• Amyloid beta 1-42 oligomerization in vitro and characterization with SDS-PAGE, MALDI and ESI MSFriedemann, Merlin; Tõugu, Vello; Kirsipuu, Tiina; Palumaa, PeepFEBS journal2013 / p. 140-141
• Copper(II) ions and the Alzheimer's amyloid-β peptide : affinity and stoichiometry of bindingTõugu, Vello; Friedemann, Merlin; Tiiman, Ann; Palumaa, PeepAIP conference proceedings2014 / p. 109-111
• Copper(II)-binding equilibria in human bloodKirsipuu, Tiina; Zadorožnaja, Anna; Smirnova, Julia; Friedemann, Merlin; Plitz, Thomas; Tõugu, Vello; Palumaa, PeepScientific reports2020 / art. 5686, 10 p. : ill https://doi.org/10.1038/s41598-020-62560-4 https://www.scopus.com/sourceid/21100200805 https://www.scopus.com/record/display.uri?eid=2-s2.0-85082732007&origin=inward&txGid=d991b1b7d93cab467022797bc4ec9f94 https://jcr.clarivate.com/jcr-jp/journal-profile?journal=SCI%20REP-UK&year=2022 https://www.webofscience.com/wos/woscc/full-record/WOS:000563300500011
• Cu(II) partially protects three histidine residues and the N-terminus of amyloid-β peptide from diethyl pyrocarbonate (DEPC) modificationFriedemann, Merlin; Tõugu, Vello; Palumaa, PeepFEBS Open Bio2020 / p. 1072-1081 https://doi.org/10.1002/2211-5463.12857 https://www.scopus.com/sourceid/21100197927 https://www.scopus.com/record/display.uri?eid=2-s2.0-85083998032&origin=inward&txGid=481a11020bdaebdfe49259e4e2ea2341 https://jcr.clarivate.com/jcr-jp/journal-profile?journal=FEBS%20OPEN%20BIO&year=2022 https://www.webofscience.com/wos/woscc/full-record/WOS:000529216200001
• 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
• Effect of methionine-35 oxidation on the aggregation of amyloid-β peptideFriedemann, Merlin; Helk, Eneken; Tiiman, Ann; Zovo, Kairit; Palumaa, Peep; Tõugu, VelloBiochemistry and biophysics reports2015 / p. 94-99 : ill http://dx.doi.org/10.1016/j.bbrep.2015.07.017
• Fibrillization of the mixtures of amyloid beta 1-40 and 1-42Krištal, Jekaterina; Friedemann, Merlin; Tõugu, Vello; Palumaa, PeepNeurodegenerative diseases2015 / p. 364 http://dx.doi.org/10.1159/000381736
• 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
• Oligomerization and conformation of amyloidogenic protein human stefin B. Insight from ESI MSKumm, Tiina; Taler-Verecic, Ajda; Skerget, Katja; Friedemann, Merlin; Zerovnik, Eva; Palumaa, PeepFEBS journal2010 / Suppl. 1, lk. 258
• Oxidation of Methionine-35 in Alzheimer's amyloid-beta peptide and the aggregation of the oxidized peptideFriedemann, Merlin; Helk, Eneken; Tiiman, Ann; Zovo, Kairit; Palumaa, Peep; Tõugu, VelloSpringerPlus2015 / p. 20, P13 http://dx.doi.org/10.1186/2193-1801-4-S1-P13
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