{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,13]],"date-time":"2026-05-13T00:22:32Z","timestamp":1778631752916,"version":"3.51.4"},"reference-count":48,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2025,11,1]],"date-time":"2025-11-01T00:00:00Z","timestamp":1761955200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2025,11,1]],"date-time":"2025-11-01T00:00:00Z","timestamp":1761955200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2025,11,1]],"date-time":"2025-11-01T00:00:00Z","timestamp":1761955200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2025,11,1]],"date-time":"2025-11-01T00:00:00Z","timestamp":1761955200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2025,11,1]],"date-time":"2025-11-01T00:00:00Z","timestamp":1761955200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2025,11,1]],"date-time":"2025-11-01T00:00:00Z","timestamp":1761955200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2025,11,1]],"date-time":"2025-11-01T00:00:00Z","timestamp":1761955200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"funder":[{"DOI":"10.13039\/501100018542","name":"Natural Science Foundation of Sichuan Province","doi-asserted-by":"publisher","award":["2024NSFSC0572"],"award-info":[{"award-number":["2024NSFSC0572"]}],"id":[{"id":"10.13039\/501100018542","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Archives of Biochemistry and Biophysics"],"published-print":{"date-parts":[[2025,11]]},"DOI":"10.1016\/j.abb.2025.110601","type":"journal-article","created":{"date-parts":[[2025,8,23]],"date-time":"2025-08-23T14:56:59Z","timestamp":1755961019000},"page":"110601","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":1,"special_numbering":"C","title":["Bile acids and polyphenols inhibit succinic anhydride-induced protein succinylation and amyloid aggregation: Mechanistic insights"],"prefix":"10.1016","volume":"773","author":[{"given":"Yilin","family":"Huang","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Xingli","family":"Huo","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Huijun","family":"Liu","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Danni","family":"Li","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Zongning","family":"Yin","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"issue":"1","key":"10.1016\/j.abb.2025.110601_bib1","doi-asserted-by":"crossref","first-page":"201","DOI":"10.1038\/s41467-023-35795-8","article-title":"Control of protein stability by post-translational modifications","volume":"14","author":"Lee","year":"2023","journal-title":"Nat. Commun."},{"key":"10.1016\/j.abb.2025.110601_bib2","doi-asserted-by":"crossref","DOI":"10.1016\/j.neuint.2024.105880","article-title":"Protein aggregation and its affecting mechanisms in neurodegenerative diseases","volume":"180","author":"Wu","year":"2024","journal-title":"Neurochem. Int."},{"issue":"1","key":"10.1016\/j.abb.2025.110601_bib3","doi-asserted-by":"crossref","first-page":"58","DOI":"10.1038\/nchembio.495","article-title":"Identification of lysine succinylation as a new post-translational modification","volume":"7","author":"Zhang","year":"2011","journal-title":"Nat. Chem. Biol."},{"issue":"5","key":"10.1016\/j.abb.2025.110601_bib4","doi-asserted-by":"crossref","first-page":"1423","DOI":"10.1007\/s10895-014-1424-x","article-title":"An insight into the biophysical characterization of insoluble collagen aggregates: implication for arthritis","volume":"24","author":"Amani","year":"2014","journal-title":"J. Fluoresc."},{"issue":"6","key":"10.1016\/j.abb.2025.110601_bib5","doi-asserted-by":"crossref","first-page":"523","DOI":"10.1007\/s00249-016-1119-0","article-title":"Aggregation as a consequence of glycation: insight into the pathogenesis of arthritis","volume":"45","author":"Shamsi","year":"2016","journal-title":"Eur. Biophys. J. : EBJ (Eur. Biophys. J.)"},{"issue":"4","key":"10.1016\/j.abb.2025.110601_bib6","doi-asserted-by":"crossref","first-page":"1242","DOI":"10.1016\/j.gendis.2022.03.009","article-title":"Protein post-translational modification by lysine succinylation: biochemistry, biological implications, and therapeutic opportunities","volume":"10","author":"Zhao","year":"2023","journal-title":"Genes Diseases"},{"issue":"10","key":"10.1016\/j.abb.2025.110601_bib7","doi-asserted-by":"crossref","first-page":"2346","DOI":"10.1007\/s11064-019-02780-x","article-title":"Succinylation links metabolism to protein functions","volume":"44","author":"Yang","year":"2019","journal-title":"Neurochem. Res."},{"issue":"1","key":"10.1016\/j.abb.2025.110601_bib8","doi-asserted-by":"crossref","first-page":"159","DOI":"10.1038\/s41467-021-27572-2","article-title":"Altered succinylation of mitochondrial proteins, APP and tau in alzheimer's disease","volume":"13","author":"Yang","year":"2022","journal-title":"Nat. Commun."},{"key":"10.1016\/j.abb.2025.110601_bib9","doi-asserted-by":"crossref","DOI":"10.3389\/fmolb.2024.1407505","article-title":"Dysregulation of protein succinylation and disease development","volume":"11","author":"Hou","year":"2024","journal-title":"Front. Mol. Biosci."},{"issue":"19","key":"10.1016\/j.abb.2025.110601_bib10","doi-asserted-by":"crossref","DOI":"10.3390\/nu15194297","article-title":"Comprehensive insights into biological roles of rosmarinic acid: implications in diabetes, cancer and neurodegenerative diseases","volume":"15","author":"Azhar","year":"2023","journal-title":"Nutrients"},{"key":"10.1016\/j.abb.2025.110601_bib11","doi-asserted-by":"crossref","DOI":"10.1155\/2020\/1245875","article-title":"Evaluation of binding of rosmarinic acid with human transferrin and its impact on the protein structure: targeting polyphenolic acid-induced protection of neurodegenerative disorders","volume":"2020","author":"Shamsi","year":"2020","journal-title":"Oxid. Med. Cell. Longev."},{"issue":"5","key":"10.1016\/j.abb.2025.110601_bib12","doi-asserted-by":"crossref","first-page":"547","DOI":"10.1016\/j.neuint.2010.06.021","article-title":"Neuroprotective effects of salidroside against beta-amyloid-induced oxidative stress in SH-SY5Y human neuroblastoma cells","volume":"57","author":"Zhang","year":"2010","journal-title":"Neurochem. Int."},{"issue":"6","key":"10.1016\/j.abb.2025.110601_bib13","doi-asserted-by":"crossref","first-page":"766","DOI":"10.1021\/acschemneuro.1c00729","article-title":"Glycosides and their corresponding small molecules inhibit aggregation and alleviate cytotoxicity of A\u03b240","volume":"13","author":"Hao","year":"2022","journal-title":"ACS Chem. Neurosci."},{"key":"10.1016\/j.abb.2025.110601_bib14","doi-asserted-by":"crossref","first-page":"60","DOI":"10.1016\/j.brainres.2014.01.047","article-title":"Neuroprotective effects of anthocyanin- and proanthocyanidin-rich extracts in cellular models of Parkinson\u05f3s disease","volume":"1555","author":"Strathearn","year":"2014","journal-title":"Brain Res."},{"issue":"6","key":"10.1016\/j.abb.2025.110601_bib15","doi-asserted-by":"crossref","first-page":"1329","DOI":"10.1271\/bbb.130101","article-title":"Inhibition of amyloid \u03b2 aggregation by acteoside, a phenylethanoid glycoside","volume":"77","author":"Kurisu","year":"2013","journal-title":"Biosci. Biotechnol. Biochem."},{"key":"10.1016\/j.abb.2025.110601_bib16","doi-asserted-by":"crossref","DOI":"10.1016\/j.foodchem.2021.129435","article-title":"Characterization, antioxidant, and neuroprotective effects of anthocyanins from Nitraria tangutorum bobr. Fruit","volume":"353","author":"Chen","year":"2021","journal-title":"Food Chem."},{"issue":"10","key":"10.1016\/j.abb.2025.110601_bib17","doi-asserted-by":"crossref","first-page":"2198","DOI":"10.1021\/acs.jpcb.3c00274","article-title":"Mechanistic insight into the amyloid fibrillation inhibition of hen egg white lysozyme by three different bile acids","volume":"127","author":"Jamuna","year":"2023","journal-title":"J. Phys. Chem. B"},{"issue":"11","key":"10.1016\/j.abb.2025.110601_bib18","doi-asserted-by":"crossref","first-page":"3658","DOI":"10.1096\/fj.201600275R","article-title":"Effects of bile acids on neurological function and disease","volume":"30","author":"McMillin","year":"2016","journal-title":"FASEB J. : Official Publ. Fed. Am. Societies Experimental Biol."},{"key":"10.1016\/j.abb.2025.110601_bib19","doi-asserted-by":"crossref","first-page":"596","DOI":"10.1016\/j.ijbiomac.2020.06.078","article-title":"Structural and biochemical investigation of MARK4 inhibitory potential of cholic acid: towards therapeutic implications in neurodegenerative diseases","volume":"161","author":"Anwar","year":"2020","journal-title":"Int. J. Biol. Macromol."},{"issue":"11","key":"10.1016\/j.abb.2025.110601_bib20","doi-asserted-by":"crossref","first-page":"4704","DOI":"10.1021\/acschemneuro.9b00482","article-title":"Biophysical elucidation of amyloid fibrillation inhibition and prevention of secondary nucleation by cholic acid: an unexplored function of cholic acid","volume":"10","author":"Majid","year":"2019","journal-title":"ACS Chem. Neurosci."},{"issue":"11","key":"10.1016\/j.abb.2025.110601_bib21","doi-asserted-by":"crossref","first-page":"4833","DOI":"10.1021\/acs.biomac.1c01107","article-title":"Modulating insulin aggregation with charge variable cholic acid-derived polymers","volume":"22","author":"Bera","year":"2021","journal-title":"Biomacromolecules"},{"issue":"12","key":"10.1016\/j.abb.2025.110601_bib22","doi-asserted-by":"crossref","DOI":"10.1016\/j.bbagen.2021.130021","article-title":"Regulatory role of acetylation on enzyme activity and fluxes of energy metabolism pathways","volume":"1865","author":"Moreno-S\u00e1nchez","year":"2021","journal-title":"Biochim. Biophys. Acta Gen. Subj."},{"key":"10.1016\/j.abb.2025.110601_bib23","doi-asserted-by":"crossref","DOI":"10.1016\/j.ijbiomac.2023.125104","article-title":"Fabrication and characterization of succinylated and glycosylated soy protein isolate and its self-assembled nanogel","volume":"244","author":"He","year":"2023","journal-title":"Int. J. Biol. Macromol."},{"key":"10.1016\/j.abb.2025.110601_bib24","doi-asserted-by":"crossref","DOI":"10.1016\/j.colsurfb.2023.113265","article-title":"The inhibitory effect and mechanism of small molecules on acetic anhydride-induced BSA acetylation and aggregation","volume":"225","author":"Huo","year":"2023","journal-title":"Colloids Surf. B Biointerfaces"},{"issue":"7","key":"10.1016\/j.abb.2025.110601_bib25","doi-asserted-by":"crossref","first-page":"1405","DOI":"10.1016\/j.bbapap.2010.04.001","article-title":"Molecular mechanism of Thioflavin-T binding to amyloid fibrils","volume":"1804","author":"Biancalana","year":"2010","journal-title":"Biochim. Biophys. Acta"},{"issue":"11","key":"10.1016\/j.abb.2025.110601_bib26","doi-asserted-by":"crossref","DOI":"10.1038\/tp.2012.109","article-title":"Early accumulation of intracellular fibrillar oligomers and late congophilic amyloid angiopathy in mice expressing the Osaka intra-A\u03b2 APP mutation","volume":"2","author":"Kulic","year":"2012","journal-title":"Transl. Psychiatry"},{"issue":"4","key":"10.1016\/j.abb.2025.110601_bib27","doi-asserted-by":"crossref","first-page":"193","DOI":"10.1111\/pin.12394","article-title":"Molecular pathogenesis of human amyloidosis: lessons from \u03b22 -microglobulin-related amyloidosis","volume":"66","author":"Naiki","year":"2016","journal-title":"Pathol. Int."},{"issue":"36","key":"10.1016\/j.abb.2025.110601_bib28","doi-asserted-by":"crossref","first-page":"12667","DOI":"10.1002\/anie.201906226","article-title":"Reevaluating protein photoluminescence: remarkable visible luminescence upon concentration and insight into the emission mechanism","volume":"58","author":"Wang","year":"2019","journal-title":"Angewandte Chemie (International ed. in English)"},{"issue":"7","key":"10.1016\/j.abb.2025.110601_bib29","doi-asserted-by":"crossref","first-page":"1496","DOI":"10.1110\/ps.0240003","article-title":"Protein stability induced by ligand binding correlates with changes in protein flexibility","volume":"12","author":"Celej","year":"2003","journal-title":"Protein Sci. : Publ. Protein Society"},{"issue":"12","key":"10.1016\/j.abb.2025.110601_bib30","doi-asserted-by":"crossref","DOI":"10.3390\/molecules25122780","article-title":"Tocopheryl succinate-induced structural changes in DPPC liposomes: DSC and ANS fluorescence studies","volume":"25","author":"Neunert","year":"2020","journal-title":"Molecules"},{"issue":"1","key":"10.1016\/j.abb.2025.110601_bib31","doi-asserted-by":"crossref","first-page":"144","DOI":"10.1016\/j.molstruc.2011.05.023","article-title":"Fluorescence quenching and ligand binding: a critical discussion of a popular methodology","volume":"998","author":"van de Weert","year":"2011","journal-title":"J. Mol. Struct."},{"key":"10.1016\/j.abb.2025.110601_bib32","doi-asserted-by":"crossref","DOI":"10.1016\/j.molstruc.2024.140345","article-title":"A cobalt coordination complex binds on a unique binding site between domain-I and domain-III of serum albumin","volume":"1322","author":"Qureshi","year":"2025","journal-title":"J. Mol. Struct."},{"issue":"5","key":"10.1016\/j.abb.2025.110601_bib33","doi-asserted-by":"crossref","DOI":"10.1016\/j.bbapap.2024.141028","article-title":"Plumbagin accelerates serum albumin's amyloid aggregation kinetics and generates fibril polymorphism by inducing non-native \u03b2-sheet structures","volume":"1872","author":"Chauhan","year":"2024","journal-title":"Biochim. Biophys. Acta Proteins Proteom."},{"issue":"4","key":"10.1016\/j.abb.2025.110601_bib34","doi-asserted-by":"crossref","first-page":"249","DOI":"10.1002\/bip.10376","article-title":"Association of fluorescent probes 1-anilinonaphthalene-8-sulfonate and 4,4'-dianilino-1,1'-binaphthyl-5,5'-disulfonic acid with T7 RNA polymerase","volume":"72","author":"Ghosh","year":"2003","journal-title":"Biopolymers"},{"issue":"7","key":"10.1016\/j.abb.2025.110601_bib35","doi-asserted-by":"crossref","first-page":"1487","DOI":"10.1007\/s11095-007-9516-9","article-title":"Extrinsic fluorescent dyes as tools for protein characterization","volume":"25","author":"Hawe","year":"2008","journal-title":"Pharm. Res."},{"key":"10.1016\/j.abb.2025.110601_bib36","doi-asserted-by":"crossref","first-page":"636","DOI":"10.1016\/j.ijbiomac.2018.10.208","article-title":"New insight on 8-anilino-1-naphthalene sulfonic acid interaction with TgFNR for hydrophobic exposure analysis","volume":"122","author":"Singh","year":"2019","journal-title":"Int. J. Biol. Macromol."},{"key":"10.1016\/j.abb.2025.110601_bib37","doi-asserted-by":"crossref","DOI":"10.1016\/j.saa.2024.124332","article-title":"The effect of chrysin binding on the conformational dynamics and unfolding pathway of human serum albumin","volume":"316","author":"Bisaria","year":"2024","journal-title":"Spectrochim. Acta Mol. Biomol. Spectrosc."},{"issue":"28","key":"10.1016\/j.abb.2025.110601_bib38","doi-asserted-by":"crossref","first-page":"4297","DOI":"10.1021\/acs.biochem.5b00309","article-title":"A comparison of three fluorophores for the detection of amyloid fibers and prefibrillar oligomeric assemblies. ThT (thioflavin T); ANS (1-Anilinonaphthalene-8-sulfonic acid); and bisANS (4,4'-Dianilino-1,1'-binaphthyl-5,5'-disulfonic acid)","volume":"54","author":"Younan","year":"2015","journal-title":"Biochemistry"},{"issue":"10","key":"10.1016\/j.abb.2025.110601_bib39","doi-asserted-by":"crossref","DOI":"10.3390\/ijms23105513","article-title":"New evidence on a distinction between A\u03b240 and A\u03b242 amyloids: Thioflavin T binding modes, clustering tendency, degradation resistance, and cross-seeding","volume":"23","author":"Sulatskaya","year":"2022","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.abb.2025.110601_bib40","doi-asserted-by":"crossref","DOI":"10.1016\/j.foodhyd.2020.106461","article-title":"Study on the structure and formation mechanism of 15S globulin of soybeans","volume":"113","author":"Ni","year":"2021","journal-title":"Food Hydrocoll."},{"issue":"1\u20132","key":"10.1016\/j.abb.2025.110601_bib41","doi-asserted-by":"crossref","first-page":"37","DOI":"10.1016\/j.ijpharm.2006.08.024","article-title":"Detection and characterization of protein aggregates by fluorescence microscopy","volume":"329","author":"Demeule","year":"2007","journal-title":"Int. J. Pharm."},{"issue":"2","key":"10.1016\/j.abb.2025.110601_bib42","doi-asserted-by":"crossref","first-page":"181","DOI":"10.1007\/s10895-007-0156-6","article-title":"Sensitive spectroscopic detection of large and denatured protein aggregates in solution by use of the fluorescent dye nile red","volume":"17","author":"Sutter","year":"2007","journal-title":"J. Fluoresc."},{"key":"10.1016\/j.abb.2025.110601_bib43","doi-asserted-by":"crossref","first-page":"357","DOI":"10.1016\/j.saa.2012.02.078","article-title":"Spectroscopic studies on the interaction of bovine serum albumin with surfactants and apigenin","volume":"94","author":"Zhao","year":"2012","journal-title":"Spectrochim. Acta Mol. Biomol. Spectrosc."},{"key":"10.1016\/j.abb.2025.110601_bib44","doi-asserted-by":"crossref","DOI":"10.1016\/j.molliq.2021.116888","article-title":"Probing the interaction of memantine, an important Alzheimer's drug, with human serum albumin: in silico and in vitro approach","volume":"340","author":"Alhumaydhi","year":"2021","journal-title":"J. Mol. Liq."},{"issue":"2","key":"10.1016\/j.abb.2025.110601_bib45","doi-asserted-by":"crossref","first-page":"359","DOI":"10.1002\/jcb.30176","article-title":"Myricetin inhibits breast and lung cancer cells proliferation via inhibiting MARK4","volume":"123","author":"Anwar","year":"2022","journal-title":"J. Cell. Biochem."},{"issue":"1","key":"10.1016\/j.abb.2025.110601_bib46","doi-asserted-by":"crossref","first-page":"75","DOI":"10.1007\/s12551-013-0130-2","article-title":"Receptor-ligand molecular docking","volume":"6","author":"Guedes","year":"2014","journal-title":"Biophys. Rev."},{"issue":"7","key":"10.1016\/j.abb.2025.110601_bib47","doi-asserted-by":"crossref","first-page":"13384","DOI":"10.3390\/molecules200713384","article-title":"Molecular docking and structure-based drug design strategies","volume":"20","author":"Ferreira","year":"2015","journal-title":"Molecules"},{"issue":"2","key":"10.1016\/j.abb.2025.110601_bib48","first-page":"320","article-title":"An overview of scoring functions used for protein-ligand interactions in molecular docking, interdisciplinary sciences","volume":"11","author":"Li","year":"2019","journal-title":"Comput. Life Sci."}],"container-title":["Archives of Biochemistry and Biophysics"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0003986125003145?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0003986125003145?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2026,5,13]],"date-time":"2026-05-13T00:00:43Z","timestamp":1778630443000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0003986125003145"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2025,11]]},"references-count":48,"alternative-id":["S0003986125003145"],"URL":"https:\/\/doi.org\/10.1016\/j.abb.2025.110601","relation":{},"ISSN":["0003-9861"],"issn-type":[{"value":"0003-9861","type":"print"}],"subject":[],"published":{"date-parts":[[2025,11]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Bile acids and polyphenols inhibit succinic anhydride-induced protein succinylation and amyloid aggregation: Mechanistic insights","name":"articletitle","label":"Article Title"},{"value":"Archives of Biochemistry and Biophysics","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.abb.2025.110601","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2025 Elsevier Inc. All rights are reserved, including those for text and data mining, AI training, and similar technologies.","name":"copyright","label":"Copyright"}],"article-number":"110601"}}