{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,24]],"date-time":"2026-09-24T13:07:12Z","timestamp":1790255232553,"version":"4.1.0"},"reference-count":65,"publisher":"Wiley","license":[{"start":{"date-parts":[[2026,9,24]],"date-time":"2026-09-24T00:00:00Z","timestamp":1790208000000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"},{"start":{"date-parts":[[2026,9,24]],"date-time":"2026-09-24T00:00:00Z","timestamp":1790208000000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/doi.wiley.com\/10.1002\/tdm_license_1.1"}],"funder":[{"DOI":"10.13039\/501100012155","name":"National Institute for Medical Research Development","doi-asserted-by":"publisher","award":["4041710"],"award-info":[{"award-number":["4041710"]}],"id":[{"id":"10.13039\/501100012155","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["febs.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["The FEBS Journal"],"abstract":"<jats:p>Insulin fibrillation and the subsequent formation of toxic amyloid aggregates are significant challenges in therapeutic development and are associated with cellular proteotoxicity. In this research, we explored how the p.M14L exenatide variant affects the formation of insulin amyloid fibrils. Applying a combination of spectroscopic and microscopic techniques, we demonstrated that this exenatide variant effectively shifts the aggregation pathway from mature fibrils toward off\u2010pathway amorphous aggregates. Atomic force microscopy (AFM) and dynamic light scattering (DLS) analyses revealed that in the presence of the exenatide variant, insulin is stabilized in off\u2010pathway amorphous aggregate structures with reduced hydrodynamic diameters. Molecular simulation studies further elucidated the molecular mechanisms underlying the interaction between insulin and the exenatide variant. Moreover, a cellular assay in SH\u2010SY5Y cells indicated that the aggregates formed in the presence of the exenatide variant significantly reduced cytotoxicity and apoptosis compared to mature fibrils. Therefore, the exenatide variant, through chaperone\u2010like behavior toward insulin, may hold potential as a candidate for improving its formulation stability and advancing the development of novel therapeutic approaches for amyloid\u2010related disorders.<\/jats:p>","DOI":"10.1111\/febs.70732","type":"journal-article","created":{"date-parts":[[2026,9,24]],"date-time":"2026-09-24T12:47:21Z","timestamp":1790254041000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Mechanistic insights into the inhibition of insulin amyloidogenesis and associated toxicity by the p.\n                    <scp>M14L<\/scp>\n                    variant of exenatide"],"prefix":"10.1111","author":[{"given":"Zahra","family":"Bahrami","sequence":"first","affiliation":[{"name":"Protein Chemistry Laboratory (PCL), Institute of Biochemistry and Biophysics (IBB), University of Tehran  Tehran Iran"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mohammad Rajab","family":"Shalgahi","sequence":"additional","affiliation":[{"name":"Protein Chemistry Laboratory (PCL), Institute of Biochemistry and Biophysics (IBB), University of Tehran  Tehran Iran"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mohammad Bagher","family":"Shahsavani","sequence":"additional","affiliation":[{"name":"Protein Chemistry Laboratory (PCL), Institute of Biochemistry and Biophysics (IBB), University of Tehran  Tehran Iran"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Zahra","family":"Mirzaei","sequence":"additional","affiliation":[{"name":"Protein Chemistry Laboratory (PCL), Institute of Biochemistry and Biophysics (IBB), University of Tehran  Tehran Iran"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Issa","family":"Zarei","sequence":"additional","affiliation":[{"name":"Department of Medicinal Chemistry, Faculty of Pharmacy Tehran University of Medical Sciences  Tehran Iran"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Massoud","family":"Amanlou","sequence":"additional","affiliation":[{"name":"Department of Medicinal Chemistry, Faculty of Pharmacy Tehran University of Medical Sciences  Tehran Iran"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Fatemeh","family":"Farjadian","sequence":"additional","affiliation":[{"name":"Pharmaceutical Sciences Research Center, School of Pharmacy Shiraz University of Medical Sciences  Shiraz Iran"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ali Akbar","family":"Moosavi\u2010Movahedi","sequence":"additional","affiliation":[{"name":"Institute of Biochemistry and Biophysics (IBB) University of Tehran  Tehran Iran"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-7396-7720","authenticated-orcid":false,"given":"Reza","family":"Yousefi","sequence":"additional","affiliation":[{"name":"Protein Chemistry Laboratory (PCL), Institute of Biochemistry and Biophysics (IBB), University of Tehran  Tehran Iran"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2026,9,24]]},"reference":[{"key":"e_1_2_11_2_1","doi-asserted-by":"crossref","first-page":"641","DOI":"10.21608\/jbaar.2024.382794","article-title":"Diabetes mellitus overview 2024","volume":"10","author":"Yameny AA","year":"2024","journal-title":"Journal of Bioscience and Applied Research"},{"key":"e_1_2_11_3_1","doi-asserted-by":"crossref","first-page":"425","DOI":"10.1038\/nrd.2015.36","article-title":"Pursuit of a perfect insulin","volume":"15","author":"Zaykov AN","year":"2016","journal-title":"Nat Rev Drug Discov"},{"key":"e_1_2_11_4_1","doi-asserted-by":"crossref","first-page":"450","DOI":"10.1016\/j.ijpharm.2018.06.023","article-title":"Chemical modifications of insulin: finding a compromise between stability and pharmaceutical performance","volume":"547","author":"Akbarian M","year":"2018","journal-title":"Int J Pharm"},{"key":"e_1_2_11_5_1","doi-asserted-by":"crossref","first-page":"537","DOI":"10.1007\/s13238-010-0069-z","article-title":"Insulin: a small protein with a long journey","volume":"1","author":"Hua Q","year":"2010","journal-title":"Protein Cell"},{"key":"e_1_2_11_6_1","doi-asserted-by":"crossref","first-page":"11354","DOI":"10.1039\/D0CC05171C","article-title":"Insulin fibrillation: toward strategies for attenuating the process","volume":"56","author":"Akbarian M","year":"2020","journal-title":"Chem Commun"},{"key":"e_1_2_11_7_1","doi-asserted-by":"crossref","DOI":"10.1126\/sciadv.adi1057","article-title":"Structural basis of insulin fibrillation","volume":"9","author":"Wang L","year":"2023","journal-title":"Sci Adv"},{"key":"e_1_2_11_8_1","doi-asserted-by":"crossref","first-page":"2613","DOI":"10.1021\/acschemneuro.2c00209","article-title":"Mechanisms behind the fibrillation and toxicity of insulin fibrils on neuron cells by engineered curcumin analogs","volume":"13","author":"Akbarian M","year":"2022","journal-title":"ACS Chem Neurosci"},{"key":"e_1_2_11_9_1","doi-asserted-by":"crossref","first-page":"327","DOI":"10.1111\/j.1468-1331.2006.01667.x","article-title":"Immune reactivity towards insulin, its amyloid and protein S100B in blood sera of Parkinson's disease patients","volume":"14","author":"Wilhelm KR","year":"2007","journal-title":"Eur J Neurol"},{"key":"e_1_2_11_10_1","doi-asserted-by":"crossref","first-page":"715","DOI":"10.1038\/s41574-021-00542-w","article-title":"One hundred years of insulin therapy","volume":"17","author":"Mathieu C","year":"2021","journal-title":"Nat Rev Endocrinol"},{"key":"e_1_2_11_11_1","doi-asserted-by":"crossref","first-page":"62326","DOI":"10.1039\/C4RA11291A","article-title":"Inhibition of insulin amyloid fibril formation by ferulic acid, a natural compound found in many vegetables and fruits","volume":"4","author":"Jayamani J","year":"2014","journal-title":"RSC Adv"},{"key":"e_1_2_11_12_1","doi-asserted-by":"crossref","first-page":"2323","DOI":"10.1021\/acs.jpcb.8b00689","article-title":"Mechanistic studies of the inhibition of insulin fibril formation by rosmarinic acid","volume":"122","author":"Zheng Q","year":"2018","journal-title":"J Phys Chem B"},{"key":"e_1_2_11_13_1","doi-asserted-by":"crossref","first-page":"959","DOI":"10.1166\/jbn.2018.2550","article-title":"Supramolecular nanoparticles of insulin and pentapeptide for inhibition of fibrillation and controlled release","volume":"14","author":"Zhou A","year":"2018","journal-title":"J Biomed Nanotechnol"},{"key":"e_1_2_11_14_1","doi-asserted-by":"crossref","first-page":"4076","DOI":"10.1021\/acsbiomaterials.8b00927","article-title":"Blocking oligomeric insulin amyloid fibrillation via perylenebisimides containing dipeptide tentacles","volume":"4","author":"Roy Chowdhury S","year":"2018","journal-title":"ACS Biomater Sci Eng"},{"key":"e_1_2_11_15_1","doi-asserted-by":"crossref","first-page":"497","DOI":"10.1016\/j.colsurfb.2011.07.040","article-title":"The synergistic chaperoning operation in a Bi\u2010chaperone system consisting of alpha\u2010crystallin and beta\u2010casein: bovine pancreatic insulin as the target protein","volume":"88","author":"Yousefi R","year":"2011","journal-title":"Colloids Surf B Biointerfaces"},{"key":"e_1_2_11_16_1","doi-asserted-by":"crossref","first-page":"453","DOI":"10.1016\/j.ijbiomac.2019.12.267","article-title":"Bifunctional carbon dots for cell imaging and inhibition of human insulin fibrillation in the whole aggregation process","volume":"147","author":"Wang B\u2010B","year":"2020","journal-title":"Int J Biol Macromol"},{"key":"e_1_2_11_17_1","first-page":"1637","article-title":"Mechanistic assessment of functionalized mesoporous silica\u2010mediated insulin fibrillation","volume":"124","author":"Akbarian M","year":"2020","journal-title":"J Phys Chem B"},{"key":"e_1_2_11_18_1","doi-asserted-by":"crossref","DOI":"10.1002\/pro.70020","article-title":"The role of amphipathic and cationic helical peptides in Parkinson's disease","volume":"34","author":"Pintado\u2010Grima C","year":"2025","journal-title":"Protein Sci"},{"key":"e_1_2_11_19_1","doi-asserted-by":"crossref","DOI":"10.1186\/s13024-023-00675-8","article-title":"Peptide\u2010based approaches to directly target alpha\u2010synuclein in Parkinson's disease","volume":"18","author":"Allen SG","year":"2023","journal-title":"Mol Neurodegener"},{"key":"e_1_2_11_20_1","first-page":"161","article-title":"Evolution of exenatide as a diabetes therapeutic","volume":"9","author":"Bhavsar S","year":"2013","journal-title":"Curr Diabetes Rev"},{"key":"e_1_2_11_21_1","doi-asserted-by":"crossref","first-page":"130","DOI":"10.1016\/j.bbagen.2022.130150","article-title":"Developing a novel exenatide\u2010based incretin mimic (\u03b1B\u2010ex): expression, purification and structural\u2010functional characterization","volume":"1866","author":"Ghanbarnezhad MM","year":"2022","journal-title":"Biochim Biophys Acta Gen Subj"},{"key":"e_1_2_11_22_1","doi-asserted-by":"crossref","first-page":"16757","DOI":"10.1021\/acs.jmedchem.4c01553","article-title":"Influence of Trp\u2010cage on the function and stability of GLP\u20101R agonist Exenatide derivatives","volume":"67","author":"Horv\u00e1th D","year":"2024","journal-title":"J Med Chem"},{"key":"e_1_2_11_23_1","doi-asserted-by":"crossref","DOI":"10.1038\/srep17599","article-title":"Inhibition of insulin fibrillation by osmolytes: mechanistic insights","volume":"5","author":"Choudhary S","year":"2015","journal-title":"Sci Rep"},{"key":"e_1_2_11_24_1","doi-asserted-by":"crossref","DOI":"10.3389\/fnagi.2022.955113","article-title":"Exendin\u20104 alleviates \u03b2\u2010amyloid peptide toxicity\u00a0via DAF\u201016 in a Caenorhabditis elegans model\u00a0of Alzheimer's disease","volume":"14","author":"Song X","year":"2022","journal-title":"Front Aging Neurosci"},{"key":"e_1_2_11_25_1","doi-asserted-by":"crossref","DOI":"10.1111\/cbdd.14426","article-title":"Exendin\u20104: a potential therapeutic strategy for Alzheimer's disease and Parkinson's disease","volume":"103","author":"Verma A","year":"2024","journal-title":"Chem Biol Drug Des"},{"key":"e_1_2_11_26_1","doi-asserted-by":"crossref","first-page":"962","DOI":"10.1007\/s13311-021-01018-5","article-title":"Neuroprotection of exendin\u20104 by enhanced autophagy in a parkinsonian rat model of \u03b1\u2010synucleinopathy","volume":"18","author":"Bu L\u2010L","year":"2021","journal-title":"Neurotherapeutics"},{"key":"e_1_2_11_27_1","doi-asserted-by":"crossref","first-page":"1415","DOI":"10.1111\/febs.70321","article-title":"M14 substitutions in exanatide modulate alpha\u2010synuclein aggregation","volume":"293","author":"Panuganti V","year":"2025","journal-title":"FEBS J"},{"key":"e_1_2_11_28_1","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0206169","article-title":"Human \u03b1B\u2010crystallin as fusion protein and molecular chaperone increases the expression and folding efficiency of recombinant insulin","volume":"13","author":"Akbarian M","year":"2018","journal-title":"PLoS One"},{"key":"e_1_2_11_29_1","doi-asserted-by":"crossref","first-page":"3903","DOI":"10.1021\/mp400364w","article-title":"Inhibition of human and bovine insulin fibril formation by designed peptide conjugates","volume":"10","author":"Mishra NK","year":"2013","journal-title":"Mol Pharm"},{"key":"e_1_2_11_30_1","doi-asserted-by":"crossref","first-page":"372","DOI":"10.1016\/j.jmb.2007.04.053","article-title":"Cytotoxicity of insulin within its self\u2010assembly and amyloidogenic pathways","volume":"370","author":"Grudzielanek S","year":"2007","journal-title":"J Mol Biol"},{"key":"e_1_2_11_31_1","doi-asserted-by":"crossref","first-page":"519","DOI":"10.1016\/j.bbadis.2010.02.008","article-title":"Amyloid fibrillation and cytotoxicity of insulin are inhibited by the amphiphilic surfactants","volume":"1802","author":"Wang SS\u2010S","year":"2010","journal-title":"Biochimica et Biophysica Acta (BBA)\u2010Molecular Basis of Disease"},{"key":"e_1_2_11_32_1","doi-asserted-by":"crossref","first-page":"507","DOI":"10.1038\/416507a","article-title":"Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases","volume":"416","author":"Bucciantini M","year":"2002","journal-title":"Nature"},{"key":"e_1_2_11_33_1","doi-asserted-by":"crossref","first-page":"1050","DOI":"10.1021\/acsptsci.2c00174","article-title":"Amyloid fibrillation of insulin: amelioration strategies and implications for translation","volume":"5","author":"Fagihi MH","year":"2022","journal-title":"ACS Pharmacol Transl Sci"},{"key":"e_1_2_11_34_1","doi-asserted-by":"crossref","first-page":"225","DOI":"10.1016\/j.ijbiomac.2017.11.168","article-title":"Inhibition of insulin amyloid fibrillation by Morin hydrate","volume":"108","author":"Patel P","year":"2018","journal-title":"Int J Biol Macromol"},{"key":"e_1_2_11_35_1","doi-asserted-by":"crossref","first-page":"1680","DOI":"10.1021\/ja208720a","article-title":"Monitoring and inhibition of insulin fibrillation by a small organic fluorogen with aggregation\u2010induced emission characteristics","volume":"134","author":"Hong Y","year":"2012","journal-title":"J Am Chem Soc"},{"key":"e_1_2_11_36_1","doi-asserted-by":"crossref","first-page":"23545","DOI":"10.1074\/jbc.M116.742460","article-title":"Inhibition of insulin amyloid fibrillation by a novel amphipathic heptapeptide","volume":"291","author":"Ratha BN","year":"2016","journal-title":"J Biol Chem"},{"key":"e_1_2_11_37_1","doi-asserted-by":"crossref","first-page":"38260","DOI":"10.1039\/D0RA07710K","article-title":"Inhibitory effect of coumarin and its analogs on insulin fibrillation\/cytotoxicity is depend on oligomerization states of the protein","volume":"10","author":"Akbarian M","year":"2020","journal-title":"RSC Adv"},{"key":"e_1_2_11_38_1","doi-asserted-by":"crossref","first-page":"981","DOI":"10.1016\/j.ijbiomac.2022.07.155","article-title":"An amphiphilic small molecule drives insulin aggregation inhibition and amyloid disintegration","volume":"218","author":"Das A","year":"2022","journal-title":"Int J Biol Macromol"},{"key":"e_1_2_11_39_1","doi-asserted-by":"crossref","first-page":"4463","DOI":"10.1002\/slct.201600692","article-title":"Gelatin as a potential inhibitor of insulin amyloid fibril formation","volume":"1","author":"Jayamani J","year":"2016","journal-title":"ChemistrySelect"},{"key":"e_1_2_11_40_1","doi-asserted-by":"crossref","first-page":"3043","DOI":"10.1021\/jz501570m","article-title":"\u03b1\u2010Casein inhibits insulin amyloid formation by preventing the onset of secondary nucleation processes","volume":"5","author":"Librizzi F","year":"2014","journal-title":"The Journal of Physical Chemistry Letters"},{"key":"e_1_2_11_41_1","doi-asserted-by":"crossref","first-page":"15395","DOI":"10.1021\/acs.jpcb.5b08215","article-title":"Controlling in vitro insulin amyloidosis with stable peptide conjugates: a combined experimental and computational study","volume":"119","author":"Mishra NK","year":"2015","journal-title":"J Phys Chem B"},{"key":"e_1_2_11_42_1","doi-asserted-by":"crossref","DOI":"10.3389\/fchem.2018.00311","article-title":"Elucidating the inhibitory potential of designed peptides against amyloid fibrillation and amyloid associated cytotoxicity","volume":"6","author":"Siddiqi MK","year":"2018","journal-title":"Front Chem"},{"key":"e_1_2_11_43_1","doi-asserted-by":"crossref","first-page":"1133","DOI":"10.1110\/ps.051879606","article-title":"Inhibition of insulin fibrillogenesis with targeted peptides","volume":"15","author":"Gibson TJ","year":"2006","journal-title":"Protein Sci"},{"key":"e_1_2_11_44_1","doi-asserted-by":"crossref","first-page":"265","DOI":"10.1007\/s12325-018-0868-9","article-title":"Optimizing fixed\u2010ratio combination therapy in type 2 diabetes","volume":"36","author":"Perreault L","year":"2019","journal-title":"Adv Ther"},{"key":"e_1_2_11_45_1","doi-asserted-by":"crossref","first-page":"242","DOI":"10.2337\/cd17-0037","article-title":"Fixed\u2010ratio combinations","volume":"35","author":"Tran E","year":"2017","journal-title":"Clin Diabetes"},{"key":"e_1_2_11_46_1","doi-asserted-by":"crossref","first-page":"35","DOI":"10.1016\/j.jbiotec.2022.01.002","article-title":"A novel method for the chaperone aided and efficient production of human proinsulin in the prokaryotic system","volume":"346","author":"Khosravi F","year":"2022","journal-title":"J Biotechnol"},{"key":"e_1_2_11_47_1","doi-asserted-by":"crossref","DOI":"10.1016\/j.bbapap.2025.141094","article-title":"The role of the N\u2010terminal p. R56Q mutation in modulating oligomerization and chaperone activity of human \u03b1B\u2010crystallin in relation to cardiomyopathy","author":"Somee LR","year":"2025","journal-title":"Biochim Biophys Acta Proteins Proteomics"},{"key":"e_1_2_11_48_1","doi-asserted-by":"crossref","first-page":"21449","DOI":"10.1074\/jbc.M314141200","article-title":"Mechanism of insulin fibrillation: the structure of insulin under amyloidogenic conditions resembles a protein\u2010folding intermediate","volume":"279","author":"Hua Q\u2010X","year":"2004","journal-title":"J Biol Chem"},{"key":"e_1_2_11_49_1","doi-asserted-by":"crossref","DOI":"10.1016\/j.bbagen.2024.130578","article-title":"Charge manipulation of the human insulin B chain C\u2010terminal to shed light on the complex mechanism of insulin fibrillation","volume":"1868","author":"Shahsavani MB","year":"2024","journal-title":"Biochim Biophys Acta Gen Subj"},{"key":"e_1_2_11_50_1","doi-asserted-by":"crossref","first-page":"1626","DOI":"10.1016\/j.bpj.2019.09.022","article-title":"Modulating insulin fibrillation using engineered B\u2010chains with mutated C\u2010termini","volume":"117","author":"Akbarian M","year":"2019","journal-title":"Biophys J"},{"key":"e_1_2_11_51_1","doi-asserted-by":"crossref","DOI":"10.1016\/j.bbapap.2023.140928","article-title":"The structural and functional consequences of\u00a0melatonin and serotonin on human \u03b1B\u2010crystallin and their dual role in the eye lens transparency","volume":"1871","author":"Nourazaran M","year":"2023","journal-title":"Biochim Biophy Acta Proteins Proteomics"},{"key":"e_1_2_11_52_1","doi-asserted-by":"crossref","first-page":"42669","DOI":"10.1074\/jbc.M504298200","article-title":"Early events in the fibrillation of monomeric insulin","volume":"280","author":"Ahmad A","year":"2005","journal-title":"J Biol Chem"},{"key":"e_1_2_11_53_1","doi-asserted-by":"crossref","first-page":"2521","DOI":"10.1016\/j.bpj.2009.07.064","article-title":"Tyrosine autofluorescence as a measure of bovine insulin fibrillation","volume":"97","author":"Bekard IB","year":"2009","journal-title":"Biophys J"},{"key":"e_1_2_11_54_1","doi-asserted-by":"crossref","DOI":"10.1016\/j.ijbiomac.2025.141895","article-title":"Structural characterization and functional analysis of human \u03b1B\u2010crystallin with the p. R11G mutation: insights into cataractogenesis and cardiomyopathy","volume":"307","author":"Salehi A","year":"2025","journal-title":"Int J Biol Macromol"},{"key":"e_1_2_11_55_1","doi-asserted-by":"crossref","first-page":"E3095","DOI":"10.1073\/pnas.1500851112","article-title":"Accurate secondary structure prediction and fold recognition for circular dichroism spectroscopy","volume":"112","author":"Micsonai A","year":"2015","journal-title":"Proc Natl Acad Sci USA"},{"key":"e_1_2_11_56_1","first-page":"175","volume-title":"BeStSel: From Secondary Structure Analysis to Protein Fold Prediction by Circular Dichroism Spectroscopy in Structural Genomics: General Applications","author":"Micsonai A.","year":"2020"},{"key":"e_1_2_11_57_1","doi-asserted-by":"crossref","first-page":"7","DOI":"10.1016\/j.ab.2014.11.016","article-title":"Concomitant Raman spectroscopy and dynamic light scattering for characterization of therapeutic proteins at high concentrations","volume":"472","author":"Zhou C","year":"2015","journal-title":"Anal Biochem"},{"key":"e_1_2_11_58_1","doi-asserted-by":"crossref","DOI":"10.1016\/j.abb.2025.110424","article-title":"The p. K90N mutation in human HSPB5 highlights the critical role of lysine 90 in chaperone function and structural integrity","author":"Ghaffari AR","year":"2025","journal-title":"Arch Biochem Biophys"},{"key":"e_1_2_11_59_1","doi-asserted-by":"crossref","first-page":"1344","DOI":"10.1529\/biophysj.104.048843","article-title":"Amyloidogenic self\u2010assembly of insulin aggregates probed by high resolution atomic force microscopy","volume":"88","author":"Jansen R","year":"2005","journal-title":"Biophys J"},{"key":"e_1_2_11_60_1","doi-asserted-by":"crossref","first-page":"4989","DOI":"10.1021\/acs.biomac.0c01178","article-title":"Identifying insulin fibril conformational differences by thioflavin\u2010T binding characteristics","volume":"21","author":"Ziaunys M","year":"2020","journal-title":"Biomacromolecules"},{"key":"e_1_2_11_61_1","doi-asserted-by":"crossref","first-page":"1889","DOI":"10.1002\/1873-3468.70043","article-title":"Structural and functional consequences of the cardiomyopathy\u2010associated p. R157C mutation in the C\u2010terminal palindromic motif of human \u03b1B\u2010crystallin","volume":"599","author":"Rezaei Somee L","year":"2025","journal-title":"FEBS Lett"},{"key":"e_1_2_11_62_1","doi-asserted-by":"crossref","first-page":"512","DOI":"10.1016\/j.micromeso.2021.111512","article-title":"Theranostic mesoporous silica nanoparticles made of multi\u2010nuclear gold or carbon quantum dots particles serving as pH responsive drug delivery system","volume":"329","author":"Akbarian M","year":"2022","journal-title":"Microporous Mesoporous Mater"},{"key":"e_1_2_11_63_1","doi-asserted-by":"crossref","first-page":"376","DOI":"10.1038\/emm.2007.42","article-title":"Resveratrol protects SH\u2010SY5Y neuroblastoma cells from apoptosis induced by dopamine","volume":"39","author":"Lee MK","year":"2007","journal-title":"Exp Mol Med"},{"key":"e_1_2_11_64_1","first-page":"157","volume-title":"Protein\u2013Protein and Protein\u2013Peptide Docking with ClusPro Server in Protein Structure Prediction","author":"Alekseenko A.","year":"2020"},{"key":"e_1_2_11_65_1","doi-asserted-by":"crossref","first-page":"255","DOI":"10.1038\/nprot.2016.169","article-title":"The ClusPro web server for protein\u2013protein docking","volume":"12","author":"Kozakov D","year":"2017","journal-title":"Nat Protoc"},{"key":"e_1_2_11_66_1","doi-asserted-by":"crossref","first-page":"210","DOI":"10.4103\/IJPSYM.IJPSYM_193_19","article-title":"The P value and statistical significance: misunderstandings, explanations, challenges, and alternatives","volume":"41","author":"Andrade C","year":"2019","journal-title":"Indian J Psychol Med"}],"container-title":["The FEBS Journal"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/febs.onlinelibrary.wiley.com\/doi\/pdf\/10.1111\/febs.70732","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/febs.onlinelibrary.wiley.com\/doi\/full-xml\/10.1111\/febs.70732","content-type":"application\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/febs.onlinelibrary.wiley.com\/doi\/pdf\/10.1111\/febs.70732","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,9,24]],"date-time":"2026-09-24T12:47:30Z","timestamp":1790254050000},"score":1,"resource":{"primary":{"URL":"https:\/\/febs.onlinelibrary.wiley.com\/doi\/10.1111\/febs.70732"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,9,24]]},"references-count":65,"alternative-id":["10.1111\/febs.70732"],"URL":"https:\/\/doi.org\/10.1111\/febs.70732","archive":["Portico"],"relation":{},"ISSN":["1742-464X","1742-4658"],"issn-type":[{"value":"1742-464X","type":"print"},{"value":"1742-4658","type":"electronic"}],"subject":[],"published":{"date-parts":[[2026,9,24]]},"assertion":[{"value":"2026-02-24","order":0,"name":"received","label":"Received","group":{"name":"publication_history","label":"Publication History"}},{"value":"2026-09-10","order":2,"name":"accepted","label":"Accepted","group":{"name":"publication_history","label":"Publication History"}},{"value":"2026-09-24","order":3,"name":"published","label":"Published","group":{"name":"publication_history","label":"Publication History"}}],"article-number":"febs.70732"}}