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Characterization of Uranyl (UO22+) ion binding to Amyloid Beta (Aβ) peptides : effects on Aβ structure and aggregationBerntsson, Elina; Vosough, Faraz; Noormägi, Andra; Padari, Kärt; Asplund, Fanny; Gielnik, Maciej; Paul, Suman; Jarvet, Jüri; Tõugu, Vello; Palumaa, PeepACS chemical neuroscience2023 / p. 2618-2633 : ill https://doi.org/10.1021/acschemneuro.3c00130 https://www.scopus.com/sourceid/19700172804 https://www.scopus.com/record/display.uri?eid=2-s2.0-85166386170&origin=inward&txGid=95211c42970240fa252c8a9971868db8 https://jcr.clarivate.com/jcr-jp/journal-profile?journal=ACS%20CHEM%20NEUROSCI&year=2023 https://www.webofscience.com/wos/woscc/full-record/WOS:001035034000001
Direct competition of ATCUN peptides with human serum albumin for copper(II) ions determined by LC-ICP MSNoormägi, Andra; Golubeva, Tatjana; Berntsson, Elina; Wärmländer, Sebastian K.T.S.; Tõugu, Vello; Palumaa, PeepACS omega2023 / p. 33912−33919 https://doi.org/10.1021/acsomega.3c04649 https://www.scopus.com/sourceid/21100828963 https://www.scopus.com/record/display.uri?eid=2-s2.0-85173171732&origin=inward&txGid=cb30adb8c605ad13cb3d3fe6c4cc5402 https://jcr.clarivate.com/jcr-jp/journal-profile?journal=ACS%20OMEGA&year=2023 https://www.webofscience.com/wos/woscc/full-record/WOS:001070106300001
Effect of agitation on the peptide ﬁbrillization: Alzheimer’s amyloid- b peptide 1-42 but not amylin and insulin ﬁbrils can grow under quiescent conditionsTiiman, Ann; Noormägi, Andra; Friedemann, Merlin; Krištal, Jekaterina; Palumaa, Peep; Tõugu, VelloJournal of peptide science2013 / p. 386-391 : ill https://doi.org/10.1002/psc.2513 https://www.scopus.com/sourceid/25898 https://www.scopus.com/record/display.uri?eid=2-s2.0-84877718000&origin=resultslist&sort=plf-f&src=s&sot=b&sdt=b&s=DOI%2810.1002%2Fpsc.2513%29&sessionSearchId=428e98ffe070f29e21a0d734bb8b86c9 https://jcr.clarivate.com/jcr-jp/journal-profile?journal=J%20PEPT%20SCI&year=2013 https://www.webofscience.com/wos/woscc/full-record/WOS:000318797200009
Effects of Zn2+ ions and environmental conditions on the fibrillization of insulin = Zn2+ ioonide ja keskkonnatingimuste mõju insuliini fibrillisatsioonileNoormägi, Andra2018 https://digi.lib.ttu.ee/i/?10378 https://www.ester.ee/record=b5148492*est
Evaluation of Zn2+- and Cu2+-binding affinities of native Cu,Zn-SOD1 and its G93A mutant by LC-ICP MSSmirnova, Julia; Gavrilova, Julia; Noormägi, Andra; Valmsen, Karin; Pupart, Hegne; Luo, Jinghui; Tõugu, Vello; Palumaa, PeepMolecules2022 / art. 3160 https://doi.org/10.3390/molecules27103160 https://www.scopus.com/sourceid/26370 https://www.scopus.com/record/display.uri?eid=2-s2.0-85131659565&origin=inward&txGid=3c41f6cc45e315b3594bc4b8cf30e559 https://jcr.clarivate.com/jcr-jp/journal-profile?journal=MOLECULES&year=2022 https://www.webofscience.com/wos/woscc/full-record/WOS:000802673200001
Insulin fibrillization at acidic and physiological pH values is controlled by different molecular mechanismsNoormägi, Andra; Valmsen, Karin; Tõugu, Vello; Palumaa, PeepThe protein journal2015 / p. 398-403 : ill https://doi.org/10.1007/s10930-015-9634-x https://www.scopus.com/sourceid/144932 https://www.scopus.com/record/display.uri?eid=2-s2.0-84949322734&origin=inward&txGid=e03e5e7565e4e0cc5d58d488d87e8348 https://jcr.clarivate.com/jcr-jp/journal-profile?journal=PROTEIN%20J&year=2015 https://www.webofscience.com/wos/woscc/full-record/WOS:000366138200002
Interference of low-molecular substances with the thioflavin-T fluorescence assay of amyloid fibrilsNoormägi, Andra; Primar, Kateryna; Tõugu, Vello; Palumaa, PeepJournal of peptide science2012 / p. 59-64 : ill https://pubmed.ncbi.nlm.nih.gov/22083646/
Mercury and Alzheimer’s disease: Hg(II) ions display specific binding to the amyloid-β peptide and hinder its fibrillizationWallin, Cecilia; Friedemann, Merlin; Sholts, Sabrina B.; Noormägi, Andra; Svantesson, Teodor; Järvet, Jüri; Roos, Per M.; Palumaa, Peep; Gräslund, Astrid; Wärmländer, Sebastian K.T.S.Biomolecules2020 / art. 44, 23 p. : ill https://doi.org/10.3390/biom10010044 https://www.scopus.com/sourceid/21100394188 https://www.scopus.com/record/display.uri?eid=2-s2.0-85077389109&origin=inward&txGid=0dcd3d40321c47116786bc0ff7d528e5 https://jcr.clarivate.com/jcr-jp/journal-profile?journal=BIOMOLECULES&year=2022 https://www.webofscience.com/wos/woscc/full-record/WOS:000514863200133
Mercury ion binding to apolipoprotein E variants ApoE2, ApoE3, and ApoE4 : similar binding affinities but different structure induction effectsBerntsson, Elina; Sardis, Merlin; Noormägi, Andra; Jarvet, Jüri; Roos, Per M.; Tõugu, Vello; Gräslund, Astrid; Wärmländer, Sebastian K.T.S.ACS omega2022 / p. 28924-28931 https://doi.org/10.1021/acsomega.2c02254 https://www.scopus.com/sourceid/21100828963 https://www.scopus.com/record/display.uri?eid=2-s2.0-85136739342&origin=inward&txGid=110b3b975d0c6e2bc3b90942b092ef4a https://jcr.clarivate.com/jcr-jp/journal-profile?journal=ACS%20OMEGA&year=2022 https://www.webofscience.com/wos/woscc/full-record/WOS:000846759000001
Zn(II) ions co-secreted with insulin suppress inherent amyloidogenic properties of monomeric insulinNoormägi, Andra; Gavrilova, Julia; Smirnova, Julia; Tõugu, Vello; Palumaa, PeepBiochemical journal2010 / p. 511-518 https://pubmed.ncbi.nlm.nih.gov/20632994/
Zn(II) ions inhibit fibrillization of monomeric insulinNoormägi, Andra; Gavrilova, Julia; Smirnova, Julia; Tõugu, Vello; Palumaa, PeepFEBS journal2010 / Suppl. 1, p. 256
The role of initial oligomers in amyloid fibril formation by human stefin BTaler-Verčič, Ajda; Kirsipuu, Tiina; Friedemann, Merlin; Noormägi, Andra; Smirnova, Julia; Palumaa, PeepInternational journal of molecular sciences2013 / p. 18362-18384 : ill https://doi.org/10.3390/ijms140918362 https://www.scopus.com/sourceid/25879 https://www.scopus.com/record/display.uri?eid=2-s2.0-84883623248&origin=resultslist&sort=plf-f&src=s&sot=b&sdt=b&s=DOI%2810.3390%2Fijms140918362%29&sessionSearchId=cd64ce411d818e3304406c7bf07ccfcb https://jcr.clarivate.com/jcr-jp/journal-profile?journal=INT%20J%20MOL%20SCI&year=2013 https://www.webofscience.com/wos/woscc/full-record/WOS:000328623900059