{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,24]],"date-time":"2026-09-24T06:11:25Z","timestamp":1790230285181,"version":"4.1.0"},"reference-count":70,"publisher":"Elsevier BV","issue":"7","license":[{"start":{"date-parts":[[2018,7,1]],"date-time":"2018-07-01T00:00:00Z","timestamp":1530403200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"}],"funder":[{"DOI":"10.13039\/501100003977","name":"Israel Science Foundation","doi-asserted-by":"publisher","award":["1130\/13"],"award-info":[{"award-number":["1130\/13"]}],"id":[{"id":"10.13039\/501100003977","id-type":"DOI","asserted-by":"publisher"}]},{"name":"Helmholtz Israel Program"},{"name":"Alliance Family Foundation"},{"DOI":"10.13039\/501100000833","name":"Rosetrees Trust","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100000833","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100011643","name":"Blavatnik Family Foundation","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100011643","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Biochimica et Biophysica Acta (BBA) - General Subjects"],"published-print":{"date-parts":[[2018,7]]},"DOI":"10.1016\/j.bbagen.2018.04.001","type":"journal-article","created":{"date-parts":[[2018,4,7]],"date-time":"2018-04-07T17:58:27Z","timestamp":1523123907000},"page":"1565-1575","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":38,"title":["Integrating in vitro and in silico approaches to evaluate the \u201cdual functionality\u201d of palmatine chloride in inhibiting and disassembling Tau-derived VQIVYK peptide fibrils"],"prefix":"10.1016","volume":"1862","author":[{"given":"Esraa","family":"Haj","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yelena","family":"Losev","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"V.","family":"Guru KrishnaKumar","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Edward","family":"Pichinuk","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hamutal","family":"Engel","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Avi","family":"Raveh","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ehud","family":"Gazit","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Daniel","family":"Segal","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.bbagen.2018.04.001_bb0005","doi-asserted-by":"crossref","first-page":"357","DOI":"10.1016\/j.it.2008.05.002","article-title":"Why neurodegenerative diseases are progressive: uncontrolled inflammation drives disease progression","volume":"29","author":"Gao","year":"2008","journal-title":"Trends Immunol."},{"key":"10.1016\/j.bbagen.2018.04.001_bb0010","doi-asserted-by":"crossref","first-page":"1579","DOI":"10.1586\/ern.11.155","article-title":"Distinguishing Alzheimer's disease from other major forms of dementia","volume":"11","author":"Karantzoulis","year":"2011","journal-title":"Expert. Rev. Neurother."},{"key":"10.1016\/j.bbagen.2018.04.001_bb0015","doi-asserted-by":"crossref","first-page":"1121","DOI":"10.1146\/annurev.neuro.24.1.1121","article-title":"Neurodegenerative tauopathies","volume":"24","author":"Lee","year":"2001","journal-title":"Annu. Rev. Neurosci."},{"key":"10.1016\/j.bbagen.2018.04.001_bb0020","doi-asserted-by":"crossref","first-page":"91","DOI":"10.1016\/0002-9343(86)90188-9","article-title":"Alzheimer's disease","volume":"81","author":"Kwentus","year":"2017","journal-title":"Am. J. Med."},{"key":"10.1016\/j.bbagen.2018.04.001_bb0025","doi-asserted-by":"crossref","first-page":"181","DOI":"10.1016\/j.neuron.2004.09.010","article-title":"Deciphering the molecular basis of memory failure in Alzheimer's disease","volume":"44","author":"Walsh","year":"2004","journal-title":"Neuron"},{"key":"10.1016\/j.bbagen.2018.04.001_bb0030","doi-asserted-by":"crossref","first-page":"505","DOI":"10.1001\/jamaneurol.2013.5847","article-title":"Amyloid-beta and tau: the trigger and bullet in Alzheimer disease pathogenesis","volume":"71","author":"Bloom","year":"2014","journal-title":"JAMA Neurol."},{"key":"10.1016\/j.bbagen.2018.04.001_bb0035","doi-asserted-by":"crossref","first-page":"421","DOI":"10.1038\/gim.2015.117","article-title":"The genetic landscape of Alzheimer disease: clinical implications and perspectives","volume":"18","author":"Van Cauwenberghe","year":"2016","journal-title":"Genet. Med."},{"key":"10.1016\/j.bbagen.2018.04.001_bb0040","doi-asserted-by":"crossref","first-page":"39","DOI":"10.1111\/j.1750-3639.1993.tb00724.x","article-title":"The molecular and cellular biology of tau","volume":"3","author":"Kosik","year":"1993","journal-title":"Brain Pathol."},{"key":"10.1016\/j.bbagen.2018.04.001_bb0045","doi-asserted-by":"crossref","first-page":"22","DOI":"10.1038\/nrn.2015.1","article-title":"Tau in physiology and pathology","volume":"17","author":"Wang","year":"2016","journal-title":"Nat. Rev. Neurosci."},{"key":"10.1016\/j.bbagen.2018.04.001_bb0050","doi-asserted-by":"crossref","first-page":"4671","DOI":"10.3390\/ijms15034671","article-title":"Tau protein modifications and interactions: their role in function and dysfunction","volume":"15","author":"Mietelska-Porowska","year":"2014","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.bbagen.2018.04.001_bb0055","doi-asserted-by":"crossref","first-page":"361","DOI":"10.1152\/physrev.00024.2003","article-title":"Role of tau protein in both physiological and pathological conditions","volume":"84","author":"Avila","year":"2004","journal-title":"Physiol. Rev."},{"key":"10.1016\/j.bbagen.2018.04.001_bb0060","doi-asserted-by":"crossref","first-page":"1858","DOI":"10.1073\/pnas.72.5.1858","article-title":"A protein factor essential for microtubule assembly","volume":"72","author":"Weingarten","year":"1975","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbagen.2018.04.001_bb0065","doi-asserted-by":"crossref","first-page":"631","DOI":"10.1212\/WNL.42.3.631","article-title":"Neurofibrillary tangles but not senile plaques parallel duration and severity of Alzheimer's disease","volume":"42","author":"Arriagada","year":"1992","journal-title":"Neurology"},{"key":"10.1016\/j.bbagen.2018.04.001_bb0070","doi-asserted-by":"crossref","first-page":"304","DOI":"10.1016\/j.expneurol.2009.08.031","article-title":"Tau-directed drug discovery for Alzheimer's disease and related tauopathies: a focus on tau assembly inhibitors","volume":"223","author":"Brunden","year":"2010","journal-title":"Exp. Neurol."},{"key":"10.1016\/j.bbagen.2018.04.001_bb0075","first-page":"731526","article-title":"Structure and pathology of tau protein in Alzheimer disease","volume":"2012","author":"Kolarova","year":"2012","journal-title":"Int. J. Alzheimers Dis."},{"key":"10.1016\/j.bbagen.2018.04.001_bb0080","doi-asserted-by":"crossref","first-page":"5945","DOI":"10.1002\/chem.201504950","article-title":"Selective inhibition of aggregation and toxicity of a tau-derived peptide using its glycosylated analogues","volume":"22","author":"Frenkel-Pinter","year":"2016","journal-title":"Chem. Eur. J."},{"key":"10.1016\/j.bbagen.2018.04.001_bb0085","doi-asserted-by":"crossref","first-page":"6923","DOI":"10.1073\/pnas.121119298","article-title":"Hyperphosphorylation induces self-assembly of tau into tangles of paired helical filaments\/straight filaments","volume":"98","author":"Alonso","year":"2001","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbagen.2018.04.001_bb0090","doi-asserted-by":"crossref","first-page":"1694","DOI":"10.1021\/bi0357006","article-title":"Tau paired helical filaments from Alzheimer's disease brain and assembled in vitro are based on beta-structure in the core domain","volume":"43","author":"Barghorn","year":"2004","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbagen.2018.04.001_bb0095","doi-asserted-by":"crossref","first-page":"4842","DOI":"10.1016\/j.febslet.2006.07.078","article-title":"Extracellular tau is toxic to neuronal cells","volume":"580","author":"G\u00f3mez-Ramos","year":"2006","journal-title":"FEBS Lett."},{"key":"10.1016\/j.bbagen.2018.04.001_bb0100","doi-asserted-by":"crossref","first-page":"464","DOI":"10.3389\/fncel.2015.00464","article-title":"Tau oligomers: the toxic player at synapses in Alzheimer's disease","volume":"9","author":"Guerrero-Mu\u00f1oz","year":"2015","journal-title":"Front. Cell. Neurosci."},{"key":"10.1016\/j.bbagen.2018.04.001_bb0105","doi-asserted-by":"crossref","first-page":"3628","DOI":"10.1074\/jbc.M410984200","article-title":"Anthraquinones inhibit tau aggregation and dissolve Alzheimer's paired helical filaments in vitro and in cells","volume":"280","author":"Pickhardt","year":"2005","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbagen.2018.04.001_bb0110","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.bbrc.2007.03.056","article-title":"High throughput screening for small molecule inhibitors of heparin-induced tau fibril formation","volume":"358","author":"Crowe","year":"2007","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.bbagen.2018.04.001_bb0115","doi-asserted-by":"crossref","first-page":"7732","DOI":"10.1021\/bi9006435","article-title":"Identification of aminothienopyridazine inhibitors of tau assembly by quantitative high-throughput screening","volume":"48","author":"Crowe","year":"2009","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbagen.2018.04.001_bb0120","doi-asserted-by":"crossref","first-page":"814","DOI":"10.2174\/156720501209151019104951","article-title":"Identification of small molecule inhibitors of tau aggregation by targeting monomeric tau as a potential therapeutic approach for tauopathies","volume":"12","author":"Pickhardt","year":"2015","journal-title":"Curr. Alzheimer Res."},{"key":"10.1016\/j.bbagen.2018.04.001_bb0125","doi-asserted-by":"crossref","first-page":"48165","DOI":"10.1074\/jbc.M105196200","article-title":"Mutations of tau protein in frontotemporal dementia promote aggregation of paired helical filaments by enhancing local beta-structure","volume":"276","author":"von Bergen","year":"2001","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbagen.2018.04.001_bb0130","doi-asserted-by":"crossref","first-page":"26846","DOI":"10.1074\/jbc.M403129200","article-title":"The flavonoid baicalein inhibits fibrillation of alpha-synuclein and disaggregates existing fibrils","volume":"279","author":"Zhu","year":"2004","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbagen.2018.04.001_bb0135","doi-asserted-by":"crossref","first-page":"743","DOI":"10.1021\/acschemneuro.6b00433","article-title":"The polyphenol altenusin inhibits in vitro fibrillization of tau and reduces induced tau pathology in primary neurons","volume":"8","author":"Chua","year":"2017","journal-title":"ACS Chem. Neurosci."},{"key":"10.1016\/j.bbagen.2018.04.001_bb0140","doi-asserted-by":"crossref","first-page":"1774","DOI":"10.1529\/biophysj.105.070136","article-title":"Structure of core domain of fibril-forming PHF\/Tau fragments","volume":"90","author":"Inouye","year":"2006","journal-title":"Biophys. J."},{"key":"10.1016\/j.bbagen.2018.04.001_bb0145","doi-asserted-by":"crossref","first-page":"4582","DOI":"10.1021\/acs.jpcb.5b00175","article-title":"Tau assembly: the dominant role of PHF6 (VQIVYK) in microtubule binding region repeat R3","volume":"119","author":"Ganguly","year":"2015","journal-title":"J. Phys. Chem. B"},{"key":"10.1016\/j.bbagen.2018.04.001_bb0150","doi-asserted-by":"crossref","first-page":"26868","DOI":"10.1074\/jbc.M402379200","article-title":"The formation of straight and twisted filaments from short tau peptides","volume":"279","author":"Goux","year":"2004","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbagen.2018.04.001_bb0155","doi-asserted-by":"crossref","first-page":"1758","DOI":"10.1021\/ja909690a","article-title":"The importance of hydrogen bonding between the glutamine side chains to the formation of amyloid VQIVYK parallel beta-sheets: an ONIOM DFT\/AM1 study","volume":"132","author":"Plumley","year":"2010","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.bbagen.2018.04.001_bb0160","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pcbi.1000238","article-title":"Formation and growth of oligomers: a monte carlo study of an amyloid tau fragment","volume":"4","author":"Li","year":"2008","journal-title":"PLoS Comput. Biol."},{"key":"10.1016\/j.bbagen.2018.04.001_bb0165","doi-asserted-by":"crossref","first-page":"5129","DOI":"10.1073\/pnas.97.10.5129","article-title":"Assembly of tau protein into Alzheimer paired helical filaments depends on a local sequence motif ((306)VQIVYK(311)) forming beta structure","volume":"97","author":"von Bergen","year":"2000","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbagen.2018.04.001_bb0170","doi-asserted-by":"crossref","first-page":"1559","DOI":"10.1021\/cn400151a","article-title":"Tau-derived-hexapeptide (306)VQIVYK(311) aggregation inhibitors: Nitrocatechol moiety as a pharmacophore in drug design","volume":"4","author":"Mohamed","year":"2013","journal-title":"ACS Chem. Neurosci."},{"key":"10.1016\/j.bbagen.2018.04.001_bb0175","doi-asserted-by":"crossref","first-page":"73","DOI":"10.1159\/000448518","article-title":"Cl-NQTrp alleviates tauopathy symptoms in a model organism through the inhibition of tau aggregation-engendered toxicity","volume":"17","author":"Frenkel-Pinter","year":"2017","journal-title":"Neurodegener. Dis."},{"key":"10.1016\/j.bbagen.2018.04.001_bb0180","doi-asserted-by":"crossref","first-page":"165","DOI":"10.3233\/JAD-150927","article-title":"Naphthoquinone-tryptophan hybrid inhibits aggregation of the tau-derived peptide PHF6 and reduces neurotoxicity","volume":"51","author":"Frenkel-Pinter","year":"2016","journal-title":"J. Alzheimers Dis."},{"key":"10.1016\/j.bbagen.2018.04.001_bb0185","doi-asserted-by":"crossref","first-page":"71","DOI":"10.1038\/s41598-017-18443-2","article-title":"Mechanistic insights into remodeled tau-derived PHF6 peptide fibrils by Naphthoquinone-tryptophan hybrids","volume":"8","author":"KrishnaKumar","year":"2018","journal-title":"Sci. Rep."},{"key":"10.1016\/j.bbagen.2018.04.001_bb0190","doi-asserted-by":"crossref","first-page":"530","DOI":"10.1080\/10826068.2016.1275012","article-title":"Simplified method to obtain enhanced expression of tau protein from E. coli and one-step purification by direct boiling","volume":"47","author":"KrishnaKumar","year":"2017","journal-title":"Prep. Biochem. Biotechnol."},{"key":"10.1016\/j.bbagen.2018.04.001_bb0195","doi-asserted-by":"crossref","first-page":"221","DOI":"10.1007\/s10822-013-9644-8","article-title":"Protein and ligand preparation: parameters, protocols, and influence on virtual screening enrichments","volume":"27","author":"Sastry","year":"2013","journal-title":"J. Comput. Aided Mol. Des."},{"key":"10.1016\/j.bbagen.2018.04.001_bb0200","doi-asserted-by":"crossref","first-page":"1739","DOI":"10.1021\/jm0306430","article-title":"Glide: a new approach for rapid, accurate docking and scoring. 1. Method and assessment of docking accuracy","volume":"47","author":"Friesner","year":"2004","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.bbagen.2018.04.001_bb0205","doi-asserted-by":"crossref","first-page":"6177","DOI":"10.1021\/jm051256o","article-title":"Extra precision glide: docking and scoring incorporating a model of hydrophobic enclosure for protein-ligand complexes","volume":"49","author":"Friesner","year":"2006","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.bbagen.2018.04.001_bb0210","doi-asserted-by":"crossref","first-page":"1750","DOI":"10.1021\/jm030644s","article-title":"Glide: a new approach for rapid, accurate docking and scoring. 2. Enrichment factors in database screening","volume":"47","author":"Halgren","year":"2004","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.bbagen.2018.04.001_bb0215","doi-asserted-by":"crossref","first-page":"597","DOI":"10.1016\/S0022-2836(02)00470-9","article-title":"On the role of the crystal environment in determining protein side-chain conformations","volume":"320","author":"Jacobson","year":"2002","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.bbagen.2018.04.001_bb0220","doi-asserted-by":"crossref","first-page":"351","DOI":"10.1002\/prot.10613","article-title":"A hierarchical approach to all-atom protein loop prediction","volume":"55","author":"Jacobson","year":"2004","journal-title":"Proteins"},{"key":"10.1016\/j.bbagen.2018.04.001_bb0225","doi-asserted-by":"crossref","first-page":"3160","DOI":"10.1016\/j.bmc.2005.12.032","article-title":"New insights about HERG blockade obtained from protein modeling, potential energy mapping, and docking studies","volume":"14","author":"Farid","year":"2006","journal-title":"Bioorg. Med. Chem."},{"key":"10.1016\/j.bbagen.2018.04.001_bb0230","doi-asserted-by":"crossref","first-page":"83","DOI":"10.1111\/j.1747-0285.2005.00327.x","article-title":"Use of an induced fit receptor structure in virtual screening","volume":"67","author":"Sherman","year":"2006","journal-title":"Chem. Biol. Drug Des."},{"key":"10.1016\/j.bbagen.2018.04.001_bb0235","doi-asserted-by":"crossref","first-page":"534","DOI":"10.1021\/jm050540c","article-title":"Novel procedure for modeling ligand\/receptor induced fit effects","volume":"49","author":"Sherman","year":"2006","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.bbagen.2018.04.001_bb0240","doi-asserted-by":"crossref","first-page":"453","DOI":"10.1038\/nature05695","article-title":"Atomic structures of amyloid cross-[beta] spines reveal varied steric zippers","volume":"447","author":"Sawaya","year":"2007","journal-title":"Nature"},{"key":"10.1016\/j.bbagen.2018.04.001_bb0245","doi-asserted-by":"crossref","first-page":"1355","DOI":"10.1107\/S0907444904011679","article-title":"PRODRG: a tool for high-throughput crystallography of protein-ligand complexes","volume":"60","author":"Schuttelkopf","year":"2004","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"10.1016\/j.bbagen.2018.04.001_bb0250","doi-asserted-by":"crossref","first-page":"843","DOI":"10.1007\/s00249-011-0700-9","article-title":"Definition and testing of the GROMOS force-field versions 54A7 and 54B7","volume":"40","author":"Schmid","year":"2011","journal-title":"Eur. Biophys. J."},{"key":"10.1016\/j.bbagen.2018.04.001_bb0255","doi-asserted-by":"crossref","first-page":"306","DOI":"10.1007\/s008940100045","article-title":"GROMACS 3.0: a package for molecular simulation and trajectory analysis","volume":"7","author":"Lindahl","year":"2001","journal-title":"Mol. Model. Annu."},{"key":"10.1016\/j.bbagen.2018.04.001_bb0260","doi-asserted-by":"crossref","first-page":"1817","DOI":"10.1080\/07391102.2013.838518","article-title":"Comparing atomistic molecular mechanics force fields for a difficult target: a case study on the Alzheimer's amyloid beta-peptide","volume":"32","author":"Gerben","year":"2014","journal-title":"J. Biomol. Struct. Dyn."},{"key":"10.1016\/j.bbagen.2018.04.001_bb0265","doi-asserted-by":"crossref","first-page":"1463","DOI":"10.1002\/(SICI)1096-987X(199709)18:12<1463::AID-JCC4>3.0.CO;2-H","article-title":"LINCS: a linear constraint solver for molecular simulations","volume":"18","author":"Hess","year":"1997","journal-title":"J. Comput. Chem."},{"key":"10.1016\/j.bbagen.2018.04.001_bb0270","doi-asserted-by":"crossref","first-page":"3144","DOI":"10.1021\/ja110545h","article-title":"Macrocyclic beta-sheet peptides that inhibit the aggregation of a tau-protein-derived hexapeptide","volume":"133","author":"Zheng","year":"2011","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.bbagen.2018.04.001_bb0275","doi-asserted-by":"crossref","first-page":"229","DOI":"10.1016\/j.jsb.2005.06.006","article-title":"Mechanism of thioflavin T binding to amyloid fibrils","volume":"151","author":"Khurana","year":"2005","journal-title":"J. Struct. Biol."},{"key":"10.1016\/j.bbagen.2018.04.001_bb0280","doi-asserted-by":"crossref","first-page":"1123","DOI":"10.1021\/ci900384c","article-title":"Insights for predicting blood-brain barrier penetration of CNS targeted molecules using QSPR approaches","volume":"50","author":"Fan","year":"2010","journal-title":"J. Chem. Inf. Model."},{"key":"10.1016\/j.bbagen.2018.04.001_bb0285","doi-asserted-by":"crossref","first-page":"11213","DOI":"10.1073\/pnas.93.20.11213","article-title":"Selective inhibition of Alzheimer disease-like tau aggregation by phenothiazines","volume":"93","author":"Wischik","year":"1996","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbagen.2018.04.001_bb0290","doi-asserted-by":"crossref","first-page":"7614","DOI":"10.1074\/jbc.M408714200","article-title":"Inhibition of heparin-induced tau filament formation by phenothiazines, polyphenols, and porphyrins","volume":"280","author":"Taniguchi","year":"2005","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbagen.2018.04.001_bb0295","doi-asserted-by":"crossref","DOI":"10.1016\/j.neurobiolaging.2010.12.012","article-title":"Lest we forget you\u2014methylene blue\u2026","volume":"32","author":"Schirmer","year":"2011","journal-title":"Neurobiol. Aging"},{"key":"10.1016\/j.bbagen.2018.04.001_bb0300","doi-asserted-by":"crossref","first-page":"656","DOI":"10.2174\/156720510793611592","article-title":"Tau in Alzheimer disease and related tauopathies","volume":"7","author":"Iqbal","year":"2010","journal-title":"Curr. Alzheimer Res."},{"key":"10.1016\/j.bbagen.2018.04.001_bb0305","doi-asserted-by":"crossref","first-page":"2657","DOI":"10.1016\/j.febslet.2007.05.009","article-title":"Phosphorylation of human microtubule-associated protein tau by protein kinases of the AGC subfamily","volume":"581","author":"Virdee","year":"2007","journal-title":"FEBS Lett."},{"key":"10.1016\/j.bbagen.2018.04.001_bb0310","doi-asserted-by":"crossref","first-page":"95","DOI":"10.1016\/S0165-0173(00)00019-9","article-title":"Tau protein isoforms, phosphorylation and role in neurodegenerative disorders","volume":"33","author":"Buee","year":"2000","journal-title":"Brain Res. Brain Res. Rev."},{"key":"10.1016\/j.bbagen.2018.04.001_bb0315","doi-asserted-by":"crossref","first-page":"1399","DOI":"10.1080\/07391102.2014.951689","article-title":"Atomistic mechanism of polyphenol amyloid aggregation inhibitors: molecular dynamics study of Curcumin, Exifone, and Myricetin interaction with the segment of tau peptide oligomer","volume":"33","author":"Berhanu","year":"2015","journal-title":"J. Biomol. Struct. Dyn."},{"key":"10.1016\/j.bbagen.2018.04.001_bb0320","doi-asserted-by":"crossref","first-page":"1013","DOI":"10.1080\/08927022.2010.499147","article-title":"Molecular dynamics simulations to investigate the stability and aggregation behaviour of the amyloid-forming peptide VQIVYK from tau protein","volume":"36","author":"Zhao","year":"2010","journal-title":"Mol. Simul."},{"key":"10.1016\/j.bbagen.2018.04.001_bb0325","doi-asserted-by":"crossref","first-page":"3469","DOI":"10.1073\/pnas.0912654107","article-title":"Minimalist design of water-soluble cross-beta architecture","volume":"107","author":"Biancalana","year":"2010","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbagen.2018.04.001_bb0330","doi-asserted-by":"crossref","first-page":"390","DOI":"10.1016\/j.jmb.2012.02.004","article-title":"Driving forces and structural determinants of steric zipper peptide oligomer formation elucidated by atomistic simulations","volume":"421","author":"Matthes","year":"2012","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.bbagen.2018.04.001_bb0335","doi-asserted-by":"crossref","first-page":"185","DOI":"10.1038\/nature23002","article-title":"Cryo-EM structures of tau filaments from Alzheimer's disease","volume":"547","author":"Fitzpatrick","year":"2017","journal-title":"Nature"},{"key":"10.1016\/j.bbagen.2018.04.001_bb0340","first-page":"35","article-title":"Pharmacological activities palmatine alkaloid compound isolated from Guatteria friesiana prospects for new drug development","volume":"6","author":"Kaline","year":"2017","journal-title":"Asian J. Biomed. Pharm. Sci."},{"key":"10.1016\/j.bbagen.2018.04.001_bb0345","doi-asserted-by":"crossref","DOI":"10.3390\/molecules21091161","article-title":"Extracts from traditional Chinese medicinal plants inhibit acetylcholinesterase, a known Alzheimer's disease target","volume":"21","author":"Kaufmann","year":"2016","journal-title":"Molecules"},{"key":"10.1016\/j.bbagen.2018.04.001_bb0350","doi-asserted-by":"crossref","first-page":"6","DOI":"10.1016\/j.jpba.2013.12.037","article-title":"Simultaneous determination of four alkaloids in mice plasma and brain by LC-MS\/MS for pharmacokinetic studies after administration of Corydalis Rhizoma and Yuanhu Zhitong extracts","volume":"92","author":"Gao","year":"2014","journal-title":"J. Pharm. Biomed. Anal."}],"container-title":["Biochimica et Biophysica Acta (BBA) - General Subjects"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0304416518300941?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0304416518300941?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2018,8,22]],"date-time":"2018-08-22T16:51:59Z","timestamp":1534956719000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0304416518300941"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2018,7]]},"references-count":70,"journal-issue":{"issue":"7","published-print":{"date-parts":[[2018,7]]}},"alternative-id":["S0304416518300941"],"URL":"https:\/\/doi.org\/10.1016\/j.bbagen.2018.04.001","relation":{},"ISSN":["0304-4165"],"issn-type":[{"value":"0304-4165","type":"print"}],"subject":[],"published":{"date-parts":[[2018,7]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Integrating in vitro and in silico approaches to evaluate the \u201cdual functionality\u201d of palmatine chloride in inhibiting and disassembling Tau-derived VQIVYK peptide fibrils","name":"articletitle","label":"Article Title"},{"value":"Biochimica et Biophysica Acta (BBA) - General Subjects","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.bbagen.2018.04.001","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2018 Elsevier B.V. All rights reserved.","name":"copyright","label":"Copyright"}]}}