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

Application of Differentiated SH-SY5Y Cells for Toxicological Studies of Alzheimer’s Amyloid Beta Peptide = Diferentseeritud SH-SY5Y rakkude kasutamine Alzheimeri amüloid beeta peptiidi toksilisuse uurimiseksKrištal, Jekaterina2020 https://digikogu.taltech.ee/et/Item/8aef400a-e1ff-4803-a0da-fc2d97c8d451

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

Chemical modification of met and his residues of amyloid β peptide. Influence of copper ions and effect on fibrillization = Metioniini ja histidiini jääkide keemiline modifitseerimine amüloid-β peptiidis. Vaskioonide mõju ja efekt fibrillisatsioonileSardis, Merlin2021 https://doi.org/10.23658/taltech.19/2021 https://www.ester.ee/record=b5416905*est https://digikogu.taltech.ee/et/Item/acced69c-c690-4cb5-a972-48e1c4ae5c66

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

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

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

Faculty of Science : [Tallinn University of Technology]2012 https://www.ester.ee/record=b2890162*est

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 Alzheimer's amyloid-ß peptides with Zn(II) and Cu(II) ions = Alzheimeri amüloid-ß peptiidide interaktsioonid Zn(II) ja Cu(II) ioonidegaTiiman, Ann2012 https://www.ester.ee/record=b2866174*est

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

Kemofoobia - ülearune paanika või põhjendatud hirmKinnunen, KatariinaStudioosus2021 / lk. 34-35 : fot https://www.ester.ee/record=b1558644*est

3. osa. Ensüümkatalüüsi põhimõisted ja kineetikaBiokeemia : lühikursus : õpik kõrgkoolidele2016 / lk. 67-127 : 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

Mürgistus koliinesteraasi inhibiitoriga - mida see tähendab?Lauri, Vahurerr.ee2020 / fot Mürgistus koliinesteraasi inhibiitoriga - mida see tähendab?

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

Role of metal ions in amyloidogenic properties of insulin and superoxide dismutase = Metallioonide roll insuliini ja superoksiidi dismutaasi amüloidogeensetes omadustesGavrilova, Julia2022 https://doi.org/10.23658/taltech.44/2022 https://digikogu.taltech.ee/et/Item/693de590-2d9f-43d6-989e-ebac0544151d https://www.ester.ee/record=b5511706*est

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

Üks küsimus : milline on teie jaoks ideaalne ülikool?Mente et Manu2020 / lk. 24-25 , 34-35, 44-45 : portr https://www.ester.ee/record=b1242496*est

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