{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,2,13]],"date-time":"2026-02-13T07:45:56Z","timestamp":1770968756230,"version":"3.50.1"},"reference-count":81,"publisher":"Elsevier BV","issue":"4","license":[{"start":{"date-parts":[[2017,8,1]],"date-time":"2017-08-01T00:00:00Z","timestamp":1501545600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2017,8,1]],"date-time":"2017-08-01T00:00:00Z","timestamp":1501545600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2018,8,22]],"date-time":"2018-08-22T00:00:00Z","timestamp":1534896000000},"content-version":"vor","delay-in-days":386,"URL":"http:\/\/www.elsevier.com\/open-access\/userlicense\/1.0\/"}],"funder":[{"name":"TIFR-DAE"},{"name":"CSIR-SPM-SRF fellowship"},{"name":"DST-INSPIRE fellowship"}],"content-domain":{"domain":["cell.com","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Biophysical Journal"],"published-print":{"date-parts":[[2017,8]]},"DOI":"10.1016\/j.bpj.2017.06.068","type":"journal-article","created":{"date-parts":[[2017,8,22]],"date-time":"2017-08-22T12:00:35Z","timestamp":1503403235000},"page":"805-816","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":39,"title":["Major Reaction Coordinates Linking Transient Amyloid-\u03b2 Oligomers to Fibrils Measured at Atomic Level"],"prefix":"10.1016","volume":"113","author":[{"given":"Bappaditya","family":"Chandra","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Debanjan","family":"Bhowmik","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Barun Kumar","family":"Maity","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Kaustubh R.","family":"Mote","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Debabrata","family":"Dhara","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ravindra","family":"Venkatramani","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Sudipta","family":"Maiti","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Perunthiruthy K.","family":"Madhu","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1016\/j.bpj.2017.06.068_bib1","doi-asserted-by":"crossref","first-page":"291","DOI":"10.1038\/418291a","article-title":"Neurodegenerative disease: amyloid pores from pathogenic mutations","volume":"418","author":"Lashuel","year":"2002","journal-title":"Nature"},{"key":"10.1016\/j.bpj.2017.06.068_bib2","doi-asserted-by":"crossref","first-page":"333","DOI":"10.1146\/annurev.biochem.75.101304.123901","article-title":"Protein misfolding, functional amyloid, and human disease","volume":"75","author":"Chiti","year":"2006","journal-title":"Annu. Rev. Biochem."},{"key":"10.1016\/j.bpj.2017.06.068_bib3","doi-asserted-by":"crossref","first-page":"535","DOI":"10.1038\/416535a","article-title":"Naturally secreted oligomers of amyloid \u03b2 protein potently inhibit hippocampal long-term potentiation in\u00a0vivo","volume":"416","author":"Walsh","year":"2002","journal-title":"Nature"},{"key":"10.1016\/j.bpj.2017.06.068_bib4","doi-asserted-by":"crossref","first-page":"885","DOI":"10.1016\/S0006-291X(84)80190-4","article-title":"Alzheimer\u2019s disease: initial report of the purification and characterization of a novel cerebrovascular amyloid protein","volume":"120","author":"Glenner","year":"1984","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.bpj.2017.06.068_bib5","doi-asserted-by":"crossref","first-page":"4245","DOI":"10.1073\/pnas.82.12.4245","article-title":"Amyloid plaque core protein in Alzheimer disease and Down syndrome","volume":"82","author":"Masters","year":"1985","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.bpj.2017.06.068_bib6","doi-asserted-by":"crossref","first-page":"6888","DOI":"10.1002\/anie.201402636","article-title":"Significant structural differences between transient amyloid-\u03b2 oligomers and less-toxic fibrils in\u00a0regions known to harbor familial Alzheimer\u2019s mutations","volume":"53","author":"Sarkar","year":"2014","journal-title":"Angew. Chem. Int. Ed. Engl."},{"key":"10.1016\/j.bpj.2017.06.068_bib7","doi-asserted-by":"crossref","first-page":"8294","DOI":"10.1021\/jacs.5b04843","article-title":"Successive stages of amyloid-\u03b2 self-assembly characterized by solid-state nuclear magnetic resonance with dynamic nuclear polarization","volume":"137","author":"Potapov","year":"2015","journal-title":"J.\u00a0Am. Chem. Soc."},{"key":"10.1016\/j.bpj.2017.06.068_bib8","doi-asserted-by":"crossref","first-page":"9","DOI":"10.1186\/alzrt107","article-title":"Molecular consequences of amyloid precursor protein and presenilin mutations causing autosomal-dominant Alzheimer\u2019s disease","volume":"4","author":"Weggen","year":"2012","journal-title":"Alzheimers Res. Ther."},{"key":"10.1016\/j.bpj.2017.06.068_bib9","doi-asserted-by":"crossref","first-page":"18349","DOI":"10.1073\/pnas.0806270105","article-title":"Molecular structural basis for polymorphism in Alzheimer\u2019s \u03b2-amyloid fibrils","volume":"105","author":"Paravastu","year":"2008","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.bpj.2017.06.068_bib10","doi-asserted-by":"crossref","first-page":"1257","DOI":"10.1016\/j.cell.2013.08.035","article-title":"Molecular structure of \u03b2-amyloid fibrils in Alzheimer\u2019s disease brain tissue","volume":"154","author":"Lu","year":"2013","journal-title":"Cell"},{"key":"10.1016\/j.bpj.2017.06.068_bib11","doi-asserted-by":"crossref","first-page":"E4976","DOI":"10.1073\/pnas.1600749113","article-title":"Atomic-resolution structure of a disease-relevant A\u03b2 (1\u201342) amyloid fibril","volume":"113","author":"W\u00e4lti","year":"2016","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.bpj.2017.06.068_bib12","doi-asserted-by":"crossref","first-page":"9663","DOI":"10.1021\/jacs.6b05129","article-title":"Atomic resolution structure of monomorphic A\u03b242 amyloid fibrils","volume":"138","author":"Colvin","year":"2016","journal-title":"J.\u00a0Am. Chem. Soc."},{"key":"10.1016\/j.bpj.2017.06.068_bib13","doi-asserted-by":"crossref","first-page":"499","DOI":"10.1038\/nsmb.2991","article-title":"A\u03b2 (1\u201342) fibril structure illuminates self-recognition and replication of amyloid in Alzheimer\u2019s disease","volume":"22","author":"Xiao","year":"2015","journal-title":"Nat. Struct. Mol. Biol."},{"key":"10.1016\/j.bpj.2017.06.068_bib14","doi-asserted-by":"crossref","first-page":"498","DOI":"10.1021\/bi051952q","article-title":"Experimental constraints on quaternary structure in Alzheimer\u2019s \u03b2-amyloid fibrils","volume":"45","author":"Petkova","year":"2006","journal-title":"Biochemistry"},{"key":"10.1016\/j.bpj.2017.06.068_bib15","doi-asserted-by":"crossref","first-page":"1290","DOI":"10.1021\/acschemneuro.5b00074","article-title":"An early folding contact between Phe19 and Leu34 is critical for amyloid-\u03b2 oligomer toxicity","volume":"6","author":"Das","year":"2015","journal-title":"ACS Chem. Neurosci."},{"key":"10.1016\/j.bpj.2017.06.068_bib16","doi-asserted-by":"crossref","first-page":"1835","DOI":"10.1021\/acs.jpcb.6b12332","article-title":"Stereoisomers probe steric zippers in amyloid-\u03b2","volume":"121","author":"Chandra","year":"2017","journal-title":"J.\u00a0Phys. Chem. B"},{"key":"10.1016\/j.bpj.2017.06.068_bib17","doi-asserted-by":"crossref","first-page":"51","DOI":"10.1016\/j.cplett.2017.02.070","article-title":"Emerging structural details of transient amyloid-\u03b2 oligomers suggest designs for effective small molecule modulators","volume":"675","author":"Chandra","year":"2017","journal-title":"Chem. Phys. Lett."},{"key":"10.1016\/j.bpj.2017.06.068_bib18","doi-asserted-by":"crossref","first-page":"997","DOI":"10.1039\/c2mb25457c","article-title":"Structural heterogeneity in\u00a0familial Alzheimer\u2019s disease mutants of amyloid-\u03b2 peptides","volume":"9","author":"Chong","year":"2013","journal-title":"Mol. Biosyst."},{"key":"10.1016\/j.bpj.2017.06.068_bib19","doi-asserted-by":"crossref","first-page":"1003","DOI":"10.1006\/bbrc.2000.3051","article-title":"Oligomerization and toxicity of \u03b2-amyloid-42 implicated in Alzheimer\u2019s disease","volume":"273","author":"El-Agnaf","year":"2000","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.bpj.2017.06.068_bib20","doi-asserted-by":"crossref","first-page":"314","DOI":"10.1111\/j.1749-6632.1999.tb07845.x","article-title":"Neurotoxicity and oxidative damage of \u03b2 amyloid 1\u201342 versus \u03b2 amyloid 1\u201340 in the mouse cerebral cortex","volume":"893","author":"Klein","year":"1999","journal-title":"Ann. N. Y. Acad. Sci."},{"key":"10.1016\/j.bpj.2017.06.068_bib21","doi-asserted-by":"crossref","first-page":"519","DOI":"10.1083\/jcb.200110119","article-title":"Selective cytotoxicity of intracellular amyloid \u03b2 peptide1\u201342 through p53 and Bax in cultured primary human neurons","volume":"156","author":"Zhang","year":"2002","journal-title":"J.\u00a0Cell Biol."},{"key":"10.1016\/j.bpj.2017.06.068_bib22","doi-asserted-by":"crossref","first-page":"1597","DOI":"10.1016\/j.bpj.2017.02.043","article-title":"Curcumin dictates divergent fates for the central salt bridges in amyloid-\u03b240 and amyloid-\u03b242","volume":"112","author":"Chandra","year":"2017","journal-title":"Biophys.\u00a0J."},{"key":"10.1016\/j.bpj.2017.06.068_bib23","doi-asserted-by":"crossref","first-page":"7717","DOI":"10.1073\/pnas.1203193109","article-title":"Toxic fibrillar oligomers of amyloid-\u03b2 have cross-\u03b2 structure","volume":"109","author":"Stroud","year":"2012","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.bpj.2017.06.068_bib24","doi-asserted-by":"crossref","first-page":"13472","DOI":"10.1021\/ja054039l","article-title":"Capturing intermediate structures of Alzheimer\u2019s \u03b2-amyloid, A\u03b2 (1\u201340), by solid-state NMR spectroscopy","volume":"127","author":"Chimon","year":"2005","journal-title":"J.\u00a0Am. Chem. Soc."},{"key":"10.1016\/j.bpj.2017.06.068_bib25","doi-asserted-by":"crossref","first-page":"561","DOI":"10.1038\/nsmb.1799","article-title":"Structural conversion of\u00a0neurotoxic amyloid-\u03b2 (1\u201342) oligomers to fibrils","volume":"17","author":"Ahmed","year":"2010","journal-title":"Nat. Struct. Mol. Biol."},{"key":"10.1016\/j.bpj.2017.06.068_bib26","doi-asserted-by":"crossref","first-page":"5099","DOI":"10.1073\/pnas.0711731105","article-title":"Stabilization of a \u03b2-hairpin in monomeric Alzheimer\u2019s amyloid-\u03b2 peptide inhibits amyloid formation","volume":"105","author":"Hoyer","year":"2008","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.bpj.2017.06.068_bib27","doi-asserted-by":"crossref","first-page":"12756","DOI":"10.1002\/anie.201406357","article-title":"A hexameric peptide barrel\u00a0as building block of amyloid-\u03b2 protofibrils","volume":"53","author":"Lendel","year":"2014","journal-title":"Angew. Chem. Int. Ed. Engl."},{"key":"10.1016\/j.bpj.2017.06.068_bib28","doi-asserted-by":"crossref","first-page":"1157","DOI":"10.1038\/nsmb1345","article-title":"Evidence of fibril-like \u03b2-sheet structures in a neurotoxic amyloid intermediate of Alzheimer\u2019s \u03b2-amyloid","volume":"14","author":"Chimon","year":"2007","journal-title":"Nat. Struct. Mol. Biol."},{"key":"10.1016\/j.bpj.2017.06.068_bib29","doi-asserted-by":"crossref","first-page":"6480","DOI":"10.1021\/jacs.5b03373","article-title":"Structural insight into an\u00a0Alzheimer\u2019s brain-derived spherical assembly of amyloid \u03b2 by solid-state NMR","volume":"137","author":"Parthasarathy","year":"2015","journal-title":"J.\u00a0Am. Chem. Soc."},{"key":"10.1016\/j.bpj.2017.06.068_bib30","doi-asserted-by":"crossref","first-page":"611","DOI":"10.1016\/0022-2836(85)90175-5","article-title":"Kinetics of sickle\u00a0hemoglobin polymerization. II. A double nucleation mechanism","volume":"183","author":"Ferrone","year":"1985","journal-title":"J.\u00a0Mol. Biol."},{"key":"10.1016\/j.bpj.2017.06.068_bib31","doi-asserted-by":"crossref","first-page":"9758","DOI":"10.1073\/pnas.1218402110","article-title":"Proliferation of amyloid-\u03b242 aggregates occurs through a secondary nucleation mechanism","volume":"110","author":"Cohen","year":"2013","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.bpj.2017.06.068_bib32","doi-asserted-by":"crossref","first-page":"15146","DOI":"10.1021\/ja508621b","article-title":"Kinetic intermediates in amyloid assembly","volume":"136","author":"Liang","year":"2014","journal-title":"J.\u00a0Am. Chem. Soc."},{"key":"10.1016\/j.bpj.2017.06.068_bib33","doi-asserted-by":"crossref","first-page":"415","DOI":"10.1042\/BJ20090379","article-title":"Antiparallel \u03b2-sheet: a signature structure of the oligomeric amyloid \u03b2-peptide","volume":"421","author":"Cerf","year":"2009","journal-title":"Biochem.\u00a0J."},{"key":"10.1016\/j.bpj.2017.06.068_bib34","doi-asserted-by":"crossref","first-page":"32149","DOI":"10.1039\/C5CP03343H","article-title":"Isotope-edited FTIR reveals distinct aggregation and structural behaviors of unmodified and pyroglutamylated amyloid \u03b2 peptides","volume":"17","author":"Goldblatt","year":"2015","journal-title":"Phys. Chem. Chem. Phys."},{"key":"10.1016\/j.bpj.2017.06.068_bib35","doi-asserted-by":"crossref","first-page":"1771","DOI":"10.1002\/anie.201610399","article-title":"Tip-enhanced Raman spectroscopy to distinguish toxic oligomers from A\u03b21\u201342 fibrils at the nanometer scale","volume":"56","author":"Bonhommeau","year":"2017","journal-title":"Angew. Chem. Int. Ed. Engl."},{"key":"10.1016\/j.bpj.2017.06.068_bib36","doi-asserted-by":"crossref","first-page":"4197","DOI":"10.1021\/acs.biochem.5b00467","article-title":"Mechanism of nucleated conformational conversion of A\u03b242","volume":"54","author":"Fu","year":"2015","journal-title":"Biochemistry"},{"key":"10.1016\/j.bpj.2017.06.068_bib37","doi-asserted-by":"crossref","first-page":"4634","DOI":"10.1021\/jacs.6b01332","article-title":"X-ray crystallographic structures of a trimer, dodecamer, and annular pore formed by an A\u03b217\u201336 \u03b2-hairpin","volume":"138","author":"Kreutzer","year":"2016","journal-title":"J.\u00a0Am. Chem. Soc."},{"key":"10.1016\/j.bpj.2017.06.068_bib38","doi-asserted-by":"crossref","first-page":"11835","DOI":"10.1073\/pnas.1612362113","article-title":"Exploring the aggregation free energy landscape of the amyloid-\u03b2 protein (1\u201340)","volume":"113","author":"Zheng","year":"2016","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.bpj.2017.06.068_bib39","doi-asserted-by":"crossref","first-page":"10573","DOI":"10.1073\/pnas.90.22.10573","article-title":"Giant multilevel cation\u00a0channels formed by Alzheimer disease amyloid \u03b2-protein [A\u03b2 P-(1\u201340)] in bilayer membranes","volume":"90","author":"Arispe","year":"1993","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.bpj.2017.06.068_bib40","doi-asserted-by":"crossref","first-page":"10427","DOI":"10.1073\/pnas.0502066102","article-title":"Amyloid ion channels: a\u00a0common structural link for protein-misfolding disease","volume":"102","author":"Quist","year":"2005","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.bpj.2017.06.068_bib41","doi-asserted-by":"crossref","first-page":"14809","DOI":"10.1038\/srep14809","article-title":"SDS-PAGE analysis of A\u03b2 oligomers is disserving research into Alzheimer's disease: appealing for ESI-IM-MS","volume":"5","author":"Pujol-Pina","year":"2015","journal-title":"Sci. Rep."},{"key":"10.1016\/j.bpj.2017.06.068_bib42","doi-asserted-by":"crossref","first-page":"2825","DOI":"10.1016\/j.bpj.2011.10.023","article-title":"Zn2+ binding disrupts the Asp23-Lys28 salt bridge without altering the hairpin-shaped cross-\u03b2 structure of A\u03b2 (42) amyloid aggregates","volume":"101","author":"Mithu","year":"2011","journal-title":"Biophys.\u00a0J."},{"key":"10.1016\/j.bpj.2017.06.068_bib43","doi-asserted-by":"crossref","first-page":"19129","DOI":"10.1039\/c3cp52732h","article-title":"A folding transition underlies the\u00a0emergence of membrane affinity in amyloid-\u03b2","volume":"15","author":"Nag","year":"2013","journal-title":"Phys. Chem. Chem. Phys."},{"key":"10.1016\/j.bpj.2017.06.068_bib44","doi-asserted-by":"crossref","first-page":"374","DOI":"10.1016\/S1046-2023(02)00096-8","article-title":"Measuring diffusion in cell\u00a0membranes by fluorescence correlation spectroscopy","volume":"27","author":"Sengupta","year":"2002","journal-title":"Methods"},{"key":"10.1016\/j.bpj.2017.06.068_bib45","doi-asserted-by":"crossref","first-page":"365","DOI":"10.1016\/S0039-9140(01)00602-6","article-title":"Diffusion coefficient measurements in microfluidic devices","volume":"56","author":"Culbertson","year":"2002","journal-title":"Talanta"},{"key":"10.1016\/j.bpj.2017.06.068_bib46","doi-asserted-by":"crossref","first-page":"219","DOI":"10.1006\/jmra.1994.1208","article-title":"Ramped-amplitude cross-polarization in magic-angle-spinning NMR","volume":"110","author":"Metz","year":"1994","journal-title":"J.\u00a0Magn. Reson. A"},{"key":"10.1016\/j.bpj.2017.06.068_bib47","doi-asserted-by":"crossref","first-page":"459","DOI":"10.1016\/j.cplett.2006.06.007","article-title":"Swept-frequency two-pulse phase modulation for heteronuclear dipolar decoupling in solid-state NMR","volume":"426","author":"Thakur","year":"2006","journal-title":"Chem. Phys. Lett."},{"key":"10.1016\/j.bpj.2017.06.068_bib48","doi-asserted-by":"crossref","first-page":"342","DOI":"10.1016\/j.cplett.2008.12.084","article-title":"Improved magnetization transfer in solid-state NMR with fast magic angle spinning","volume":"469","author":"Weingarth","year":"2009","journal-title":"Chem. Phys. Lett."},{"key":"10.1016\/j.bpj.2017.06.068_bib49","doi-asserted-by":"crossref","first-page":"479","DOI":"10.1016\/S1090-7807(03)00082-X","article-title":"Chemical shift referencing in MAS solid state NMR","volume":"162","author":"Morcombe","year":"2003","journal-title":"J.\u00a0Magn. Reson."},{"key":"10.1016\/j.bpj.2017.06.068_bib50","doi-asserted-by":"crossref","first-page":"27","DOI":"10.1016\/0263-7855(96)00018-5","article-title":"VMD: visual molecular dynamics","volume":"14","author":"Humphrey","year":"1996","journal-title":"J.\u00a0Mol. Graph."},{"key":"10.1016\/j.bpj.2017.06.068_bib51","doi-asserted-by":"crossref","first-page":"1781","DOI":"10.1002\/jcc.20289","article-title":"Scalable molecular dynamics with NAMD","volume":"26","author":"Phillips","year":"2005","journal-title":"J.\u00a0Comput. Chem."},{"key":"10.1016\/j.bpj.2017.06.068_bib52","doi-asserted-by":"crossref","first-page":"3586","DOI":"10.1021\/jp973084f","article-title":"All-atom empirical potential for molecular modeling and dynamics studies of proteins","volume":"102","author":"MacKerell","year":"1998","journal-title":"J.\u00a0Phys. Chem. B"},{"key":"10.1016\/j.bpj.2017.06.068_bib53","doi-asserted-by":"crossref","first-page":"e70521","DOI":"10.1371\/journal.pone.0070521","article-title":"Conformational stability of\u00a0fibrillar amyloid-\u03b2 oligomers via protofilament pair formation\u2014a systematic computational study","volume":"8","author":"Kahler","year":"2013","journal-title":"PLoS One"},{"key":"10.1016\/j.bpj.2017.06.068_bib54","doi-asserted-by":"crossref","first-page":"10506","DOI":"10.1021\/bi0341410","article-title":"The amyloid-\u03b2 peptide (A\u03b2 (1\u201340)) is thermodynamically soluble at physiological concentrations","volume":"42","author":"Sengupta","year":"2003","journal-title":"Biochemistry"},{"key":"10.1016\/j.bpj.2017.06.068_bib55","doi-asserted-by":"crossref","first-page":"13827","DOI":"10.1074\/jbc.M110.199885","article-title":"Nature of the amyloid-\u03b2 monomer and the monomer-oligomer equilibrium","volume":"286","author":"Nag","year":"2011","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.bpj.2017.06.068_bib56","doi-asserted-by":"crossref","first-page":"1977","DOI":"10.1016\/S0006-3495(03)75006-1","article-title":"Measuring size distribution in highly heterogeneous systems with fluorescence correlation spectroscopy","volume":"84","author":"Sengupta","year":"2003","journal-title":"Biophys.\u00a0J."},{"key":"10.1016\/j.bpj.2017.06.068_bib57","doi-asserted-by":"crossref","first-page":"181","DOI":"10.1016\/S0065-3233(08)60528-8","article-title":"Vibrational spectroscopy and conformation of peptides, polypeptides, and proteins","volume":"38","author":"Krimm","year":"1986","journal-title":"Adv. Protein Chem."},{"key":"10.1016\/j.bpj.2017.06.068_bib58","doi-asserted-by":"crossref","first-page":"3507","DOI":"10.1021\/ja003266e","article-title":"Frequency selective heteronuclear dipolar recoupling in rotating solids: accurate 13C-15N distance measurements in uniformly 13C,15N-labeled peptides","volume":"123","author":"Jaroniec","year":"2001","journal-title":"J.\u00a0Am. Chem. Soc."},{"key":"10.1016\/j.bpj.2017.06.068_bib59","doi-asserted-by":"crossref","first-page":"15288","DOI":"10.1021\/jp1065264","article-title":"Disordered versus fibril-like amyloid \u03b2 (25\u201335) dimers in water: structure and thermodynamics","volume":"114","author":"Kittner","year":"2010","journal-title":"J.\u00a0Phys. Chem. B"},{"key":"10.1016\/j.bpj.2017.06.068_bib60","doi-asserted-by":"crossref","first-page":"8412","DOI":"10.1021\/jp2118778","article-title":"Structures of A\u03b217\u201342 trimers in isolation and with five small-molecule drugs using a hierarchical computational procedure","volume":"116","author":"Chebaro","year":"2012","journal-title":"J.\u00a0Phys. Chem. B"},{"key":"10.1016\/j.bpj.2017.06.068_bib61","doi-asserted-by":"crossref","first-page":"576","DOI":"10.1016\/j.bpj.2012.06.027","article-title":"Role of \u03b2-hairpin formation in aggregation: the self-assembly of the amyloid-\u03b2(25\u201335) peptide","volume":"103","author":"Larini","year":"2012","journal-title":"Biophys.\u00a0J."},{"key":"10.1016\/j.bpj.2017.06.068_bib62","doi-asserted-by":"crossref","first-page":"3338","DOI":"10.1016\/j.jmb.2013.06.021","article-title":"A\u03b2 monomers transiently sample oligomer and fibril-like configurations: ensemble characterization using a combined MD\/NMR approach","volume":"425","author":"Rosenman","year":"2013","journal-title":"J.\u00a0Mol. Biol."},{"key":"10.1016\/j.bpj.2017.06.068_bib63","doi-asserted-by":"crossref","first-page":"3518","DOI":"10.1021\/cr500638n","article-title":"Amyloid \u03b2 protein and Alzheimer\u2019s disease: when computer simulations complement experimental studies","volume":"115","author":"Nasica-Labouze","year":"2015","journal-title":"Chem. Rev."},{"key":"10.1016\/j.bpj.2017.06.068_bib64","doi-asserted-by":"crossref","first-page":"10478","DOI":"10.1021\/acs.jpcb.5b05593","article-title":"Structures of the Alzheimer\u2019s wild-type A\u03b21\u201340 dimer from atomistic simulations","volume":"119","author":"Tarus","year":"2015","journal-title":"J.\u00a0Phys. Chem. B"},{"key":"10.1016\/j.bpj.2017.06.068_bib65","doi-asserted-by":"crossref","first-page":"823","DOI":"10.1021\/acschemneuro.6b00053","article-title":"Impact of the\u00a0A2V mutation on the heterozygous and homozygous A\u03b21\u201340 dimer\u00a0structures from atomistic simulations","volume":"7","author":"Nguyen","year":"2016","journal-title":"ACS Chem. Neurosci."},{"key":"10.1016\/j.bpj.2017.06.068_bib66","doi-asserted-by":"crossref","first-page":"12111","DOI":"10.1021\/acs.jpcb.6b10722","article-title":"Dimerization mechanism of Alzheimer A\u03b240 peptides: the high content of intrapeptide-stabilized conformations in A2V and A2T heterozygous dimers retards amyloid fibril formation","volume":"120","author":"Nguyen","year":"2016","journal-title":"J.\u00a0Phys. Chem. B"},{"key":"10.1016\/j.bpj.2017.06.068_bib67","doi-asserted-by":"crossref","first-page":"657","DOI":"10.1002\/cbic.201500623","article-title":"An account of amyloid oligomers: facts and figures obtained from experiments and simulations","volume":"17","author":"Nagel-Steger","year":"2016","journal-title":"ChemBioChem"},{"key":"10.1016\/j.bpj.2017.06.068_bib68","doi-asserted-by":"crossref","first-page":"1024","DOI":"10.1002\/prot.25270","article-title":"Structural properties of\u00a0amyloid \u03b2 (1\u201340) dimer explored by replica exchange molecular dynamics simulations","volume":"85","author":"Watts","year":"2017","journal-title":"Proteins"},{"key":"10.1016\/j.bpj.2017.06.068_bib69","doi-asserted-by":"crossref","first-page":"22822","DOI":"10.1074\/jbc.M112.367474","article-title":"Solid-state NMR reveals a close structural relationship between amyloid-\u03b2 protofibrils and oligomers","volume":"287","author":"Scheidt","year":"2012","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.bpj.2017.06.068_bib70","doi-asserted-by":"crossref","first-page":"2837","DOI":"10.1002\/anie.201007265","article-title":"Solid-state NMR spectroscopic investigation of A\u03b2 protofibrils: implication of a \u03b2-sheet remodeling upon maturation into terminal amyloid fibrils","volume":"50","author":"Scheidt","year":"2011","journal-title":"Angew. Chem. Int. Ed. Engl."},{"key":"10.1016\/j.bpj.2017.06.068_bib71","doi-asserted-by":"crossref","first-page":"30182","DOI":"10.1038\/srep30182","article-title":"A critical role for the self-assembly of amyloid-\u03b21\u201342 in neurodegeneration","volume":"6","author":"Marshall","year":"2016","journal-title":"Sci. Rep."},{"key":"10.1016\/j.bpj.2017.06.068_bib72","doi-asserted-by":"crossref","first-page":"4443","DOI":"10.1073\/pnas.1111305109","article-title":"Antiparallel \u03b2-sheet architecture in Iowa-mutant \u03b2-amyloid fibrils","volume":"109","author":"Qiang","year":"2012","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.bpj.2017.06.068_bib73","doi-asserted-by":"crossref","first-page":"18673","DOI":"10.1074\/jbc.M113.457739","article-title":"Structural insights into A\u03b242 oligomers using site-directed spin labeling","volume":"288","author":"Gu","year":"2013","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.bpj.2017.06.068_bib74","doi-asserted-by":"crossref","first-page":"045102","DOI":"10.1063\/1.2822322","article-title":"Quasihomogeneous nucleation of amyloid-\u03b2 yields numerical bounds for the critical radius, the surface tension, and the free energy barrier for nucleus formation","volume":"128","author":"Garai","year":"2008","journal-title":"J.\u00a0Chem. Phys."},{"key":"10.1016\/j.bpj.2017.06.068_bib75","doi-asserted-by":"crossref","first-page":"1454","DOI":"10.1016\/j.bpj.2009.05.055","article-title":"On the stability of the soluble amyloid aggregates","volume":"97","author":"Sahoo","year":"2009","journal-title":"Biophys.\u00a0J."},{"key":"10.1016\/j.bpj.2017.06.068_bib76","doi-asserted-by":"crossref","first-page":"492","DOI":"10.1038\/nature19470","article-title":"Alzheimer\u2019s disease: structure of aggregates revealed","volume":"537","author":"Tycko","year":"2016","journal-title":"Nature"},{"key":"10.1016\/j.bpj.2017.06.068_bib77","doi-asserted-by":"crossref","first-page":"84","DOI":"10.3389\/fphys.2013.00084","article-title":"Thermodynamically stable amyloid-\u03b2 monomers have much lower membrane affinity than the small oligomers","volume":"4","author":"Sarkar","year":"2013","journal-title":"Front. Physiol."},{"key":"10.1016\/j.bpj.2017.06.068_bib78","doi-asserted-by":"crossref","first-page":"4049","DOI":"10.1021\/la502679t","article-title":"Rapid, cell-free assay for membrane-active forms of amyloid-\u03b2","volume":"31","author":"Bhowmik","year":"2015","journal-title":"Langmuir"},{"key":"10.1016\/j.bpj.2017.06.068_bib79","doi-asserted-by":"crossref","first-page":"9070","DOI":"10.1021\/acsnano.5b03175","article-title":"Cell-membrane-mimicking lipid-coated nanoparticles confer Raman enhancement to\u00a0membrane proteins and reveal membrane-attached amyloid-\u03b2 conformation","volume":"9","author":"Bhowmik","year":"2015","journal-title":"ACS Nano"},{"key":"10.1016\/j.bpj.2017.06.068_bib80","doi-asserted-by":"crossref","first-page":"2433","DOI":"10.1096\/fj.01-0377com","article-title":"Amyloid \u03b2-protein forms ion\u00a0channels: implications for Alzheimer\u2019s disease pathophysiology","volume":"15","author":"Lin","year":"2001","journal-title":"FASEB\u00a0J."},{"key":"10.1016\/j.bpj.2017.06.068_bib81","doi-asserted-by":"crossref","first-page":"20324","DOI":"10.1073\/pnas.0911281106","article-title":"Amyloid seeds formed by\u00a0cellular uptake, concentration, and aggregation of the amyloid-\u03b2 peptide","volume":"106","author":"Hu","year":"2009","journal-title":"Proc. Natl. Acad. Sci. USA"}],"container-title":["Biophysical Journal"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0006349517307890?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0006349517307890?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,11,2]],"date-time":"2025-11-02T16:32:53Z","timestamp":1762101173000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0006349517307890"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2017,8]]},"references-count":81,"journal-issue":{"issue":"4","published-print":{"date-parts":[[2017,8]]}},"alternative-id":["S0006349517307890"],"URL":"https:\/\/doi.org\/10.1016\/j.bpj.2017.06.068","relation":{},"ISSN":["0006-3495"],"issn-type":[{"value":"0006-3495","type":"print"}],"subject":[],"published":{"date-parts":[[2017,8]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Major Reaction Coordinates Linking Transient Amyloid-\u03b2 Oligomers to Fibrils Measured at Atomic Level","name":"articletitle","label":"Article Title"},{"value":"Biophysical Journal","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.bpj.2017.06.068","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2017 Biophysical Society.","name":"copyright","label":"Copyright"}]}}