Affinity of zinc and copper ions for insulin monomersGavrilova, Julia; Tõugu, Vello; Palumaa, PeepMetallomics2014 / p. 1296-1300 : ill

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

Binding of zinc(II) and copper(II) to the full-length Alzheimer's amyloid-[beeta] peptideTõugu, Vello; Karafin, Ann; Palumaa, PeepJournal of neurochemistry2008 / p. 1249-1259 : ill https://pubmed.ncbi.nlm.nih.gov/18289347/

1,1'-bis(anilino)-4-,4'-bis(naphtalene)-8,8'-disulfonate acts as an inhibitor of lipoprotein lipase and competes for binding with apolipoprotein CIILõokene, Aivar; Zhang, L.; Tõugu, Vello; Olivecrona, G.Journal of biological chemistry2003 / p. 37183-37194 https://doi.org/10.1074/jbc.m303894200

Coordination of zinc ions to the key proteins of neurodegenerative diseases: A[beeta], APP, [alfa]-synuclein and PrPTõugu, Vello; Palumaa, PeepCoordination chemistry reviews2012 / p. 2219-2224 : ill https://www.researchgate.net/publication/236131300_Coordination_of_zinc_ions_to_the_key_proteins_of_neurodegenerative_diseases_Ab_APP_a-synuclein_and_PrP

Copper(I)-binding properties of de-coppering drugs for the treatment of Wilson disease. α-Lipoic acid as a potential anti-copper agentSmirnova, Julia; Kabin, Ekaterina; Järving, Ivar; Bragina, Olga; Tõugu, Vello; Plitz, Thomas; Palumaa, PeepScientific reports2018 / art. 1463, 9 p. : ill https://doi.org/10.1038/s41598-018-19873-2 Journal metrics at Scopus Article at Scopus Journal metrics at WOS Article at WOS

Copper(I)-binding properties of de-coppering drugs for treatment of Wilson diseaseSmirnova, Julia; Kabin, Ekaterina; Järving, Ivar; Tõugu, Vello; Plitz, T.; Palumaa, PeepThe FEBS journal2017 / p. 337 https://doi.org/10.1111/febs.14174

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 Journal metrics at Scopus Article at Scopus Journal metrics at WOS Article at WOS

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 Journal metrics at Scopus Article at Scopus Journal metrics at WOS Article at WOS

Direct competition of ATCUN peptides with human serum albumin for copper(II) ions determined by LC-ICP MSNoormägi, Andra; Golubeva, Tatjana; Berntssson, Elina; Warmländer, Sebastian K.T.S.; Tõugu, Vello; Palumaa, PeepACS omega2023 / p. 33912−33919 https://doi.org/10.1021/acsomega.3c04649

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

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

Effect of Zn(II) and Cu(II) ions on aggregation and fibrillation of amyloid-beta(1-42) peptidePalumaa, Peep; Karafin, Ann; Zovo, Kairit; Chung, Roger S.; Howells, Claire; West, Adrian K.; Tõugu, VelloSinapsa Neuroscience Conference '09 : Ljubljana, 26-29 September 2009 : abstract book2009 / p. 34

Ensümaatilise atsüüliülekande reaktsiooni kasutamine orgaaniliste ühendite sünteesilTõugu, VelloXVI Eesti keemiapäevad : teaduskonverentsi ettekannete referaadid = 16th Estonian chemistry days : abstracts of scientific conference1995 / lk. 145-146

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 Journal metrics at Scopus Article at Scopus Journal metrics at WOS Article at WOS

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

In vitro fibrillization of Alzheimer's amyloid-β peptide (1-42)Tiiman, Ann; Krištal, Jekaterina; Palumaa, Peep; Tõugu, VelloAIP advances2015 / p. 092401-1 - 092401-12 : ill http://dx.doi.org/10.1063/1.4921071

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 http://dx.doi.org/10.1007/s10930-015-9634-x

Interactions of zinc(II) and copper(II) to the full-length Alzheimer's amyloid-B peptide in vitroKarafin, Ann; Palumaa, Peep; Tõugu, VelloFEBS journal2008 / Suppl. 1, p. 222

Interactions of Zn(II) and Cu(II) ions with Alzheimer’s amyloid-beta peptide. Metal ion binding, contribution to fibrillization and toxicityTõugu, Vello; Tiiman, Ann; Palumaa, PeepMetallomics2011 / p. 250-261 : ill

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

Label-free high-throughput screening assay for inhibitors of Alzheimer's amyloid-[beeta] peptide aggregation based on MALDI MSZovo, Kairit; Helk, Eneken; Karafin, Ann; Tõugu, Vello; Palumaa, PeepAnalytical chemistry2010 / p. 8558-8565

Lipase action on some non-triglyceride substratesVallikivi, Imre; Lille, Ülo; Lõokene, Aivar; Metsala, Andrus; Sikk, Peeter; Tõugu, Vello; Vija, Heiki; Villo, Ly; Parve, OmarJournal of molecular catalysis B : enzymatic2003 / 5/6, p. 279-298 : ill

Lipase-catalysed enantioselective hydrolysis : interpretation of the kinetic results in terms of frontier orbital localisationParve, Omar; Vallikivi, Imre; Metsala, Andrus; Lille, Ülo; Tõugu, Vello; Sikk, Peeter; Käämbre, Tuuli; Vija, Heiki; Pehk, TõnisTetrahedron1997 / 13, p. 4889-4900

Lipase-catalysed enantioselective hydrolysis of bicyclo[3.2.0]heptanol esters in supercritical carbon dioxideParve, Omar; Vallikivi, Imre; Lahe, Lilja; Metsala, Andrus; Lille, Ülo; Tõugu, Vello; Vija, Heiki; Pehk, TõnisBioorganic & medicinal chemistry letters1997 / 7, p. 811-816

"Lipolase" allub sekundaarsete alkoholide enantioeelistuse üldisele reeglile nii vesi kui ka superkriitilise SKCO2 keskkonnas = "Lipolase" obeys the general enantiopreference rule of secondary alcohols in water and supercritical (SC)CO2 media as wellLille, Ülo; Metsala, Andrus; Parve, Omar; Tõugu, Vello; Vija, HeikiXVII Eesti keemiapäevad : teaduskonverentsi ettekannete referaadid = 17th Estonian Chemistry Days : abstracts of scientific conference1996 / lk. 101-102

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 Journal metrics at Scopus Article at Scopus Journal metrics at WOS Article at WOS

Metallothionein 2A affects the cell respiration by suppressing the expression of mitochondrial protein cytochrome c oxidase subunit IIBragina, Olga; Gurjanova, Karina; Krištal, Jekaterina; Kulp, Maria; Karro, Niina; Tõugu, Vello; Palumaa, PeepJournal of bioenergetics and biomembranes2015 / p. 209-216 : ill http://dx.doi.org/10.1007/s10863-015-9609-9

Monitoring of A-beta fibrillization using an improved fluorimetric methodKarafin, Ann; Palumaa, Peep; Tõugu, VelloNew Trends in Alzheimer and Parkinson Disorders : ADPD 20092009 / p. 255-259 https://www.etis.ee/Portal/Publications/Display/979eb21d-601b-4aa1-b941-121eff184407

Monitoring of amyloid-beta fibrillization using an improved fluorimetric method [Electronic resource]Karafin, Ann; Palumaa, Peep; Tõugu, VelloNeurodegenerative diseases2009 / S1, Alzheimer's and Parkinson's Diseases : Advances, Concepts and New Challenges, p. 799 [CD-ROM] https://www.etis.ee/Portal/Publications/Display/979eb21d-601b-4aa1-b941-121eff184407

NMR monitoring of lipase-catalyzed reactions of prostaglandins : preliminary estimation of reaction velocitiesVallikivi, Imre; Järving, Ivar; Pehk, Tõnis; Samel, Nigulas; Tõugu, Vello; Parve, OmarJournal of molecular catalysis B : enzymatic2004 / p. 15-19 : ill

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

Redox and metal ion binding properties of human insulin-like growth factor 1 determined by electrospray ionization mass spectrometrySmirnova, Julia; Muhhina, Jekaterina; Tõugu, Vello; Palumaa, PeepBiochemistry2012 / p. 5851-5859 : ill https://pubs.acs.org/doi/10.1021/bi300494s

Redox properties of Cys2His2 and Cys4 zinc fingers determined by electrospray ionization mass spectrometrySmirnova, Julia; Kabin, Ekaterina; Tõugu, Vello; Palumaa, PeepFEBS Open Bio2018 / p. 923 - 931 https.//doi.org/10.1002/2211-5463.12422 Journal metrics at Scopus Article at Scopus Journal metrics at WOS Article at WOS

Surface carboxylation or PEGylation decreases CuO nanoparticles’ cytotoxicity to human cells in vitro without compromising their antibacterial propertiesKubo, Anna-Liisa; Vasiliev, Grigory; Vija, Heiki; Krištal, Jekaterina; Tõugu, Vello; Visnapuu, Meeri; Kisand, Vambola; Kahru, Anne; Bondarenko, OlesjaArchives of toxicology2020 / p. 1561-1573 : ill https://doi.org/10.1007/s00204-020-02720-7

Zn(II) and Cu(II)-induced non-fibrillar aggregates of amyloid-[beta](1-42) peptide are transformed to amyloid fibrils both spontaneously and under the influence of metal chelatorsTõugu, Vello; Karafin, Ann; Zovo, Kairit; Chung, Roger S.; Howells, Claire; West, Adrian; Palumaa, PeepJournal of neurochemistry2009 / 6, p. 1784-1795 : ill

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 missing link in the amyloid cascade of Alzheimer's disease - metal ionsTiiman, Ann; Palumaa, Peep; Tõugu, VelloNeurochemistry international2013 / p. 367-378 : ill

The modelling and kinetic investigation of the lipase-catalysed acetylation of steroisomeric prostaglandinsVallikivi, Imre; Fransson, Linda; Hult, Karl; Järving, Ivar; Pehk, Tõnis; Samel, Nigulas; Tõugu, Vello; Villo, Ly; Parve, OmarJournal of molecular catalysis B : enzymatic2005 / p. 62-69 : ill

Toxicity of amyloid beta 1-40 and 1-42 on SH-SY5Y cell lineKrištal, Jekaterina; Bragina, Olga; Metsla, Kristel; Palumaa, Peep; Tõugu, VelloSpringerPlus2015 / p. 21-22, P19 http://dx.doi.org/10.1186/2193-1801-4-S1-P19

Toxicity of amyloid-β peptides varies depending on differentiation route of SH-SY5Y cellsKrištal, Jekaterina; Metsla, Kristel; Bragina, Olga; Tõugu, Vello; Palumaa, PeepJournal of Alzheimer's disease2019 / p. 879−887 https://doi.org/10.3233/JAD-190705 Journal metrics at Scopus Article at Scopus Journal metrics at WOS Article at WOS

Vaskioonide roll Alzheimeri amüloidse beeta peptiide [p. o. peptiidi] agregatsioonil ja toksilisuselTõugu, Vello; Tiiman, Ann; Palumaa, PeepXXXII Eesti Keemiapäevad : teaduskonverentsi teesid2011 / lk. 102

α-Lipoic acid has the potential to normalize copper metabolism, which is dysregulated in Alzheimer’s diseaseMetsla, Kristel; Kirss, Sigrid; Laks, Katrina; Sildnik, Gertrud; Palgi, Mari; Palumaa, Teele; Tõugu, Vello; Palumaa, PeepJournal of Alzheimer's Disease2022 / p. 715-728 https://doi.org/10.3233/JAD-215026 Journal metrics at Scopus Article at Scopus Journal metrics at WOS Article at WOS

Электростатический солевой эффект во взаимодействиях ацетилхолинэстеразы и трипсина с катионными лигандами : автореферат диссертации ... кандидата химических наук (02.00.03)Tõugu, Vello1991 https://www.ester.ee/record=b1190402*est