.06.010_bb0280","doi-asserted-by":"crossref","first-page":"6073","DOI":"10.1073\/pnas.97.11.6073","article-title":"Mimicking dominant negative inhibition of prion replication through structure-based drug design","volume":"97","author":"Perrier","year":"2000","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.ebiom.2016.06.010_bb0285","doi-asserted-by":"crossref","first-page":"113","DOI":"10.1007\/BF02780661","article-title":"Inhibition of scrapie-associated PrP accumulation. Probing the role of glycosaminoglycans in amyloidogenesis","volume":"8","author":"Priola","year":"1994","journal-title":"Mol. Neurobiol."},{"key":"10.1016\/j.ebiom.2016.06.010_bb0290","doi-asserted-by":"crossref","first-page":"13433","DOI":"10.1128\/JVI.02072-13","article-title":"Absence of CD14 delays progression of prion diseases accompanied by increased microglial activation","volume":"87","author":"Sakai","year":"2013","journal-title":"J. Virol."},{"key":"10.1016\/j.ebiom.2016.06.010_bb0295","doi-asserted-by":"crossref","first-page":"173","DOI":"10.1007\/s12013-010-9138-4","article-title":"Novel cell- and tissue-based assays for detecting misfolded and aggregated protein accumulation within aggresomes and inclusion bodies","volume":"60","author":"Shen","year":"2011","journal-title":"Cell Biochem. Biophys."},{"key":"10.1016\/j.ebiom.2016.06.010_bb0300","doi-asserted-by":"crossref","first-page":"8182","DOI":"10.1073\/pnas.1217730110","article-title":"In silico discovery of small-molecule Ras inhibitors that display antitumor activity by blocking the Ras-effector interaction","volume":"110","author":"Shima","year":"2013","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.ebiom.2016.06.010_bb0305","doi-asserted-by":"crossref","first-page":"501","DOI":"10.1038\/nrmicro2349","article-title":"Structure-based discovery of antibacterial drugs","volume":"8","author":"Simmons","year":"2010","journal-title":"Nat. Rev. Microbiol."},{"key":"10.1016\/j.ebiom.2016.06.010_bb0310","doi-asserted-by":"crossref","first-page":"504","DOI":"10.1038\/nsmb.2035","article-title":"Structural organization of brain-derived mammalian prions examined by hydrogen-deuterium exchange","volume":"18","author":"Smirnovas","year":"2011","journal-title":"Nat. Struct. Mol. Biol."},{"key":"10.1016\/j.ebiom.2016.06.010_bb0315","first-page":"37","article-title":"Current application of selective COX-2 inhibitors in cancer prevention and treatment","volume":"16","author":"Stratton","year":"2002","journal-title":"Oncology (Williston Park)"},{"key":"10.1016\/j.ebiom.2016.06.010_bb0320","doi-asserted-by":"crossref","first-page":"632","DOI":"10.1111\/j.1440-1789.2009.01058.x","article-title":"Continuous intraventricular infusion of pentosan polysulfate: clinical trial against prion diseases","volume":"29","author":"Tsuboi","year":"2009","journal-title":"Neuropathology"},{"key":"10.1016\/j.ebiom.2016.06.010_bb0325","doi-asserted-by":"crossref","first-page":"3563","DOI":"10.1021\/jm034093h","article-title":"Antimalarial drug quinacrine binds to C-terminal helix of cellular prion protein","volume":"46","author":"Vogtherr","year":"2003","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.ebiom.2016.06.010_bb0330","doi-asserted-by":"crossref","first-page":"795","DOI":"10.1007\/s00401-013-1114-9","article-title":"Anle138b: a novel oligomer modulator for disease-modifying therapy of neurodegenerative diseases such as prion and Parkinson's disease","volume":"125","author":"Wagner","year":"2013","journal-title":"Acta Neuropathol."},{"key":"10.1016\/j.ebiom.2016.06.010_bb0335","doi-asserted-by":"crossref","first-page":"1157","DOI":"10.1002\/jcc.20035","article-title":"Development and testing of a general amber force field","volume":"25","author":"Wang","year":"2004","journal-title":"J. Comput. Chem."},{"key":"10.1016\/j.ebiom.2016.06.010_bb0340","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0052868","article-title":"p62\/SQSTM1-dependent autophagy of Lewy body-like alpha-synuclein inclusions","volume":"7","author":"Watanabe","year":"2012","journal-title":"PLoS One"},{"key":"10.1016\/j.ebiom.2016.06.010_bb0345","doi-asserted-by":"crossref","first-page":"153","DOI":"10.55782\/ane-2002-1434","article-title":"Molecular biology of prions","volume":"62","author":"Weissmann","year":"2002","journal-title":"Acta Neurobiol. Exp. (Wars)"},{"key":"10.1016\/j.ebiom.2016.06.010_bb0350","doi-asserted-by":"crossref","first-page":"80","DOI":"10.1038\/nature01457","article-title":"Monoclonal antibodies inhibit prion replication and delay the development of prion disease","volume":"422","author":"White","year":"2003","journal-title":"Nature"},{"key":"10.1016\/j.ebiom.2016.06.010_bb0355","doi-asserted-by":"crossref","first-page":"3563","DOI":"10.1073\/pnas.052703499","article-title":"Structural studies of the scrapie prion protein by electron crystallography","volume":"99","author":"Wille","year":"2002","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.ebiom.2016.06.010_bb0360","doi-asserted-by":"crossref","first-page":"16990","DOI":"10.1073\/pnas.0909006106","article-title":"Natural and synthetic prion structure from X-ray fiber diffraction","volume":"106","author":"Wille","year":"2009","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.ebiom.2016.06.010_bb0365","doi-asserted-by":"crossref","first-page":"9826","DOI":"10.1021\/jp5034245","article-title":"Hot spot of structural ambivalence in prion protein revealed by secondary structure principal component analysis","volume":"118","author":"Yamamoto","year":"2014","journal-title":"J. Phys. Chem. B"}],"container-title":["EBioMedicine"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S2352396416302547?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S2352396416302547?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2024,6,17]],"date-time":"2024-06-17T15:13:40Z","timestamp":1718637220000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S2352396416302547"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2016,7]]},"references-count":73,"alternative-id":["S2352396416302547"],"URL":"https:\/\/doi.org\/10.1016\/j.ebiom.2016.06.010","relation":{},"ISSN":["2352-3964"],"issn-type":[{"value":"2352-3964","type":"print"}],"subject":[],"published":{"date-parts":[[2016,7]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Structure-Based Drug Discovery for Prion Disease Using a Novel Binding Simulation","name":"articletitle","label":"Article Title"},{"value":"EBioMedicine","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.ebiom.2016.06.010","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2016 The Author(s). Published by Elsevier B.V.","name":"copyright","label":"Copyright"}]}}