• A structural-dynamical characterization of human Cox17Banci, Lucia; Bertini, Ivano; Ciofi-Baffoni, Simone; Janicka, Anna; Martinelli, Manuele; Kozlowski, Henryk; Palumaa, PeepJournal of biological chemistry2008 / 12, p. 7912-7920 : ill https://pubmed.ncbi.nlm.nih.gov/18093982/
• Affinity gradients drive copper to cellular destinationsBanci, Lucia; Bertini, Ivano; Ciofi-Baffoni, Simone; Kozyreva, Tatiana; Zovo, Kairit; Palumaa, PeepNature2010 / p. 645-648 : ill https://doi.org/10.1038/nature09018
• Affinity of zinc and copper ions for insulin monomersGavrilova, Julia; Tõugu, Vello; Palumaa, PeepMetallomics2014 / p. 1296-1300 : ill https://doi.org/10.1039/c4mt00059e https://www.scopus.com/sourceid/19700173303 https://www.scopus.com/record/display.uri?eid=2-s2.0-84903576911&origin=inward&txGid=c134f20b2858424cdf549d3334dc5637 https://jcr.clarivate.com/jcr-jp/journal-profile?journal=METALLOMICS&year=2014 https://www.webofscience.com/wos/woscc/full-record/WOS:000338638000014
• Amino acid profiling in human follicular fluid and plasma of IVF patientsKirsipuu, Tiina; Laks, Katrina; Velthut, Agne; Palumaa, PeepFEBS journal2013 / p. 282
• 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
• Assessment of blood contamination in biological fluids using MALDI-TOF MSLaks, Katrina; Kirsipuu, Tiina; Dmitrijeva, Tuuli; Salumets, Andres; Palumaa, PeepThe protein journal2016 / 171-176 https://doi.org/10.1007/s10930-016-9657-y https://www.scopus.com/sourceid/144932 https://www.scopus.com/record/display.uri?eid=2-s2.0-84962214114&origin=inward&txGid=bd7c9754fd531a0cb17cff0add151fff https://jcr.clarivate.com/jcr-jp/journal-profile?journal=PROTEIN%20J&year=2016 https://www.webofscience.com/wos/woscc/full-record/WOS:000377917000001
• Assessment of blood contamination in biological fluids using MALDI-TOF MSLaks, Katrina; Kirsipuu, Tiina; Dmitrijeva, Tuuli; Salumets, Andres; Palumaa, PeepFEBS journal2013 / p. 489
• 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/
• Bioanorgaaniline keemia - probleemid ja perspektiivid metallotioneiini näitelPalumaa, PeepXXV Eesti keemiapäevad : teaduskonverentsi ettekannete referaadid = 25th Estonian Chemistry Days : abstracts of scientific conference1999 / lk. 126
• Biokeemia : lühikursus : õpik kõrgkoolideleTymoczko, John L; Berg, Jeremy M; Stryer, Lubert2016 https://www.ester.ee/record=b4562473*est
• Biological redox switchesPalumaa, PeepAntioxidants & redox signaling2009 / 5, p. 981-983 https://pubmed.ncbi.nlm.nih.gov/19186997/
• Brain-specific metallothionein-3 has higher metal-binding capacity than ubiquitous metallothioneins and binds metals noncooperativelyPalumaa, Peep; Eriste, Elo; Njunkova, Olga; Pokras, Lesja; Jornvall, H.; Sillard, RannarBiochemistry2002 / 19, p.6158-6163 https://pubmed.ncbi.nlm.nih.gov/11994011/
• 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
• 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
• Comparison of confirmations of zinc- and cadmium-substituted metallothionein-3 by ESI MSPalumaa, Peep; Eriste, Elo; Njunkova, Olga; Pokras, Lesja; Jörnvall, Hans; Sillard, RannarThe 50th ASMS Conference on Mass Spectrometry and Allied Topics2002 / ? p
• Comprehensive elucidation of amino acid profile in human follicular fluid and plasma of in vitro fertilization patientsKirsipuu, Tiina; Laks, Katrina; Velthut-Meikas, Agne; Levkov, Lev; Salumets, Andres; Palumaa, PeepGynecological endocrinology2015 / p. 9-17 : ill http://dx.doi.org/10.3109/09513590.2015.1085186
• 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 chaperones. The concept of conformational control in the metabolism of copperPalumaa, PeepFEBS letters2013 / p. 1902-1910 : ill https://www.scopus.com/sourceid/17481 https://www.scopus.com/record/display.uri?eid=2-s2.0-84878937497&origin=resultslist&sort=plf-f&src=s&sot=b&sdt=b&s=DOI%2810.1016%2Fj.febslet.2013.05.019%29&sessionSearchId=627c52b3557ef2545451d137647da466 https://jcr.clarivate.com/jcr-jp/journal-profile?journal=FEBS%20LETT&year=2013 https://www.webofscience.com/wos/woscc/full-record/WOS:000320910300012
• Copper metabolism in health and disease : focus on copper in adipogenesis and α-lipoic acid in Wilson disease = Vase ainevahetus tervise ja haiguse tingimustes : fookus vasele adipogeneesil ja α-lipoehappele Wilsoni tõve korralKabin, Ekaterina2023 https://doi.org/10.23658/taltech.69/2023 https://digikogu.taltech.ee/et/Item/6b47422f-75fd-4e9a-b16c-8edd3c3e201a https://www.ester.ee/record=b5645433*est
• 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 https://www.scopus.com/sourceid/21100200805 https://www.scopus.com/record/display.uri?eid=2-s2.0-85040995230&origin=inward&txGid=0840f1f33a09cb5d0bfdafe61faa86d7 https://jcr.clarivate.com/jcr-jp/journal-profile?journal=SCI%20REP-UK&year=2022 https://www.webofscience.com/wos/woscc/full-record/WOS:000423046600007
• 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 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
• Cox17, a copper chaperone for cytochrome c oxidase : expression, purification and formation of mixed disulphide adducts with thiol reagentsVoronova, Anastassia; Kazantseva, Jekaterina; Tuuling, Marina; Sokolova, Niina; Sillard, Rannar; Palumaa, PeepProtein expression and purification2007 / 1, p. 138-144 : ill https://www.sciencedirect.com/science/article/pii/S1046592806003901 https://www.sciencedirect.com/science/article/pii/S1046592806003901
• 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
• Determination of metal-protein complexes and posttranslational modifications by LC-(ESI-TOF)-MSSillard, Rannar; Eriste, Elo; Njunkova, Olga; Pokras, Lesja; Jörnvall, Hans; Wadensten, Henrik; Renlund, Staffan; Palumaa, PeepProceedings of the 49th ASMS Conference on Mass Spectrometry and Allied Topics : Chicago, Illinois, May 27-31, 20012001 / p. 11-12 : ill
• Direct competition of ATCUN peptides with human serum albumin for copper(II) ions determined by LC-ICP MSNoormägi, Andra; Golubeva, Tatjana; Berntsson, Elina; Warmländer, 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
• Eessõna eestikeelsele väljaandelePalumaa, PeepBiokeemia : lühikursus : õpik kõrgkoolidele2016 / 1 p https://www.ester.ee/record=b4562473*est
• Eesti biokeemik hoiatab: koroonaviirus püsib nakkusohtlikuna õhus mitu tundi, pindadel isegi mitu päeva!Palumaa, PeepÕhtuleht2020 / Lk. 6 https://tervis.ohtuleht.ee/995397/eesti-biokeemik-hoiatab-koroonaviirus-pusib-nakkusohtlikuna-ohus-mitu-tundi-pindadel-isegi-mitu-paeva https://www.ester.ee/record=b1408161*est
• Eesti biokeemik hoiatab: koroonaviirus võib olla inimest nakatavate viiruste seas absoluutne maailmameister! [Võrguteavik]Palumaa, PeepÕhtuleht2020 https://tervis.ohtuleht.ee/998137/eesti-biokeemik-hoiatab-koroonaviirus-voib-olla-inimest-nakatavate-viiruste-seas-absoluutne-maailmameister
• Eesti biokeemik hoiatab: ohtlik koroonaviirus suudab nõrga tervisega inimesele tekitada korvamatut kahjuPalumaa, PeepÕhtuleht.ee2020 https://tervis.ohtuleht.ee/996404/eesti-biokeemik-hoiatab-ohtlik-koroonaviirus-suudab-norga-tervisega-inimesele-tekitada-korvamatut-kahju
• Eesti biokeemik: iga samm võib olla saatuslik, pandeemia edukas läbimine sõltub tervisekäitumisestPalumaa, Peeptervis.ohtuleht.ee2020 / fot https://tervis.ohtuleht.ee/997553/eesti-biokeemik-iga-samm-voib-olla-saatuslik-pandeemia-edukas-labimine-soltub-tervisekaitumisest
• Eesti biokeemik: peame end kaitsma surmava viirusedoosi eest kõigi võimalike vahenditega!Palumaa, PeepÕhtuleht2020 / Lk. 4-5 : portr https://www.ester.ee/record=b1408161*est
• Eesti teadlased aitavad EAS-i raha abil võidelda Alzheimeri tõve vastu : [Peep Palumaa kommentaariga uuringutest ravimi tootmiseks]Feldmanis, Andris; Palumaa, PeepEesti Päevaleht2005 / 6. aug., lk. 4 : fot
• 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
• 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 https://www.ester.ee/record=b5148492*est
• Elu alus. Energia ja energeetikaPalumaa, PeepHorisont2012 / lk. 10-19 : ill https://artiklid.elnet.ee/record=b2467453*est
• Erratum to: Assessment of Blood Contamination in Biological Fluids Using MALDI-TOF MS (Protein J, 10.1007/s10930-016-9657-y)Laks, Katrina; Kirsipuu, Tiina; Dmitrijeva, Tuuli; Salumets, Andres; Palumaa, PeepProtein Journal2016 / p. 177 - 178 https://doi.org/10.1007/s10930-016-9660-3 https://www.scopus.com/sourceid/144932 https://www.scopus.com/record/display.uri?eid=2-s2.0-84964389135&origin=resultslist&sort=plf-f&src=s&sid=50973f8aeb3d1c19e096d56f835e7904&sot=b&sdt=b&s=DOI%2810.1007%2Fs10930-016-9660-3%29&sl=35&sessionSearchId=50973f8aeb3d1c19e096d56f835e7904&relpos=0 https://jcr.clarivate.com/jcr-jp/journal-profile?journal=PROTEIN%20J&year=2016 https://www.webofscience.com/wos/woscc/full-record/WOS:000377917000002
• ESI TOF MS in protein structure analysisPalumaa, Peep; Eriste, Elo; Njunkova, Olga; Pokras, Lesja; Jörnvall, Hans; Sillard, RannarThe 1st International Symposium on Short-chain Dehydrogenases/reductases in Cancer and other Diseases2002 / ? p
• 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
• Evidence for non-isostructural replacement of Zn(2+) with Cd(2+) in the beta-domain of brain-specific metallothionein-3Palumaa, Peep; Njunkova, Olga; Pokras, Lesja; Eriste, Elo; Jornvall, H.; Sillard, RannarFEBS letters2002 / 1/3, p. 76-80 : ill https://www.sciencedirect.com/science/article/pii/S0014579302031691
• 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
• Formation of [4Fe-4S] clusters in the mitochondrial iron−sulfur cluster assembly machineryBrancaccio, Diego; Zovo, Kairit; Palumaa, PeepJournal of the American Chemical Society2014 / p. 16240-16250 : ill https://doi.org/10.1021/ja507822j https://www.scopus.com/sourceid/22680 https://www.scopus.com/record/display.uri?eid=2-s2.0-84912553487&origin=inward&txGid=df42c501914939ca82bac99c565fc9dd https://jcr.clarivate.com/jcr-jp/journal-profile?journal=J%20AM%20CHEM%20SOC&year=2014 https://www.webofscience.com/wos/woscc/full-record/WOS:000345308700022
• Functional characterization of the cellular copper proteome = Rakulise vase proteoomi funtsionaalne iseloomustamineZovo, Kairit2011
• Genoomika, proteoomika... ehk kuhu liigub bioloogiateadus?Palumaa, PeepTallinna Tehnikaülikooli aastaraamat 20032004 / lk. 18-22
• A hint for the function of human Sco1 from different structuresBanci, Lucia; Bertini, Ivano; Palumaa, PeepProceedings of the National Academy of Sciences of the United States of America2006 / 23, p. 8595-8600 https://pubmed.ncbi.nlm.nih.gov/16735468/ https://www.academia.edu/14865179/A_hint_for_the_function_of_human_Sco1_from_different_structures
• Human Sco1 functional studies and pathological implications of P174L mutantBanci, Lucia; Bertini, Ivano; Palumaa, Peep; Sillard, RannarProceedings of the National Academy of Sciences of the United States of America2007 / 1, p. 15-20 https://www.researchgate.net/publication/6617178_Human_Sco1_functional_studies_and_pathological_implications_of_the_P174L_mutant
• Human superoxide dismutase 1 (hSOD1) maturation through interaction with human copper chaperone for SOD1 (hCCS)Banci, Lucia; Bertini, Ivano; Cantini, Francesca; Kozyreva, Tatiana; Massagni, Chiara; Palumaa, Peep; Rubino, Jeffrey; Zovo, KairitProceedings of the National Academy of Sciences2012 / p. 13555-13560 https://www.researchgate.net/publication/230624025_Human_superoxide_dismutase_1_hSOD1_maturation_through_interaction_with_human_copper_chaperone_for_SOD1_hCCS
• In situ fibrillizing amyloid-beta 1-42 induces neurite degeneration and apoptosis of differentiated SH-SY5Y cellsKrishtal, Jekaterina; Bragina, Olga; Metsla, Kristel; Palumaa, Peep; Tõugu, VelloPLoS ONE2017 / art. e0186636, 16 p. : ill https://doi.org/10.1371/journal.pone.0186636 https://www.scopus.com/sourceid/10600153309 https://www.scopus.com/record/display.uri?eid=2-s2.0-85032228179&origin=inward&txGid=c463fa27e0c4bbc85e6dd169933d01e7 https://jcr.clarivate.com/jcr-jp/journal-profile?journal=PLOS%20ONE&year=2017 https://www.webofscience.com/wos/woscc/full-record/WOS:000413568900023
• 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
• Interaction between oligomers of stefin B and amyloid-[beeta] in vitro and in cellsŠkerget, Katja; Taler-Veričič, Ajda; Kumm, Tiina; Palumaa, PeepJournal of biological chemistry2010 / 5, p. 3201-3210 https://pubmed.ncbi.nlm.nih.gov/19955183/
• 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 https://pubmed.ncbi.nlm.nih.gov/22083646/
• Investigation of properties and reaction mechanisms of redox-active proteins by ESI MS = Redoks-aktiivsete valkude omaduste ja reaktsioonimehhanismide uurimine ESI-MS abilSmirnova, Julia2013 https://www.ester.ee/record=b2965120*est
• Kuida elab Eesti teadus?Palumaa, PeepSirp2020 / lk. 36-37 : ill https://www.sirp.ee/s1-artiklid/c21-teadus/kuidas-elab-eesti-teadus/
• 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 https://www.researchgate.net/publication/46392320_Label-Free_High-Throughput_Screening_Assay_for_Inhibitors_of_Alzheimer's_Amyloid-beta_Peptide_Aggregation_Based_on_MALDI_MS
• Large-scale HPCL purification of Calbindin D9k from porcine intestineBonetto, V.; Kangur, Liina; Palumaa, Peep; Mutt, V.; Jörnvall, Hans; Sillard, RannarProtein expression and purification1999 / 3, p. 387-391 https://pubmed.ncbi.nlm.nih.gov/10600456/
• Lipoic acid ameliorates consequences of copper overload by upregulating selenoproteins and decreasing redox misbalance : poster presentationsKabin, Ekaterina; Dong, Yixuan; Summers, Kelly; Yang, Haojun; Dev, Som; Wang, Yu; Devenney, Benjamin; Roy, Shubhrajit; Palumaa, Peep; Lutsenko, SvetlanaActa physiologica2023 / art. e14044 https://doi.org/10.1111/apha.14044
• Lisad, sõnastik, ülesannete vastused, indeksBiokeemia : lühikursus : õpik kõrgkoolidele2016 / [87] lk. : ill
• Mammalian copper chaperone Cox17 exist in two metalloforms linked by oxydative switchPalumaa, Peep; Voronova, Anastassia; Kangur, Liina; Sillard, Rannar; Meyer-Klauke, W.; Meyer, Thomas; Rompel, AnetteThe FEBS journal2005 / Supplement 1, p. 386-387
• Maximum entropy reconstruction of joint [phi], [psi]-distribution with a coil-library prior : the backbone conformation of the peptide hormone motilin in aqueous solution from [phi] and [psi]-dependent J-couplingsMassad, Tariq; Jarvet, Jüri; Tanner, Risto; Tomson, Katrin; Smirnova, Julia; Palumaa, Peep; Sugai, Mariko; Kohno, Toshiyuki; Vanatalu, Kalju; Damberg, PeterJournal of biomolecular NMR2007 / 2, p. 107-123 https://www.researchgate.net/publication/6369716_Maximum_entropy_reconstruction_of_joint_phps-distribution_with_a_coil-library_prior_The_backbone_conformation_of_the_peptide_hormone_motilin_in_aqueous_solution_from_ph_and_ps-dependent_J-couplings
• 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
• Metabolism of copper and possibilities for its regulationPalumaa, PeepProceedings of the Estonian Academy of Sciences2023 / p. 382-392 https://doi.org/10.3176/proc.2023.4.03 https://www.scopus.com/sourceid/11500153303 https://www.scopus.com/record/display.uri?eid=2-s2.0-85189098909&origin=inward&txGid=63dfe464c5ad0f2a4d97a924f2e5289b https://jcr.clarivate.com/jcr-jp/journal-profile?journal=P%20EST%20ACAD%20SCI&year=2023 https://www.webofscience.com/wos/woscc/full-record/WOS:001152072100004
• Metal binding of metallothionein-3 versus metallothionein-2 : lower affinity and higher plasticityPalumaa, Peep; Tammiste, Indrek; Kruusel, Keiu; Kangur, Liina; Jörnvall, Hans; Sillard, RannarBiochimica et biophysica acta : proteins and proteomics2005 / 2, p. 205-211 : ill https://www.sciencedirect.com/science/article/pii/S1570963904003164
• Metal binding to brain-specific metallothionein-3 studied by electrospray ionization mass spectrometryPalumaa, Peep; Eriste, Elo; Kruusel, Keiu; Kangur, Liina; Jörnvall, Hans; Sillard, RannarCellular and molecular biology2003 / 5, p. 763-768 https://pubmed.ncbi.nlm.nih.gov/14528913/
• Metal-binding mechanism of Cox17, a copper chaperone for cytochrome c oxidasePalumaa, Peep; Kangur, Liina; Voronova, Anastassia; Sillard, RannarBiochemical journal2004 / 1, p. 307-314 https://pubmed.ncbi.nlm.nih.gov/15142040/
• Metal-binding properties of unique Cys-deficient mammalian metallothionein - sheep MT-3Smirnova, Julia; Zovo, Kairit; Chung, Roger S.; West, A.K.; Palumaa, PeepFEBS journal2008 / Suppl. 1, p. 230
• 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
• Metallothionein induces a regenerative reactive astrocyte phenotype via JAK/STAT and RhoA signalling pathwaysLeung, Y.; Pankhurst, M.; Palumaa, Peep; Sillard, RannarExperimental neurology2010 / 1, p. 98-106 : ill https://www.sciencedirect.com/science/article/pii/S0014488609004233
• Metallotioneiin-ligand seostumiskonstantide määramineKangur, Liina; Toomik, Peeter; Palumaa, PeepXXV Eesti keemiapäevad : teaduskonverentsi ettekannete referaadid = 25th Estonian Chemistry Days : abstracts of scientific conference1999 / lk. 45-46
• Mitochondrial copper(I) transfer from Cox17 to Sco1 is coupled to electron transferBanci, Lucia; Bertini, Ivano; Ciofi-Baffoni, Simone; Hadjiloi, Theodoros; Martinelli, Manuele; Palumaa, PeepPNAS2008 / 19, p. 6803-6808 : ill https://pubmed.ncbi.nlm.nih.gov/18458339/
• Modulation of redox switches of copper chaperone Cox17 by Xn(II) ions determined by new ESI MS-based approachZovo, Kairit; Palumaa, PeepAntioxidants & redox signaling2009 / 5, p. 985-995 https://pubmed.ncbi.nlm.nih.gov/19018666/
• 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
• Nähtamatud käskjalad - hormoonid : [selgitab Peep Palumaa]Palumaa, Peep; Laanpere, EhaKodutohter2003 / 2, lk. 54-56 https://artiklid.elnet.ee/record=b2037360*est
• 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
• Organization and assembly of metal-thiolate clusters in epithelium-specific metallothionein-4Meloni, Gabriele; Zovo, Kairit; Kazantseva, Jekaterina; Palumaa, Peep; Vašak, MilanJournal of biological chemistry2006 / 21, p. 14588-14595 : ill https://www.researchgate.net/publication/7221929_Organization_and_Assembly_of_Metal-Thiolate_Clusters_in_Epithelium-specific_Metallothionein-4
• 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
• Oxidative switches in functioning of mammalian copper chaperone Cox17Voronova, Anastassia; Meyer-Klaucke, Wolfram; Meyer, Thomas; Rompel, Anette; Krebs, Bernt; Kazantseva, Jekaterina; Sillard, Rannar; Palumaa, PeepBiochemical journal2007 / p. 139-148 https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2049083/
• Peep Palumaa : PRG744 ehk ühe granditaotluse sekeldused ETAg-i hindamisnõukogus [Võrguväljaanne]Palumaa, Peepnovaator.err.ee2020 / fot https://novaator.err.ee/1109145/peep-palumaa-prg744-ehk-uhe-granditaotluse-sekeldused-etag-i-hindamisnoukogus
• Porfüriinid ja bilirubiin pärsivad Alzheimeri amüloid beta peptiidi agregatsiooniTšekulajeva, Ludmilla; Ševtšuk, Igor; Tšekulajev, Vladimir; Palumaa, PeepXXX Eesti keemiapäevad : teaduskonverentsi teesid = 30th Estonian Chemistry Days : abstracts of scientific conference2007 / lk. 165-166 https://www.ester.ee/record=b2314480*est
• Purification of recombinant human apometallothionein-3 and reconstitution with zincEriste, Elo; Kruusel, Keiu; Palumaa, Peep; Jörnvall, Hans; Sillard, RannarProtein expression and purification2003 / 1, p. 161-165 : ill https://pubmed.ncbi.nlm.nih.gov/12963354/
• Quantitative electrospray ionization mass spectrometry of zinc finger oxidation : the reaction of XPA zinc finger with H2O2Smirnova, Julia; Zhukova, Liliya; Palumaa, PeepAnalytical biochemistry2007 / 2, p. 226-231 : ill
• Rakulise vase proteoomi süsteemibioloogiaPalumaa, Peep; Zovo, KairitXXXII Eesti Keemiapäevad : teaduskonverentsi teesid2011 / lk. 73 : ill
• Ravimatut Wilsoni tõbe aitab kontrolli all hoida looduslik antioksüdant, Эстонские ученые обнаружили лечебные свойства у популярного антиоксидантаPalumaa, Peepnovaator.err.ee2023 https://novaator.err.ee/1609141705/ravimatut-wilsoni-tobe-aitab-kontrolli-all-hoida-looduslik-antioksudant https://nauka.err.ee/1609142699/jestonskie-uchenye-obnaruzhili-lechebnye-svojstva-u-populjarnogo-antioksidanta
• Reaction of the XPA zinc finger with S-nitrosoglutathioneSmirnova, Julia; Zhukova, Liliya; Witkiewicz-Kucharcyk, Aleksandra; Kopera, Edyta; Oledzki, Jacek; Wyslouch-Cieszynska, Aleksandra; Palumaa, Peep; Hartwig, Andrea; Bal, WojciechChemical research in toxicology2008 / p. 386-392 : ill https://pubs.acs.org/doi/10.1021/tx700297f
• Reactivity of Cd7-metallothionein with Cu(II) ions : evidence for a cooperative formation of Cd3, Cu(I)5-metallothioneinVaher, Maret; Romero-Isart, Nuria; Vašak, Milan; Palumaa, PeepJournal of inorganic biochemistry2001 / p. 1-6 : ill https://pubmed.ncbi.nlm.nih.gov/11192694/
• 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 https://www.scopus.com/sourceid/21100197927 https://www.scopus.com/record/display.uri?eid=2-s2.0-85045896131&origin=inward&txGid=b521ae5ba7d843f83b5a55fd53ca4222 https://jcr.clarivate.com/jcr-jp/journal-profile?journal=FEBS%20OPEN%20BIO&year=2022 https://www.webofscience.com/wos/woscc/full-record/WOS:000434220500004
• Redox-active Cu(II)–Aβ causes substantial changes in axonal integrity in cultured cortical neurons in an oxidative-stress dependent mannerHowells, Claire; Saar, Katrina; Eaton, Emma; Ray, Shannon; Palumaa, PeepExperimental neurology2012 / p. 499-506 : ill https://www.sciencedirect.com/science/article/pii/S0014488612002373
• 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
• Stability and conformation of polycopper-thiolate clusters studied by density functional approachAhte, Priit; Palumaa, Peep; Tamm, ToomasJournal of physical chemistry A2009 / 32, p. 9157-9164 : ill https://pubs.acs.org/doi/10.1021/jp8114644
• Structural and functional insight into trafficking of copper in the cellPalumaa, Peep; Banci, Lucia; Bertini, Ivano; Ciofi-Baffoni, Simone; Zovo, KairitJournal of biological inorganic chemistry2014 / p. S851
• Structure and functioning of copper chaperonesPalumaa, PeepFEBS journal2013 / p. 151
• Šveitsi Tudengite Teaduspreemia 2002 välja antud : [TTÜ geenitehnoloogia magistrandile Olga Njunkovale : lühisõnum]Palumaa, PeepMente et Manu2002 / lk. 2 https://www.ester.ee/record=b1242496*est
• Šveitsi Tudengite Teaduspreemia võitja selgunud : [TTÜ infotehnika teaduskonna doktorant Jaan Raik : lühisõnum]Palumaa, PeepMente et Manu2001 / lk. 2 https://www.ester.ee/record=b1242496*est
• 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
• "Talendid koju" Eesti moodi : [tippteadlaste/professorite töö tasustamisest]Palumaa, PeepÕpetajate Leht2010 / lk. 7 https://artiklid.elnet.ee/record=b2179365*est
• Teaduspreemia keemia ja molekulaarbioloogia alal uurimuste tsükli "Tsingi ja vase rakulised funktsioonid ja roll Alzheimeri tõve patoloogias" eest : Peep PalumaaPalumaa, PeepEesti Vabariigi teaduspreemiad 20112011 / lk. 58-79 : portr., ill
• The effects of physiologically important nonmetallic ligands in the reactivity of metallothionein towards 5,5'-dithiobis(2-nitrobenzoic acid) : a new method for the determination of ligand interactions with metallothioneinKangur, Liina; Palumaa, PeepEuropean journal of biochemistry2001 / p. 4979-4984 : ill https://pubmed.ncbi.nlm.nih.gov/11559367/
• The missing link in the amyloid cascade of Alzheimer's disease - metal ionsTiiman, Ann; Palumaa, Peep; Tõugu, VelloNeurochemistry international2013 / p. 367-378 : ill https://doi.org/10.1016/j.neuint.2013.01.023 https://www.sciencedirect.com/science/article/pii/S0197018613000326 https://www.scopus.com/sourceid/17486 https://www.scopus.com/record/display.uri?eid=2-s2.0-84874587315&origin=resultslist&sort=plf-f&src=s&sot=b&sdt=b&s=DOI%2810.1016%2Fj.neuint.2013.01.023%29 https://jcr.clarivate.com/jcr-jp/journal-profile?journal=NEUROCHEM%20INT&year=2013 https://www.webofscience.com/wos/woscc/full-record/WOS:000317443200004
• The native copper- and zinc- binding protein metallothionein blocks copper-mediated A[beeta] aggregation and toxicity in rat cortical neuronsChung, Roger S.; Howells, Claire; Zovo, Kairit; Palumaa, Peep; Sillard, RannarPLoS ONE2010 / 8, p. e12030 [11 p.] https://pmc.ncbi.nlm.nih.gov/articles/PMC2920313/
• 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
• 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 https://www.scopus.com/sourceid/16246 https://www.scopus.com/record/display.uri?eid=2-s2.0-85073080866&origin=inward&txGid=ac2e7c908ea238bdb778e9e65dbbeb9c https://jcr.clarivate.com/jcr-jp/journal-profile?journal=J%20ALZHEIMERS%20DIS&year=2022 https://www.webofscience.com/wos/woscc/full-record/WOS:000488819100015
• Tsingi ja vase rakulised funktsioonid ja roll Alzheimeri tõve patoloogias : kommentaar Eesti Vabariigi teaduse aastapreemia pälvinud tööde tsüklilePalumaa, PeepTallinna Tehnikaülikooli aastaraamat 20112012 / lk. 193-214 : ill
• TTÜ geenitehnoloogid otsivad ravimit Alzheimeri tõvelePalumaa, Peep; Helme, KristiMente et Manu2013 / lk. 14-16 : fot
• Uudne TTÜ teadlaste analüüs hõlbustab Alzheimeri tõve diagnoosimist [Võrguväljaanne]Palumaa, Peepnovaator.err.ee2020 / fot https://novaator.err.ee/1094396/uudne-ttu-teadlaste-analuus-holbustab-alzheimeri-tove-diagnoosimist
• Uudsed suunad Alzheimeri tõve ravimiarendusesPalumaa, PeepTallinna Tehnikaülikooli aastaraamat 20072008 / lk. 113-116
• 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 ameliorates consequences of copper overload by up-regulating selenoproteins and decreasing redox misbalanceKabin, Ekaterina; Dong, Yixuan; Roy, Shubhrajit; Smirnova, Julia; Smith, Joshua W.; Ralle, Martina; Summers, Kelly; Yang, Haojun; Dev, Som; Wang, Yu; Devenney, Benjamin; Cole, Robert N.; Palumaa, Peep; Lutsenko, SvetlanaProceedings of the National Academy of Sciences2023 / art. e2305961120 https://doi.org/10.1073/pnas.2305961120 https://www.scopus.com/sourceid/21121 https://www.scopus.com/record/display.uri?eid=2-s2.0-85172698338&origin=inward&txGid=0eb8c8c72d172641dc181674779bbeb0 https://jcr.clarivate.com/jcr-jp/journal-profile?journal=P%20NATL%20ACAD%20SCI%20USA&year=2023 https://www.webofscience.com/wos/woscc/full-record/WOS:001119347300022
• 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 https://www.scopus.com/sourceid/16246 https://www.scopus.com/record/display.uri?eid=2-s2.0-85123320316&origin=inward&txGid=a30ac2911c3162eb5d69df7458702b28 https://jcr.clarivate.com/jcr-jp/journal-profile?journal=J%20ALZHEIMERS%20DIS&year=2022 https://www.webofscience.com/wos/woscc/full-record/WOS:000747048000021
• α-Lipoic acid: a potential regulator of copper metabolism in Alzheimer’s diseaseKirss, Sigrid; Reinapu, Anette; Kabin, Ekaterina; Smirnova, Julia; Tõugu, Vello; Palumaa, PeepFrontiers in Molecular Biosciences2024 / art. 1451536 https://doi.org/10.3389/fmolb.2024.1451536