{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,7]],"date-time":"2026-10-07T15:00:16Z","timestamp":1791385216235,"version":"4.3.3"},"reference-count":50,"publisher":"American Chemical Society (ACS)","issue":"10","license":[{"start":{"date-parts":[[2026,8,28]],"date-time":"2026-08-28T00:00:00Z","timestamp":1787875200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2026,8,28]],"date-time":"2026-08-28T00:00:00Z","timestamp":1787875200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2026,8,28]],"date-time":"2026-08-28T00:00:00Z","timestamp":1787875200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-045"}],"funder":[{"DOI":"10.13039\/100000049","name":"National Institute on Aging","doi-asserted-by":"publisher","award":["R01AG079283"],"award-info":[{"award-number":["R01AG079283"]}],"id":[{"id":"10.13039\/100000049","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2026,10,7]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>Apolipoprotein E4 (ApoE4), one of the three common isoforms of ApoE, differs from ApoE3 and ApoE2 by just one amino acid substitution each. Yet these changes in ApoE4 profoundly impact protein structure and function to make it the strongest genetic risk factor for late-onset Alzheimer\u2019s disease (AD). ApoE4 exhibits a tendency to form oligomers (e.g., tetramers) that complicate high-resolution structural characterization in aqueous environments. Very little is known about the self-associated oligomeric structures. In this study, we employed ultracentrifugation, native mass spectrometry (MS), and fast photochemical oxidation of proteins (FPOP), a mass spectrometry-based protein footprinting approach, to investigate conformational differences among wild-type ApoE4 and two of its mutant variants ApoE4(V236E) (Jacksonville, JV) and ApoE4(V236E\/L268E) (VL). These substitutions shift the oligomeric equilibrium toward dimeric and monomeric states, respectively, and allow the tetramer state to be compared with the dimer and monomer. Comparative footprinting reveals that conformational changes driven by these mutations result in altered solvent accessibility in key regions of the protein, suggesting disruption of interfaces responsible for oligomerization and altered access of lipid-binding regions. Given ApoE4\u2019s central role in lipid metabolism and its altered interaction with lipid surfaces compared to other isoforms, these structural changes likely modulate lipid binding affinity and may contribute to its pathological role in AD. Our findings highlight the importance of conformational states in ApoE4 function and provide new insights into the structural basis of its disease-associated behavior.<\/jats:p>","DOI":"10.1021\/jasms.6c00167","type":"journal-article","created":{"date-parts":[[2026,9,2]],"date-time":"2026-09-02T03:44:57Z","timestamp":1788320697000},"page":"2368-2378","source":"Crossref","is-referenced-by-count":0,"title":["Mass Spectrometry-Based\nStructural Proteomics and\nAnalytical Ultracentrifugation Characterize the Structures of Oligomeric\nApolipoprotein E4 and Its Variants"],"prefix":"10.1021","volume":"37","author":[{"ORCID":"https:\/\/orcid.org\/0009-0000-4920-9380","authenticated-orcid":true,"given":"Hsin-Chieh","family":"Yang","sequence":"first","affiliation":[{"name":"Washington University in St. Louis , , , ,","place":["St. Louis, Missouri, United States, 63130"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Gregory","family":"DeKoster","sequence":"additional","affiliation":[{"name":"Washington University School of Medicine , , , ,","place":["St. Louis, Missouri, United States, 63110"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Berevan","family":"Baban","sequence":"additional","affiliation":[{"name":"Washington University School of Medicine , , , ,","place":["St. Louis, Missouri, United States, 63110"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Carl","family":"Frieden","sequence":"additional","affiliation":[{"name":"Washington University School of Medicine , , , ,","place":["St. Louis, Missouri, United States, 63110"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-1159-4636","authenticated-orcid":true,"given":"Michael L.","family":"Gross","sequence":"additional","affiliation":[{"name":"Washington University in St. Louis , , , ,","place":["St. Louis, Missouri, United States, 63130"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"316","published-online":{"date-parts":[[2026,8,28]]},"reference":[{"issue":"13","key":"2026100710065405900_cit1","doi-asserted-by":"publisher","first-page":"1485","DOI":"10.1096\/fasebj.10.13.8940294","article-title":"Human Apolipoprotein\nE: The Alzheimer\u2019s Disease\nConnection","volume":"10","author":"Weisgraber","year":"1996","journal-title":"FASEB J."},{"issue":"2","key":"2026100710065405900_cit2","doi-asserted-by":"publisher","first-page":"165","DOI":"10.1016\/j.pathol.2018.11.002","article-title":"Apolipoprotein\nE in Lipoprotein Metabolism, Health and Cardiovascular Disease","volume":"51","author":"Marais","year":"2019","journal-title":"Pathology"},{"issue":"7","key":"2026100710065405900_cit3","doi-asserted-by":"publisher","first-page":"739","DOI":"10.1007\/s00109-016-1427-y","article-title":"Apolipoprotein\nE: From Cardiovascular Disease to Neurodegenerative Disorders","volume":"94","author":"Mahley","year":"2016","journal-title":"J. Mol. Med."},{"issue":"5123","key":"2026100710065405900_cit4","doi-asserted-by":"publisher","first-page":"921","DOI":"10.1126\/science.8346443","article-title":"Gene Dose of Apolipoprotein E Type\n4 Allele and the\nRisk of Alzheimer\u2019s Disease in Late Onset Families","volume":"261","author":"Corder","year":"1993","journal-title":"Science"},{"issue":"4","key":"2026100710065405900_cit5","doi-asserted-by":"publisher","first-page":"569","DOI":"10.1093\/hmg\/3.4.569","article-title":"\u03f54 Allele\nas a Major Risk Factor\nfor Sporadic Early and Late-Onset Forms of Alzheimer\u2019s Disease:\nAnalysis of the 19q13.2 Chromosomal Region","volume":"3","author":"Chartier-Hariln","year":"1994","journal-title":"Hum. Mol. Genet."},{"issue":"9","key":"2026100710065405900_cit6","doi-asserted-by":"publisher","first-page":"773","DOI":"10.1007\/s40263-016-0361-4","article-title":"Apolipoprotein E as\na Therapeutic Target in Alzheimer\u2019s Disease: A Review of Basic\nResearch and Clinical Evidence","volume":"30","author":"Yamazaki","year":"2016","journal-title":"CNS Drugs"},{"issue":"1","key":"2026100710065405900_cit7","doi-asserted-by":"publisher","first-page":"63","DOI":"10.1186\/s13024-020-00413-4","article-title":"APOE2: Protective Mechanism\nand Therapeutic Implications for Alzheimer\u2019s\nDisease","volume":"15","author":"Li","year":"2020","journal-title":"Mol. Neurodegener."},{"key":"2026100710065405900_cit8","doi-asserted-by":"publisher","first-page":"1199434","DOI":"10.3389\/fnagi.2023.1199434","article-title":"Neuronal ApoE4\nin Alzheimer\u2019s Disease and Potential\nTherapeutic Targets","volume":"15","author":"Zhang","year":"2023","journal-title":"Front. 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Y.-C.\n          \n          Mass Spectrometry-Based\nStrategies for Protein Biophysics: Effects of Modification, Structure,\nand Interactions; PhD Dissertation, Washington\nUniversity in St. Louis, 2012."},{"issue":"12","key":"2026100710065405900_cit29","doi-asserted-by":"publisher","first-page":"3942","DOI":"10.1038\/s41596-020-0396-3","article-title":"Protein Higher-Order-Structure\nDetermination\nby Fast Photochemical Oxidation of Proteins and Mass Spectrometry\nAnalysis","volume":"15","author":"Liu","year":"2020","journal-title":"Nat. Protoc."},{"issue":"3","key":"2026100710065405900_cit30","doi-asserted-by":"publisher","first-page":"1606","DOI":"10.1016\/S0006-3495(00)76713-0","article-title":"Size-Distribution\nAnalysis of Macromolecules by Sedimentation Velocity Ultracentrifugation\nand Lamm Equation Modeling","volume":"78","author":"Schuck","year":"2000","journal-title":"Biophys. J."},{"key":"2026100710065405900_cit31","doi-asserted-by":"publisher","first-page":"185","DOI":"10.1016\/S0076-6879(04)84012-6","article-title":"Calculating\nSedimentation Coefficient Distributions\nby Direct Modeling of Sedimentation Velocity Concentration Profiles","volume":"384","author":"Dam","year":"2004","journal-title":"Methods Enzymol."},{"issue":"7","key":"2026100710065405900_cit32","doi-asserted-by":"publisher","first-page":"966","DOI":"10.1093\/bioinformatics\/btq054","article-title":"Skyline: An Open\nSource Document Editor for Creating\nand Analyzing Targeted Proteomics Experiments","volume":"26","author":"MacLean","year":"2010","journal-title":"Bioinformatics"},{"issue":"5","key":"2026100710065405900_cit33","doi-asserted-by":"publisher","first-page":"876","DOI":"10.1007\/s13361-019-02148-z","article-title":"Native Mass Spectrometry,\nIon Mobility,\nElectron-Capture Dissociation, and Modeling Provide Structural Information\nfor Gas-Phase Apolipoprotein E Oligomers","volume":"30","author":"Wang","year":"2019","journal-title":"J.\nAm. Soc. Mass Spectrom."},{"issue":"613","key":"2026100710065405900_cit34","doi-asserted-by":"publisher","DOI":"10.1126\/scitranslmed.abc9375","article-title":"APOE3 -Jacksonville (V236E) Variant Reduces Self-Aggregation and Risk\nof Dementia","volume":"13","author":"Liu","year":"2021","journal-title":"Sci. Transl. Med."},{"issue":"12","key":"2026100710065405900_cit35","doi-asserted-by":"publisher","first-page":"2057","DOI":"10.1016\/j.jasms.2005.09.008","article-title":"Laser Flash Photolysis\nof Hydrogen Peroxide to Oxidize\nProtein Solvent-Accessible Residues on the Microsecond Timescale","volume":"16","author":"Hambly","year":"2005","journal-title":"J. Am. Soc. 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NMR Assign."},{"issue":"5014","key":"2026100710065405900_cit42","doi-asserted-by":"publisher","first-page":"1817","DOI":"10.1126\/science.2063194","article-title":"Three-Dimensional\nStructure of the LDL Receptor-Binding Domain of Human Apolipoprotein\nE","volume":"252","author":"Wilson","year":"1991","journal-title":"Science"},{"issue":"9","key":"2026100710065405900_cit43","doi-asserted-by":"publisher","first-page":"2826","DOI":"10.1021\/bi002417n","article-title":"Interaction\nof the N-Terminal Domain of Apolipoprotein E4 with Heparin","volume":"40","author":"Dong","year":"2001","journal-title":"Biochemistry"},{"issue":"4","key":"2026100710065405900_cit44","doi-asserted-by":"publisher","first-page":"2576","DOI":"10.1074\/jbc.275.4.2576","article-title":"Effect\nof Arginine 172 on the Binding of Apolipoprotein\nE to the Low Density Lipoprotein Receptor","volume":"275","author":"Morrow","year":"2000","journal-title":"J.\nBiol. 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Dis."},{"issue":"11","key":"2026100710065405900_cit47","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pone.0027037","article-title":"Biophysical\nAnalysis of Apolipoprotein E3 Variants Linked with Development of\nType III Hyperlipoproteinemia","volume":"6","author":"Georgiadou","year":"2011","journal-title":"PLoS One"},{"issue":"42","key":"2026100710065405900_cit48","doi-asserted-by":"publisher","first-page":"40723","DOI":"10.1074\/jbc.M304814200","article-title":"Effects of Polymorphism on the Lipid\nInteraction of Human Apolipoprotein E","volume":"278","author":"Saito","year":"2003","journal-title":"J. Biol.\nChem."},{"issue":"10","key":"2026100710065405900_cit49","doi-asserted-by":"publisher","first-page":"2583","DOI":"10.1021\/bi602407r","article-title":"The C-Terminal Lipid-Binding Domain\nof Apolipoprotein E Is a Highly Efficient Mediator of ABCA1-Dependent\nCholesterol Efflux That Promotes the Assembly of High-Density Lipoproteins","volume":"46","author":"Vedhachalam","year":"2007","journal-title":"Biochemistry"},{"issue":"10","key":"2026100710065405900_cit50","doi-asserted-by":"publisher","first-page":"4236","DOI":"10.1073\/pnas.1018381108","article-title":"C-Terminal-Truncated\nApolipoprotein (Apo) E4 Inefficiently Clears\nAmyloid-\u03b2 (A\u03b2) and Acts in Concert with A\u03b2 to Elicit\nNeuronal and Behavioral Deficits in Mice","volume":"108","author":"Bien-Ly","year":"2011","journal-title":"Proc.\nNatl. Acad. Sci. U. S. A."}],"container-title":["Journal of the American\nSociety for Mass Spectrometry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/pubs.acs.org\/doi\/pdf\/10.1021\/jasms.6c00167","content-type":"application\/pdf","content-version":"vor","intended-application":"unspecified"},{"URL":"https:\/\/pubs.acs.org\/jamsef\/article-pdf\/37\/10\/2368\/67601917\/jasms.6c00167.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/pubs.acs.org\/jamsef\/article-pdf\/37\/10\/2368\/67601917\/jasms.6c00167.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,10,7]],"date-time":"2026-10-07T14:30:57Z","timestamp":1791383457000},"score":1,"resource":{"primary":{"URL":"https:\/\/pubs.acs.org\/jamsef\/article\/37\/10\/2368\/5349009\/Mass-Spectrometry-Based-Structural-Proteomics-and"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,8,28]]},"references-count":50,"journal-issue":{"issue":"10","published-online":{"date-parts":[[2026,8,28]]},"published-print":{"date-parts":[[2026,10,7]]}},"URL":"https:\/\/doi.org\/10.1021\/jasms.6c00167","relation":{},"ISSN":["1044-0305","1879-1123"],"issn-type":[{"value":"1044-0305","type":"print"},{"value":"1879-1123","type":"electronic"}],"subject":[],"published":{"date-parts":[[2026,8,28]]}}}