{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,15]],"date-time":"2026-08-15T14:26:17Z","timestamp":1786803977816,"version":"build-2736575974"},"reference-count":73,"publisher":"American Chemical Society (ACS)","issue":"37","license":[{"start":{"date-parts":[[2018,8,20]],"date-time":"2018-08-20T00:00:00Z","timestamp":1534723200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2018,8,20]],"date-time":"2018-08-20T00:00:00Z","timestamp":1534723200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2018,8,20]],"date-time":"2018-08-20T00:00:00Z","timestamp":1534723200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-045"}],"funder":[{"DOI":"10.13039\/100000165","name":"Division of Chemistry","doi-asserted-by":"publisher","award":["1507840"],"award-info":[{"award-number":["1507840"]}],"id":[{"id":"10.13039\/100000165","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000165","name":"Division of Chemistry","doi-asserted-by":"publisher","award":["1808096"],"award-info":[{"award-number":["1808096"]}],"id":[{"id":"10.13039\/100000165","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100008227","name":"Achievement Rewards for College Scientists Foundation","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100008227","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000057","name":"National Institute of General Medical Sciences","doi-asserted-by":"publisher","award":["097562"],"award-info":[{"award-number":["097562"]}],"id":[{"id":"10.13039\/100000057","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2018,9,19]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>Soluble oligomers of the \u03b2-amyloid peptide, A\u03b2, are associated with the progression of Alzheimer\u2019s disease. Although many small molecules bind to these assemblies, the details of how these molecules interact with A\u03b2 oligomers remain unknown. This paper reports that crystal violet, and other C3 symmetric triphenylmethane dyes, bind to C3 symmetric trimers derived from A\u03b217\u201336. Binding changes the color of the dyes from purple to blue, and causes them to fluoresce red when irradiated with green light. Job plot and analytical ultracentrifugation experiments reveal that two trimers complex with one dye molecule. Studies with several triphenylmethane dyes reveal that three N,N-dialkylamino substituents are required for complexation. Several mutant trimers, in which Phe19, Phe20, and Ile31 were mutated to cyclohexylalanine, valine, and cyclohexylglycine, were prepared to probe the triphenylmethane dye binding site. Size exclusion chromatography, SDS-PAGE, and X-ray crystallographic studies demonstrate that these mutations do not impact the structure or assembly of the triangular trimer. Fluorescence spectroscopy and analytical ultracentrifugation experiments reveal that the dye packs against an aromatic surface formed by the Phe20 side chains and is clasped by the Ile31 side chains. Docking and molecular modeling provide a working model of the complex in which the triphenylmethane dye is sandwiched between two triangular trimers. Collectively, these findings demonstrate that the X-ray crystallographic structures of triangular trimers derived from A\u03b2 can be used to guide the discovery of ligands that bind to soluble oligomers derived from A\u03b2.<\/jats:p>","DOI":"10.1021\/jacs.8b06568","type":"journal-article","created":{"date-parts":[[2018,8,20]],"date-time":"2018-08-20T18:48:13Z","timestamp":1534790893000},"page":"11745-11754","source":"Crossref","is-referenced-by-count":44,"title":["Repurposing\nTriphenylmethane Dyes to Bind to Trimers\nDerived from A\u03b2"],"prefix":"10.1021","volume":"140","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-0962-6010","authenticated-orcid":true,"given":"Patrick\nJ.","family":"Salveson","sequence":"first","affiliation":[{"name":"University of California Irvine , , , ,","place":["Irvine, California, United States, 92697-2025"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-1539-2345","authenticated-orcid":true,"given":"Sepehr","family":"Haerianardakani","sequence":"additional","affiliation":[{"name":"University of California Irvine , , , ,","place":["Irvine, California, United States, 92697-2025"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-9841-0758","authenticated-orcid":true,"given":"Alexander","family":"Thuy-Boun","sequence":"additional","affiliation":[{"name":"University of California Irvine , , , ,","place":["Irvine, California, United States, 92697-2025"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-8982-7631","authenticated-orcid":true,"given":"Stan","family":"Yoo","sequence":"additional","affiliation":[{"name":"University of California Irvine , , , ,","place":["Irvine, California, United States, 92697-2025"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-9724-6298","authenticated-orcid":true,"given":"Adam G.","family":"Kreutzer","sequence":"additional","affiliation":[{"name":"University of California Irvine , , , ,","place":["Irvine, California, United States, 92697-2025"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-2414-9518","authenticated-orcid":true,"given":"Borries","family":"Demeler","sequence":"additional","affiliation":[{"name":"University of Texas Health Science Center , , , ,","place":["San Antonio, Texas, United States, 78229-3900"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-2273-1029","authenticated-orcid":true,"given":"James S.","family":"Nowick","sequence":"additional","affiliation":[{"name":"University of California Irvine , , , ,","place":["Irvine, California, United States, 92697-2025"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"316","published-online":{"date-parts":[[2018,8,20]]},"reference":[{"key":"2026081501073883600_cit1","first-page":"487","article-title":"Fluorescent stains, with special reference to amyloid\nand connective tissue","volume":"68","author":"Vassar","year":"1959","journal-title":"Arch. Pathol."},{"key":"2026081501073883600_cit2","doi-asserted-by":"publisher","first-page":"244","DOI":"10.1016\/0003-2697(89)90046-8","article-title":"Fluorometric determination\nof amyloid fibrils in vitro using the fluorescent dye, thioflavine\nT","volume":"177","author":"Naiki","year":"1989","journal-title":"Anal. Biochem."},{"key":"2026081501073883600_cit3","doi-asserted-by":"publisher","first-page":"3","DOI":"10.1016\/S0076-6879(99)09003-5","article-title":"Staining methods\nfor identification\nof amyloid in tissue","volume":"309","author":"Westermark","year":"1999","journal-title":"Methods Enzymol."},{"key":"2026081501073883600_cit4","doi-asserted-by":"publisher","first-page":"135","DOI":"10.1016\/j.brainresrev.2006.08.001","article-title":"Congo red\nand protein aggregation\nin neurodegenerative diseases","volume":"53","author":"Frid","year":"2007","journal-title":"Brain Res. Rev."},{"key":"2026081501073883600_cit5","doi-asserted-by":"publisher","first-page":"1487","DOI":"10.1007\/s11095-007-9516-9","article-title":"Extrinsic\nfluorescent dyes as tools\nfor protein characterization","volume":"25","author":"Hawe","year":"2008","journal-title":"Pharm. Res."},{"key":"2026081501073883600_cit6","doi-asserted-by":"publisher","first-page":"865","DOI":"10.1126\/science.1101262","article-title":"Harnessing\nchaperones to generate\nsmall-molecule inhibitors of amyloid-\u03b2 aggregation","volume":"306","author":"Gestwicki","year":"2004","journal-title":"Science"},{"key":"2026081501073883600_cit7","doi-asserted-by":"publisher","first-page":"306","DOI":"10.1002\/ana.20009","article-title":"Imaging brain amyloid\nin Alzheimer\u2019s disease with Pittsburgh Compound-B","volume":"55","author":"Klunk","year":"2004","journal-title":"Ann. Neurol."},{"key":"2026081501073883600_cit8","doi-asserted-by":"publisher","first-page":"885","DOI":"10.1056\/NEJMp1208061","article-title":"Brain amyloid imaging-FDA approval\nof florbetapir F18 injection","volume":"367","author":"Yang","year":"2012","journal-title":"N. Engl. J. Med."},{"key":"2026081501073883600_cit9","doi-asserted-by":"publisher","first-page":"2136","DOI":"10.1021\/jacs.6b10809","article-title":"Analyzing\namyloid \u03b2 aggregates\nwith a combinatorial fluorescent molecular sensor","volume":"139","author":"Hatai","year":"2017","journal-title":"J. Am. Chem. Soc."},{"key":"2026081501073883600_cit10","doi-asserted-by":"publisher","first-page":"e11101","DOI":"10.1371\/journal.pone.0011101","article-title":"Complete phenotypic\nrecovery of an Alzheimer\u2019s disease model by a quinone-tryptophan\nhybrid aggregation inhibitor","volume":"5","author":"Scherzer-Attali","year":"2010","journal-title":"PLoS One"},{"key":"2026081501073883600_cit11","doi-asserted-by":"publisher","first-page":"e1001080","DOI":"10.1371\/journal.pbio.1001080","article-title":"Toward a pharmacophore for amyloid","volume":"9","author":"Landau","year":"2011","journal-title":"PLoS Biol."},{"key":"2026081501073883600_cit12","doi-asserted-by":"publisher","first-page":"550","DOI":"10.1016\/j.bpj.2012.07.008","article-title":"Binding of Congo red to amyloid protofibrils\nof the Alzheimer A\u03b29\u201340 peptide probed by molecular dynamics\nsimulations","volume":"103","author":"Wu","year":"2012","journal-title":"Biophys. J."},{"key":"2026081501073883600_cit13","doi-asserted-by":"publisher","first-page":"15114","DOI":"10.1021\/ja405530p","article-title":"Identification of a common binding\nmode for imaging agents to amyloid fibrils from molecular dynamics\nsimulations","volume":"135","author":"Skeby","year":"2013","journal-title":"J. Am. Chem. Soc."},{"key":"2026081501073883600_cit14","doi-asserted-by":"publisher","first-page":"1780","DOI":"10.1021\/jp309066p","article-title":"Methylations\nof tryptophan-modified naphthoquinone\naffect its inhibitory potnetial toward A\u03b2 aggregation","volume":"117","author":"Scherzer-Attali","year":"2013","journal-title":"J. Phys. Chem. B"},{"key":"2026081501073883600_cit15","doi-asserted-by":"publisher","first-page":"845","DOI":"10.1021\/cn300091a","article-title":"The role of molecular simulations in the development\nof inhibitors of amyloid-\u03b2 peptide aggregation for the treatment\nof Alzheimer\u2019s disease","volume":"3","author":"Lemkul","year":"2012","journal-title":"ACS Chem. Neurosci."},{"key":"2026081501073883600_cit16","doi-asserted-by":"publisher","first-page":"11568","DOI":"10.1021\/acs.jpcb.5b06112","article-title":"Molecular mechanisms\nof Alzheimer\u2019s biomaker\nFDDNP binding to A\u03b2 amyloid fibril","volume":"119","author":"Parikh","year":"2015","journal-title":"J.\nPhys. Chem. B"},{"key":"2026081501073883600_cit17","doi-asserted-by":"publisher","first-page":"90","DOI":"10.1016\/j.cbpa.2017.06.008","article-title":"Small molecule probes\nof protein\naggregation","volume":"39","author":"Young","year":"2017","journal-title":"Curr. Opin. Chem. Biol."},{"key":"2026081501073883600_cit18","doi-asserted-by":"publisher","first-page":"1211","DOI":"10.1021\/acs.jpcb.6b10460","article-title":"Identification of binding\nmodes for amino naphthalene 2-cyanoacrylate\n(ANCA) probes to amyloid fibrils from molecular dynamics simulations","volume":"121","author":"He","year":"2017","journal-title":"J. Phys. Chem. B"},{"key":"2026081501073883600_cit19","doi-asserted-by":"publisher","first-page":"1231","DOI":"10.1002\/pro.3391","article-title":"Atomic\nstructures of corkscrew-forming segments of SOD1 reveal varied oligomer\nconformations","volume":"27","author":"Sangwan","year":"2018","journal-title":"Protein Sci."},{"key":"2026081501073883600_cit20","doi-asserted-by":"publisher","first-page":"e00857","DOI":"10.7554\/eLife.01252","article-title":"Structure-based\ndiscovery of fiber-binding compounds\nthat reduce the cytotoxicity of amyloid-\u03b2","volume":"2","author":"Jiang","year":"2013","journal-title":"eLife"},{"key":"2026081501073883600_cit21","doi-asserted-by":"publisher","first-page":"457","DOI":"10.1111\/j.1471-4159.2007.04972.x","article-title":"Congo red\nand thioflavin-T analogs\ndetect A\u03b2 oligomers","volume":"104","author":"Maezawa","year":"2008","journal-title":"J. Neurochem."},{"key":"2026081501073883600_cit22","doi-asserted-by":"publisher","first-page":"13503","DOI":"10.1021\/jacs.5b06190","article-title":"Chemical fluorescent\nprobe for detection of A\u03b2\noligomers","volume":"137","author":"Teoh","year":"2015","journal-title":"J. Am. Chem. Soc."},{"key":"2026081501073883600_cit23","doi-asserted-by":"publisher","first-page":"8865","DOI":"10.1039\/C6CC02741E","article-title":"A spiropyran-based\nfluorescent probe for the specific detection of \u03b2-amyloid peptide\noligomers in Alzheimer\u2019s disease","volume":"52","author":"Lv","year":"2016","journal-title":"Chem.\nCommun."},{"key":"2026081501073883600_cit24","doi-asserted-by":"publisher","first-page":"8279","DOI":"10.1039\/C7SC03974C","article-title":"Fluoro-substituted\ncyanine for reliable in vivo labelling\nof amyloid-\u03b2 oligomers and neuroprotection against amyloid-\u03b2\ninduced toxicity","volume":"8","author":"Li","year":"2017","journal-title":"Chem. Sci."},{"key":"2026081501073883600_cit25","doi-asserted-by":"publisher","first-page":"2087","DOI":"10.1021\/acs.jpcb.5b09663","article-title":"An environmentally\nsensitive fluorescent dye as a multidimensional probe of amyloid formation","volume":"120","author":"Yates","year":"2016","journal-title":"J. Phys. Chem. B"},{"key":"2026081501073883600_cit26","doi-asserted-by":"publisher","first-page":"9322","DOI":"10.1021\/acs.analchem.7b02090","article-title":"Monitoring\nearly-stage protein aggregation by an aggregation-induced emission\nfluorogen","volume":"89","author":"Kumar","year":"2017","journal-title":"Anal. Chem."},{"key":"2026081501073883600_cit27","doi-asserted-by":"publisher","first-page":"797","DOI":"10.4155\/fmc-2017-0026","article-title":"Inhibition of amyloid\noligomerization into different supramolecular architectures by small\nmolecules: mechanistic insights and design rules","volume":"9","author":"Brahmachari","year":"2017","journal-title":"Future Med. Chem."},{"key":"2026081501073883600_cit28","doi-asserted-by":"publisher","first-page":"399","DOI":"10.1111\/j.1747-0285.2011.01110.x","article-title":"Insight into amyloid structure using chemical probes","volume":"77","author":"Reinke","year":"2011","journal-title":"Chem. Biol. Drug Des."},{"key":"2026081501073883600_cit29","doi-asserted-by":"publisher","first-page":"205","DOI":"10.1016\/j.neurobiolaging.2016.03.019","article-title":"What amyloid ligands\ncan tell us about molecular polymorphism\nand disease","volume":"42","author":"LeVine","year":"2016","journal-title":"Neurobiol. Aging"},{"key":"2026081501073883600_cit30","doi-asserted-by":"publisher","first-page":"1907","DOI":"10.1016\/j.bbapap.2014.08.016","volume":"1844","author":"De Genst","year":"2014","journal-title":"Biochim. Biophys. Acta"},{"key":"2026081501073883600_cit31","doi-asserted-by":"publisher","first-page":"966","DOI":"10.1021\/jacs.6b11748","article-title":"Stabilization, assembly, and toxicity\nof trimers derived from A\u03b2","volume":"139","author":"Kreutzer","year":"2017","journal-title":"J. Am. Chem.\nSoc."},{"key":"2026081501073883600_cit32","doi-asserted-by":"publisher","first-page":"5595","DOI":"10.1021\/ja5017409","article-title":"X-ray crystallographic structures of trimers and higher-order\noligomeric assemblies of a peptide derived from A\u03b217\u201336","volume":"136","author":"Spencer","year":"2014","journal-title":"J. Am. Chem. Soc."},{"key":"2026081501073883600_cit34","doi-asserted-by":"publisher","first-page":"486","DOI":"10.1126\/science.1079469","article-title":"Common structure of soluble amyloid\noligomers implies common mechanism of pathogenesis","volume":"300","author":"Kayed","year":"2003","journal-title":"Science"},{"key":"2026081501073883600_cit35","doi-asserted-by":"publisher","first-page":"349","DOI":"10.1038\/nn.3028","article-title":"The toxic A\u03b2 oligomer and Alzheimer\u2019s\ndisease: an emperor in need of clothes","volume":"15","author":"Benilova","year":"2012","journal-title":"Nat.\nNeurosci."},{"key":"2026081501073883600_cit36","doi-asserted-by":"publisher","first-page":"96","DOI":"10.1038\/nature10154","article-title":"Structure-based\ndesign of non-natural\namino-acid inhibitors of amyloid fibril formation","volume":"475","author":"Sievers","year":"2011","journal-title":"Nature"},{"key":"2026081501073883600_cit37","doi-asserted-by":"publisher","first-page":"170","DOI":"10.1038\/nchem.2889","article-title":"Structure-based\ninhibitors of tau aggregation","volume":"10","author":"Seidler","year":"2018","journal-title":"Nat. Chem."},{"key":"2026081501073883600_cit38","doi-asserted-by":"publisher","first-page":"381","DOI":"10.1021\/cr00017a018","article-title":"The photochemistry\nand photophysics of triphenylmethane dyes in solid and liquid media","volume":"93","author":"Duxbury","year":"1993","journal-title":"Chem. Rev."},{"key":"2026081501073883600_cit39","doi-asserted-by":"publisher","first-page":"4678","DOI":"10.1021\/jp981185n","article-title":"Effect of BSA on photophysical and photochemical properties\nof triarylmethane dyes","volume":"102","author":"Baptista","year":"1998","journal-title":"J. Phys. Chem. B"},{"key":"2026081501073883600_cit40","doi-asserted-by":"publisher","first-page":"219","DOI":"10.1016\/S0143-7208(99)00062-5","article-title":"Spectroscopic and\nphotochemical properties of malachite\ngreen noncovalently bound to bovine serum albumin","volume":"43","author":"Bartlett","year":"1999","journal-title":"Dyes Pigm."},{"key":"2026081501073883600_cit41","doi-asserted-by":"publisher","first-page":"1623","DOI":"10.1080\/01932691.2015.1073597","article-title":"The interaction between crystal violet\nand bovine serum\nalbumin: spectroscopic and molecular docking investigations","volume":"37","author":"Qin","year":"2016","journal-title":"J. Dispersion Sci. Technol."},{"key":"2026081501073883600_cit42","doi-asserted-by":"publisher","first-page":"5361","DOI":"10.1039\/c1cs15113d","article-title":"Aggregation-induced\nemission","volume":"40","author":"Hong","year":"2011","journal-title":"Chem. Soc. Rev."},{"key":"2026081501073883600_cit43","doi-asserted-by":"publisher","first-page":"11718","DOI":"10.1021\/acs.chemrev.5b00263","article-title":"Aggregation-induced\nemission: Together we shine, united we soar!","volume":"115","author":"Mei","year":"2015","journal-title":"Chem. Rev."},{"key":"2026081501073883600_cit44","first-page":"113","article-title":"Formation\nand stability of inorganic complexes in solution","volume":"9","author":"Job","year":"1928","journal-title":"Ann. Chim."},{"key":"2026081501073883600_cit45","doi-asserted-by":"publisher","first-page":"833","DOI":"10.1021\/ed069p833","article-title":"Quantitative analysis\nof continuous-variation plots with a comparison of several methods","volume":"69","author":"Bruneau","year":"1992","journal-title":"J. Chem. Educ."},{"key":"2026081501073883600_cit46","doi-asserted-by":"publisher","first-page":"8406","DOI":"10.1021\/jo201624p","article-title":"Getting more out of a Job Plot: determination of reactant\nto product stoichiometry in cases of displacement reactions and n:n\ncomplex formation","volume":"76","author":"Olson","year":"2011","journal-title":"J. Org. Chem."},{"key":"2026081501073883600_cit47","doi-asserted-by":"publisher","first-page":"13891","DOI":"10.1021\/jacs.6b06001","article-title":"Coassembly of peptides\nderived from \u03b2-sheet regions\nof \u03b2-amyloid","volume":"138","author":"Truex","year":"2016","journal-title":"J. Am. Chem. Soc."},{"key":"2026081501073883600_cit48","doi-asserted-by":"publisher","first-page":"1746","DOI":"10.1021\/acs.joc.5b02909","article-title":"Recognizing the limited\napplicability of job plots in studying host-guest interactions in\nsupramolecular chemistry","volume":"81","author":"Ulatowski","year":"2016","journal-title":"J. Org. Chem."},{"key":"2026081501073883600_cit49","doi-asserted-by":"publisher","first-page":"159","DOI":"10.1124\/mol.55.1.159","article-title":"Aminotriarylmethane\ndyes are high-affinity noncompetitive\nantagonists of the nicotinic acetylcholine receptor","volume":"55","author":"Lurtz","year":"1999","journal-title":"Mol. Pharmacol."},{"key":"2026081501073883600_cit50","doi-asserted-by":"publisher","first-page":"2158","DOI":"10.1126\/science.1066020","article-title":"Structural mechanisms of QacR induction and multidrug\nrecognition","volume":"294","author":"Schumacher","year":"2001","journal-title":"Science"},{"key":"2026081501073883600_cit51","doi-asserted-by":"publisher","first-page":"2014","DOI":"10.1021\/bi051752e","article-title":"Molecular\nmechanisms and binding site location for the noncompetitive antagonist\ncrystal violet on nicotinic acetylcholine receptors","volume":"45","author":"Arias","year":"2006","journal-title":"Biochemistry"},{"key":"2026081501073883600_cit52","doi-asserted-by":"publisher","first-page":"2078","DOI":"10.1038\/ncomms3078","article-title":"The crystal structure of multidrug-resistance\nregulator RamR with multiple drugs","volume":"4","author":"Yamasaki","year":"2013","journal-title":"Nat. Commun."},{"key":"2026081501073883600_cit53","doi-asserted-by":"publisher","first-page":"1433","DOI":"10.3390\/molecules22091433","article-title":"An unusual\ndimeric inhibitor of acetylcholinesterase:\nCooperative binding of crystal violet","volume":"22","author":"Allgardsson","year":"2017","journal-title":"Molecules"},{"key":"2026081501073883600_cit54","doi-asserted-by":"publisher","first-page":"2785","DOI":"10.1002\/jcc.21256","article-title":"Autodock4\nand AutoDockTools4: automated\ndocking with selective receptor flexibility","volume":"30","author":"Morris","year":"2009","journal-title":"J. Comput. Chem."},{"key":"2026081501073883600_cit55","doi-asserted-by":"publisher","first-page":"5842","DOI":"10.1021\/jacs.8b02658","article-title":"Controlling\nthe oligomerization state of A\u03b2 -derived peptides with light","volume":"140","author":"Salveson","year":"2018","journal-title":"J. Am. Chem. Soc."},{"key":"2026081501073883600_cit56","doi-asserted-by":"publisher","first-page":"5430","DOI":"10.1039\/C8CC01733F","article-title":"Ring structure\nmodifications of phenylalanine 19 increase fibrillation kinetics and\nreduce toxicity of amyloid \u03b2 (1\u201340)","volume":"54","author":"Korn","year":"2018","journal-title":"Chem. Commun."},{"key":"2026081501073883600_cit57","doi-asserted-by":"publisher","first-page":"107","DOI":"10.1038\/290107a0","article-title":"Structure of the hydrophobic protein crambin determined\ndirectly from the anomalous scattering of sulphur","volume":"290","author":"Hendrickson","year":"1981","journal-title":"Nature"},{"key":"2026081501073883600_cit58","doi-asserted-by":"publisher","first-page":"707","DOI":"10.1107\/S0907444906014946","article-title":"In-house sulfur SAD phasing: a case study of the effects\nof data quality and resolution cutoffs","volume":"62","author":"Sarma","year":"2006","journal-title":"Acta\nCrystallogr., Sect. D: Biol. Crystallogr."},{"key":"2026081501073883600_cit59","doi-asserted-by":"publisher","first-page":"1033","DOI":"10.1126\/science.1218753","article-title":"Structures\nfrom anomalous diffraction of native biological macromolecules","volume":"336","author":"Liu","year":"2012","journal-title":"Science"},{"key":"2026081501073883600_cit60","doi-asserted-by":"publisher","first-page":"1314","DOI":"10.1107\/S0907444913001479","article-title":"Robust structural analysis of native\nbiological macromolecules from multi-crystal anomalous diffraction\ndata","volume":"69","author":"Liu","year":"2013","journal-title":"Acta Crystallogr., Sect. D: Biol. Crystallogr."},{"key":"2026081501073883600_cit61","doi-asserted-by":"publisher","first-page":"99","DOI":"10.1016\/j.sbi.2015.08.003","article-title":"Crystallographic\nphasing from weak anomalous signals","volume":"34","author":"Liu","year":"2015","journal-title":"Curr. Opin.\nStruct. Biol."},{"key":"2026081501073883600_cit62","doi-asserted-by":"publisher","first-page":"377","DOI":"10.1007\/978-1-4939-7000-1_16","article-title":"Contemporary\nuse of anomalous diffraction in biomolecular\nstructure analysis","volume":"1607","author":"Liu","year":"2017","journal-title":"Methods Mol. Biol."},{"key":"2026081501073883600_cit65","doi-asserted-by":"publisher","first-page":"3978","DOI":"10.1021\/acs.jpclett.6b01745","article-title":"Reversible\ninsulin hexamer assembly promoted by ethyl violet: pH-controlled uptake\nand release","volume":"7","author":"Mohanty","year":"2016","journal-title":"J. Phys. Chem. Lett."},{"key":"2026081501073883600_cit66","doi-asserted-by":"publisher","first-page":"1141","DOI":"10.1021\/acschemneuro.6b00108","article-title":"Oligomeric\namyloid-\u03b2 toxicity\ncan be inhibited by blocking its cellular binding in cortical neuronal\ncultures with addition of the triphenylmethane dye brilliant blue\nG","volume":"7","author":"Jana","year":"2016","journal-title":"ACS Chem. Neurosci."},{"key":"2026081501073883600_cit68","doi-asserted-by":"publisher","first-page":"645","DOI":"10.1021\/cn200056g","article-title":"A safe, blood-brain\nbarrier permeable triphenylmethane dye inhibits amyloid-\u03b2 neurotoxicity\nby generating nontoxic aggregates","volume":"2","author":"Wong","year":"2011","journal-title":"ACS Chem.\nNeurosci."},{"key":"2026081501073883600_cit69","doi-asserted-by":"publisher","first-page":"94","DOI":"10.1016\/j.neuroscience.2014.08.036","article-title":"Brilliant\nblue G improves cognition in an animal model of Alzheimer\u2019s\ndisease and inhibits amyloid-\u03b2-induced loss of filopodia and\ndendrite spines in hippocampal neurons","volume":"279","author":"Chen","year":"2014","journal-title":"Neuroscience"},{"key":"2026081501073883600_cit70","doi-asserted-by":"publisher","first-page":"663","DOI":"10.2174\/1567205013666160208142456","article-title":"Oral triphenymethane\nfood dye analog,\nbrilliant blue G, prevents neuronal loss in APPSwDI\/NOS2\u2013\/\u2013\nmouse model","volume":"13","author":"Irwin","year":"2016","journal-title":"Curr. Alzheimer Res."},{"key":"2026081501073883600_cit71","first-page":"336","article-title":"Methyl\ngreen as a differentiator and counterstain in the methyl violet technique\nfor the demonstration of amyloid","volume":"38","author":"Bancroft","year":"1983","journal-title":"Stain Technol."},{"key":"2026081501073883600_cit72","doi-asserted-by":"publisher","first-page":"7941","DOI":"10.1021\/cr200213s","article-title":"Fluorescent\ndyes and their supramolecular\nhost\/guest complexes with macrocycles in aqueous solution","volume":"111","author":"Dsouza","year":"2011","journal-title":"Chem. Rev."},{"key":"2026081501073883600_cit73","doi-asserted-by":"publisher","first-page":"7893","DOI":"10.1021\/cr500553d","article-title":"Chromogenic\/fluorogenic ensemble chemosensing systems","volume":"115","author":"Wu","year":"2015","journal-title":"Chem. Rev."},{"key":"2026081501073883600_cit74","doi-asserted-by":"publisher","first-page":"14716","DOI":"10.1021\/ja037994o","article-title":"Aptamers switch on fluorescence of\ntriphenylmethane dyes","volume":"125","author":"Babendure","year":"2003","journal-title":"J. Am. Chem. Soc."},{"key":"2026081501073883600_cit75","doi-asserted-by":"publisher","first-page":"4120","DOI":"10.1002\/anie.200604757","article-title":"Efficient fluorescence\nenhancement and cooperative binding of an organic dye in a supra-biomolecular\nhost-protein assembly","volume":"46","author":"Bhasikuttan","year":"2007","journal-title":"Angew. Chem., Int. Ed."},{"key":"2026081501073883600_cit76","doi-asserted-by":"publisher","first-page":"235","DOI":"10.1038\/nbt1368","article-title":"Fluorogen-activating\nsingle-chain antibodies for imaging\ncell surface proteins","volume":"26","author":"Szent-Gyorgyi","year":"2008","journal-title":"Nat. Biotechnol."},{"key":"2026081501073883600_cit77","doi-asserted-by":"publisher","first-page":"3583","DOI":"10.1021\/jacs.7b10724","article-title":"Direct selection\nof fluorescence-enhancing RNA aptamers","volume":"140","author":"Gotrik","year":"2018","journal-title":"J. Am.\nChem. Soc."}],"container-title":["Journal of the American Chemical Society"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/pubs.acs.org\/doi\/pdf\/10.1021\/jacs.8b06568","content-type":"application\/pdf","content-version":"vor","intended-application":"unspecified"},{"URL":"https:\/\/pubs.acs.org\/jacsat\/article-pdf\/140\/37\/11745\/15530468\/ja8b06568.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/pubs.acs.org\/jacsat\/article-pdf\/140\/37\/11745\/15530468\/ja8b06568.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,8,15]],"date-time":"2026-08-15T13:28:20Z","timestamp":1786800500000},"score":1,"resource":{"primary":{"URL":"https:\/\/pubs.acs.org\/jacsat\/article\/140\/37\/11745\/1465952\/Repurposing-Triphenylmethane-Dyes-to-Bind-to"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2018,8,20]]},"references-count":73,"journal-issue":{"issue":"37","published-online":{"date-parts":[[2018,8,20]]},"published-print":{"date-parts":[[2018,9,19]]}},"URL":"https:\/\/doi.org\/10.1021\/jacs.8b06568","relation":{},"ISSN":["0002-7863","1520-5126"],"issn-type":[{"value":"0002-7863","type":"print"},{"value":"1520-5126","type":"electronic"}],"subject":[],"published":{"date-parts":[[2018,8,20]]}}}