{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,6]],"date-time":"2026-06-06T05:13:48Z","timestamp":1780722828719,"version":"3.54.1"},"reference-count":105,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2025,12,1]],"date-time":"2025-12-01T00:00:00Z","timestamp":1764547200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2025,12,1]],"date-time":"2025-12-01T00:00:00Z","timestamp":1764547200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2025,12,1]],"date-time":"2025-12-01T00:00:00Z","timestamp":1764547200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2025,12,1]],"date-time":"2025-12-01T00:00:00Z","timestamp":1764547200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2025,12,1]],"date-time":"2025-12-01T00:00:00Z","timestamp":1764547200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2025,12,1]],"date-time":"2025-12-01T00:00:00Z","timestamp":1764547200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2025,12,1]],"date-time":"2025-12-01T00:00:00Z","timestamp":1764547200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"funder":[{"DOI":"10.13039\/501100004160","name":"Mazandaran University of Medical Sciences","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100004160","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100016293","name":"University of Mazandaran","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100016293","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Biochemical and Biophysical Research Communications"],"published-print":{"date-parts":[[2025,12]]},"DOI":"10.1016\/j.bbrc.2025.153017","type":"journal-article","created":{"date-parts":[[2025,11,21]],"date-time":"2025-11-21T21:57:25Z","timestamp":1763762245000},"page":"153017","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":1,"special_numbering":"C","title":["Modulation of amyloid formation in the hSOD1 R115G mutant by an ionic liquid ([BMIM][SCN])"],"prefix":"10.1016","volume":"793","author":[{"given":"Kimiya","family":"Rezaei","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-3854-9328","authenticated-orcid":false,"given":"Bagher","family":"Seyedalipour","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0009-0001-7308-639X","authenticated-orcid":false,"given":"Nasrin Keivan","family":"Behjou","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Seyed Mahdi Hosseini","family":"Faradonbeh","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Saman","family":"Hosseinkhani","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.bbrc.2025.153017_bib1","doi-asserted-by":"crossref","DOI":"10.3389\/fnana.2022.910427","article-title":"Deconvoluting the complexity of reactive oxygen species (ROS) in neurodegenerative diseases","volume":"16","author":"Zhou","year":"2022","journal-title":"Front. Neuroanat."},{"key":"10.1016\/j.bbrc.2025.153017_bib2","doi-asserted-by":"crossref","first-page":"5938","DOI":"10.3390\/ijms23115938","article-title":"An overview of oxidative stress, neuroinflammation, and neurodegenerative diseases","volume":"23","author":"Teleanu","year":"2022","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.bbrc.2025.153017_bib3","first-page":"12","volume":"vol. 13","author":"Ma","year":"2024"},{"key":"10.1016\/j.bbrc.2025.153017_bib4","doi-asserted-by":"crossref","first-page":"2219","DOI":"10.1038\/s41467-024-46554-8","article-title":"Neuropathogenesis-on-chips for neurodegenerative diseases","volume":"15","author":"Amartumur","year":"2024","journal-title":"Nat. Commun."},{"key":"10.1016\/j.bbrc.2025.153017_bib5","unstructured":"S. Choudhury, A.K. Dasmahapatra, Destabilization of Alzheimer \u2019 S Amyloid-\u03b2 Protofibrils by Bai- Calein : Mechanistic Insights from all-atom Molecular Dynamics Simulations, n.d."},{"key":"10.1016\/j.bbrc.2025.153017_bib6","doi-asserted-by":"crossref","DOI":"10.1016\/j.jbc.2022.102062","article-title":"Protein interaction networks in neurodegenerative diseases: from physiological function to aggregation","volume":"298","author":"Calabrese","year":"2022","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbrc.2025.153017_bib7","doi-asserted-by":"crossref","first-page":"2498","DOI":"10.3390\/molecules25112498","article-title":"Molecular spectroscopic markers of abnormal protein aggregation","volume":"25","author":"Wilkosz","year":"2020","journal-title":"Molecules"},{"key":"10.1016\/j.bbrc.2025.153017_bib8","doi-asserted-by":"crossref","first-page":"1391","DOI":"10.3390\/ph17101391","article-title":"Amyotrophic lateral sclerosis: insights and new prospects in disease pathophysiology, biomarkers and therapies","volume":"17","author":"Al-Khayri","year":"2024","journal-title":"Pharmaceuticals"},{"key":"10.1016\/j.bbrc.2025.153017_bib9","doi-asserted-by":"crossref","DOI":"10.1111\/ene.16140","article-title":"Breaking barriers with tofersen: enhancing therapeutic opportunities in amyotrophic lateral sclerosis","volume":"31","author":"Saini","year":"2024","journal-title":"Eur. J. Neurol."},{"key":"10.1016\/j.bbrc.2025.153017_bib10","doi-asserted-by":"crossref","first-page":"59","DOI":"10.1038\/362059a0","article-title":"Mutations in Cu\/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis","volume":"362","author":"Rosen","year":"1993","journal-title":"Nature"},{"key":"10.1016\/j.bbrc.2025.153017_bib11","doi-asserted-by":"crossref","DOI":"10.1016\/j.compbiomed.2022.106319","article-title":"Amyotrophic lateral sclerosis disease-related mutations disrupt the dimerization of superoxide dismutase 1-A comparative molecular dynamics simulation study","volume":"151","author":"Basith","year":"2022","journal-title":"Comput. Biol. Med."},{"key":"10.1016\/j.bbrc.2025.153017_bib12","doi-asserted-by":"crossref","first-page":"1345","DOI":"10.1002\/humu.22157","article-title":"ALSoD: a user\u2010friendly online bioinformatics tool for amyotrophic lateral sclerosis genetics","volume":"33","author":"Abel","year":"2012","journal-title":"Hum. Mutat."},{"key":"10.1016\/j.bbrc.2025.153017_bib13","doi-asserted-by":"crossref","DOI":"10.1016\/j.abb.2020.108701","article-title":"SOD1, more than just an antioxidant","volume":"697","author":"Eleutherio","year":"2021","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/j.bbrc.2025.153017_bib14","doi-asserted-by":"crossref","DOI":"10.1016\/j.ijbiomac.2024.136701","article-title":"Bisdemethoxycurcumin, a novel potent polyphenolic compound, effectively inhibits the formation of amyloid aggregates in ALS-associated hSOD1 mutant (L38R)","volume":"282","author":"Kouhi","year":"2024","journal-title":"Int. J. Biol. Macromol."},{"key":"10.1016\/j.bbrc.2025.153017_bib15","doi-asserted-by":"crossref","first-page":"170","DOI":"10.1016\/j.biochi.2022.05.001","article-title":"Zinc binding loop mutations of hSOD1 promote amyloid fibrils under physiological conditions: implications for initiation of amyotrophic lateral sclerosis","volume":"199","author":"Baziyar","year":"2022","journal-title":"Biochimie"},{"key":"10.1016\/j.bbrc.2025.153017_bib16","doi-asserted-by":"crossref","first-page":"10776","DOI":"10.1039\/C9RA09870D","article-title":"T54R mutation destabilizes the dimer of superoxide dismutase 1 T54R by inducing steric clashes at the dimer interface","volume":"10","author":"Ghosh","year":"2020","journal-title":"RSC Adv."},{"key":"10.1016\/j.bbrc.2025.153017_bib17","doi-asserted-by":"crossref","first-page":"3658","DOI":"10.1007\/s10528-023-10619-y","article-title":"Implications of ALS-associated mutations on biochemical and biophysical features of hSOD1 and Aggregation Formation","volume":"62","author":"Mohammadi","year":"2024","journal-title":"Biochem. Genet."},{"key":"10.1016\/j.bbrc.2025.153017_bib18","doi-asserted-by":"crossref","first-page":"885","DOI":"10.1002\/prot.26765","article-title":"Insight into factors influencing the aggregation process in wild\u2010type and P66R mutant SOD1: computational and spectroscopic approaches","volume":"93","author":"Farrokhzad","year":"2025","journal-title":"Proteins: Struct., Funct., Bioinf."},{"key":"10.1016\/j.bbrc.2025.153017_bib19","doi-asserted-by":"crossref","first-page":"177","DOI":"10.1186\/s13065-024-01289-x","article-title":"Mutation\/metal deficiency in the\" electrostatic loop\" enhanced aggregation process in apo\/holo SOD1 variants: implications for ALS diseases","volume":"18","author":"Ashkaran","year":"2024","journal-title":"BMC Chem"},{"key":"10.1016\/j.bbrc.2025.153017_bib20","doi-asserted-by":"crossref","first-page":"2645","DOI":"10.1080\/07391102.2016.1227723","article-title":"Computational simulation analysis on human SOD1 mutant (H80R) exposes the structural destabilization and the deviation of Zn binding that directs familial amyotrophic lateral sclerosis","volume":"35","author":"Srinivasan","year":"2017","journal-title":"J. Biomol. Struct. Dyn."},{"key":"10.1016\/j.bbrc.2025.153017_bib21","doi-asserted-by":"crossref","first-page":"494","DOI":"10.1016\/j.bbrc.2019.06.086","article-title":"Far positioned ALS associated mutants of Cu\/Zn SOD forms partially metallated, destabilized misfolding intermediates","volume":"516","author":"Tompa","year":"2019","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.bbrc.2025.153017_bib22","doi-asserted-by":"crossref","first-page":"1201","DOI":"10.1110\/ps.041256705","article-title":"Structural consequences of the familial amyotrophic lateral sclerosis SOD1 mutant His46Arg","volume":"14","author":"Antonyuk","year":"2005","journal-title":"Protein Sci."},{"key":"10.1016\/j.bbrc.2025.153017_bib23","doi-asserted-by":"crossref","first-page":"3147","DOI":"10.1073\/pnas.0511266103","article-title":"Common dynamical signatures of familial amyotrophic lateral sclerosis-associated structurally diverse Cu, Zn superoxide dismutase mutants","volume":"103","author":"Khare","year":"2006","journal-title":"Proc. Natl. Acad. Sci."},{"key":"10.1016\/j.bbrc.2025.153017_bib24","doi-asserted-by":"crossref","first-page":"19544","DOI":"10.1074\/jbc.M109.086074","article-title":"SOD1 mutations targeting surface hydrogen bonds promote amyotrophic lateral sclerosis without reducing apo-state stability","volume":"285","author":"Bystr\u00f6m","year":"2010","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbrc.2025.153017_bib25","doi-asserted-by":"crossref","first-page":"904","DOI":"10.1016\/j.ijbiomac.2019.09.181","article-title":"Changes in hydrophobicity mainly promotes the aggregation tendency of ALS associated SOD1 mutants","volume":"145","author":"Tompa","year":"2020","journal-title":"Int. J. Biol. Macromol."},{"key":"10.1016\/j.bbrc.2025.153017_bib26","article-title":"A double point mutation of SOD1 targeting net charge promotes aggregation under destabilizing conditions: correlation of charge distribution and ALS-provoking mutation","volume":"1867","author":"Mavadat","year":"2023","journal-title":"Biochim. Biophys. Acta (BBA)-General Subj."},{"key":"10.1016\/j.bbrc.2025.153017_bib27","doi-asserted-by":"crossref","DOI":"10.1016\/j.ijbiomac.2023.125289","article-title":"Role of charged residues of the \u201celectrostatic loop\u201d of hSOD1 in promotion of aggregation: implications for the mechanism of ALS-associated mutations under amyloidogenic conditions","volume":"244","author":"Mavadat","year":"2023","journal-title":"Int. J. Biol. Macromol."},{"key":"10.1016\/j.bbrc.2025.153017_bib28","doi-asserted-by":"crossref","first-page":"2261","DOI":"10.1093\/hmg\/3.12.2261","article-title":"Autosomal dominant amyotrophic lateral sclerosis: a novel mutation in the Cu\/Zn superoxide dismutase-1 gene","volume":"3","author":"Kostrzewa","year":"1994","journal-title":"Hum. Mol. Genet."},{"key":"10.1016\/j.bbrc.2025.153017_bib29","doi-asserted-by":"crossref","first-page":"1298","DOI":"10.1007\/s00415-010-5512-9","article-title":"The epidemiology of CuZn-SOD mutations in Germany: a study of 217 families","volume":"257","author":"Rabe","year":"2010","journal-title":"J. Neurol."},{"key":"10.1016\/j.bbrc.2025.153017_bib30","article-title":"Structural insights into SOD1: from in silico and molecular dynamics to experimental analyses of ALS-associated E49K and R115G mutants","volume":"12","author":"Faradonbeh","year":"2025","journal-title":"Front. Mol. Biosci."},{"key":"10.1016\/j.bbrc.2025.153017_bib31","doi-asserted-by":"crossref","DOI":"10.1136\/bmj-2023-075037","article-title":"Advances in molecular pathology, diagnosis, and treatment of amyotrophic lateral sclerosis","volume":"383","author":"Ilieva","year":"2023","journal-title":"Bmj"},{"key":"10.1016\/j.bbrc.2025.153017_bib32","doi-asserted-by":"crossref","first-page":"1601","DOI":"10.3390\/jpm12101601","article-title":"Status of ALS treatment, insights into therapeutic challenges and dilemmas","volume":"12","author":"Khamaysa","year":"2022","journal-title":"J. Pers. Med."},{"key":"10.1016\/j.bbrc.2025.153017_bib33","series-title":"In Silico Analyses of a Promising Drug Candidate for the Treatment of Amyotrophic Lateral Sclerosis Targeting Superoxide Dismutase I Protein","author":"Rodrigues","year":"2023"},{"key":"10.1016\/j.bbrc.2025.153017_bib34","article-title":"Investigating edaravone use for management of amyotrophic lateral sclerosis (ALS): a narrative review","volume":"15","author":"Neupane","year":"2023","journal-title":"Cureus"},{"key":"10.1016\/j.bbrc.2025.153017_bib35","doi-asserted-by":"crossref","first-page":"482","DOI":"10.1002\/bit.20442","article-title":"Interactions of lysozyme in guanidinium chloride solutions from static and dynamic light-scattering measurements","volume":"90","author":"Liu","year":"2005","journal-title":"Biotechnol. Bioeng."},{"key":"10.1016\/j.bbrc.2025.153017_bib36","series-title":"Ionic Liquids in Protein Amyloidogenesis : a Brief Screenshot of the state-of-the-art","author":"Pillai","year":"2018"},{"key":"10.1016\/j.bbrc.2025.153017_bib37","doi-asserted-by":"crossref","first-page":"3521","DOI":"10.1007\/s00018-018-2872-2","article-title":"Inhibition of protein misfolding and aggregation by natural phenolic compounds","volume":"75","author":"Dhouafli","year":"2018","journal-title":"Cell. Mol. Life Sci."},{"key":"10.1016\/j.bbrc.2025.153017_bib38","doi-asserted-by":"crossref","first-page":"899","DOI":"10.1080\/08927022.2024.2365377","article-title":"Exploring the anti-amyloid potential of salvianolic acid A against the ALS-associated mutant SOD1: insights from molecular docking and molecular dynamic simulations","volume":"50","author":"Abdullah Waheed","year":"2024","journal-title":"Mol. Simul."},{"key":"10.1016\/j.bbrc.2025.153017_bib39","doi-asserted-by":"crossref","DOI":"10.1016\/j.molliq.2022.118761","article-title":"Tetrabutylammonium based ionic liquids (ILs) inhibit the amyloid aggregation of superoxide dismutase 1 (SOD1)","volume":"353","author":"Kumari","year":"2022","journal-title":"J. Mol. Liq."},{"key":"10.1016\/j.bbrc.2025.153017_bib40","doi-asserted-by":"crossref","first-page":"853","DOI":"10.1007\/s12551-018-0421-8","article-title":"Suppression and dissolution of amyloid aggregates using ionic liquids","volume":"10","author":"Takekiyo","year":"2018","journal-title":"Biophys. Rev."},{"key":"10.1016\/j.bbrc.2025.153017_bib41","doi-asserted-by":"crossref","first-page":"8116","DOI":"10.1039\/D0GC02387F","article-title":"Biocompatible ionic liquids and their applications in pharmaceutics","volume":"22","author":"Md Moshikur","year":"2020","journal-title":"Green Chem."},{"key":"10.1016\/j.bbrc.2025.153017_bib42","doi-asserted-by":"crossref","DOI":"10.1016\/j.molliq.2021.115340","article-title":"Characterisation techniques for analysis of imidazolium-based ionic liquids and application in polymer preparation: a review","volume":"326","author":"Noorhisham","year":"2021","journal-title":"J. Mol. Liq."},{"key":"10.1016\/j.bbrc.2025.153017_bib43","doi-asserted-by":"crossref","first-page":"422","DOI":"10.1021\/acssuschemeng.5b00936","article-title":"Suppression effect on the Formation of insulin amyloid by the use of ionic liquids","volume":"4","author":"Takekiyo","year":"2016","journal-title":"ACS Sustain. Chem. Eng."},{"key":"10.1016\/j.bbrc.2025.153017_bib44","doi-asserted-by":"crossref","first-page":"4487","DOI":"10.1039\/C3RA44477E","article-title":"The stability of insulin in the presence of short alkyl chain imidazolium-based ionic liquids","volume":"4","author":"Kumar","year":"2014","journal-title":"RSC Adv."},{"key":"10.1016\/j.bbrc.2025.153017_bib45","doi-asserted-by":"crossref","first-page":"D204","DOI":"10.1093\/nar\/gku989","article-title":"UniProt: a hub for protein information","volume":"43","author":"Bateman","year":"2015","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.bbrc.2025.153017_bib46","doi-asserted-by":"crossref","first-page":"305","DOI":"10.1038\/s41577-020-00473-z","article-title":"NOD-like receptor-mediated plant immunity: from structure to cell death","volume":"21","author":"Saur","year":"2021","journal-title":"Nat. Rev. Immunol."},{"key":"10.1016\/j.bbrc.2025.153017_bib47","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1371\/journal.pone.0247841","article-title":"Comprehensive in silico analysis and molecular dynamics of the superoxide dismutase 1 (SOD1) variants related to amyotrophic lateral sclerosis","volume":"16","author":"Pereira","year":"2021","journal-title":"PLoS One"},{"key":"10.1016\/j.bbrc.2025.153017_bib48","doi-asserted-by":"crossref","first-page":"2981","DOI":"10.1093\/bioinformatics\/btu426","article-title":"YASARA View\u2014Molecular graphics for all devices\u2014from smartphones to workstations","volume":"30","author":"Krieger","year":"2014","journal-title":"Bioinformatics"},{"key":"10.1016\/j.bbrc.2025.153017_bib49","article-title":"Polyphenolic flavonoid compounds act as the inhibitory potential of aggregation process: implications for the prevention and therapeutics against FALS-associated D101G SOD1 mutant","volume":"107","author":"maitham Qassim","year":"2023","journal-title":"Comput. Biol. Chem."},{"key":"10.1016\/j.bbrc.2025.153017_bib50","doi-asserted-by":"crossref","first-page":"D1516","DOI":"10.1093\/nar\/gkae1059","article-title":"PubChem 2025 update","volume":"53","author":"Kim","year":"2025","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.bbrc.2025.153017_bib51","doi-asserted-by":"crossref","first-page":"3900","DOI":"10.1080\/07391102.2020.1785943","article-title":"In silico prediction of enzymatic reactions catalyzed by acid phosphatases","volume":"39","author":"Zamani Amirzakaria","year":"2021","journal-title":"J. Biomol. Struct. Dyn."},{"key":"10.1016\/j.bbrc.2025.153017_bib52","doi-asserted-by":"crossref","first-page":"3315","DOI":"10.1021\/jm051197e","article-title":"MolDock: a new technique for high-accuracy molecular docking","volume":"49","author":"Thomsen","year":"2006","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.bbrc.2025.153017_bib53","doi-asserted-by":"crossref","first-page":"67","DOI":"10.7555\/JBR.30.20130158","article-title":"Molecular docking simulation analysis of the interaction of dietary flavonols with heat shock protein 90","volume":"30","author":"Singh","year":"2016","journal-title":"J. Biomed. Res."},{"key":"10.1016\/j.bbrc.2025.153017_bib54","first-page":"455","article-title":"Software news and update AutoDock Vina: improving the speed and accuracy of docking with a new scoring function","volume":"31","author":"Trott","year":"2009","journal-title":"Effic. Optim. Multithreading"},{"key":"10.1016\/j.bbrc.2025.153017_bib55","doi-asserted-by":"crossref","first-page":"2785","DOI":"10.1002\/jcc.21256","article-title":"AutoDock4 and AutoDockTools4: automated docking with selective receptor flexibility","volume":"30","author":"Morris","year":"2009","journal-title":"J. Comput. Chem."},{"key":"10.1016\/j.bbrc.2025.153017_bib56","doi-asserted-by":"crossref","first-page":"1639","DOI":"10.1002\/(SICI)1096-987X(19981115)19:14<1639::AID-JCC10>3.0.CO;2-B","article-title":"Automated docking using a Lamarckian genetic algorithm and an empirical binding free energy function","volume":"19","author":"Morris","year":"1998","journal-title":"J. Comput. Chem."},{"key":"10.1016\/j.bbrc.2025.153017_bib57","doi-asserted-by":"crossref","first-page":"843","DOI":"10.1007\/s00249-011-0700-9","article-title":"Definition and testing of the GROMOS force-field versions 54A7 and 54B7","volume":"40","author":"Schmid","year":"2011","journal-title":"Eur. Biophys. J."},{"key":"10.1016\/j.bbrc.2025.153017_bib58","series-title":"Validation of the GROMOS 54A7 Force Field with Respect to \u0392 -Peptide Folding","first-page":"1237","author":"Huang","year":"2011"},{"key":"10.1016\/j.bbrc.2025.153017_bib59","doi-asserted-by":"crossref","first-page":"4203","DOI":"10.1021\/acschemneuro.5c00350","article-title":"Understanding structural destabilization and amyloid aggregation in ALS-Related neurodegenerative disorder: an in silico and experimental analysis of SOD1 variants","volume":"16","author":"Soleimanifard","year":"2025","journal-title":"ACS Chem. Neurosci."},{"key":"10.1016\/j.bbrc.2025.153017_bib60","series-title":"New Tricks for Modelers from the Crystallography Toolkit : the Particle Mesh Ewald Algorithm and its Use in Nucleic Acid Simulations","first-page":"55","author":"Darden","year":"1999"},{"key":"10.1016\/j.bbrc.2025.153017_bib61","doi-asserted-by":"crossref","first-page":"1951","DOI":"10.1021\/ci500020m","article-title":"G_mmpbsa\u2014 A GROMACS tool for high-throughput MM-PBSA calculations","volume":"54","author":"Kumari","year":"2014","journal-title":"J. Chem. Inf. Model."},{"key":"10.1016\/j.bbrc.2025.153017_bib62","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/S0005-2736(98)00081-9","article-title":"Fluorescence quenching data interpretation in biological systems. The use of microscopic models for data analysis and interpretation of complex systems","volume":"1373","author":"Castanho","year":"1998","journal-title":"Biochim. Biophys. Acta - Biomembr."},{"key":"10.1016\/j.bbrc.2025.153017_bib63","doi-asserted-by":"crossref","first-page":"1287","DOI":"10.1021\/jp3114557","article-title":"Binding sites of resveratrol, genistein, and curcumin with milk \u03b1-and \u03b2-caseins","volume":"117","author":"Bourassa","year":"2013","journal-title":"J. Phys. Chem. B"},{"key":"10.1016\/j.bbrc.2025.153017_bib64","unstructured":"A. Srivastava, A. Israelson, B. Ahmad, Curcumin binds to the pre-fibrillar aggregates of Cu\/Zn superoxide dismutase (SOD1) and alters its amyloidogenic Related papers, 1 (n.d.)."},{"key":"10.1016\/j.bbrc.2025.153017_bib65","doi-asserted-by":"crossref","first-page":"4145","DOI":"10.1007\/s00018-019-03108-2","article-title":"Network mapping of the conformational heterogeneity of SOD1 by deploying statistical cluster analysis of FTIR spectra","volume":"76","author":"Chowdhury","year":"2019","journal-title":"Cell. Mol. Life Sci."},{"key":"10.1016\/j.bbrc.2025.153017_bib66","doi-asserted-by":"crossref","DOI":"10.3390\/app10175918","article-title":"Peak fitting applied to fourier transform infrared and raman spectroscopic analysis of proteins","volume":"10","author":"Sadat","year":"2020","journal-title":"Appl. Sci."},{"key":"10.1016\/j.bbrc.2025.153017_bib67","doi-asserted-by":"crossref","first-page":"693","DOI":"10.1007\/s11814-012-0060-x","article-title":"Techniques for monitoring protein misfolding and aggregation in vitro and in living cells","volume":"29","author":"Gregoire","year":"2012","journal-title":"Korean J. Chem. Eng."},{"key":"10.1016\/j.bbrc.2025.153017_bib68","doi-asserted-by":"crossref","first-page":"131","DOI":"10.1016\/j.ejpb.2005.08.005","article-title":"Changes in the amide I FT-IR bands of poly-l-lysine on spray-drying from \u03b1-helix, \u03b2-sheet or random coil conformations","volume":"62","author":"Mauerer","year":"2006","journal-title":"Eur. J. Pharm. Biopharm."},{"key":"10.1016\/j.bbrc.2025.153017_bib69","article-title":"Detrimental effect of the inescapable endogenous neurotoxin","author":"Esmaeili","year":"2019","journal-title":"Chem. Biol. Interact."},{"key":"10.1016\/j.bbrc.2025.153017_bib70","doi-asserted-by":"crossref","first-page":"749","DOI":"10.2533\/chimia.2006.749","article-title":"Biological scanning transmission electron microscopy: imaging and single molecule mass determination","volume":"60","author":"M\u00fcller","year":"2006","journal-title":"Chimia"},{"key":"10.1016\/j.bbrc.2025.153017_bib71","doi-asserted-by":"crossref","DOI":"10.1016\/j.bioorg.2025.108740","article-title":"Exploring the role of ethylammonium bromide as an ionic liquid in amyloid aggregation modulation for ALS-linked hSOD1 E49K mutant","volume":"163","author":"Keivan Behjou","year":"2025","journal-title":"Bioorg. Chem."},{"key":"10.1016\/j.bbrc.2025.153017_bib72","doi-asserted-by":"crossref","first-page":"419","DOI":"10.1080\/07391102.2023.2281641","article-title":"Fighting against amyotrophic lateral sclerosis (ALS) with flavonoids: a computational approach to inhibit superoxide dismutase (SOD1) mutant aggregation","volume":"43","author":"Noorbakhsh Varnosfaderani","year":"2025","journal-title":"J. Biomol. Struct. Dyn."},{"key":"10.1016\/j.bbrc.2025.153017_bib73","article-title":"Taming the ringmaster of the genome (PCNA): phytomolecules for anticancer therapy against a potential non-oncogenic target","volume":"337","author":"Bhardwaj","year":"2021","journal-title":"J. Mol. Liq."},{"key":"10.1016\/j.bbrc.2025.153017_bib74","doi-asserted-by":"crossref","DOI":"10.1016\/j.comptc.2022.113929","article-title":"Comparative analyses and molecular videography of MD simulations on WT human SOD1","volume":"1217","author":"Workman","year":"2022","journal-title":"Comput. Theor. Chem."},{"key":"10.1016\/j.bbrc.2025.153017_bib75","author":"Study"},{"key":"10.1016\/j.bbrc.2025.153017_bib76","doi-asserted-by":"crossref","first-page":"2461","DOI":"10.1021\/acschemneuro.3c00276","article-title":"Myricetin: a potent anti-amyloidogenic polyphenol against superoxide dismutase 1 aggregation","volume":"14","author":"Sharma","year":"2023","journal-title":"ACS Chem. Neurosci."},{"key":"10.1016\/j.bbrc.2025.153017_bib77","series-title":"Protein Thermal Stability , Hydrogen Bonds , and Ion Pairs","author":"Vogt","year":"1997"},{"key":"10.1016\/j.bbrc.2025.153017_bib78","doi-asserted-by":"crossref","first-page":"378","DOI":"10.1016\/j.jmgm.2017.09.014","article-title":"Journal of Molecular graphics and modelling regression model for predicting pathogenic properties of SOD1 mutants based on the analysis of conformational stability and conservation of hydrogen bonds","volume":"77","author":"Alemasov","year":"2017","journal-title":"J. Mol. Graph. Model."},{"key":"10.1016\/j.bbrc.2025.153017_bib79","doi-asserted-by":"crossref","first-page":"1502","DOI":"10.1071\/CH12316","article-title":"Role of cation in enhancing the conversion of the Alzheimer's peptide into amyloid fibrils using protic ionic liquids","volume":"65","author":"Debeljuh","year":"2012","journal-title":"Aust. J. Chem."},{"key":"10.1016\/j.bbrc.2025.153017_bib80","doi-asserted-by":"crossref","first-page":"1093","DOI":"10.1007\/s00894-009-0454-9","article-title":"Solvent accessible surface area approximations for rapid and accurate protein structure prediction","volume":"15","author":"Durham","year":"2009","journal-title":"J. Mol. Model."},{"key":"10.1016\/j.bbrc.2025.153017_bib81","doi-asserted-by":"crossref","first-page":"588","DOI":"10.1110\/ps.06002","article-title":"High probability of disrupting a disulphide bridge mediated by an endogenous excited tryptophan residue","volume":"11","author":"Neves\u2010Petersen","year":"2002","journal-title":"Protein Sci."},{"key":"10.1016\/j.bbrc.2025.153017_bib82","doi-asserted-by":"crossref","first-page":"1191","DOI":"10.1016\/S0006-3495(95)80295-X","article-title":"Approaches to teaching fluorescence spectroscopy","volume":"68","author":"Royer","year":"1995","journal-title":"Biophys. J."},{"key":"10.1016\/j.bbrc.2025.153017_bib83","doi-asserted-by":"crossref","first-page":"12306","DOI":"10.1021\/jp2071925","article-title":"New insight into molecular interactions of imidazolium ionic liquids with bovine serum albumin","volume":"115","author":"Shu","year":"2011","journal-title":"J. Phys. Chem. B"},{"key":"10.1016\/j.bbrc.2025.153017_bib84","doi-asserted-by":"crossref","first-page":"468","DOI":"10.1016\/j.jpba.2008.11.035","article-title":"Study of curcumin and genistein interactions with human serum albumin","volume":"49","author":"Mandeville","year":"2009","journal-title":"J. Pharm. Biomed. Anal."},{"key":"10.1016\/j.bbrc.2025.153017_bib85","doi-asserted-by":"crossref","first-page":"1159","DOI":"10.1016\/j.colsurfa.2013.08.045","article-title":"Synthesis and binding with BSA of a new gemini surfactant","volume":"436","author":"Wang","year":"2013","journal-title":"Colloids Surfaces A Physicochem. Eng. Asp."},{"key":"10.1016\/j.bbrc.2025.153017_bib86","doi-asserted-by":"crossref","first-page":"253","DOI":"10.1016\/j.molliq.2018.09.075","article-title":"Effect of cations and anions of ionic liquids on the stability and activity of lysozyme: concentration and temperature effect","volume":"272","author":"Kumari","year":"2018","journal-title":"J. Mol. Liq."},{"key":"10.1016\/j.bbrc.2025.153017_bib87","doi-asserted-by":"crossref","first-page":"582","DOI":"10.1016\/j.ijbiomac.2021.03.113","article-title":"The role of amyloid oligomers in neurodegenerative pathologies","volume":"181","author":"Wells","year":"2021","journal-title":"Int. J. Biol. Macromol."},{"key":"10.1016\/j.bbrc.2025.153017_bib88","doi-asserted-by":"crossref","first-page":"589","DOI":"10.1042\/bj2820589","article-title":"Spectrofluorimetric assessment of the surface hydrophobicity of proteins","volume":"282","author":"Cardamone","year":"1992","journal-title":"Biochem. J."},{"key":"10.1016\/j.bbrc.2025.153017_bib89","doi-asserted-by":"crossref","first-page":"252","DOI":"10.1016\/j.jtice.2016.04.006","article-title":"Experimental and theoretical studies on some selected ionic liquids with different cations\/anions as corrosion inhibitors for mild steel in acidic medium","volume":"64","author":"Yesudass","year":"2016","journal-title":"J. Taiwan Inst. Chem. Eng."},{"key":"10.1016\/j.bbrc.2025.153017_bib90","doi-asserted-by":"crossref","first-page":"2643","DOI":"10.1016\/j.ijbiomac.2017.10.152","article-title":"Influence of the ionic liquid 1-butyl-3-methylimidazolium bromide on amyloid fibrillogenesis in lysozyme: evidence from photophysical and imaging studies","volume":"107","author":"Basu","year":"2018","journal-title":"Int. J. Biol. Macromol."},{"key":"10.1016\/j.bbrc.2025.153017_bib91","doi-asserted-by":"crossref","first-page":"2328","DOI":"10.1016\/j.bbamem.2013.04.012","article-title":"ATR-FTIR: a \u201crejuvenated\u201d tool to investigate amyloid proteins","volume":"1828","author":"Sarroukh","year":"2013","journal-title":"Biochim. Biophys. Acta, Biomembr."},{"key":"10.1016\/j.bbrc.2025.153017_bib92","doi-asserted-by":"crossref","first-page":"378","DOI":"10.1094\/CCHEM.2003.80.4.378","article-title":"Factors associated with dough stickiness as sensed by attenuated total reflectance infrared spectroscopy","volume":"80","author":"van Velzen","year":"2003","journal-title":"Cereal Chem."},{"key":"10.1016\/j.bbrc.2025.153017_bib93","doi-asserted-by":"crossref","first-page":"3770","DOI":"10.1021\/bm201005k","article-title":"Peptide mixtures can self-assemble into large amyloid fibers of varying size and morphology","volume":"12","author":"Ridgley","year":"2011","journal-title":"Biomacromolecules"},{"key":"10.1016\/j.bbrc.2025.153017_bib94","doi-asserted-by":"crossref","first-page":"592","DOI":"10.1039\/D0CB00203H","article-title":"Membrane composition and lipid to protein ratio modulate amyloid kinetics of yeast prion protein","volume":"2","author":"Bandyopadhyay","year":"2021","journal-title":"RSC Chem. Biol."},{"key":"10.1016\/j.bbrc.2025.153017_bib95","doi-asserted-by":"crossref","first-page":"404","DOI":"10.1002\/pro.5560020312","article-title":"Thioflavine T interaction with synthetic Alzheimer's disease \u03b2\u2010amyloid peptides: detection of amyloid aggregation in solution","volume":"2","author":"Levine","year":"1993","journal-title":"Protein Sci."},{"key":"10.1016\/j.bbrc.2025.153017_bib96","series-title":"Amyloid Amyloidosis 1990 Vith Int. Symp. Amyloidosis August 5\u20138, 1990","first-page":"393","article-title":"Fluorometric examination of tissue amyloid fibrils in murine senile amyloidosis: use of the fluorescent indicator, thioflavine T","author":"Naiki","year":"1991"},{"key":"10.1016\/j.bbrc.2025.153017_bib97","doi-asserted-by":"crossref","first-page":"170","DOI":"10.1016\/j.biochi.2022.05.001","article-title":"Biochimie Zinc binding loop mutations of hSOD1 promote amyloid fi brils under physiological conditions : implications for initiation of amyotrophic lateral sclerosis","volume":"199","author":"Baziyar","year":"2022","journal-title":"Biochimie"},{"key":"10.1016\/j.bbrc.2025.153017_bib98","doi-asserted-by":"crossref","DOI":"10.1016\/j.cbi.2019.108884","article-title":"Pyridine-2,3-dicarboxylate, quinolinic acid, induces 1N4R Tau amyloid aggregation in vitro: another evidence for the detrimental effect of the inescapable endogenous neurotoxin","volume":"315","author":"Esmaeili","year":"2020","journal-title":"Chem. Biol. Interact."},{"key":"10.1016\/j.bbrc.2025.153017_bib99","doi-asserted-by":"crossref","first-page":"67","DOI":"10.1016\/j.abb.2008.04.028","article-title":"Appraisal of casein's inhibitory effects on aggregation accompanying carbonic anhydrase refolding and heat-induced ovalbumin fibrillogenesis","volume":"477","author":"Khodarahmi","year":"2008","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/j.bbrc.2025.153017_bib100","doi-asserted-by":"crossref","first-page":"1570","DOI":"10.1016\/j.bbapap.2008.08.007","article-title":"Polyphenol-induced dissociation of various amyloid fibrils results in a methionine-independent formation of ROS","volume":"1784","author":"Shoval","year":"2008","journal-title":"Biochim. Biophys. Acta, Proteins Proteomics"},{"key":"10.1016\/j.bbrc.2025.153017_bib101","doi-asserted-by":"crossref","first-page":"290","DOI":"10.1016\/j.ijbiomac.2015.01.022","article-title":"Mitochondrial membrane disruption by aggregation products of ALS-causing superoxide dismutase-1 mutants","volume":"75","author":"Salehi","year":"2015","journal-title":"Int. J. Biol. Macromol."},{"key":"10.1016\/j.bbrc.2025.153017_bib102","doi-asserted-by":"crossref","first-page":"1129","DOI":"10.1021\/acschemneuro.9b00677","article-title":"Quercetin and baicalein act as potent antiamyloidogenic and fibril destabilizing agents for SOD1 fibrils","volume":"11","author":"Bhatia","year":"2020","journal-title":"ACS Chem. Neurosci."},{"key":"10.1016\/j.bbrc.2025.153017_bib103","doi-asserted-by":"crossref","first-page":"1332","DOI":"10.1038\/s41593-018-0235-9","article-title":"Protein misfolding, aggregation, and conformational strains in neurodegenerative diseases","volume":"21","author":"Soto","year":"2018","journal-title":"Nat. Neurosci."},{"key":"10.1016\/j.bbrc.2025.153017_bib104","series-title":"Neurochem. Basis Brain Funct. Dysfunct.","article-title":"Trends of protein aggregation in neurodegenerative diseases","author":"Agbas","year":"2018"},{"key":"10.1016\/j.bbrc.2025.153017_bib105","series-title":"Uncovering the Protein Aggregation Process Through Effect of G41D Mutant SOD1 Charge Variation in ALS Disease","first-page":"1","author":"Waheed","year":"2025"}],"container-title":["Biochemical and Biophysical Research Communications"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0006291X25017334?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0006291X25017334?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,12,19]],"date-time":"2025-12-19T01:34:42Z","timestamp":1766108082000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0006291X25017334"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2025,12]]},"references-count":105,"alternative-id":["S0006291X25017334"],"URL":"https:\/\/doi.org\/10.1016\/j.bbrc.2025.153017","relation":{},"ISSN":["0006-291X"],"issn-type":[{"value":"0006-291X","type":"print"}],"subject":[],"published":{"date-parts":[[2025,12]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Modulation of amyloid formation in the hSOD1 R115G mutant by an ionic liquid ([BMIM][SCN])","name":"articletitle","label":"Article Title"},{"value":"Biochemical and Biophysical Research Communications","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.bbrc.2025.153017","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":"153017"}}