{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,3]],"date-time":"2026-10-03T03:47:03Z","timestamp":1790999223625,"version":"4.1.0"},"reference-count":51,"publisher":"MDPI AG","issue":"9","license":[{"start":{"date-parts":[[2021,9,15]],"date-time":"2021-09-15T00:00:00Z","timestamp":1631664000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":["www.mdpi.com"],"crossmark-restriction":true},"short-container-title":["Antioxidants"],"abstract":"<jats:p>In order to study how polyphenols and vitamin C (vitC) together affect protein aggregation to amyloid fibrils, we performed similar in vitro studies as before using stefin B as a model and a potentially amyloid-forming protein (it aggregates upon overexpression, under stressful conditions and some progressive myoclonus epilepsy of tape 1\u2014EPM1-missense mutations). In addition to the chosen polyphenol, this time, we added a proven antioxidant concentration of 0.5 mM vitC into the fibrillation mixture and varied concentrations of resveratrol, quercetin, and curcumin. Synergy with vitC was observed with curcumin and quercetin.<\/jats:p>","DOI":"10.3390\/antiox10091471","type":"journal-article","created":{"date-parts":[[2021,9,15]],"date-time":"2021-09-15T12:00:44Z","timestamp":1631707244000},"page":"1471","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":8,"title":["Synergy of the Inhibitory Action of Polyphenols Plus Vitamin C on Amyloid Fibril Formation: Case Study of Human Stefin B"],"prefix":"10.3390","volume":"10","author":[{"given":"Alma","family":"Jahi\u0107 Mujki\u0107","sequence":"first","affiliation":[{"name":"Department of Biochemistry and Molecular and Structural Biology, Jo\u017eef Stefan Institute, Jamova 39, 1000 Ljubljana, Slovenia"},{"name":"Department of Biochemistry, Faculty of Pharmacy, University of Tuzla, Univerzitetska 1, 75000 Tuzla, Bosnia and Herzegovina"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Magda","family":"Tu\u0161ek \u017dnidari\u010d","sequence":"additional","affiliation":[{"name":"Department of Biotechnology and Systems Biology, National Institute of Biology, Ve\u010dna pot 111, 1000 Ljubljana, Slovenia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Selma","family":"Berbi\u0107","sequence":"additional","affiliation":[{"name":"Department of Biochemistry, Faculty of Pharmacy, University of Tuzla, Univerzitetska 1, 75000 Tuzla, Bosnia and Herzegovina"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-9793-8200","authenticated-orcid":false,"given":"Eva","family":"\u017derovnik","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Molecular and Structural Biology, Jo\u017eef Stefan Institute, Jamova 39, 1000 Ljubljana, Slovenia"},{"name":"Jo\u017eef Stefan International Postgraduate School, Jamova 39, 1000 Ljubljana, Slovenia"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2021,9,15]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"729","DOI":"10.1038\/418729a","article-title":"Getting out of shape","volume":"418","author":"Dobson","year":"2002","journal-title":"Nature"},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/S0167-4838(01)00295-3","article-title":"Human stefin B readily forms amyloid fibrils in vitro","volume":"1594","author":"Zerovnik","year":"2002","journal-title":"Biochim. 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