{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,28]],"date-time":"2026-04-28T14:45:53Z","timestamp":1777387553174,"version":"3.51.4"},"reference-count":45,"publisher":"Proceedings of the National Academy of Sciences","issue":"31","content-domain":{"domain":["www.pnas.org"],"crossmark-restriction":true},"short-container-title":["Proc. Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[2012,7,31]]},"abstract":"<jats:p>Oligomers are intermediates of the \u03b2-amyloid (A\u03b2) peptide fibrillogenic pathway and are putative pathogenic culprits in Alzheimer\u2019s disease (AD). Here we report the biotechnological generation and biochemical characterization of an oligomer-specific antibody fragment, KW1. KW1 not only discriminates between oligomers and other A\u03b2 conformations, such as fibrils or disaggregated peptide; it also differentiates between different types of A\u03b2 oligomers, such as those formed by A\u03b2 (1\u201340) and A\u03b2 (1\u201342) peptide. This high selectivity of binding contrasts sharply with many other conformational antibodies that interact with a large number of structurally analogous but sequentially different antigens. X-ray crystallography, NMR spectroscopy, and peptide array measurements imply that KW1 recognizes oligomers through a hydrophobic and significantly aromatic surface motif that includes A\u03b2 residues 18\u201320. KW1-positive oligomers occur in human AD brain samples and induce synaptic dysfunctions in living brain tissues. Bivalent KW1 potently neutralizes this effect and interferes with A\u03b2 assembly. By altering a specific step of the fibrillogenic cascade, it prevents the formation of mature A\u03b2 fibrils and induces the accumulation of nonfibrillar aggregates. Our data illuminate significant mechanistic differences in oligomeric and fibril recognition and suggest the considerable potential of KW1 in future studies to detect or inhibit specific types of A\u03b2 conformers.<\/jats:p>","DOI":"10.1073\/pnas.1206433109","type":"journal-article","created":{"date-parts":[[2012,7,20]],"date-time":"2012-07-20T05:41:21Z","timestamp":1342762881000},"page":"12503-12508","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":78,"title":["Molecular basis of \u03b2-amyloid oligomer recognition with a conformational antibody fragment"],"prefix":"10.1073","volume":"109","author":[{"given":"Isabel","family":"Morgado","sequence":"first","affiliation":[{"name":"Institute for Biochemistry and Biotechnology, Martin Luther University Halle-Wittenberg, 06120 Halle (Saale), Germany;"}]},{"given":"Karin","family":"Wieligmann","sequence":"additional","affiliation":[{"name":"Leibniz Institute for Natural Product Research and Infection Biology, Hans Kn\u00f6ll Institute, 07745 Jena, Germany;"}]},{"given":"Magdalena","family":"Bereza","sequence":"additional","affiliation":[{"name":"Leibniz Institute for Natural Product Research and Infection Biology, Hans Kn\u00f6ll Institute, 07745 Jena, Germany;"}]},{"given":"Raik","family":"R\u00f6nicke","sequence":"additional","affiliation":[{"name":"Leibniz Institute for Neurobiology, German Center for Neurodegenerative Diseases, 39118 Magdeburg, Germany;"}]},{"given":"Katrin","family":"Meinhardt","sequence":"additional","affiliation":[{"name":"Max Planck Research Unit for Enzymology of Protein Folding, 06120 Halle (Saale), Germany;"}]},{"given":"Karthikeyan","family":"Annamalai","sequence":"additional","affiliation":[{"name":"Max Planck Research Unit for Enzymology of Protein Folding, 06120 Halle (Saale), Germany;"}]},{"given":"Monika","family":"Baumann","sequence":"additional","affiliation":[{"name":"Fachbereich Physik, Naturwissenschaftliche Fakult\u00e4t II, Martin Luther University Halle-Wittenberg, 06120 Halle\/Saale, Germany;"}]},{"given":"Jessica","family":"Wacker","sequence":"additional","affiliation":[{"name":"Max Planck Research Unit for Enzymology of Protein Folding, 06120 Halle (Saale), Germany;"}]},{"given":"Peter","family":"Hortschansky","sequence":"additional","affiliation":[{"name":"Leibniz Institute for Natural Product Research and Infection Biology, Hans Kn\u00f6ll Institute, 07745 Jena, Germany;"}]},{"given":"Miroslav","family":"Male\u0161evi\u0107","sequence":"additional","affiliation":[{"name":"Max Planck Research Unit for Enzymology of Protein Folding, 06120 Halle (Saale), Germany;"}]},{"given":"Christoph","family":"Parthier","sequence":"additional","affiliation":[{"name":"Institute for Biochemistry and Biotechnology, Martin Luther University Halle-Wittenberg, 06120 Halle (Saale), Germany;"}]},{"given":"Christian","family":"Mawrin","sequence":"additional","affiliation":[{"name":"Institute for Neuropathology, Otto von Guericke University, 39120 Magdeburg, Germany; and"}]},{"given":"Cordelia","family":"Schiene-Fischer","sequence":"additional","affiliation":[{"name":"Max Planck Research Unit for Enzymology of Protein Folding, 06120 Halle (Saale), Germany;"}]},{"given":"Klaus G.","family":"Reymann","sequence":"additional","affiliation":[{"name":"Leibniz Institute for Neurobiology, German Center for Neurodegenerative Diseases, 39118 Magdeburg, Germany;"}]},{"given":"Milton T.","family":"Stubbs","sequence":"additional","affiliation":[{"name":"Institute for Biochemistry and Biotechnology, Martin Luther University Halle-Wittenberg, 06120 Halle (Saale), Germany;"}]},{"given":"Jochen","family":"Balbach","sequence":"additional","affiliation":[{"name":"Fachbereich Physik, Naturwissenschaftliche Fakult\u00e4t II, Martin Luther University Halle-Wittenberg, 06120 Halle\/Saale, Germany;"}]},{"given":"Matthias","family":"G\u00f6rlach","sequence":"additional","affiliation":[{"name":"Leibniz Institute for Age Research, Fritz Lipmann Institute, 07745 Jena, Germany"}]},{"given":"Uwe","family":"Horn","sequence":"additional","affiliation":[{"name":"Leibniz Institute for Natural Product Research and Infection Biology, Hans Kn\u00f6ll Institute, 07745 Jena, Germany;"}]},{"given":"Marcus","family":"F\u00e4ndrich","sequence":"additional","affiliation":[{"name":"Institute for Biochemistry and Biotechnology, Martin Luther University Halle-Wittenberg, 06120 Halle (Saale), Germany;"},{"name":"Max Planck Research Unit for Enzymology of Protein Folding, 06120 Halle (Saale), Germany;"}]}],"member":"341","published-online":{"date-parts":[[2012,7,18]]},"reference":[{"key":"e_1_3_4_1_2","doi-asserted-by":"crossref","first-page":"13","DOI":"10.1159\/000100355","article-title":"Amyloid-\u03b2 aggregation","volume":"4","author":"Finder VH","year":"2007","unstructured":"VH Finder, R Glockshuber, Amyloid-\u03b2 aggregation. Neurodegener Dis 4, 13\u201327 (2007).","journal-title":"Neurodegener Dis"},{"key":"e_1_3_4_2_2","doi-asserted-by":"crossref","first-page":"101","DOI":"10.1038\/nrm2101","article-title":"Soluble protein oligomers in neurodegeneration: Lessons from the Alzheimer\u2019s amyloid \u03b2-peptide","volume":"8","author":"Haass C","year":"2007","unstructured":"C Haass, DJ Selkoe, Soluble protein oligomers in neurodegeneration: Lessons from the Alzheimer\u2019s amyloid \u03b2-peptide. Nat Rev Mol Cell Biol 8, 101\u2013112 (2007).","journal-title":"Nat Rev Mol Cell Biol"},{"key":"e_1_3_4_3_2","doi-asserted-by":"crossref","first-page":"529","DOI":"10.1016\/j.jmb.2011.02.032","article-title":"Pattern recognition with a fibril-specific antibody fragment reveals the surface variability of natural amyloid fibrils","volume":"408","author":"Haupt C","year":"2011","unstructured":"C Haupt, et al., Pattern recognition with a fibril-specific antibody fragment reveals the surface variability of natural amyloid fibrils. J Mol Biol 408, 529\u2013540 (2011).","journal-title":"J Mol Biol"},{"key":"e_1_3_4_4_2","doi-asserted-by":"crossref","first-page":"834","DOI":"10.1111\/j.1471-4159.2005.03407.x","article-title":"Globular amyloid \u03b2-peptide oligomer - a homogenous and stable neuropathological protein in Alzheimer\u2019s disease","volume":"95","author":"Barghorn S","year":"2005","unstructured":"S Barghorn, et al., Globular amyloid \u03b2-peptide oligomer - a homogenous and stable neuropathological protein in Alzheimer\u2019s disease. J Neurochem 95, 834\u2013847 (2005).","journal-title":"J Neurochem"},{"key":"e_1_3_4_5_2","doi-asserted-by":"crossref","first-page":"4230","DOI":"10.1074\/jbc.M808591200","article-title":"Annular protofibrils are a structurally and functionally distinct type of amyloid oligomer","volume":"284","author":"Kayed R","year":"2009","unstructured":"R Kayed, et al., Annular protofibrils are a structurally and functionally distinct type of amyloid oligomer. J Biol Chem 284, 4230\u20134237 (2009).","journal-title":"J Biol Chem"},{"key":"e_1_3_4_6_2","doi-asserted-by":"crossref","first-page":"345","DOI":"10.1016\/S0197-0186(02)00050-5","article-title":"Abeta toxicity in Alzheimer\u2019s disease: Globular oligomers (ADDLs) as new vaccine and drug targets","volume":"41","author":"Klein WL","year":"2002","unstructured":"WL Klein, Abeta toxicity in Alzheimer\u2019s disease: Globular oligomers (ADDLs) as new vaccine and drug targets. Neurochem Int 41, 345\u2013352 (2002).","journal-title":"Neurochem Int"},{"key":"e_1_3_4_7_2","doi-asserted-by":"crossref","first-page":"19232","DOI":"10.1073\/pnas.0703793104","article-title":"Directed selection of a conformational antibody domain that prevents mature amyloid fibril formation by stabilizing Abeta protofibrils","volume":"104","author":"Habicht G","year":"2007","unstructured":"G Habicht, et al., Directed selection of a conformational antibody domain that prevents mature amyloid fibril formation by stabilizing Abeta protofibrils. Proc Natl Acad Sci USA 104, 19232\u201319237 (2007).","journal-title":"Proc Natl Acad Sci USA"},{"key":"e_1_3_4_8_2","doi-asserted-by":"crossref","first-page":"15595","DOI":"10.1073\/pnas.1001740107","article-title":"Stabilization of neurotoxic Alzheimer amyloid-\u03b2 oligomers by protein engineering","volume":"107","author":"Sandberg A","year":"2010","unstructured":"A Sandberg, et al., Stabilization of neurotoxic Alzheimer amyloid-\u03b2 oligomers by protein engineering. Proc Natl Acad Sci USA 107, 15595\u201315600 (2010).","journal-title":"Proc Natl Acad Sci USA"},{"key":"e_1_3_4_9_2","doi-asserted-by":"crossref","DOI":"10.1016\/j.jmb.2012.01.006","article-title":"Oligomeric intermediates in amyloid formation: Structure determination and mechanisms of toxicity","author":"F\u00e4ndrich M","year":"2012","unstructured":"M F\u00e4ndrich, Oligomeric intermediates in amyloid formation: Structure determination and mechanisms of toxicity. J Mol Biol, 2012).","journal-title":"J Mol Biol"},{"key":"e_1_3_4_10_2","doi-asserted-by":"crossref","first-page":"561","DOI":"10.1038\/nsmb.1799","article-title":"Structural conversion of neurotoxic amyloid-\u03b2(1-42) oligomers to fibrils","volume":"17","author":"Ahmed M","year":"2010","unstructured":"M Ahmed, et al., Structural conversion of neurotoxic amyloid-\u03b2(1-42) oligomers to fibrils. Nat Struct Mol Biol 17, 561\u2013567 (2010).","journal-title":"Nat Struct Mol Biol"},{"key":"e_1_3_4_11_2","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 S","year":"2007","unstructured":"S Chimon, et al., Evidence of fibril-like \u03b2-sheet structures in a neurotoxic amyloid intermediate of Alzheimer\u2019s \u03b2-amyloid. Nat Struct Mol Biol 14, 1157\u20131164 (2007).","journal-title":"Nat Struct Mol Biol"},{"key":"e_1_3_4_12_2","doi-asserted-by":"crossref","first-page":"1576","DOI":"10.1002\/anie.201105638","article-title":"Structural basis of \u03b2-amyloid-dependent synaptic dysfunctions","volume":"51","author":"Haupt C","year":"2012","unstructured":"C Haupt, et al., Structural basis of \u03b2-amyloid-dependent synaptic dysfunctions. Angew Chem Int Ed Engl 51, 1576\u20131579 (2012).","journal-title":"Angew Chem Int Ed Engl"},{"key":"e_1_3_4_13_2","doi-asserted-by":"crossref","first-page":"1228","DOI":"10.1126\/science.1213151","article-title":"Atomic view of a toxic amyloid small oligomer","volume":"335","author":"Laganowsky A","year":"2012","unstructured":"A Laganowsky, et al., Atomic view of a toxic amyloid small oligomer. Science 335, 1228\u20131231 (2012).","journal-title":"Science"},{"key":"e_1_3_4_14_2","doi-asserted-by":"crossref","first-page":"602","DOI":"10.1038\/nchembio.624","article-title":"Amyloid-\u03b2 forms fibrils by nucleated conformational conversion of oligomers","volume":"7","author":"Lee J","year":"2011","unstructured":"J Lee, EK Culyba, ET Powers, JW Kelly, Amyloid-\u03b2 forms fibrils by nucleated conformational conversion of oligomers. Nat Chem Biol 7, 602\u2013609 (2011).","journal-title":"Nat Chem Biol"},{"key":"e_1_3_4_15_2","doi-asserted-by":"crossref","first-page":"8585","DOI":"10.1074\/jbc.M110.172411","article-title":"Abeta42 neurotoxicity is mediated by ongoing nucleated polymerization process rather than by discrete Abeta42 species","volume":"286","author":"Jan A","year":"2011","unstructured":"A Jan, et al., Abeta42 neurotoxicity is mediated by ongoing nucleated polymerization process rather than by discrete Abeta42 species. J Biol Chem 286, 8585\u20138596 (2011).","journal-title":"J Biol Chem"},{"key":"e_1_3_4_16_2","doi-asserted-by":"crossref","first-page":"14745","DOI":"10.1073\/pnas.0905127106","article-title":"Structure-neurotoxicity relationships of amyloid \u03b2-protein oligomers","volume":"106","author":"Ono K","year":"2009","unstructured":"K Ono, MM Condron, DB Teplow, Structure-neurotoxicity relationships of amyloid \u03b2-protein oligomers. Proc Natl Acad Sci USA 106, 14745\u201314750 (2009).","journal-title":"Proc Natl Acad Sci USA"},{"key":"e_1_3_4_17_2","doi-asserted-by":"crossref","first-page":"14411","DOI":"10.1523\/JNEUROSCI.3537-10.2010","article-title":"Amyloid \u03b2-protein dimers rapidly form stable synaptotoxic protofibrils","volume":"30","author":"O\u2019Nuallain B","year":"2010","unstructured":"B O\u2019Nuallain, et al., Amyloid \u03b2-protein dimers rapidly form stable synaptotoxic protofibrils. J Neurosci 30, 14411\u201314419 (2010).","journal-title":"J Neurosci"},{"key":"e_1_3_4_18_2","doi-asserted-by":"crossref","first-page":"352","DOI":"10.1038\/nature04533","article-title":"A specific amyloid-\u03b2 protein assembly in the brain impairs memory","volume":"440","author":"Lesn\u00e9 S","year":"2006","unstructured":"S Lesn\u00e9, et al., A specific amyloid-\u03b2 protein assembly in the brain impairs memory. Nature 440, 352\u2013357 (2006).","journal-title":"Nature"},{"key":"e_1_3_4_19_2","doi-asserted-by":"crossref","first-page":"837","DOI":"10.1038\/nm1782","article-title":"Amyloid-\u03b2 protein dimers isolated directly from Alzheimer\u2019s brains impair synaptic plasticity and memory","volume":"14","author":"Shankar GM","year":"2008","unstructured":"GM Shankar, et al., Amyloid-\u03b2 protein dimers isolated directly from Alzheimer\u2019s brains impair synaptic plasticity and memory. Nat Med 14, 837\u2013842 (2008).","journal-title":"Nat Med"},{"key":"e_1_3_4_20_2","doi-asserted-by":"crossref","first-page":"11590","DOI":"10.1074\/jbc.M607483200","article-title":"Abeta oligomers induce neuronal oxidative stress through an N-methyl-D-aspartate receptor-dependent mechanism that is blocked by the Alzheimer drug memantine","volume":"282","author":"De Felice FG","year":"2007","unstructured":"FG De Felice, et al., Abeta oligomers induce neuronal oxidative stress through an N-methyl-D-aspartate receptor-dependent mechanism that is blocked by the Alzheimer drug memantine. J Biol Chem 282, 11590\u201311601 (2007).","journal-title":"J Biol Chem"},{"key":"e_1_3_4_21_2","doi-asserted-by":"crossref","first-page":"71","DOI":"10.1016\/j.jneumeth.2006.03.023","article-title":"Demonstration of a common artifact in immunosorbent assays of brain extracts: Development of a solid-phase extraction protocol to enable measurement of amyloid-\u03b2 from wild-type rodent brain","volume":"157","author":"Lanz TA","year":"2006","unstructured":"TA Lanz, JB Schachter, Demonstration of a common artifact in immunosorbent assays of brain extracts: Development of a solid-phase extraction protocol to enable measurement of amyloid-\u03b2 from wild-type rodent brain. J Neurosci Methods 157, 71\u201381 (2006).","journal-title":"J Neurosci Methods"},{"key":"e_1_3_4_22_2","doi-asserted-by":"crossref","first-page":"84","DOI":"10.1016\/j.abb.2010.02.001","article-title":"Size-dependent neurotoxicity of \u03b2-amyloid oligomers","volume":"496","author":"Cizas P","year":"2010","unstructured":"P Cizas, et al., Size-dependent neurotoxicity of \u03b2-amyloid oligomers. Arch Biochem Biophys 496, 84\u201392 (2010).","journal-title":"Arch Biochem Biophys"},{"key":"e_1_3_4_23_2","doi-asserted-by":"crossref","first-page":"589","DOI":"10.1016\/j.biochi.2004.09.012","article-title":"Probing the origins, diagnosis and treatment of amyloid diseases using antibodies","volume":"86","author":"Dumoulin M","year":"2004","unstructured":"M Dumoulin, CM Dobson, Probing the origins, diagnosis and treatment of amyloid diseases using antibodies. Biochimie 86, 589\u2013600 (2004).","journal-title":"Biochimie"},{"key":"e_1_3_4_24_2","doi-asserted-by":"crossref","first-page":"486","DOI":"10.1126\/science.1079469","article-title":"Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis","volume":"300","author":"Kayed R","year":"2003","unstructured":"R Kayed, et al., Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis. Science 300, 486\u2013489 (2003).","journal-title":"Science"},{"key":"e_1_3_4_25_2","doi-asserted-by":"crossref","first-page":"1485","DOI":"10.1073\/pnas.022662599","article-title":"Conformational Abs recognizing a generic amyloid fibril epitope","volume":"99","author":"O\u2019Nuallain B","year":"2002","unstructured":"B O\u2019Nuallain, R Wetzel, Conformational Abs recognizing a generic amyloid fibril epitope. Proc Natl Acad Sci USA 99, 1485\u20131490 (2002).","journal-title":"Proc Natl Acad Sci USA"},{"key":"e_1_3_4_26_2","doi-asserted-by":"crossref","first-page":"341","DOI":"10.1016\/j.jmb.2010.10.059","article-title":"Amyloid fibril recognition with the conformational B10 antibody fragment depends on electrostatic interactions","volume":"405","author":"Haupt C","year":"2011","unstructured":"C Haupt, et al., Amyloid fibril recognition with the conformational B10 antibody fragment depends on electrostatic interactions. J Mol Biol 405, 341\u2013348 (2011).","journal-title":"J Mol Biol"},{"key":"e_1_3_4_27_2","doi-asserted-by":"crossref","first-page":"821","DOI":"10.1098\/rstb.2002.1240","article-title":"Synaptic plasticity in animal models of early Alzheimer\u2019s disease","volume":"358","author":"Rowan MJ","year":"2003","unstructured":"MJ Rowan, I Klyubin, WK Cullen, R Anwyl, Synaptic plasticity in animal models of early Alzheimer\u2019s disease. Philos Trans R Soc Lond B Biol Sci 358, 821\u2013828 (2003).","journal-title":"Philos Trans R Soc Lond B Biol Sci"},{"key":"e_1_3_4_28_2","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 vivo","volume":"416","author":"Walsh DM","year":"2002","unstructured":"DM Walsh, et al., Naturally secreted oligomers of amyloid \u03b2 protein potently inhibit hippocampal long-term potentiation in vivo. Nature 416, 535\u2013539 (2002).","journal-title":"Nature"},{"key":"e_1_3_4_29_2","doi-asserted-by":"crossref","first-page":"712","DOI":"10.1021\/ja01464a042","article-title":"The infrared spectra of polypeptides in various conformations: Amide I and II bands","volume":"83","author":"Miyazawa T","year":"1961","unstructured":"T Miyazawa, ER Blout, The infrared spectra of polypeptides in various conformations: Amide I and II bands. J Am Chem Soc 83, 712\u2013719 (1961).","journal-title":"J Am Chem Soc"},{"key":"e_1_3_4_30_2","doi-asserted-by":"crossref","first-page":"508","DOI":"10.1016\/j.cocis.2011.06.016","article-title":"Assembly of Alzheimer's A\u03b2 peptide into nanostructured amyloid fibrils","volume":"16","author":"Morgado I","year":"2011","unstructured":"I Morgado, M F\u00e4ndrich, Assembly of Alzheimer's A\u03b2 peptide into nanostructured amyloid fibrils. Curr Opin Colloid Interface Sci 16, 508\u2013514 (2011).","journal-title":"Curr Opin Colloid Interface Sci"},{"key":"e_1_3_4_31_2","doi-asserted-by":"crossref","first-page":"1244","DOI":"10.1016\/j.str.2010.08.009","article-title":"Biology of amyloid: Structure, function, and regulation","volume":"18","author":"Greenwald J","year":"2010","unstructured":"J Greenwald, R Riek, Biology of amyloid: Structure, function, and regulation. Structure 18, 1244\u20131260 (2010).","journal-title":"Structure"},{"key":"e_1_3_4_32_2","doi-asserted-by":"crossref","first-page":"84","DOI":"10.1073\/pnas.1111232108","article-title":"Structure-based design of conformation- and sequence-specific antibodies against amyloid \u03b2","volume":"109","author":"Perchiacca JM","year":"2012","unstructured":"JM Perchiacca, ARA Ladiwala, M Bhattacharya, PM Tessier, Structure-based design of conformation- and sequence-specific antibodies against amyloid \u03b2. Proc Natl Acad Sci USA 109, 84\u201389 (2012).","journal-title":"Proc Natl Acad Sci USA"},{"key":"e_1_3_4_33_2","doi-asserted-by":"crossref","first-page":"24414","DOI":"10.1074\/jbc.M602363200","article-title":"Distinct early folding and aggregation properties of Alzheimer amyloid-\u03b2 peptides A\u03b240 and A\u03b242","volume":"281","author":"Chen Y-R","year":"2006","unstructured":"Y-R Chen, CG Glabe, Distinct early folding and aggregation properties of Alzheimer amyloid-\u03b2 peptides A\u03b240 and A\u03b242. J Biol Chem 281, 24414\u201324422 (2006).","journal-title":"J Biol Chem"},{"key":"e_1_3_4_34_2","doi-asserted-by":"crossref","first-page":"150","DOI":"10.1073\/pnas.012584899","article-title":"Structure determination of micelle-like intermediates in amyloid \u03b2 -protein fibril assembly by using small angle neutron scattering","volume":"99","author":"Yong W","year":"2002","unstructured":"W Yong, et al., Structure determination of micelle-like intermediates in amyloid \u03b2 -protein fibril assembly by using small angle neutron scattering. Proc Natl Acad Sci USA 99, 150\u2013154 (2002).","journal-title":"Proc Natl Acad Sci USA"},{"key":"e_1_3_4_35_2","doi-asserted-by":"crossref","first-page":"11027","DOI":"10.1021\/jp050716m","article-title":"Evidence of the existence of micelles in the fibrillogenesis of \u03b2-amyloid peptide","volume":"109","author":"Sabat\u00e9 R","year":"2005","unstructured":"R Sabat\u00e9, J Estelrich, Evidence of the existence of micelles in the fibrillogenesis of \u03b2-amyloid peptide. J Phys Chem B 109, 11027\u201311032 (2005).","journal-title":"J Phys Chem B"},{"key":"e_1_3_4_36_2","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 AK","year":"2008","unstructured":"AK Paravastu, RD Leapman, WM Yau, R Tycko, Molecular structural basis for polymorphism in Alzheimer\u2019s \u03b2-amyloid fibrils. Proc Natl Acad Sci USA 105, 18349\u201318354 (2008).","journal-title":"Proc Natl Acad Sci USA"},{"key":"e_1_3_4_37_2","doi-asserted-by":"crossref","first-page":"19813","DOI":"10.1073\/pnas.0905007106","article-title":"Comparison of Alzheimer Abeta(1-40) and Abeta(1-42) amyloid fibrils reveals similar protofilament structures","volume":"106","author":"Schmidt M","year":"2009","unstructured":"M Schmidt, et al., Comparison of Alzheimer Abeta(1-40) and Abeta(1-42) amyloid fibrils reveals similar protofilament structures. Proc Natl Acad Sci USA 106, 19813\u201319818 (2009).","journal-title":"Proc Natl Acad Sci USA"},{"key":"e_1_3_4_38_2","doi-asserted-by":"crossref","first-page":"7462","DOI":"10.1073\/pnas.0712290105","article-title":"Paired \u03b2-sheet structure of an Abeta(1-40) amyloid fibril revealed by electron microscopy","volume":"105","author":"Sachse C","year":"2008","unstructured":"C Sachse, M F\u00e4ndrich, N Grigorieff, Paired \u03b2-sheet structure of an Abeta(1-40) amyloid fibril revealed by electron microscopy. Proc Natl Acad Sci USA 105, 7462\u20137466 (2008).","journal-title":"Proc Natl Acad Sci USA"},{"key":"e_1_3_4_39_2","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 W","year":"2012","unstructured":"W Qiang, WM Yau, Y Luo, MP Mattson, R Tycko, Antiparallel \u03b2-sheet architecture in Iowa-mutant \u03b2-amyloid fibrils. Proc Natl Acad Sci USA 109, 4443\u20134448 (2012).","journal-title":"Proc Natl Acad Sci USA"},{"key":"e_1_3_4_40_2","doi-asserted-by":"crossref","first-page":"16938","DOI":"10.1073\/pnas.1112600108","article-title":"Molecular basis for amyloid-\u03b2 polymorphism","volume":"108","author":"Colletier JP","year":"2011","unstructured":"JP Colletier, et al., Molecular basis for amyloid-\u03b2 polymorphism. Proc Natl Acad Sci USA 108, 16938\u201316943 (2011).","journal-title":"Proc Natl Acad Sci USA"},{"key":"e_1_3_4_41_2","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 HA","year":"2011","unstructured":"HA Scheidt, I Morgado, S Rothemund, D Huster, M F\u00e4ndrich, Solid-state NMR spectroscopic investigation of A\u03b2 protofibrils: Implication of a \u03b2-sheet remodeling upon maturation into terminal amyloid fibrils. Angew Chem Int Ed Engl 50, 2837\u20132840 (2011).","journal-title":"Angew Chem Int Ed Engl"},{"key":"e_1_3_4_42_2","doi-asserted-by":"crossref","first-page":"9191","DOI":"10.1073\/pnas.0810364106","article-title":"\u03b1-Helix targeting reduces amyloid-\u03b2 peptide toxicity","volume":"106","author":"Nerelius C","year":"2009","unstructured":"C Nerelius, et al., \u03b1-Helix targeting reduces amyloid-\u03b2 peptide toxicity. Proc Natl Acad Sci USA 106, 9191\u20139196 (2009).","journal-title":"Proc Natl Acad Sci USA"},{"key":"e_1_3_4_43_2","doi-asserted-by":"crossref","first-page":"e1000334","DOI":"10.1371\/journal.pbio.1000334","article-title":"Sequestration of the Abeta peptide prevents toxicity and promotes degradation in vivo","volume":"8","author":"Luheshi LM","year":"2010","unstructured":"LM Luheshi, et al., Sequestration of the Abeta peptide prevents toxicity and promotes degradation in vivo. PLoS Biol 8, e1000334 (2010).","journal-title":"PLoS Biol"},{"key":"e_1_3_4_44_2","doi-asserted-by":"crossref","first-page":"2125","DOI":"10.1110\/ps.051470405","article-title":"Mutagenic analysis of the nucleation propensity of oxidized Alzheimer\u2019s \u03b2-amyloid peptide","volume":"14","author":"Christopeit T","year":"2005","unstructured":"T Christopeit, et al., Mutagenic analysis of the nucleation propensity of oxidized Alzheimer\u2019s \u03b2-amyloid peptide. Protein Sci 14, 2125\u20132131 (2005).","journal-title":"Protein Sci"},{"key":"e_1_3_4_45_2","doi-asserted-by":"crossref","first-page":"385","DOI":"10.1016\/j.bbrc.2011.04.141","article-title":"Phosphate and HEPES buffers potently affect the fibrillation and oligomerization mechanism of Alzheimer\u2019s A\u03b2 peptide","volume":"409","author":"Garvey M","year":"2011","unstructured":"M Garvey, et al., Phosphate and HEPES buffers potently affect the fibrillation and oligomerization mechanism of Alzheimer\u2019s A\u03b2 peptide. Biochem Biophys Res Commun 409, 385\u2013388 (2011).","journal-title":"Biochem Biophys Res Commun"}],"container-title":["Proceedings of the National Academy of Sciences"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/pnas.org\/doi\/pdf\/10.1073\/pnas.1206433109","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2022,6,7]],"date-time":"2022-06-07T05:05:24Z","timestamp":1654578324000},"score":1,"resource":{"primary":{"URL":"https:\/\/pnas.org\/doi\/full\/10.1073\/pnas.1206433109"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2012,7,18]]},"references-count":45,"journal-issue":{"issue":"31","published-print":{"date-parts":[[2012,7,31]]}},"alternative-id":["10.1073\/pnas.1206433109"],"URL":"https:\/\/doi.org\/10.1073\/pnas.1206433109","relation":{"has-review":[{"id-type":"doi","id":"10.3410\/f.717967638.793467421","asserted-by":"object"}]},"ISSN":["0027-8424","1091-6490"],"issn-type":[{"value":"0027-8424","type":"print"},{"value":"1091-6490","type":"electronic"}],"subject":[],"published":{"date-parts":[[2012,7,18]]},"assertion":[{"value":"2012-07-18","order":2,"name":"published","label":"Published","group":{"name":"publication_history","label":"Publication History"}}]}}