{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,24]],"date-time":"2025-10-24T11:03:28Z","timestamp":1761303808198,"version":"build-2065373602"},"reference-count":65,"publisher":"Springer Science and Business Media LLC","issue":"7","license":[{"start":{"date-parts":[[2025,9,20]],"date-time":"2025-09-20T00:00:00Z","timestamp":1758326400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.springernature.com\/gp\/researchers\/text-and-data-mining"},{"start":{"date-parts":[[2025,9,20]],"date-time":"2025-09-20T00:00:00Z","timestamp":1758326400000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/www.springernature.com\/gp\/researchers\/text-and-data-mining"}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["Metab Brain Dis"],"DOI":"10.1007\/s11011-025-01677-9","type":"journal-article","created":{"date-parts":[[2025,9,20]],"date-time":"2025-09-20T08:54:06Z","timestamp":1758358446000},"update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Bay leaves: the neuroprotective dietary spice via inhibition of amyloid-like aggregation"],"prefix":"10.1007","volume":"40","author":[{"ORCID":"https:\/\/orcid.org\/0009-0008-6418-6808","authenticated-orcid":false,"given":"Nazish","family":"Mustafa","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Sana","family":"Khan","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Laila","family":"Anwar","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Mir Muhammad","family":"Uzairullah","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Huma Aslam","family":"Bhatti","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Syed Abid","family":"Ali","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-6559-766X","authenticated-orcid":false,"given":"Ghulam","family":"Abbas","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"297","published-online":{"date-parts":[[2025,9,20]]},"reference":[{"issue":"3","key":"1677_CR1","doi-asserted-by":"publisher","first-page":"237","DOI":"10.1038\/nrd3050","volume":"9","author":"A Aguzzi","year":"2010","unstructured":"Aguzzi A, O\u2019connor T (2010) Protein aggregation diseases: pathogenicity and therapeutic perspectives. Nat Rev Drug Discov 9(3):237","journal-title":"Nat Rev Drug Discov"},{"issue":"5","key":"1677_CR2","doi-asserted-by":"publisher","first-page":"561","DOI":"10.1038\/nsmb.1799","volume":"17","author":"M Ahmed","year":"2010","unstructured":"Ahmed M, Davis J, Aucoin D, Sato T, Ahuja S, Aimoto S et al (2010) Structural conversion of neurotoxic amyloid-\u03b21\u201342 oligomers to fibrils. Nat Struct Mol Biol 17(5):561","journal-title":"Nat Struct Mol Biol"},{"key":"1677_CR3","volume-title":"Collection of drugs (materia media)","author":"M Aqili Khorasani","year":"1992","unstructured":"Aqili Khorasani M (1992) Collection of drugs (materia media). Engelab\u2013e\u2013Eslami Publishing and Educational organization, Tehran"},{"issue":"4","key":"1677_CR4","doi-asserted-by":"publisher","DOI":"10.3390\/molecules27041210","volume":"27","author":"C Ma","year":"2022","unstructured":"Ma C, Hong F, Yang S (2022) Amyloidosis in Alzheimer\u2019s disease: pathogeny, etiology, and related therapeutic directions. Molecules 27(4):1210","journal-title":"Molecules"},{"key":"1677_CR5","doi-asserted-by":"publisher","first-page":"131","DOI":"10.1016\/j.conb.2021.03.003","volume":"69","author":"S Wegmann","year":"2021","unstructured":"Wegmann S, Biernat J, Mandelkow E (2021) A current view on Tau protein phosphorylation in Alzheimer\u2019s disease. Curr Opin Neurobiol 69:131\u2013138","journal-title":"Curr Opin Neurobiol"},{"issue":"1","key":"1677_CR6","doi-asserted-by":"publisher","first-page":"101","DOI":"10.2174\/1570159X13666150716165726","volume":"14","author":"H Ferreira-Vieira","year":"2016","unstructured":"Ferreira-Vieira H, Guimaraes TM, Silva IR, F., Ribeiro M, F (2016) Alzheimer\u2019s disease: targeting the cholinergic system. Curr Neuropharmacol 14(1):101\u2013115","journal-title":"Curr Neuropharmacol"},{"issue":"5","key":"1677_CR7","doi-asserted-by":"publisher","first-page":"519","DOI":"10.3892\/br.2016.630","volume":"4","author":"WJ Huang","year":"2016","unstructured":"Huang WJ, Zhang XIA, Chen WW (2016) Role of oxidative stress in Alzheimer\u2019s disease. Biomed Rep 4(5):519\u2013522","journal-title":"Biomed Rep"},{"issue":"4","key":"1677_CR8","doi-asserted-by":"publisher","first-page":"548","DOI":"10.1016\/j.bcp.2013.12.012","volume":"88","author":"SM de la Monte","year":"2014","unstructured":"de la Monte SM, Tong M (2014) Brain metabolic dysfunction at the core of Alzheimer\u2019s disease. Biochem Pharmacol 88(4):548\u2013559","journal-title":"Biochem Pharmacol"},{"issue":"7","key":"1677_CR9","doi-asserted-by":"publisher","first-page":"772","DOI":"10.1258\/ebm.2011.010355","volume":"236","author":"IV Murray","year":"2011","unstructured":"Murray IV, Proza JF, Sohrabji F, Lawler JM (2011) Vascular and metabolic dysfunction in Alzheimer\u2019s disease: a review. Exp Biol Med 236(7):772\u2013782","journal-title":"Exp Biol Med"},{"issue":"1","key":"1677_CR10","doi-asserted-by":"publisher","DOI":"10.1186\/s13195-022-01117-1","volume":"14","author":"AL Brand","year":"2022","unstructured":"Brand AL, Lawler PE, Bollinger JG, Li Y, Schindler SE, Li M, Bateman RJ (2022) The performance of plasma amyloid beta measurements in identifying amyloid plaques in Alzheimer\u2019s disease: a literature review. Alzheimers Res Ther 14(1):195","journal-title":"Alzheimers Res Ther"},{"issue":"1","key":"1677_CR11","doi-asserted-by":"publisher","DOI":"10.1038\/s41392-023-01484-7","volume":"8","author":"Y Zhang","year":"2023","unstructured":"Zhang Y, Chen H, Li R, Sterling K, Song W (2023) Amyloid \u03b2-based therapy for alzheimer\u2019s disease: challenges, successes and future. Signal Transduct Target Ther 8(1):248. https:\/\/doi.org\/10.1038\/s41392-023-01484-7","journal-title":"Signal Transduct Target Ther"},{"issue":"16","key":"1677_CR12","doi-asserted-by":"publisher","DOI":"10.3390\/ijms21165858","volume":"21","author":"MS Uddin","year":"2020","unstructured":"Uddin MS, Kabir MT, Rahman MS, Behl T, Jeandet P, Ashraf GM, Najda A, Bin-Jumah MN, El-Seedi HR, Abdel-Daim MM (2020) Revisiting the amyloid cascade hypothesis: from anti-A\u03b2 therapeutics to auspicious new ways for Alzheimer\u2019s disease. Int J Mol Sci 21(16):5858. https:\/\/doi.org\/10.3390\/ijms21165858","journal-title":"Int J Mol Sci"},{"issue":"19","key":"1677_CR13","doi-asserted-by":"publisher","DOI":"10.3390\/ijms241914794","volume":"24","author":"KS Orobets","year":"2023","unstructured":"Orobets KS, Karamyshev AL (2023) Amyloid precursor protein and Alzheimer\u2019s disease. Int J Mol Sci 24(19):14794","journal-title":"Int J Mol Sci"},{"issue":"1","key":"1677_CR14","doi-asserted-by":"publisher","first-page":"83","DOI":"10.3233\/JAD-215699","volume":"87","author":"CK Kim","year":"2022","unstructured":"Kim CK, Lee YR, Ong L, Gold M, Kalali A, Sarkar J (2022) Alzheimer\u2019s disease: key insights from two decades of clinical trial failures. J Alzheimers Dis 87(1):83\u2013100. https:\/\/doi.org\/10.3233\/JAD-215699","journal-title":"J Alzheimers Dis"},{"issue":"3","key":"1677_CR15","doi-asserted-by":"publisher","first-page":"512","DOI":"10.1016\/j.jalz.2019.09.085","volume":"16","author":"RJ Caselli","year":"2020","unstructured":"Caselli RJ, Langlais BT, Dueck AC, Chen Y, Su Y, Locke DEC, Woodruff BK, Reiman EM (2020) Neuropsychological decline up to 20 years before incident mild cognitive impairment. Alzheimers Dement 16(3):512\u2013523. https:\/\/doi.org\/10.1016\/j.jalz.2019.09.085","journal-title":"Alzheimers Dement"},{"issue":"19","key":"1677_CR16","doi-asserted-by":"publisher","first-page":"1924","DOI":"10.1001\/jama.2015.4668","volume":"313","author":"WJ Jansen","year":"2015","unstructured":"Jansen WJ, Ossenkoppele R, Knol DL, Tijms BM, Scheltens P, Verhey FR, Visser PJ, Amyloid Biomarker Study Group, Aalten P, Aarsland D, Alcolea D, Alexander M, Almdahl IS, Arnold SE, Baldeiras I, Barthel H, van Berckel BN, Bibeau K, Blennow K, Brooks DJ, Zetterberg H (2015) Prevalence of cerebral amyloid pathology in persons without dementia: a meta-analysis. JAMA 313(19):1924\u20131938. https:\/\/doi.org\/10.1001\/jama.2015.4668","journal-title":"JAMA"},{"issue":"3","key":"1677_CR17","doi-asserted-by":"publisher","first-page":"281","DOI":"10.2174\/1567205013666151218150322","volume":"13","author":"JC Vickers","year":"2016","unstructured":"Vickers JC, Mitew S, Woodhouse A, Fernandez-Martos CM, Kirkcaldie MT, Canty AJ, McCormack GH, King AE (2016) Defining the earliest pathological changes of Alzheimer\u2019s disease. Curr Alzheimer Res 13(3):281\u2013287. https:\/\/doi.org\/10.2174\/1567205013666151218150322","journal-title":"Curr Alzheimer Res"},{"key":"1677_CR18","doi-asserted-by":"publisher","first-page":"8473","DOI":"10.2147\/IJN.S179484","volume":"13","author":"KR Kanubaddi","year":"2018","unstructured":"Kanubaddi KR, Yang SH, Wu LW, Lee CH, Weng CF (2018) Nanoparticle-conjugated nutraceuticals exert prospectively palliative of amyloid aggregation. Int J Nanomed 13:8473\u20138485. https:\/\/doi.org\/10.2147\/IJN.S179484","journal-title":"Int J Nanomed"},{"issue":"10","key":"1677_CR19","doi-asserted-by":"publisher","first-page":"724","DOI":"10.1016\/j.neurol.2019.08.005","volume":"175","author":"GC Rom\u00e1n","year":"2019","unstructured":"Rom\u00e1n GC, Jackson RE, Gadhia R, Rom\u00e1n AN, Reis J (2019) Mediterranean diet: the role of long-chain \u03c9-3 fatty acids in fish; polyphenols in fruits, vegetables, cereals, coffee, tea, Cacao and wine; probiotics and vitamins in prevention of stroke, age-related cognitive decline, and Alzheimer disease. Rev Neurol 175(10):724\u2013741. https:\/\/doi.org\/10.1016\/j.neurol.2019.08.005","journal-title":"Rev Neurol"},{"issue":"1","key":"1677_CR20","doi-asserted-by":"publisher","first-page":"41","DOI":"10.1586\/14737175.2015.986101","volume":"15","author":"S Rigacci","year":"2015","unstructured":"Rigacci S, Stefani M (2015) Nutraceuticals and amyloid neurodegenerative diseases: a focus on natural phenols. Expert Rev Neurother 15(1):41\u201352. https:\/\/doi.org\/10.1586\/14737175.2015.986101","journal-title":"Expert Rev Neurother"},{"issue":"3","key":"1677_CR21","doi-asserted-by":"publisher","first-page":"186","DOI":"10.1016\/j.jalz.2007.04.381","volume":"3","author":"R Brookmeyer","year":"2007","unstructured":"Brookmeyer R, Johnson E, Ziegler-Graham K, Arrighi HM (2007) Forecasting the global burden of Alzheimer\u2019s disease. Alzheimers Dement 3(3):186\u2013191","journal-title":"Alzheimers Dement"},{"key":"1677_CR22","doi-asserted-by":"publisher","DOI":"10.1016\/j.arcmed.2012.09.009","author":"RJ Castellani","year":"2012","unstructured":"Castellani RJ, Perry G (2012) Pathogenesis and disease-modifying therapy in Alzheimer\u2019s disease: the flat line of progress. Arch Med Res. https:\/\/doi.org\/10.1016\/j.arcmed.2012.09.009","journal-title":"Arch Med Res"},{"key":"1677_CR23","doi-asserted-by":"publisher","first-page":"333","DOI":"10.1146\/annurev.biochem.75.101304.123901","volume":"75","author":"F Chiti","year":"2006","unstructured":"Chiti F, Dobson CM (2006) Protein misfolding, functional amyloid, and human disease. Annu Rev Biochem 75:333\u2013366","journal-title":"Annu Rev Biochem"},{"issue":"35","key":"1677_CR24","doi-asserted-by":"publisher","first-page":"32046","DOI":"10.1074\/jbc.M201750200","volume":"277","author":"KN Dahlgren","year":"2002","unstructured":"Dahlgren KN, Manelli AM, Stine WB, Baker LK, Krafft GA, LaDu MJ (2002) Oligomeric and fibrillar species of amyloid-\u03b2 peptides differentially affect neuronal viability. J Biol Chem 277(35):32046\u201332053","journal-title":"J Biol Chem"},{"key":"1677_CR25","unstructured":"Duke JA (1997) The green pharmacy: New discoveries in herbal remedies for common diseases and conditions from the world\u2019s foremost authority on healing herbs. Rodale"},{"key":"1677_CR26","doi-asserted-by":"crossref","unstructured":"Fa M, Orozco IJ, Francis YI, Saeed F, Gong Y, Arancio O (2010) Preparation of oligomeric \u03b2-amyloid1-42 and induction of synaptic plasticity impairment on hippocampal slices. J Visualized Experiments: JoVE (41)","DOI":"10.3791\/1884"},{"issue":"2\u20133","key":"1677_CR27","doi-asserted-by":"publisher","first-page":"213","DOI":"10.1016\/j.tox.2005.09.011","volume":"217","author":"\u0130 G\u00fcl\u00e7in","year":"2006","unstructured":"G\u00fcl\u00e7in \u0130 (2006) Antioxidant activity of caffeic acid (3, 4-dihydroxycinnamic acid). Toxicology 217(2\u20133):213\u2013220","journal-title":"Toxicology"},{"issue":"1","key":"1677_CR28","doi-asserted-by":"publisher","first-page":"118","DOI":"10.4062\/biomolther.2011.19.1.118","volume":"19","author":"A-R Ham","year":"2011","unstructured":"Ham A-R, Shin J-H, Oh K-b, Lee S-J, Nam K-W, Koo U et al (2011) Neuroprotective effect of the n-hexane extracts of Laurus nobilis L. in models of parkinsons disease. Biomol Ther 19(1):118\u2013125","journal-title":"Biomol Ther"},{"issue":"2","key":"1677_CR29","doi-asserted-by":"publisher","DOI":"10.3390\/antiox10020259","volume":"10","author":"I Brinza","year":"2021","unstructured":"Brinza I, Boiangiu RS, Hancianu M, Cioanca O, Erdogan Orhan I, Hritcu L (2021) Bay leaf (Laurus nobilis L.) incense improved Scopolamine-induced amnesic rats by restoring cholinergic dysfunction and brain antioxidant status. Antioxidants 10(2):259. https:\/\/doi.org\/10.3390\/antiox10020259","journal-title":"Antioxidants"},{"issue":"1","key":"1677_CR30","doi-asserted-by":"publisher","first-page":"9","DOI":"10.3844\/ajbbsp.2022.9.22","volume":"18","author":"AO Falade","year":"2022","unstructured":"Falade AO, Omolaiye GI, Adewole KE, Agunloye OM, Ishola AA, Okaiyeto K, Oboh G, Oguntibeju OO (2022) Aqueous extracts of bay leaf (Laurus nobilis) and rosemary (Rosmarinus officinalis) inhibit iron-induced lipid peroxidation and key-enzymes implicated in Alzheimer\u2019s disease in rat brain-in vitro. Am J Biochem Biotechnol 18(1):9\u201322. https:\/\/doi.org\/10.3844\/ajbbsp.2022.9.22","journal-title":"Am J Biochem Biotechnol"},{"key":"1677_CR31","doi-asserted-by":"crossref","unstructured":"Algabri SO, Doro BM, Abadi AM, Shiba MA, Salem AH Bay leaves have antimicrobial and antioxidant activities. Journal of Pathogen Research, 1(1), 3., Polovka M, Suhaj M (2018) (2010). Detection of caraway and bay leaves irradiation based on their extracts\u2019 antioxidant properties evaluation. Food chemistry, 119(1):391\u2013401","DOI":"10.1016\/j.foodchem.2009.07.005"},{"issue":"1","key":"1677_CR32","doi-asserted-by":"publisher","first-page":"391","DOI":"10.1016\/j.foodchem.2009.07.005","volume":"119","author":"M Polovka","year":"2010","unstructured":"Polovka M, Suhaj M (2010) Detection of caraway and bay leaves irradiation based on their extracts\u2019 antioxidant properties evaluation. Food Chem 119(1):391\u2013401","journal-title":"Food Chem"},{"issue":"2","key":"1677_CR33","first-page":"20","volume":"14","author":"S Ishtiaque","year":"2015","unstructured":"Ishtiaque S, Naz S, Soomro N, Khan K, Siddiqui R (2015) Antioxidant activity and total phenolics content of extracts from Murraya koenigii (curry leaves), Laurus nobilis (bay leaves), and Camellia sinensis (tea). Quaid-E-Awam Univ Res J Eng Sci Technol 14(2):20\u201325","journal-title":"Quaid-E-Awam Univ Res J Eng Sci Technol"},{"issue":"4","key":"1677_CR34","doi-asserted-by":"publisher","first-page":"611","DOI":"10.1021\/tx5000415","volume":"27","author":"S Pacifico","year":"2014","unstructured":"Pacifico S, Gallicchio M, Lorenz P, Duckstein SM, Potenza N, Galasso S, Monaco P (2014) Neuroprotective potential of Laurus nobilis antioxidant polyphenol-enriched leaf extracts. Chem Res Toxicol 27(4):611\u2013626","journal-title":"Chem Res Toxicol"},{"key":"1677_CR35","doi-asserted-by":"crossref","unstructured":"Haque MA, Kaur P, Islam A, Hassan MI (2022) Application of circular dichroism spectroscopy in studying protein folding, stability, and interaction. Advances in protein molecular and structural biology methods. Elsevier, pp 213\u2013224","DOI":"10.1016\/B978-0-323-90264-9.00014-3"},{"issue":"2","key":"1677_CR36","doi-asserted-by":"publisher","first-page":"639","DOI":"10.1016\/S0006-291X(05)80083-X","volume":"173","author":"K Hirayama","year":"1990","unstructured":"Hirayama K, Akashi S, Furuya M, Fukuhara K-i (1990) Rapid confirmation and revision of the primary structure of bovine serum albumin by ESIMS and frit-FAB LC\/MS. Biochem Biophys Res Commun 173(2):639\u2013646","journal-title":"Biochem Biophys Res Commun"},{"issue":"9","key":"1677_CR37","doi-asserted-by":"publisher","first-page":"1128","DOI":"10.1016\/j.bbapap.2007.06.008","volume":"1774","author":"NK Holm","year":"2007","unstructured":"Holm NK, Jespersen SK, Thomassen LV, Wolff TY, Sehgal P, Thomsen LA et al (2007) Aggregation and fibrillation of bovine serum albumin. Biochimica et Biophysica Acta (BBA) 1774(9):1128\u20131138","journal-title":"Biochimica et Biophysica Acta (BBA)"},{"issue":"2","key":"1677_CR38","doi-asserted-by":"publisher","first-page":"142","DOI":"10.1007\/s12035-011-8168-2","volume":"44","author":"R Kannappan","year":"2011","unstructured":"Kannappan R, Gupta SC, Kim JH, Reuter S, Aggarwal BB (2011) Neuroprotection by spice-derived nutraceuticals: you are what you eat! Mol Neurobiol 44(2):142\u2013159","journal-title":"Mol Neurobiol"},{"key":"1677_CR39","doi-asserted-by":"publisher","DOI":"10.1016\/j.ijbiomac.2025.143725","author":"S Basha","year":"2025","unstructured":"Basha S, Mukunda DC, Pai AR, Mahato KK (2025) Assessing amyloid fibrils and amorphous aggregates: a review. Int J Biol Macromol. https:\/\/doi.org\/10.1016\/j.ijbiomac.2025.143725","journal-title":"Int J Biol Macromol"},{"issue":"19","key":"1677_CR40","doi-asserted-by":"publisher","first-page":"3521","DOI":"10.1007\/s00018-018-2872-2","volume":"75","author":"Z Dhouafli","year":"2018","unstructured":"Dhouafli Z, Cuanalo-Contreras K, Hayouni EA, Mays CE, Soto C, Moreno-Gonzalez I (2018) Inhibition of protein misfolding and aggregation by natural phenolic compounds. Cell Mol Life Sci 75(19):3521\u20133538. https:\/\/doi.org\/10.1007\/s00018-018-2872-2","journal-title":"Cell Mol Life Sci"},{"issue":"2","key":"1677_CR41","doi-asserted-by":"publisher","first-page":"120","DOI":"10.34012\/jpms.v5i2.4401","volume":"5","author":"D Puspitasari","year":"2023","unstructured":"Puspitasari D, Suyono T, Chiuman L (2023) Effectiveness of bay leaf extract in reducing malondialdehyde levels. Jurnal Prima Medika Sains 5(2):120\u2013125","journal-title":"Jurnal Prima Medika Sains"},{"issue":"1","key":"1677_CR42","doi-asserted-by":"publisher","DOI":"10.1042\/BSR20181415","volume":"39","author":"EI Yakupova","year":"2019","unstructured":"Yakupova EI, Bobyleva LG, Vikhlyantsev IM, Bobylev AG (2019) Congo red and amyloids: history and relationship. Biosci Rep 39(1):BSR20181415. https:\/\/doi.org\/10.1042\/BSR20181415","journal-title":"Biosci Rep"},{"issue":"21","key":"1677_CR43","doi-asserted-by":"publisher","first-page":"8104","DOI":"10.1002\/anie.201916630","volume":"59","author":"A Espargar\u00f3","year":"2020","unstructured":"Espargar\u00f3 A, Llabr\u00e9s S, Saupe SJ, Curutchet C, Luque FJ, Sabat\u00e9 R (2020) On the binding of Congo Red to amyloid fibrils. Angew Chem Int Ed Engl 59(21):8104\u20138107. https:\/\/doi.org\/10.1002\/anie.201916630","journal-title":"Angew Chem Int Ed Engl"},{"issue":"1","key":"1677_CR44","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pone.0054541","volume":"8","author":"AM Streets","year":"2013","unstructured":"Streets AM, Sourigues Y, Kopito RR, Melki R, Quake SR (2013) Simultaneous measurement of amyloid fibril formation by dynamic light scattering and fluorescence reveals complex aggregation kinetics. PLoS One 8(1):e54541. https:\/\/doi.org\/10.1371\/journal.pone.0054541","journal-title":"PLoS One"},{"key":"1677_CR45","doi-asserted-by":"publisher","DOI":"10.1016\/j.jtemb.2021.126766","volume":"67","author":"E Shardlow","year":"2021","unstructured":"Shardlow E, Khan B, Exley C (2021) Monitoring the early aggregatory behaviour and size of A\u03b21-42 in the absence & presence of metal ions using dynamic light scattering. J Trace Elem Med Biology: Organ Soc Minerals Trace Elem (GMS) 67:126766. https:\/\/doi.org\/10.1016\/j.jtemb.2021.126766","journal-title":"J Trace Elem Med Biology: Organ Soc Minerals Trace Elem (GMS)"},{"issue":"3","key":"1677_CR46","doi-asserted-by":"publisher","first-page":"765","DOI":"10.1039\/C4AN01495B","volume":"140","author":"R Lu","year":"2015","unstructured":"Lu R, Li WW, Katzir A, Raichlin Y, Yu HQ, Mizaikoff B (2015) Probing the secondary structure of bovine serum albumin during heat-induced denaturation using mid-infrared fiberoptic sensors. Analyst 140(3):765\u2013770","journal-title":"Analyst"},{"issue":"5","key":"1677_CR47","doi-asserted-by":"publisher","first-page":"653","DOI":"10.1007\/BF01025605","volume":"8","author":"K Takeda","year":"1989","unstructured":"Takeda K, Wada A, Yamamoto K, Moriyama Y, Aoki K (1989) Conformational change of bovine serum albumin by heat treatment. J Protein Chem 8(5):653\u2013659. https:\/\/doi.org\/10.1007\/BF01025605","journal-title":"J Protein Chem"},{"key":"1677_CR48","doi-asserted-by":"publisher","first-page":"538","DOI":"10.1134\/S0006297916050114","volume":"81","author":"EI Grigorashvili","year":"2016","unstructured":"Grigorashvili EI, Selivanova OM, Dovidchenko NV, Dzhus UF, Mikhailina AO, Suvorina MY, Marchenkov VV, Surin AK, Galzitskaya OV (2016) Determination of size of folding nuclei of fibrils formed from recombinant A\u03b2 (1\u201340) peptide. Biochemistry (Moscow) 81:538\u2013547","journal-title":"Biochemistry (Moscow)"},{"issue":"15","key":"1677_CR49","doi-asserted-by":"publisher","first-page":"2687","DOI":"10.1016\/j.jmb.2019.04.044","volume":"431","author":"L Feng","year":"2019","unstructured":"Feng L, Watanabe H, Molino P, Wallace GG, Phung SL, Uchihashi T, Higgins MJ (2019) Dynamics of inter-molecular interactions between single A\u03b242 oligomeric and aggregate species by high-speed atomic force microscopy. J Mol Biol 431(15):2687\u20132699","journal-title":"J Mol Biol"},{"key":"1677_CR50","doi-asserted-by":"crossref","unstructured":"Ghosh P, Kumar A, Datta B, Rangachari V (2010, October) Dynamics of protofibril elongation and association involved in A\u03b242 peptide aggregation in alzheimer\u2019s disease. BMC bioinformatics, vol 11. BioMed Central, pp 1\u201319","DOI":"10.1186\/1471-2105-11-S6-S24"},{"issue":"2","key":"1677_CR51","doi-asserted-by":"publisher","first-page":"106","DOI":"10.2459\/JCM.0000000000000917","volume":"21","author":"R Proietti","year":"2020","unstructured":"Proietti R, AlTurki A, Vio R, Licchelli L, Rivezzi F, Marafi M, Russo Vincenzo, Potpara Tatjana S., Kalman Jonathan M., de Villers-Sidani Etiene, Bunch TJ (2020) The association between atrial fibrillation and Alzheimer\u2019s disease: fact or fallacy? A systematic review and meta-analysis. J Cardiovasc Med 21(2):106\u2013112","journal-title":"J Cardiovasc Med"},{"issue":"1","key":"1677_CR52","doi-asserted-by":"publisher","first-page":"61","DOI":"10.3233\/JAD-170970","volume":"62","author":"M Ihara","year":"2018","unstructured":"Ihara M, Washida K (2018) Linking atrial fibrillation with Alzheimer\u2019s disease: epidemiological, pathological, and mechanistic evidence. J Alzheimers Dis 62(1):61\u201372","journal-title":"J Alzheimers Dis"},{"key":"1677_CR53","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1186\/alzrt226","volume":"5","author":"EY Hayden","year":"2013","unstructured":"Hayden EY, Teplow DB (2013) Amyloid \u03b2-protein oligomers and Alzheimer\u2019s disease. Alzheimers Res Ther 5:1\u201311","journal-title":"Alzheimers Res Ther"},{"issue":"24","key":"1677_CR54","doi-asserted-by":"publisher","first-page":"5977","DOI":"10.1021\/acs.jpcb.7b04689","volume":"121","author":"VH Man","year":"2017","unstructured":"Man VH, Nguyen PH, Derreumaux P (2017) High-resolution structures of the amyloid-\u03b2 1\u201342 dimers from the comparison of four atomistic force fields. J Phys Chem B 121(24):5977\u20135987","journal-title":"J Phys Chem B"},{"issue":"5","key":"1677_CR55","doi-asserted-by":"publisher","first-page":"831","DOI":"10.1016\/j.neuron.2006.10.035","volume":"52","author":"H Hsieh","year":"2006","unstructured":"Hsieh H, Boehm J, Sato C, Iwatsubo T, Tomita T, Sisodia S, Malinow R (2006) AmpAR removal underlies A\u03b2-induced synaptic depression and dendritic spine loss. Neuron 52(5):831\u2013843","journal-title":"Neuron"},{"issue":"11","key":"1677_CR56","doi-asserted-by":"publisher","first-page":"4050","DOI":"10.1523\/JNEUROSCI.20-11-04050.2000","volume":"20","author":"L Mucke","year":"2000","unstructured":"Mucke L, Masliah E, Yu GQ, Mallory M, Rockenstein EM, Tatsuno G, McConlogue L (2000) High-level neuronal expression of A\u03b21\u201342 in wild-type human amyloid protein precursor transgenic mice: synaptotoxicity without plaque formation. J Neurosci 20(11):4050\u20134058","journal-title":"J Neurosci"},{"issue":"6880","key":"1677_CR57","doi-asserted-by":"publisher","first-page":"535","DOI":"10.1038\/416535a","volume":"416","author":"DM Walsh","year":"2002","unstructured":"Walsh DM, Klyubin I, Fadeeva JV, Cullen WK, Anwyl R, Wolfe MS, Selkoe DJ (2002) Naturally secreted oligomers of amyloid \u03b2 protein potently inhibit hippocampal long-term potentiation in vivo. Nature 416(6880):535\u2013539","journal-title":"Nature"},{"issue":"6","key":"1677_CR58","doi-asserted-by":"publisher","first-page":"925","DOI":"10.1016\/S0896-6273(03)00124-7","volume":"37","author":"F Kamenetz","year":"2003","unstructured":"Kamenetz F, Tomita T, Hsieh H, Seabrook G, Borchelt D, Iwatsubo T, Malinow R (2003) App processing and synaptic function. Neuron 37(6):925\u2013937","journal-title":"Neuron"},{"issue":"7","key":"1677_CR59","doi-asserted-by":"publisher","first-page":"a006338","DOI":"10.1101\/cshperspect.a006338","volume":"2","author":"L Mucke","year":"2012","unstructured":"Mucke L, Selkoe DJ (2012) Neurotoxicity of amyloid \u03b2-protein: synaptic and network dysfunction. Cold Spring Harbor Perspect Med 2(7):a006338. https:\/\/doi.org\/10.1101\/cshperspect.a006338","journal-title":"Cold Spring Harbor Perspect Med"},{"issue":"6","key":"1677_CR60","doi-asserted-by":"publisher","first-page":"788","DOI":"10.1016\/j.neuron.2009.05.012","volume":"62","author":"S Li","year":"2009","unstructured":"Li S, Hong S, Shepardson NE, Walsh DM, Shankar GM, Selkoe D (2009) Soluble oligomers of amyloid \u03b2 protein facilitate hippocampal long-term depression by disrupting neuronal glutamate uptake. Neuron 62(6):788\u2013801","journal-title":"Neuron"},{"key":"1677_CR61","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1186\/s13041-015-0163-5","volume":"8","author":"N Mamada","year":"2015","unstructured":"Mamada N, Tanokashira D, Hosaka A, Kametani F, Tamaoka A, Araki W (2015) Amyloid \u03b2-protein oligomers upregulate the \u03b2-secretase, BACE1, through a post-translational mechanism involving its altered subcellular distribution in neurons. Mol Brain 8:1\u201312","journal-title":"Mol Brain"},{"issue":"2","key":"1677_CR62","doi-asserted-by":"publisher","first-page":"145","DOI":"10.4062\/biomolther.2019.113","volume":"28","author":"EY Choi","year":"2019","unstructured":"Choi EY, Kang SS, Lee SK, Han BH (2019) Polyphenolic biflavonoids inhibit amyloid-beta fibrillation and disaggregate preformed amyloid-beta fibrils. Biomol Ther 28(2):145","journal-title":"Biomol Ther"},{"issue":"3","key":"1677_CR63","doi-asserted-by":"publisher","first-page":"608","DOI":"10.1016\/j.neuron.2014.10.038","volume":"84","author":"R Sperling","year":"2014","unstructured":"Sperling R, Mormino E, Johnson K (2014) The evolution of preclinical Alzheimer\u2019s disease: implications for prevention trials. Neuron 84(3):608\u2013622. https:\/\/doi.org\/10.1016\/j.neuron.2014.10.038","journal-title":"Neuron"},{"key":"1677_CR64","doi-asserted-by":"crossref","unstructured":"Pallavi MCP, Kumar HMS (2018) Nutraceuticals in prophylaxis and therapy of neurodegenerative diseases. Discovery and development of neuroprotective agents from natural products. Elsevier, pp 359\u2013376","DOI":"10.1016\/B978-0-12-809593-5.00008-2"},{"key":"1677_CR65","first-page":"8","volume":"12","author":"K Mahmood","year":"2020","unstructured":"Mahmood K, Saeed R, Naz T, Cheema MAR, Haleem DJ (2020) Nutraceuticals for prevention and treatment of neurodegenerative diseases. EC Neurol 12:8\u201312","journal-title":"EC Neurol"}],"container-title":["Metabolic Brain Disease"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1007\/s11011-025-01677-9.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/link.springer.com\/article\/10.1007\/s11011-025-01677-9\/fulltext.html","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1007\/s11011-025-01677-9.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,24]],"date-time":"2025-10-24T10:58:52Z","timestamp":1761303532000},"score":1,"resource":{"primary":{"URL":"https:\/\/link.springer.com\/10.1007\/s11011-025-01677-9"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2025,9,20]]},"references-count":65,"journal-issue":{"issue":"7","published-online":{"date-parts":[[2025,10]]}},"alternative-id":["1677"],"URL":"https:\/\/doi.org\/10.1007\/s11011-025-01677-9","relation":{},"ISSN":["1573-7365"],"issn-type":[{"type":"electronic","value":"1573-7365"}],"subject":[],"published":{"date-parts":[[2025,9,20]]},"assertion":[{"value":"16 May 2024","order":1,"name":"received","label":"Received","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"10 July 2025","order":2,"name":"accepted","label":"Accepted","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"20 September 2025","order":3,"name":"first_online","label":"First Online","group":{"name":"ArticleHistory","label":"Article History"}},{"order":1,"name":"Ethics","group":{"name":"EthicsHeading","label":"Declaration"}},{"value":"The study protocol was approved and strictly monitored by the Institutional Animal Ethical Committee (IAEC; animal study protocol no. ASP # 2017-0057) at the animal resource facility, ICCBS, University of Karachi.","order":2,"name":"Ethics","group":{"name":"EthicsHeading","label":"Ethical approval"}},{"value":"The authors declare no competing interests.","order":3,"name":"Ethics","group":{"name":"EthicsHeading","label":"Competing interests"}}],"article-number":"273"}}