{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,2]],"date-time":"2026-10-02T19:25:47Z","timestamp":1790969147466,"version":"4.1.0"},"reference-count":41,"publisher":"Elsevier BV","issue":"3","license":[{"start":{"date-parts":[[2011,10,1]],"date-time":"2011-10-01T00:00:00Z","timestamp":1317427200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"}],"funder":[{"DOI":"10.13039\/100000957","name":"Alzheimer\u2019s Association","doi-asserted-by":"crossref","award":["NIRG-09-133555"],"award-info":[{"award-number":["NIRG-09-133555"]}],"id":[{"id":"10.13039\/100000957","id-type":"DOI","asserted-by":"crossref"}]},{"DOI":"10.13039\/100000967","name":"American Health Assistance Foundation","doi-asserted-by":"crossref","award":["A2010362"],"award-info":[{"award-number":["A2010362"]}],"id":[{"id":"10.13039\/100000967","id-type":"DOI","asserted-by":"crossref"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Biochemical and Biophysical Research Communications"],"published-print":{"date-parts":[[2011,10]]},"DOI":"10.1016\/j.bbrc.2011.09.097","type":"journal-article","created":{"date-parts":[[2011,10,3]],"date-time":"2011-10-03T10:19:10Z","timestamp":1317637150000},"page":"512-516","source":"Crossref","is-referenced-by-count":30,"title":["Key residues for the oligomerization of A\u03b242 protein in Alzheimer\u2019s disease"],"prefix":"10.1016","volume":"414","author":[{"given":"Sam","family":"Ngo","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Zhefeng","family":"Guo","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.bbrc.2011.09.097_b0005","doi-asserted-by":"crossref","first-page":"860","DOI":"10.1002\/1531-8249(199912)46:6<860::AID-ANA8>3.0.CO;2-M","article-title":"Soluble pool of Abeta amyloid as a determinant of severity of neurodegeneration in Alzheimer\u2019s disease","volume":"46","author":"McLean","year":"1999","journal-title":"Ann. Neurol."},{"key":"10.1016\/j.bbrc.2011.09.097_b0010","doi-asserted-by":"crossref","first-page":"29639","DOI":"10.1074\/jbc.R800016200","article-title":"Structural classification of toxic amyloid oligomers","volume":"283","author":"Glabe","year":"2008","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbrc.2011.09.097_b0015","doi-asserted-by":"crossref","first-page":"4749","DOI":"10.1074\/jbc.R800036200","article-title":"Amyloid \u03b2-protein assembly and Alzheimer disease","volume":"284","author":"Roychaudhuri","year":"2009","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbrc.2011.09.097_b0020","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","year":"2006","journal-title":"Nature"},{"key":"10.1016\/j.bbrc.2011.09.097_b0025","doi-asserted-by":"crossref","first-page":"6448","DOI":"10.1073\/pnas.95.11.6448","article-title":"Diffusible, nonfibrillar ligands derived from Ab1\u201342 are potent central nervous system neurotoxins","volume":"95","author":"Lambert","year":"1998","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.bbrc.2011.09.097_b0030","doi-asserted-by":"crossref","first-page":"12749","DOI":"10.1021\/bi030029q","article-title":"Self-assembly of Ab1\u201342 into globular neurotoxins","volume":"42","author":"Chromy","year":"2003","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbrc.2011.09.097_b0035","doi-asserted-by":"crossref","first-page":"834","DOI":"10.1111\/j.1471-4159.2005.03407.x","article-title":"Globular amyloid b-peptide1\u201342 oligomer - a homogenous and stable neuropathological protein in Alzheimer\u2019s disease","volume":"95","author":"Barghorn","year":"2005","journal-title":"J. Neurochem."},{"key":"10.1016\/j.bbrc.2011.09.097_b0040","doi-asserted-by":"crossref","first-page":"6370","DOI":"10.1073\/pnas.1237107100","article-title":"Spherical aggregates of b-amyloid (amylospheroid) show high neurotoxicity and activate tau protein kinase I\/glycogen synthase kinase-3b","volume":"100","author":"Hoshi","year":"2003","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.bbrc.2011.09.097_b0045","doi-asserted-by":"crossref","first-page":"330","DOI":"10.1073\/pnas.222681699","article-title":"Amyloid b-protein (Ab) assembly: Ab40 and Ab42 oligomerize through distinct pathways","volume":"100","author":"Bitan","year":"2003","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.bbrc.2011.09.097_b0050","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.bbrc.2011.09.097_b0055","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","year":"2009","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbrc.2011.09.097_b0060","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","year":"2003","journal-title":"Science"},{"key":"10.1016\/j.bbrc.2011.09.097_b0065","doi-asserted-by":"crossref","first-page":"1870","DOI":"10.1021\/bi802046n","article-title":"Structural characterization of a soluble amyloid b-peptide oligomer","volume":"48","author":"Yu","year":"2009","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbrc.2011.09.097_b0070","doi-asserted-by":"crossref","first-page":"561","DOI":"10.1038\/nsmb.1799","article-title":"Structural conversion of neurotoxic amyloid-b(1\u201342) oligomers to fibrils","volume":"17","author":"Ahmed","year":"2010","journal-title":"Nat. Struct. Mol. Biol."},{"key":"10.1016\/j.bbrc.2011.09.097_b0075","doi-asserted-by":"crossref","first-page":"106","DOI":"10.1016\/j.jmb.2006.01.042","article-title":"High-resolution atomic force microscopy of soluble Ab42 oligomers","volume":"358","author":"Mastrangelo","year":"2006","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.bbrc.2011.09.097_b0080","doi-asserted-by":"crossref","first-page":"1157","DOI":"10.1038\/nsmb1345","article-title":"Evidence of fibril-like beta-sheet structures in a neurotoxic amyloid intermediate of Alzheimer\u2019s b-amyloid","volume":"14","author":"Chimon","year":"2007","journal-title":"Nat. Struct. Mol. Biol."},{"key":"10.1016\/j.bbrc.2011.09.097_b0085","doi-asserted-by":"crossref","first-page":"658","DOI":"10.1111\/j.1742-4658.2005.05102.x","article-title":"Mutagenesis of the central hydrophobic cluster in Ab42 Alzheimer\u2019s pepticle\u2013Side-chain properties correlate with aggregation propensities","volume":"273","author":"S\u00e1nchez de Groot","year":"2006","journal-title":"FEBS J."},{"key":"10.1016\/j.bbrc.2011.09.097_b0090","doi-asserted-by":"crossref","first-page":"32","DOI":"10.1186\/1741-7007-4-32","article-title":"Modulation of Ab42 low-n oligomerization using a novel yeast reporter system","volume":"4","author":"Bagriantsev","year":"2006","journal-title":"BMC Biol."},{"key":"10.1016\/j.bbrc.2011.09.097_b0095","doi-asserted-by":"crossref","first-page":"27081","DOI":"10.1074\/jbc.M111.257378","article-title":"Characterization of oligomer formation of amyloid-b peptide using a split-luciferase complementation assay","volume":"286","author":"Hashimoto","year":"2011","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbrc.2011.09.097_b0100","doi-asserted-by":"crossref","first-page":"477","DOI":"10.1016\/j.bbrc.2011.05.029","article-title":"Oligomerization and toxicity of Ab fusion proteins","volume":"409","author":"Caine","year":"2011","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.bbrc.2011.09.097_b0105","doi-asserted-by":"crossref","first-page":"1281","DOI":"10.1096\/fasebj.12.13.1281","article-title":"Cys-scanning mutagenesis: a novel approach to structure function relationships in polytopic membrane proteins","volume":"12","author":"Frillingos","year":"1998","journal-title":"FASEB J."},{"key":"10.1016\/j.bbrc.2011.09.097_b0110","doi-asserted-by":"crossref","first-page":"540","DOI":"10.1016\/S0076-6879(05)98044-0","article-title":"Using deubiquitylating enzymes as research tools","volume":"398","author":"Baker","year":"2005","journal-title":"Methods Enzymol."},{"key":"10.1016\/j.bbrc.2011.09.097_b0115","doi-asserted-by":"crossref","first-page":"801","DOI":"10.1016\/j.bbrc.2007.05.186","article-title":"Stable activity of a deubiquitylating enzyme (Usp2-cc) in the presence of high concentrations of urea and its application to purify aggregation-prone peptides","volume":"359","author":"Shahnawaz","year":"2007","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.bbrc.2011.09.097_b0120","doi-asserted-by":"crossref","first-page":"20","DOI":"10.1016\/S0076-6879(06)13002-5","article-title":"Preparation of amyloid b-protein for structural and functional studies","volume":"413","author":"Teplow","year":"2006","journal-title":"Methods Enzymol."},{"key":"10.1016\/j.bbrc.2011.09.097_b0125","doi-asserted-by":"crossref","first-page":"457","DOI":"10.1111\/j.1471-4159.2007.04972.x","article-title":"Congo red and thioflavin-T analogs detect Ab oligomers","volume":"104","author":"Maezawa","year":"2008","journal-title":"J. Neurochem."},{"key":"10.1016\/j.bbrc.2011.09.097_b0130","doi-asserted-by":"crossref","first-page":"171","DOI":"10.1016\/j.jneumeth.2010.05.001","article-title":"An improved method for generating consistent soluble amyloid-b oligomer preparations for in vitro neurotoxicity studies","volume":"190","author":"Ryan","year":"2010","journal-title":"J. Neurosci. Methods"},{"key":"10.1016\/j.bbrc.2011.09.097_b0135","doi-asserted-by":"crossref","first-page":"34882","DOI":"10.1074\/jbc.M300825200","article-title":"Elucidation of primary structure elements controlling early amyloid b-protein oligomerization","volume":"278","author":"Bitan","year":"2003","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbrc.2011.09.097_b0140","doi-asserted-by":"crossref","first-page":"9564","DOI":"10.1074\/jbc.270.16.9564","article-title":"Aggregation of secreted amyloid b-protein into sodium dodecyl sulfate-stable oligomers in cell culture","volume":"270","author":"Podlisny","year":"1995","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbrc.2011.09.097_b0145","doi-asserted-by":"crossref","first-page":"860","DOI":"10.1002\/1531-8249(199912)46:6<860::AID-ANA8>3.0.CO;2-M","article-title":"Soluble pool of Ab amyloid as a determinant of severity of neurodegeneration in Alzheimer\u2019s disease","volume":"46","author":"McLean","year":"1999","journal-title":"Ann. Neurol."},{"key":"10.1016\/j.bbrc.2011.09.097_b0150","doi-asserted-by":"crossref","first-page":"535","DOI":"10.1038\/416535a","article-title":"Naturally secreted oligomers of amyloid b protein potently inhibit hippocampal long-term potentiation in vivo","volume":"416","author":"Walsh","year":"2002","journal-title":"Nature"},{"key":"10.1016\/j.bbrc.2011.09.097_b0155","doi-asserted-by":"crossref","first-page":"16522","DOI":"10.1073\/pnas.0705197104","article-title":"Familial Alzhemier\u2019s disease mutations alter the stability of the amyloid b-protein monomer folding nucleus","volume":"104","author":"Grant","year":"2007","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.bbrc.2011.09.097_b0160","doi-asserted-by":"crossref","first-page":"17342","DOI":"10.1073\/pnas.0506723102","article-title":"3D structure of Alzheimer\u2019s amyloid-b(1\u201342) fibrils","volume":"102","author":"L\u00fchrs","year":"2005","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.bbrc.2011.09.097_b0165","doi-asserted-by":"crossref","first-page":"460","DOI":"10.1016\/0022-2836(92)90835-8","article-title":"Substitutions of hydrophobic amino acids reduce the amyloidogenicity of Alzheimer\u2019s disease b A4 peptides","volume":"228","author":"Hilbich","year":"1992","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.bbrc.2011.09.097_b0170","doi-asserted-by":"crossref","first-page":"13914","DOI":"10.1021\/bi961302+","article-title":"Point substitution in the central hydrophobic cluster of a human b-amyloid congener disrupts peptide folding and abolishes plaque competence","volume":"35","author":"Esler","year":"1996","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbrc.2011.09.097_b0175","doi-asserted-by":"crossref","first-page":"993","DOI":"10.1074\/jbc.M505091200","article-title":"Scanning cysteine mutagenesis analysis of Ab-(1\u201340) amyloid fibrils","volume":"281","author":"Shivaprasad","year":"2006","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbrc.2011.09.097_b0180","doi-asserted-by":"crossref","first-page":"1279","DOI":"10.1016\/S0022-2836(02)00399-6","article-title":"Mutations that reduce aggregation of the Alzheimer\u2019s Ab42 peptide: an unbiased search for the sequence determinants of Ab amyloidogenesis","volume":"319","author":"Wurth","year":"2002","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.bbrc.2011.09.097_b0185","doi-asserted-by":"crossref","first-page":"14175","DOI":"10.1073\/pnas.0807163105","article-title":"C-terminal peptides coassemble into Ab42 oligomers and protect neurons against Ab42-induced neurotoxicity","volume":"105","author":"Fradinger","year":"2008","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.bbrc.2011.09.097_b0190","doi-asserted-by":"crossref","first-page":"150","DOI":"10.1111\/j.1742-4658.2005.05051.x","article-title":"Structure of amyloid b fragments in aqueous environments","volume":"273","author":"Takano","year":"2006","journal-title":"FEBS J."},{"key":"10.1016\/j.bbrc.2011.09.097_b0195","doi-asserted-by":"crossref","first-page":"1419","DOI":"10.1523\/JNEUROSCI.4259-10.2011","article-title":"Crystal structure of the amyloid-b p3 fragment provides a model for oligomer formation in Alzheimer\u2019s disease","volume":"31","author":"Streltsov","year":"2011","journal-title":"J. Neurosci."},{"key":"10.1016\/j.bbrc.2011.09.097_b0200","doi-asserted-by":"crossref","first-page":"214707","DOI":"10.1063\/1.3010881","article-title":"Simulating oligomerization at experimental concentrations and long timescales: a Markov state model approach","volume":"129","author":"Kelley","year":"2008","journal-title":"J. Chem. Phys."},{"key":"10.1016\/j.bbrc.2011.09.097_b0205","doi-asserted-by":"crossref","first-page":"e21776","DOI":"10.1371\/journal.pone.0021776","article-title":"Rationally designed turn promoting mutation in the amyloid-b peptide sequence stabilizes oligomers in solution","volume":"6","author":"Rajadas","year":"2011","journal-title":"PLoS One"}],"container-title":["Biochemical and Biophysical Research Communications"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0006291X11017013?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0006291X11017013?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2024,4,13]],"date-time":"2024-04-13T02:30:52Z","timestamp":1712975452000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0006291X11017013"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2011,10]]},"references-count":41,"journal-issue":{"issue":"3","published-print":{"date-parts":[[2011,10]]}},"alternative-id":["S0006291X11017013"],"URL":"https:\/\/doi.org\/10.1016\/j.bbrc.2011.09.097","relation":{},"ISSN":["0006-291X"],"issn-type":[{"value":"0006-291X","type":"print"}],"subject":[],"published":{"date-parts":[[2011,10]]}}}