See veebileht kasutab küpsiseid kasutaja sessiooni andmete hoidmiseks. Veebilehe kasutamisega nõustute ETISe kasutustingimustega. Loe rohkem
Olen nõus

Peep Palumaa

https://www.etis.ee/CV/Peep_Palumaa/est
30.06.1959
6204410
5025559
peep.palumaa@taltech.ee
AAF-7617-2020

Teenistuskäik

Töökohad ja ametid
01.01.2019–...   
Tallinna Tehnikaülikool, Loodusteaduskond, Keemia ja biotehnoloogia instituut, Täisprofessor tenuuris (1,00)
01.01.2017–31.12.2018   
Tallinna Tehnikaülikool, Loodusteaduskond, Keemia ja biotehnoloogia instituut, Professor (1,00)
01.01.2010–31.12.2015   
Tervisetehnoloogiate Arenduskeskus AS (endine Reproduktiivmeditsiini TAK AS) ; Vanemteadur (0.50)
01.01.2002–31.12.2016   
Tallinna Tehnikaülikool, Matemaatika-loodusteaduskond, Geenitehnoloogia instituut, Genoomika ja proteoomika õppetool, Professor (1,00)
01.01.2001–31.12.2002   
Tallinna Tehnikaülikool, Geenitehnoloogia Keskus, vanemteadur
01.01.1999–31.12.2001   
Tallinna Tehnikaülikool, Alus- ja Rakenduskeemia Instituut, vanemteadur
01.01.1996–31.12.1996   
Zürichi Ülikool, Biokeemia Instituut, külalisprofessor
01.01.1995–31.12.1995   
Münsteri Ülikool, Anorgaanilise Keemiainstituut, külalisprofessor
01.01.1993–31.12.1999   
Tartu Ülikool, Molekulaar- ja Rakubioloogia Instituut, biokeemia professor
01.01.1992–31.12.1993   
Tartu Ülikool, Bioorgaanilise Keemia Laboratoorium, vanemteadur
01.01.1991–31.12.1992   
Zürichi Ülikool, Biokeemia Instituut, postdoktorant / vanemassistent
01.01.1990–31.12.1991   
Zürichi Ülikool, Biokeemia Instituut, postdoktorant / assistent
01.01.1989–31.12.1990   
Zürichi Ülikool, Biokeemia Instituut, postdoktorant
01.01.1989–31.12.1989   
Kuopio Ülikool, Soome, külalisteadur
01.01.1986–31.12.1989   
Tartu Ülikool, Bioorgaanilise Keemia Laboratoorium, teadur
 
 
Haridustee
1986–1986   
Ph.D. (teaduste kandidaadi kraad orgaanilises keemias), Eesti TA Keemiainstituut
1982–1986   
Tartu Ülikool, orgaanilise keemia kateeder, aspirant
1977–1982   
Tartu Ülikool, keemiaosakond, diplom cum laude bioorgaanilises keemias
1966–1977   
Võru I Keskkool, kuldmedal
 
 
Teadusorganisatsiooniline ja -administratiivne tegevus
2011−...   
EMBO (Euroopa Molekulaarbioloogia Organisatsioon) liige
2009−...   
Ajakirja Antioxidants and Redox Signaling toimetuskolleegiumi liige
1999−...   
Retsensent ajakirjadesse PNAS, Biochemistry, BBA, Coordination Chemistry Reviews, Protein Engineering, Talanta, Antioxidants and Redox Signaling jne. saadetud käsikirjadele
2011−2016   
Eesti Biokeemia Selts, president
2006−2009   
Ameerika Keemia Seltsi (American Chemical Society) liige
2002−2005   
EL 5 Raamprogrammi projekti: The role of zinc metabolism in Alzheimers disease. Elaboration of a new strategy for prevention and therapy of Alzheimers disease" koordinaator
2000−2002   
Swiss Science Officer – Sveitsiga teaduskoostöö organisaator Tallinna Tehnikaülikoolis
1995−1998   
EÜ TEMPUS JEP projekti “Restructuring of Biochemical Education in the University of Tartu” koordinaator

Kvalifikatsioon

Teaduskraadid
Peep Palumaa, doktorikraad, 1986, (juh) Jaak Järv, Affinity modification of acetylcholinesterase by N,N-dimethyl-2-phenylaziridinium ion., Eesti Teaduste Akadeemia Keemia Instituut, Tallinn.
 
 
Teaduspreemiad ja tunnustused
2013, Peep Palumaa, Tallinna Tehnikaülikooli 2012. aasta parima teadlase preemia
2011, Peep Palumaa, Eesti riiklik teaduspreemia keemia ja molekulaarbioloogia alal
2011, Peep Palumaa, Valimine esimeseks ja seni ainukeseks EMBO liikmeks Eestist
2010, Peep Palumaa, Tallinna Tehnikaülikooli aasta parima teadusartikli preemia
2010, Peep Palumaa, Tallinna Tehnikaülikooli rakenduslike teadustööde konkursi teine preemia
 
 
Teadustöö põhisuunad
ETIS KLASSIFIKAATOR: 1. Bio- ja keskkonnateadused; 1.1. Biokeemia; CERCS KLASSIFIKAATOR: P310 Proteiinid, ensümoloogia
ETIS KLASSIFIKAATOR: 3. Terviseuuringud; 3.11. Terviseuuringutega seotud uuringud, näiteks biokeemia, geneetika, mikrobioloogia, biotehnoloogia, molekulaarbioloogia, rakubioloogia, biofüüsika ja bioinformaatika; CERCS KLASSIFIKAATOR: B190 Kliiniline keemia
 
 
Lisainfo
teaduste kandidaat (Ph.D.)
Eesti Teaduste Akadeemia Keemiainstituut

Jooksvad projektid

Lõppenud projektid

Juhendamisel väitekirjad

Juhendatud väitekirjad

Juhendatud järeldoktorid

  • 01.10.2009−30.09.2011 Katja Gehenn "New MS-based approaches for studies of conformation and aggregation of amyloidogenic peptides" Tallinna Tehnikaülikool

Publikatsioonid

Klass
Aasta
Publikatsioon
 
1.1.
2021
Metsla, Kristel; Kirss, Sigrid; Laks, Katrina; Sildnik, Gertrud; Palgi, Mari; Palumaa, Teele; Tõugu, Vello; Palumaa, Peep (2021). α-Lipoic Acid Has the Potential to Normalize Copper Metabolism, Which Is Dysregulated in Alzheimer’s Disease. Journal of Alzheimer's Disease, 1−14. DOI: 10.3233/JAD-215026.
1.1.
2020
Kirsipuu, T.; Zadorožnaja, A.; Smirnova, J.; Friedemann, M.; Plitz, T.; Tõugu, V.; Palumaa, P. (2020). Copper(II)-binding equilibria in human blood. Scientific Reports, 10 (1), #5686. DOI: 10.1038/s41598-020-62560-4.
1.1.
2020
Friedemann, M.; Tõugu, V.; Palumaa, P. (2020). Copper(II) partially protects three histidine residues and the N-terminus of amyloid-β peptide from diethyl pyrocarbonate (DEPC) modification. FEBS Open Bio, 10 (6), 1072−1081. DOI: 10.1002/2211-5463.12857.
6.3.
2020
Palumaa, P. (2020). EESTI BIOKEEMIK: COVID-19 on ohtlik ja tugev viirus, kuid terve inimese organism paistab olevat tugevam. Sirje Maasikamäe (Toim.). Õhtuleht.24.03.2020.
6.3.
2020
Palumaa, P. (2020). EESTI BIOKEEMIK: peame end kaitsma surmava viirusedoosi eest kõigi võimalike vahenditega! Sirje Maasikamäe (Toim.). Õhtuleht.19.03.2020.
6.3.
2020
Palumaa, P. (2020). EESTI BIOKEEMIK HOIATAB: koroonaviirus püsib nakkusohtlikuna õhus mitu tundi, pindadel isegi mitu päeva! Sirje Maasikamäe (Toim.). Õhtuleht.15.03.2020.
6.3.
2020
Palumaa, P. (2020). EESTI BIOKEEMIK: iga samm võib olla saatuslik, pandeemia edukas läbimine sõltub tervisekäitumisest. Sirje Maasikamäe (Toim.). Õhtuleht.05.04.2020.
6.3.
2020
Palumaa, P. (2020). EESTI BIOKEEMIK HOIATAB: koroonaviirus võib olla inimest nakatavate viiruste seas absoluutne maailmameister! Sirje Maasikamäe. Õhtuleht.10.04.2020.
6.3.
2020
Palumaa, P. (2020). Kuidas elab Eesti teadus? Sirp (1−5).22.05.2020.
6.3.
2020
Palumaa, P. (2020). Peep Palumaa: PRG744 ehk ühe granditaotluse sekeldused ETAg-i hindamisnõukogus. Novaator | ERR.
1.1.
2019
Krištal, J.; Metsla, K.; Bragina, O.; Tõugu, V.; Palumaa, P. (2019). Toxicity of Amyloid-β Peptides Varies Depending on Differentiation Route of SH-SY5Y Cells. Journal of Alzheimer's Disease, 879−887. DOI: 10.3233/JAD-190705.
1.1.
2019
Wallin, C.; Friedemann, M.; Sholts, S. B; Noormägi, A.; Svantesson, T.; Jarvet, J.; Roos, P. M.; Palumaa, P.; Gräslund, A.; Wärmländer, S. K. T. S. (2019). Mercury and Alzheimer's disease: Hg(II) ions display specific binding to the amyloid-β peptide and hinder its fibrillization. Biomolecules, 10 (1), 1−23. DOI: 10.3390/biom10010044.
5.2.
2019
Metsla, K.; Kirss, S.; Tõugu, V.; Palumaa, P. (2019). Interaction of copper ions with copper proteins and amyloid-beta.Trial for correction of copper metabolism in Alzheimer's disease. International Symposium: "Amyloid diseases: from biochemistry to clinical applications": Stockholm, Sweden, August 14-17, 2019. Stockholm: The Wenner-Gren Foundations.
5.2.
2019
Krishtal, J.; Metsla, K.; Bragina, O.; Tõugu, V.; Palumaa, P. (2019). Cell differentiating agents alter sensitivity of SH-SY5Y cells to amyloid beta. In: . 14th International Conference on AD/PD, Lisbon, Portugal, 26-31 March 2019.
5.2.
2019
Krishtal, J.; Metsla, K.; Bragina, O.; Tõugu, V.; Palumaa, P. (2019). In vitro studying of amyloid beta peptides toxic effects. FEBS 3+, Latvia Riga, June 17th-19th 2019. Riga: University of Latvia.
5.2.
2019
Metsla, K.; Tõugu, V.; Palumaa, P. (2019). Neurotoxicity of copper ions and the effect of metal chelating agents. In: . 14th International Conference on AD/PD, Lisbon, Portugal, 26-31 March 2019.
1.1.
2018
Smirnova, J.; Kabin, E.; Järving, I.; Bragina, O.; Tõugu, V.; Plitz, T.; Palumaa, P. (2018). Copper(I)-binding properties of de-coppering drugs for the treatment of Wilson disease. α-Lipoic acid as a potential anti-copper agent. Scientific Reports, 8 (1, 1463), 1−9. DOI: 10.1038/s41598-018-19873-2.
1.1.
2018
Smirnova, J.; Kabin, E.; Tougu, V.; Palumaa, P. (2018). Redox properties of Cys(2)His(2) and Cys(4) zinc fingers determined by electrospray ionization mass spectrometry. FEBS Open Bio, 8 (6), 923−931. DOI: 10.1002/2211-5463.12422.
1.1.
2017
Krishtal, J.; Bragina, O.; Metsla, K.; Palumaa, P.; Tõugu, V. (2017). In situ fibrillizing Amyloid-beta 1-42 Induce Neurite Degeneration and Apoptosis of Differentiated SH-SY5Y Cells. PLoS ONE. DOI: 10.1371/journal.pone.0186636.
5.1.
2017
Smirnova, J.; Golendukhina, E.; Järving, I.; Tõugu, V.; Plitz, T.; Palumaa, P. (2017). Copper(I)-binding properties of de-coppering drugs for treatment of Wilson disease. FEBS Journal, 284 (S1), 337.
1.1.
2016
Laks, K.; Kirsipuu, T.; Dmitrijeva, T.; Salumets, A.; Palumaa, P. (2016). Assessment of Blood Contamination in Biological Fluids Using MALDI-TOF MS. The Protein Journal, 35 (3), 171−176. DOI: 10.1007/s10930-016-9657-y.
1.1.
2015
Noormägi, A.; Valmsen, K.; Tõugu, V.; Palumaa, P. (2015). Insulin Fibrillization at Acidic and Physiological pH Values is Controlled by Different Molecular Mechanisms. The Protein Journal, 34 (6), 398−403. DOI: 10.1007/s10930-015-9634-x.
1.1.
2015
Tiiman, Ann; Krishtal, Jekaterina; Palumaa, Peep; Tõugu, Vello (2015). In vitro fibrillization of Alzheimer’s amyloid-β peptide (1-42). AIP Advances, 5, 092401. DOI: 10.1063/1.4921071.
1.1.
2015
Bragina, O.; Gurjanova, K.; Krishtal, J.; Kulp, M.; Karro, N.; Tõugu, V.; Palumaa, P. (2015). Metallothionein 2A affects the cell respiration by suppressing the expression of mitochondrial protein cytochrome c oxidase subunit II. Journal of Bioenergetics and Biomembranes, 47 (3), 209−216. DOI: 10.1007/s10863-015-9609-9.
1.1.
2015
Kirsipuu, T.; Laks, K.; Velthut-Meikas, A.; Levkov, L.; Salumets, A.; Palumaa, P. (2015). Comprehensive elucidation of amino acid profile in human follicular fluid and plasma of in vitro fertilization patients. Gynecological Endocrinology, 31 (SUP1), 9−17. DOI: 10.3109/09513590.2015.1085186.
1.1.
2015
Friedemann, M.; Helk, E.; Tiiman, A.; Zovo, K.; Palumaa, P.; Tõugu, V. (2015). Effect of methionine-35 oxidation on the aggregation of amyloid-β peptide. Biochemistry and Biophysics Reports, 3, 94−99. DOI: 10.1016/j.bbrep.2015.07.017.
5.1.
2015
Friedemann, Merlin; Helk, Eneken; Tiiman, Ann; Zovo, Kairit; Palumaa, Peep; Tõugu, Vello (2015). Oxidation of Methionine-35 in Alzheimer’s amyloid-beta peptide and the aggregation of the oxidized peptide. SpringerPlus, 4: European Society of Neurochemistry Coference: Molecular Mechanisms of Regualtion in the Nervous System, Tartu, Estonia, June 14-17, 2015. Springer, P13. (S1).
5.1.
2015
Krishtal, Jekaterina; Friedemann, Merlin; Tõugu, Vello; Palumaa, Peep (2015). FIBRILLIZATION OF THE MIXTURES OF AMYLOID BETA 1 -40 AND 1 -42. Neurodegenerative Diseases: 12th International Conference on Alzheimer's and Parkinson's Diseases Nice, France March 18-22, 2015.
5.1.
2015
Krishtal, Jekaterina; Bragina, Olga; Metsla, Kristel; Palumaa, Peep; Tõugu, Vello (2015). Toxicity of amyloid beta 1-40 and 1-42 on Sh-SY5Y cell line. SpringerPlus, 4: European Society of Neurochemistry Coference: Molecular Mechanisms of Regualtion in the Nervous System, Tartu, Estonia, June 14-17, 2015. Springer, P19. (S1).
1.1.
2014
Brancaccio, D.; Gallo, A.; Mikolajczyk, M.; Zovo, K.; Palumaa, P.; Novellino, E.; Piccioli, M.; Ciofi-Baffoni, S.; Banci, L. (2014). Formation of [4Fe-4S] clusters in the mitochondrial iron-sulfur cluster assembly machinery. Journal of the American Chemical Society, 136, 16240−16250.
1.1.
2014
Gavrilova, Julia; Tõugu, Vello: Palumaa, Peep (2014). Affinity of zinc and copper ions to insulin monomers. Metallomics, 6, 1296−1300. DOI: 10.1039/C4MT00059E.
3.1.
2014
Tõugu, Vello; Friedemann, Merlin; Tiiman, Ann; Palumaa, Peep (2014). Copper(II) ions and the Alzheimer's amyloid-β peptide: Affinity and stoichiometry of binding. AIP Conference Proceedings: International Conference of Computational Methods in Sciences and Engineering (ICCMSE) 2014, Athens, Greece, 4-7 April 2014. Ed. T. E. Simos , Z. Kalogiratou, T. Monovasilis. American Institute of Physics, 109−111. (1618). DOI: 10.1063/1.4897689.
5.1.
2014
Palumaa, P.; Banci, L.; Bertini, I.; Ciofi-Baffoni, S.; Zovo, K. (2014). Structural and functional insight into trafficking of copper in the cell. Journal of Biological Inorganic Chemistry, 19: 12th European Biological Inorganic Chemistry Conference (EuroBIC), Zürich, SWITZERLAND, AUG 24-28, 2014. Springer Verlag, S851−S851. (Supplement 2).
1.1.
2013
Taler-Verčič, A.; Kirsipuu, T.; Friedemann, M.; Noormägi, A.; Polajnar, M.; Smirnova, J.; Znidarič, MT.; Zganec, M.; Skarabot, M.; Vilfan, A.; Staniforth, RA.; Palumaa, P.; Zerovnik, E. (2013). The role of initial oligomers in amyloid fibril formation by human stefin B. International Journal of Molecular Sciences, 14 (9), 18362−18384. DOI: 10.3390/ijms140918362.
1.1.
2013
Palumaa, P. (2013). Copper chaperones. The concept of conformational control in the metabolism of copper. FEBS Letters, 587 (13), 1902−1910.
1.1.
2013
Tiiman, Ann; Noormägi, Andra; Friedemann, Merlin; Krishtal, Jekaterina; Palumaa, Peep; Tõugu, Vello (2013). Effect of agitation on the peptide fibrillization: Alzheimer’s amyloid- b peptide 1-42 but not amylin and insulin fibrils can grow under quiescent conditions. Journal of Peptide Science, 19 (6), 386−391. DOI: 10.1002/psc.2513.
1.1.
2013
Tiiman, Ann; Palumaa, Peep; Tõugu, Vello (2013). The Missing Link in the Amyloid Cascade of Alzheimer's Disease - Metal Ions. Neurochemistry International, 62 (4), 367−378.
5.1.
2013
Palumaa, P. (2013). Structure and functioning of copper chaperones. FEBS Journal, 280: 38th Congress of the Federation-of-European-Biochemical-Societies (FEBS), Saint Petersburg, RUSSIA, JUL 06-11, 2013. Wiley-Blackwell, 151−151. (Special Issue: SI; Supplement: 1).
5.1.
2013
Friedemann, Merlin; Tougu, Vello; Kirsipuu, Tiina; Palumaa, Peep. (2013). Amyloid beta 1-42 oligomerization in vitro and characterization with SDS-PAGE, MALDI and ESI MS. FEBS Journal SI, 280: 38th Congress of the Federation-of-European-Biochemical-Societies (FEBS), Saint Petersburg, RUSSIA, JUL 06-11, 2013. Wiley-Blackwell, 140−141.
5.1.
2013
Kirsipuu, Tiina; Laks, Katrina; Velthut-Meikas, Agne; Palumaa, Peep. (2013). Amino acid profiling in human follicular fluid and plasma of IVF patients. FEBS Journal, 280: 38th Congress of the Federation-of-European-Biochemical-Societies (FEBS), Saint Petersburg, RUSSIA, JUL 06-11, 2013. Wiley-Blackwell, 282−282. (SI).
5.1.
2013
Laks, Katrina; Kirsipuu, Tiina; Dmitrijeva, Tuuli; Salumets, Andres; Palumaa, Peep (2013). Assessment of blood contamination in biological fluids using MALDI-TOF MS. FEBS Journal, 280: 38th Congress of the Federation-of-European-Biochemical-Societies (FEBS), Saint Petersburg, RUSSIA, JUL 06-11, 2013. Wiley-Blackwell, 489−489. (SI).
1.1.
2012
Howells, C.; Saar, K.; Eaton, E.; Ray, S.; Palumaa, P.; Shabala, L.; Adlard, PA.; Bennett, W.; West, AK.; Guillemin, GJ.; Chung, RS. Exp Neurol. (2012). Redox-active Cu(II)-Aβ causes substantial changes in axonal integrity in cultured cortical neurons in an oxidative-stress dependent manner. Experimental Neurology, 237 (2), 499−506.
1.1.
2012
Banci, L.; Bertini, I.; Cantini, F.; Kozyreva, T.; Massagni, C.; Palumaa, P.; Rubino, JT.; Zovo, K. (2012). Human superoxide dismutase 1 (hSOD1) maturation through interaction with human copper chaperone for SOD1 (hCCS). Proceedings of the National Academy of Sciences, 109 (34), 13555−13560.
1.1.
2012
Tõugu, V.; Palumaa, P. (2012). Coordination of zinc ions to the key proteins of neurodegenerative diseases: amyloid-β peptide, APP, α-synuclein and prion protein. Coordination Chemistry Reviews, 256, 2219−2224.
1.1.
2012
Smimova, Julia; Muhhina, Jekaterina; Tougu, Vello; Palumaa, Peep (2012). Redox and Metal Ion Binding Properties of Human Insulin-like Growth Factor 1 Determined by Electrospray Ionization Mass Spectrometry. Biochemistry, 51 (29), 5851−5859. DOI: 10.1021/bi300494s.
1.1.
2012
Noormägi, A.; Primar, K.; Tõugu, V.; Palumaa, P. (2012). Interference of low-molecular substances with the thioflavin-T fluorescence assay of amyloid fibrils. Journal of Peptide Science, 18 (1), 59−64. DOI: 10.1002/psc.1416.
6.3.
2012
Palumaa, P. (2012). Elu alus. Energia ja energeetika. Horisont, 1, 10−19.
1.1.
2011
Tõugu, Vello; Tiiman, Ann; Palumaa, Peep (2011). Interactions of Zn(II) and Cu(II) ions with Alzheimer’s amyloid-beta peptide. Metal ion binding, contribution to fibrillization and toxicity. Metallomics, 3, 250−261. DOI: 10.1039/c0mt00073f.
1.1.
2010
Zovo, Kairit; Helk, Eneken; Karafin, Ann; Tõugu, Vello; Palumaa, Peep (2010). Label-Free High-Throughput Screening Assay for Inhibitors of Alzheimer’s Amyloid-β Peptide Aggregation Based on MALDI MS. Analytical Chemistry, 82 (20), 8558−8565. DOI: 10.1021/ac101583q.
1.1.
2010
Chung, RS.;, Howells, C.; Eaton, ED.; Shabala, L.; Zovo, K.; Palumaa, P.; Sillard, R.; Woodhouse, A.; Bennett, WR.; Ray, S.; Vickers, JC.; West, AK. (2010). The native copper- and zinc-binding protein metallothionein blocks copper-mediated Abeta aggregation and toxicity in rat cortical neurons. PLoS ONE, 5 (8), 1−11.
1.1.
2010
Noormägi, A.; Gavrilova, J.; Smirnova, J.; Tõugu, V.; Palumaa, P. (2010). Zn(II) ions co-secreted with insulin suppress inherent amyloidogenic properties of monomeric insulin. Biochemical Journal, 430 (3), 511−518. DOI: 10.1042/BJ20100627.
1.1.
2010
Banci, L.; Bertini, I.; Ciofi-Baffoni, S.; Kozyreva, T.; Zovo, K.; Palumaa, P. (2010). Affinity gradients drive copper to cellular destinations. Nature, 465 (7298), 645−648. DOI: 10.1038/nature09018.
1.1.
2010
Skerget, K.; Taler-Vercic, A.; Bavdek, A.; Hodnik, V.; Ceru, S.; Tusek-Znidaric, M.; Kumm, T.; Pitsi, D.; Pompe-Novak, M.; Palumaa, P.; Soriano, S.; Kopitar-Jerala, N.; Turk, V.; Anderluh, G.; Zerovnik, E. (2010). Interaction between oligomers of stefin B and amyloid-beta in vitro and in cells. Journal of Biological Chemistry, 285 (5), 3201−3210. DOI: 10.1074/jbc.M109.024620.
1.1.
2010
Leung, Y.; Pankhurst, M.; Dunlop, S.; Ray, S.; Dittmann, J.; Eaton, E.; Palumaa, P.; Sillard, R.; Chuah, M.; West, A.; Chung, R. (2010). Metallothionein induces a regenerative reactive astrocyte phenotype via JAK/STAT and RhoA signalling pathways. Experimental Neurology, 221 (1), 98−106. DOI: 10.1016/j.expneurol.2009.10.006.
5.1.
2010
Noormägi, A.; Gavrilova, J.; Smirnova, J; Tõugu, V.; Palumaa, P. (2010). Zn(II) ions inhibit fibrillization of monomeric insulin. FEBS Journal, 277: 35th FEBS Congress, Göteburg 26. juuni- 1. juuli 2010. Wiley-Blackwell, 256−256. (Suppl. 1).
5.1.
2010
Kumm, Tiina; Taler-Vercic, Ajda; Skerget, Katja; Friedemann, Merlin; Zerovnik, Eva; Palumaa, Peep (2010). Oligomerization and conformation of amyloidogenic protein human stefin B. Insight from ESI MS. FEBS Journal, 277, 258−258.
1.1.
2009
Ahte, P.; Palumaa, P.; Tamm, T. (2009). Stability and conformation of polycopper-thiolate clusters studied by density functional approach. The Journal of Physical Chemistry A, 113 (32), 9157−9164.
1.1.
2009
Tõugu, V.; Karafin, A.; Zovo, K.; Chung, R.S.; Howells, C.; West, A.K.; Palumaa, P. (2009). Zn(II) and Cu(II)-induced nonfibrillar aggregates of amyloid-beta peptide are transformed to amyloid fibrils, both spontaneously and under the influence of metal chelators. Journal of Neurochemistry, 110, 1784−1795. DOI: 10.1111/j.1471-4159.2009.06269.x.
1.1.
2009
Palumaa, P. (2009). Biological redox switches. Antioxidants and Redox Signaling, 11 (5), 981−983. DOI: 10.1089/ars.2009.2468.
1.1.
2009
Palumaa, P; Zovo, K. (2009). Modulation of redox switches of copper chaperone Cox17 by Zn(II) ions, determined by new ESI MS based approach. Antioxidants and Redox Signaling, 11 (5), 985−995. DOI: 10.1089/ars.2008.2262.
3.1.
2009
Karafin, A.; Palumaa, P.; Tõugu, V. (2009). Monitoring of Aβ fibrillization using an improved fluorimetric method. New Trends in Alzheimer and Parkinson Disorders: ADPD 2009: Alzheimer's and Parkinson's Diseases: Advances, Concepts and New Challenges. 9th International Conference AD/PD 2009. Prague, Czech Republic, March 11-15, 2009. Ed. Fisher, A.; Hanin, I. Bologna, Italy: Medimond, 255−259.
5.2.
2009
Palumaa, Peep; Karafin, Ann; Zovo, Kairit; Chung, Roger S.; Howells, Claire; West, Adrian K.; Tõugu, Vello (2009). Effect of Zn(II) and Cu(II) ions on aggregation and fibrillation of amyloid-β(1-42) peptide. Abstract Book: Sinapsa Neuroscience Conference '09, LjUbljana 26th - 29th September 2009. Toim. Kortnik, Blaž; Oskedar, Damian; Vodušek, Vid V. Ljubljana, Slovenia: SiNAPSA, Slovenian Neuroscience Association, 34.
5.2.
2009
Karafin, Ann; Palumaa, Peep; Tõugu, Vello (2009). Monitoring of amyloid-beta fibrillization using an improved fluorimetric method. In: (799−799).Alzheimer's and Parkinson's Diseases Advances, Concepts and New Challenges Congress, Prague, March 2009. Karger.
1.1.
2008
Banci, L.; Bertini, I.; Ciofi-Baffoni, S.; Hadjiloi, T.; Martinelli, M.; Palumaa, P. (2008). Mitochondrial copper(I) transfer from Cox17 to Sco1 is coupled to electron transfer. Proceedings of the National Academy of Sciences of the United States of America, 19, 6803−6808.
1.1.
2008
Smirnova, J.; Zhukova, L.; Witkiewicz-Kucharczyk, A.; Kopera, E.; Olędzki, J.; Wysłouch-Cieszyńska, A.; Palumaa, P.; Hartwig, A.; Bal, W. (2008). Reaction of the XPA zinc finger with S-nitrosoglutathione. Chemical Research in Toxicology, 21, 386−392.
1.1.
2008
Tõugu, Vello;Karafin, Ann;Palumaa, Peep (2008). Binding of zinc(II) and copper(II) to the full-length Alzheimer's amyloid-β peptide. Journal of Neurochemistry, 104, 1249−1259.
1.1.
2008
Banci, L.; Bertini, I.; Ciofi-Baffoni, S.; Janicka, A.; Martinelli, M.; Kozlowski, H.; Palumaa, P. (2008). A structural-dynamical characterization of Human Cox17. Journal of Biological Chemistry, 283 (12), 7912−7919.
5.1.
2008
Smirnova, J.; Zovo, K.; Chung, R. S.; West, A. K.; Palumaa, P. (2008). Metal-binding properties of unique Cys-deficient mammalian metallothionein - sheep MT-3. FEBS Journal: 33rd FEBS Meeting, Athens, June 28 - July 3, 2008. , 230−230. (275 ).
5.1.
2008
Karafin, A; Palumaa, P; Tougu, V. (2008). Interactions of zinc(II) and copper(II) to the full-length Alzheimer's amyloid-B peptide in vitro. FEBS Journal: 33rd FEBS Meeting, Athens, June 28-July 3, 2008. , 222−222. (275).
1.1.
2007
Voronova, A.; Meyer-Klaucke, W.; Meyer, T.; Rompel, A.; Krebs, B.; Kazantseva, J.; Sillard, R.; Palumaa, P. (2007). Oxidative switches in functioning of mammalian copper chaperone Cox17. Biochemical Journal, 408 (1), 139−148. DOI: 10.1042/BJ20070804.
1.1.
2007
Banci, L.; Bertini, I.; Ciofi-Baffoni, S.; Leontari, I.; Martinelli, M.; Palumaa, P.; Sillard, R.; Wang, S. (2007). Human Sco1 functional studies and pathological implications of P174L mutant. Proceedings of the National Academy of Sciences of the United States of America, 104 (1), 15−20.
1.1.
2007
Massad, T.; Jarvet, J.; Tanner, R.; Tomson, K.; Smirnova, J.; Palumaa, P.; Sugai, M.; Kohno, T.; Vanatalu, K.; Damberg, P. (2007). 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-couplings. Journal of Biomolecular NMR, 38 (2), 107−123.
1.1.
2007
Smirnova, J.; Zhukova, L.; Witkiewicz-Kucharczyk, A.; Kopera, E.; Olędzki, J.; Wysłouch-Cieszyńska, A.; Palumaa, P.; Hartwig, A.; Bal, W. (2007). Quantitative electrospray ionization mass spectrometry of zinc finger oxidation: The reaction of XPA zinc finger with H(2)O(2). Analytical Biochemistry, 369 (2), 226−231.
1.1.
2007
Voronova, A.; Kazantseva, J.; Tuuling, M.; Sokolova, N.; Sillard, R.;L Palumaa, P. (2007). Cox17, a copper chaperone for cytochrome c oxidase: Expression, purification and formation of mixed disulfide adducts with thiol reagents. Protein Expression and Purification, 53 (1), 138−144. DOI: 10.1016/j.pep.2006.11.014.
5.2.
2007
Chekulayeva, L.; Shevchuk, I.; Chekulayev, V.; Palumaa, P. (2007). Porphyrins and bilirubin can suppress the aggregation of Alzheimer beta-amyloid peptide. 30th Estonian Chemistry Days Abstracts of Scientific Conference: 30th Estonian Chemistry Days, Tartu 2007. Taru, Estonia: Tartu University, 165−166.
1.1.
2006
Banci, L.; Bertini, I.; Calderone, V.; Ciofi-Baffoni, S.; Mangani, S.; Martinelli, M.; Palumaa, P.; Wang, S. (2006). A hint for the function of human Sco1 from different structures. Proceedings of the National Academy of Sciences of the United States of America, 103 (23), 8595−8600.
1.1.
2006
Meloni, G.; Zovo, K.; Kazantseva, J.; Palumaa, P.; Vasak, M. (2006). Organization and assembly of metal-thiolate clusters in epithelium-specific metallothionein-4. Journal of Biological Chemistry, 281 (21), 14588−14595. DOI: 10.1074/jbc.M601724200.
1.1.
2005
Palumaa, P.; Tammiste, I.; Kangur, L.; Kruusel, K.; Jörnvall, H.; Sillard, R. (2005). Metal-binding of metallothionein-3 versus metallothionein-2: lower affinity and higher plasticity (2005), BBA. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 1747 (2), 205−211.
5.1.
2005
Palumaa, P.; Voronova, A.; Kangur, L.; Sillard, R.; Meyer-Klaucke, W.; Meyer, T.; Rompel, A. (2005). Mammalian copper chaperone Cox17 exists in two metalloforms, linked by oxidative switch. FEBS Journal, 272, 386−387.
5.2.
2005
Tomson, K.; Vanatalu, K.; Smirnova, J.; Palumaa, P.; Tanner, R.; Jarvet, J.; Gräslund, A. (2005). Production and labeling of recombinant motilin in Escherichia coli. International Conference on Environmental, Industrial and Applied Microbiology, Badajoz, Spain, 15-18 March 2005.
1.1.
2004
Palumaa, P.; Kangur, L.; Voronova, A.; Sillard, R (2004). Metal-binding mechanism of Cox17, a copper chaperone for cytochrome c oxidase. Biochemical Journal, 382, 307−314.
5.2.
2004
Palumaa, P., Sillard, R. (2004). Metal binding mechanism of cytochrome c oxidase copper chaperone Cox17. Abstract book: MBB Conference, Södertälje, Sweden, 11 – 12 March 2004. Stockholm, 46−46.
5.2.
2004
Palumaa, P., Tammiste, I., Kruusel, K., Kangur, L., Jörnvall, H., Sillard, R. (2004). Biochemical and metal-binding properties of brain-specific metallothionein-3. Abstarct book: Swiss Society of Neuropathology XXth International Winter Meeting: „Growth and Death in the Nervous System“ St. Moritz, Switzerland, 24-28 March 2004. Zürich, 45−45.
5.2.
2004
Palumaa, P.; Meyer, T.; Rompel, A.; Kangur, L.; Voronova, A.; Sillard, R. (2004). Mechanism of metal binding by Cox17, a copper chaperone for cytochrome c oxidase. Biometals 2004: 4th International Biometals Symposium (IBS-4), Garmish-Partenkirchen, Germany, 3-5 September 2004. 51−51.
1.1.
2003
Palumaa, P.; Eriste, E.; Kruusel, K.; Kangur, L.; Jornvall, H.; Sillard, R (2003). Metal binding to brain-specific metallotifhonein-3 studied by electrospray ionization mass spectrometry. Cellular and Molecular Biology, 49 (5), 763−768.
1.1.
2003
Eriste, E.; Kruusel, K.; Palumaa, P.; Jornvall, H.; Sillard, R (2003). Purification of recombinant human apometallothionein-3 and reconstitution with zinc. Protein Expression and Purification, 31 (1), 161−165.
1.1.
2002
Palumaa, P.; Njunkova, O.; Pokras, L.; Eriste, E.; Sillard, R. (2002). Evidence for non-isostructural replacement of Zn<2+> with Cd<2+> in the beta-domain of brain-specific metallothionein-3. FEBS Letters, 527, 76−80.
1.1.
2002
Palumaa, P.; Eriste, E.; Njunkova, O.; Pokras, L.; Jörnvall, H.; Sillard, R. (2002). Brain-specific metallothionein-3 has higher metal-binding capacity than ubiquitous metallothioneins and binds metals noncooperatively. Biochemistry, 41 (19), 6158−6163.
5.2.
2002
"Palumaa, Peep;Eriste, Elo;Njunkova, Olga;Pokras, Lesja;Jörnvall, H.;Sillard, Rannar" (2002). Comparison of confirmations of zinc- and cadmium-substituted metallothionein-3 by ESI MS. The 50th ASMS Conference on Mass Spectrometry and Allied Topics. Orlando, puudub−puudub.
1.1.
2001
Vaher, M.; Romero-Isart, N.; Vasak, M.; Palumaa, P (2001). Reactivity of Cd-7-metallothionein with Cu(II) ions: evidence for a cooperative formation of Cd-3,Cu(I)(5)-metallothionein. Journal of Inorganic Biochemistry, 83 (1), 1−6.
1.1.
2001
Kangur, L.; Palumaa, P (2001). The effects of physiologically important nonmetallic ligands in the reactivity of metallothionein towards 5,5'-dithiobis(2-nitrobenzoic acid). European Journal of Biochemistry, 268 (18), 4979−4984.
5.2.
2001
Sillard, R.; Eriste, E.; Njunkova, O.; Pokras, L.; Jörnvall, H.; Wadensten, H.; Renlund, S.; Palumaa, P. (2001). Determination of metal-protein complexes and posttranslational modifications by LC-(ESI-TOF)-MS. Proceedings of the 49th ASMS Conference on Mass Spectrometry and Allied Topics : Chicago, Illinois, May 27-31, 2001. , 11−12.
1.1.
1999
Bonetto, V.; Kangur, L.; Palumaa, P.; Mutt, V.; Jornvall, H.; Sillard, R. (1999). Large-scale HPLC purification of calbindin D9k from porcine intestine. Protein Expression and Purification, 17 (3), 387−391.
3.1.
1998
Palumaa, P.; Lehtme, R. (1998). Biochemical characterization of monomeric and dimeric cadmium-substituted metallothionein-3. Metallothionein IV (63−69).. Basel: Birkhäuser, Boston.
1.1.
1996
Palumaa, P.; Vaher, M. (1996). Metal-induced dimerization of Cd7-metallothionein. Role of Anions. Annals of clinical and laboratory science, 26 (3), 264−268.
1.1.
1993
Palumaa, P.; Vasak, M. (1993). Formation and spectroscopic characterization of a novel monomeric cadmium- and phosphate-containing form of metallothionein. Biochemistry, 32, 2874−2879.
1.1.
1992
Santa, H.; Laatikainen, R.; Lötjonen, S.; Palumaa, P. (1992). Dynamic NMR determination of the N,N-dimethyl inversion rate and apparent Inversion free energy in 2-hydroxy-N,N-dimethyl-2-phenylethylamine. Journal of Chemical Research, (S) (6), 198−199.
1.1.
1992
Palumaa, P.; Vasak, M. (1992). Binding of inorganic phosphate to the cadmium-induced dimeric form of metallothionein from rabbit liver. European Journal of Biochemistry, 205, 1131−1135.
1.1.
1992
Palumaa, P.; Mackay, E A.; Vasak, M. (1992). Nonoxidative cadmium-dependent dimerization of Cd7-metallothionein from rabbit liver. Biochemistry, 31, 2181−2186.
1.1.
1991
Zorko, M.; Palumaa, P.; Kask, K. (1991). Binding of some aromatic ligands to the active site of acetylcholinesterase. Periodicum Biologorum, 2, 355−356.
1.1.
1990
Zorko, M.; Langel, Ü.; Palumaa, P. (1990). Simultaneous action of quaternary ammonium ligands and alkanesulfonylchlorides on electric eel acetylcholinesterase. Periodicum Biologorum, 4, 385−391.
1.1.
1989
Palumaa, P.; Kask, K. (1989). Biomimetic modelling of spatial structure of acetylcholinesterase active site with cyclodextrins. Organic Reactivity, 26, 122−141.
1.1.
1988
Eller, M.; Jarv, J.; Palumaa, P. (1988). Influence of non-radioactive ligands on kinetics of normal-methyl-[3h]scopolamine binding to muscarinic receptor. Organic Reactivity, 25, 372−386.
1.1.
1987
Palumaa, P.; Järv, J.; Schevchenko, V.; Myasojedov, N. (1987). Synthesis f -(N,N-dimethylamino)4,-3H-acetophenon. Radiokhim (USSR), 29 (2), 231−232.
1.1.
1987
Soomets, UV.; Palumaa, PJ.; Yarv, JL. (1987). Mechanism of reaction of n,n-dimethyl-2-phenyl-aziridinium ion in acetylcholinesterase active-center. Bioorganicheskaya Khimiya, 13 (2), 198−203.
1.1.
1985
Palumaa, PJ.; Jarv, JL. (1985). Alkylboronic acid acceleration of acetylcholinesterase alkylation with n,n-dimethyl-2-phenylaziridinium ion. Bioorganicheskaya Khimiya, 11 (9), 1210−1216.
1.1.
1985
Palumaa, P.; Soomets, U.; Jarv, J. (1985). Effects of reaction medium and temperature on solvolysis of n,n-dimethyl-2-phenylaziridinium ion. Organic Reactivity, 22 (2), 238−257.
1.1.
1985
Palumaa, PJ.; Raidaru, GI.; Jarv, JL.; Schevchenko, VP.; Myasoyedov, NF. (1985). Synthesis of tritium labeled n,n-dimethyl-2-phenylaziridinium and its reaction with acetylcholinesterase. Bioorganicheskaya Khimiya, 11 (10), 1348−1352.
1.1.
1984
Palumaa, P.; Jarv, J. (1984). Alkylboronic acids accelerate affinity labeling of acetylcholinesterase with n,n-dimethyl-2-phenylaziridinium ion. Biochimica et Biophysica Acta, 784 (1), 35−39.
1.1.
1984
Palumaa, P.; Raba, R.; Jarv, J. (1984). Site-specificity of butyrylcholinesterase alkylation with n,n-dimethyl-2-phenylaziridinium ion. Biochimica et Biophysica Acta, 791 (1), 15−20.
1.1.
1983
Palumaa, PJ.; Kaambre, TH.; Jarv, JL. (1983). Kinetics of the reaction of n,n-dimethyl-2-phenylaziridinium ions with muscarinic receptor and acetylcholinesterases. Биоорганическая химия, 9 (10), 1348−1356.
1.1.
1982
Palumaa, P.; Mahar, A.; Jarv, J. (1982). Kinetic-analysis of butyrylcholinesterase inhibition with n,n-dimethyl-2-phenylaziridinium ion. Bioorganic Chemistry, 11 (4), 394−403.

Tööstusomand

16.12.2021

Peep Palumaa

https://www.etis.ee/CV/Peep_Palumaa/eng
30.06.1959
6204410
5025559
peep.palumaa@taltech.ee
AAF-7617-2020

Career

Institutions and positions
01.01.2019–...   
Tallinn University of Technology , School of Science, Department of Chemistry and Biotechnology, Professor (1,00)
01.01.2017–31.12.2018   
Tallinn University of Technology , School of Science, Department of Chemistry and Biotechnology, Professor (1,00)
01.01.2010–31.12.2015   
Competence Centre on Health Technologies; Senior Researcher (0.50)
01.01.2002–31.12.2016   
Tallinn University of Technology , Faculty of Science, Department of Gene Technology, Chair of Genomics and Proteomics, Professor (1,00)
01.01.2001–31.12.2002   
Tallinn Technical University, Center of Gene Technology, Senior Research Scientist
01.01.1999–31.12.2001   
Tallinn Technical University, Institute of Basic and Applied Chemistry, Senior Research Scientist
01.01.1996–31.12.1996   
Univesity of Zürich, Institute of Biochemistry, visiting professor
01.01.1995–31.12.1995   
University of Münster, Institute of Inorganic Chemistry, visiting professor
01.01.1993–31.12.1999   
University of Tartu, Institute of Molecular and Cell Biology, professor of biochemistry
01.01.1992–31.12.1993   
University of Tartu, Laboratory of Bioorganic Chemistry, Senior Research Scientist
01.01.1991–31.12.1992   
Univesity of Zürich, Institute of Biochemistry, postdoctoral fellow/senior assistant
01.01.1990–31.12.1991   
Univesity of Zürich, Institute of Biochemistry, postdoctoral fellow/assistant
01.01.1989–31.12.1990   
Univesity of Zürich, Institute of Biochemistry, postdoctoral fellow
01.01.1989–31.12.1989   
University of Kuopio, Department of Chemistry, visiting scientist
01.01.1986–31.12.1989   
University of Tartu, Laboratory of Bioorganic Chemistry, research scientist
 
 
Education
1986–1986   
Candidate of sciences (Ph.D.), Institute of Chemistry, Estonian Academy of Sciences
1982–1986   
University of Tartu, Department of Organic Chemistry, PhD studies
1977–1982   
University of Tartu, Department of Chemistry, Diploma Cum Laude (Bioorganic Chemistry)
1966–1977   
Gymnasium of Võru, gold medal
 
 
R&D related managerial and administrative work
2011−...   
Member of EMBO (The European Molecular Biology Organization)
2009−...   
Journal Antioxidants and Redox Signaling - member of editorial board
1999−...   
Reviewer for journals PNAS, Biochemistry, BBA, Coordination Chemistry Reviews, Protein Engineering, Talanta, Antioxidants and Redox Signaling etc.
2011−2016   
Estonian Biochemical Society, president
2006−2009   
American Chemical Society, member
2002−2005   
EU 5th FP Concerted action project ”Role of zinc in Alzheimers disease. Elaboration of new strategy for prevention and therapy of Alzheimers disease”. Coordinator
2000−2002   
Swiss Science Officer at Tallinn Technical University
1995−1998   
EU TEMPUS JEP “Restructuring of Biochemical Education in the University of Tartu” Coordinator

Qualifications

Academic degrees
Peep Palumaa, Doctor's Degree, 1986, (sup) Jaak Järv, Affinity modification of acetylcholinesterase by N,N-dimethyl-2-phenylaziridinium ion., Eesti Teaduste Akadeemia Keemia Instituut, Tallinn.
 
 
Honours & awards
2013, Peep Palumaa, Tallinn University of Technology scientist of a year 2012
2011, Peep Palumaa, Estonian science award in chemistry and molecular biology
2011, Peep Palumaa, Election to the first and till now the only member of EMBO from Estonia
2010, Peep Palumaa, Award of Tallinn University of Technology for best scientific paper
2010, Peep Palumaa, Competition of Tallinn University of Technology for best applied work - second award
 
 
Fields of research
ETIS CLASSIFICATION: 1. Biosciences and Environment; 1.1. Biochemistry; CERCS CLASSIFICATION: P310 Proteins, enzymology
ETIS CLASSIFICATION: 3. Health; 3.11. Biochemistry, Genetics, Microbiology, Biotechnology, Molecular Biology, Cell Biology, Biophysics and Bioinformatics relating to Health Studies; CERCS CLASSIFICATION: B190 Clinical chemistry
 
 
Additional information
candidate of sciences (Ph.D.)
Institute of Chemistry, Estonian Academy of Sciences

Projects in progress

Completed projects

Dissertations under supervision

Supervised dissertations

Supervision of postdoctoral researchers

  • 01.10.2009−30.09.2011    Katja Gehenn  "New MS-based approaches for studies of conformation and aggregation of amyloidogenic peptides" (Tallinn University of Technology)

Publications

Category
Year
Publication
 
1.1.
2021
Metsla, Kristel; Kirss, Sigrid; Laks, Katrina; Sildnik, Gertrud; Palgi, Mari; Palumaa, Teele; Tõugu, Vello; Palumaa, Peep (2021). α-Lipoic Acid Has the Potential to Normalize Copper Metabolism, Which Is Dysregulated in Alzheimer’s Disease. Journal of Alzheimer's Disease, 1−14. DOI: 10.3233/JAD-215026.
1.1.
2020
Kirsipuu, T.; Zadorožnaja, A.; Smirnova, J.; Friedemann, M.; Plitz, T.; Tõugu, V.; Palumaa, P. (2020). Copper(II)-binding equilibria in human blood. Scientific Reports, 10 (1), #5686. DOI: 10.1038/s41598-020-62560-4.
1.1.
2020
Friedemann, M.; Tõugu, V.; Palumaa, P. (2020). Copper(II) partially protects three histidine residues and the N-terminus of amyloid-β peptide from diethyl pyrocarbonate (DEPC) modification. FEBS Open Bio, 10 (6), 1072−1081. DOI: 10.1002/2211-5463.12857.
6.3.
2020
Palumaa, P. (2020). EESTI BIOKEEMIK: COVID-19 on ohtlik ja tugev viirus, kuid terve inimese organism paistab olevat tugevam [ESTONIAN BIOCHEMIST: COVID-19 is a dangerous and strong virus, but healthy human body seems to be stronger. ]. Sirje Maasikamäe (Toim.). Õhtuleht.24.03.2020.
6.3.
2020
Palumaa, P. (2020). EESTI BIOKEEMIK: peame end kaitsma surmava viirusedoosi eest kõigi võimalike vahenditega! [ESTONIAN BIOCHEMIST: We must protect ourselves from a deadly viral dose by all possible means!]. Sirje Maasikamäe (Toim.). Õhtuleht.19.03.2020.
6.3.
2020
Palumaa, P. (2020). EESTI BIOKEEMIK HOIATAB: koroonaviirus püsib nakkusohtlikuna õhus mitu tundi, pindadel isegi mitu päeva! [ESTONIAN BIOCHEMIST WARNS: the coronavirus remains infectious in the air for several hours and on surfaces even for several days!]. Sirje Maasikamäe (Toim.). Õhtuleht.15.03.2020.
6.3.
2020
Palumaa, P. (2020). EESTI BIOKEEMIK: iga samm võib olla saatuslik, pandeemia edukas läbimine sõltub tervisekäitumisest [ESTONIAN BIOCHEMIST: every step can be fatal, a successful pass through pandemic depends on health behavior.]. Sirje Maasikamäe (Toim.). Õhtuleht.05.04.2020.
6.3.
2020
Palumaa, P. (2020). EESTI BIOKEEMIK HOIATAB: koroonaviirus võib olla inimest nakatavate viiruste seas absoluutne maailmameister! Sirje Maasikamäe. Õhtuleht.10.04.2020.
6.3.
2020
Palumaa, P. (2020). Kuidas elab Eesti teadus? Sirp (1−5).22.05.2020.
6.3.
2020
Palumaa, P. (2020). Peep Palumaa: PRG744 ehk ühe granditaotluse sekeldused ETAg-i hindamisnõukogus. Novaator | ERR.
1.1.
2019
Krištal, J.; Metsla, K.; Bragina, O.; Tõugu, V.; Palumaa, P. (2019). Toxicity of Amyloid-β Peptides Varies Depending on Differentiation Route of SH-SY5Y Cells. Journal of Alzheimer's Disease, 879−887. DOI: 10.3233/JAD-190705.
1.1.
2019
Wallin, C.; Friedemann, M.; Sholts, S. B; Noormägi, A.; Svantesson, T.; Jarvet, J.; Roos, P. M.; Palumaa, P.; Gräslund, A.; Wärmländer, S. K. T. S. (2019). Mercury and Alzheimer's disease: Hg(II) ions display specific binding to the amyloid-β peptide and hinder its fibrillization. Biomolecules, 10 (1), 1−23. DOI: 10.3390/biom10010044.
5.2.
2019
Metsla, K.; Kirss, S.; Tõugu, V.; Palumaa, P. (2019). Interaction of copper ions with copper proteins and amyloid-beta.Trial for correction of copper metabolism in Alzheimer's disease. International Symposium: "Amyloid diseases: from biochemistry to clinical applications": Stockholm, Sweden, August 14-17, 2019. Stockholm: The Wenner-Gren Foundations.
5.2.
2019
Krishtal, J.; Metsla, K.; Bragina, O.; Tõugu, V.; Palumaa, P. (2019). Cell differentiating agents alter sensitivity of SH-SY5Y cells to amyloid beta. In: . 14th International Conference on AD/PD, Lisbon, Portugal, 26-31 March 2019.
5.2.
2019
Krishtal, J.; Metsla, K.; Bragina, O.; Tõugu, V.; Palumaa, P. (2019). In vitro studying of amyloid beta peptides toxic effects. FEBS 3+, Latvia Riga, June 17th-19th 2019. Riga: University of Latvia.
5.2.
2019
Metsla, K.; Tõugu, V.; Palumaa, P. (2019). Neurotoxicity of copper ions and the effect of metal chelating agents. In: . 14th International Conference on AD/PD, Lisbon, Portugal, 26-31 March 2019.
1.1.
2018
Smirnova, J.; Kabin, E.; Järving, I.; Bragina, O.; Tõugu, V.; Plitz, T.; Palumaa, P. (2018). Copper(I)-binding properties of de-coppering drugs for the treatment of Wilson disease. α-Lipoic acid as a potential anti-copper agent. Scientific Reports, 8 (1, 1463), 1−9. DOI: 10.1038/s41598-018-19873-2.
1.1.
2018
Smirnova, J.; Kabin, E.; Tougu, V.; Palumaa, P. (2018). Redox properties of Cys(2)His(2) and Cys(4) zinc fingers determined by electrospray ionization mass spectrometry. FEBS Open Bio, 8 (6), 923−931. DOI: 10.1002/2211-5463.12422.
1.1.
2017
Krishtal, J.; Bragina, O.; Metsla, K.; Palumaa, P.; Tõugu, V. (2017). In situ fibrillizing Amyloid-beta 1-42 Induce Neurite Degeneration and Apoptosis of Differentiated SH-SY5Y Cells. PLoS ONE. DOI: 10.1371/journal.pone.0186636.
5.1.
2017
Smirnova, J.; Golendukhina, E.; Järving, I.; Tõugu, V.; Plitz, T.; Palumaa, P. (2017). Copper(I)-binding properties of de-coppering drugs for treatment of Wilson disease. FEBS Journal, 284 (S1), 337.
1.1.
2016
Laks, K.; Kirsipuu, T.; Dmitrijeva, T.; Salumets, A.; Palumaa, P. (2016). Assessment of Blood Contamination in Biological Fluids Using MALDI-TOF MS. The Protein Journal, 35 (3), 171−176. DOI: 10.1007/s10930-016-9657-y.
1.1.
2015
Noormägi, A.; Valmsen, K.; Tõugu, V.; Palumaa, P. (2015). Insulin Fibrillization at Acidic and Physiological pH Values is Controlled by Different Molecular Mechanisms. The Protein Journal, 34 (6), 398−403. DOI: 10.1007/s10930-015-9634-x.
1.1.
2015
Tiiman, Ann; Krishtal, Jekaterina; Palumaa, Peep; Tõugu, Vello (2015). In vitro fibrillization of Alzheimer’s amyloid-β peptide (1-42). AIP Advances, 5, 092401. DOI: 10.1063/1.4921071.
1.1.
2015
Bragina, O.; Gurjanova, K.; Krishtal, J.; Kulp, M.; Karro, N.; Tõugu, V.; Palumaa, P. (2015). Metallothionein 2A affects the cell respiration by suppressing the expression of mitochondrial protein cytochrome c oxidase subunit II. Journal of Bioenergetics and Biomembranes, 47 (3), 209−216. DOI: 10.1007/s10863-015-9609-9.
1.1.
2015
Kirsipuu, T.; Laks, K.; Velthut-Meikas, A.; Levkov, L.; Salumets, A.; Palumaa, P. (2015). Comprehensive elucidation of amino acid profile in human follicular fluid and plasma of in vitro fertilization patients. Gynecological Endocrinology, 31 (SUP1), 9−17. DOI: 10.3109/09513590.2015.1085186.
1.1.
2015
Friedemann, M.; Helk, E.; Tiiman, A.; Zovo, K.; Palumaa, P.; Tõugu, V. (2015). Effect of methionine-35 oxidation on the aggregation of amyloid-β peptide. Biochemistry and Biophysics Reports, 3, 94−99. DOI: 10.1016/j.bbrep.2015.07.017.
5.1.
2015
Friedemann, Merlin; Helk, Eneken; Tiiman, Ann; Zovo, Kairit; Palumaa, Peep; Tõugu, Vello (2015). Oxidation of Methionine-35 in Alzheimer’s amyloid-beta peptide and the aggregation of the oxidized peptide. SpringerPlus, 4: European Society of Neurochemistry Coference: Molecular Mechanisms of Regualtion in the Nervous System, Tartu, Estonia, June 14-17, 2015. Springer, P13. (S1).
5.1.
2015
Krishtal, Jekaterina; Friedemann, Merlin; Tõugu, Vello; Palumaa, Peep (2015). FIBRILLIZATION OF THE MIXTURES OF AMYLOID BETA 1 -40 AND 1 -42. Neurodegenerative Diseases: 12th International Conference on Alzheimer's and Parkinson's Diseases Nice, France March 18-22, 2015.
5.1.
2015
Krishtal, Jekaterina; Bragina, Olga; Metsla, Kristel; Palumaa, Peep; Tõugu, Vello (2015). Toxicity of amyloid beta 1-40 and 1-42 on Sh-SY5Y cell line. SpringerPlus, 4: European Society of Neurochemistry Coference: Molecular Mechanisms of Regualtion in the Nervous System, Tartu, Estonia, June 14-17, 2015. Springer, P19. (S1).
1.1.
2014
Brancaccio, D.; Gallo, A.; Mikolajczyk, M.; Zovo, K.; Palumaa, P.; Novellino, E.; Piccioli, M.; Ciofi-Baffoni, S.; Banci, L. (2014). Formation of [4Fe-4S] clusters in the mitochondrial iron-sulfur cluster assembly machinery. Journal of the American Chemical Society, 136, 16240−16250.
1.1.
2014
Gavrilova, Julia; Tõugu, Vello: Palumaa, Peep (2014). Affinity of zinc and copper ions to insulin monomers. Metallomics, 6, 1296−1300. DOI: 10.1039/C4MT00059E.
3.1.
2014
Tõugu, Vello; Friedemann, Merlin; Tiiman, Ann; Palumaa, Peep (2014). Copper(II) ions and the Alzheimer's amyloid-β peptide: Affinity and stoichiometry of binding. AIP Conference Proceedings: International Conference of Computational Methods in Sciences and Engineering (ICCMSE) 2014, Athens, Greece, 4-7 April 2014. Ed. T. E. Simos , Z. Kalogiratou, T. Monovasilis. American Institute of Physics, 109−111. (1618). DOI: 10.1063/1.4897689.
5.1.
2014
Palumaa, P.; Banci, L.; Bertini, I.; Ciofi-Baffoni, S.; Zovo, K. (2014). Structural and functional insight into trafficking of copper in the cell. Journal of Biological Inorganic Chemistry, 19: 12th European Biological Inorganic Chemistry Conference (EuroBIC), Zürich, SWITZERLAND, AUG 24-28, 2014. Springer Verlag, S851−S851. (Supplement 2).
1.1.
2013
Taler-Verčič, A.; Kirsipuu, T.; Friedemann, M.; Noormägi, A.; Polajnar, M.; Smirnova, J.; Znidarič, MT.; Zganec, M.; Skarabot, M.; Vilfan, A.; Staniforth, RA.; Palumaa, P.; Zerovnik, E. (2013). The role of initial oligomers in amyloid fibril formation by human stefin B. International Journal of Molecular Sciences, 14 (9), 18362−18384. DOI: 10.3390/ijms140918362.
1.1.
2013
Palumaa, P. (2013). Copper chaperones. The concept of conformational control in the metabolism of copper. FEBS Letters, 587 (13), 1902−1910.
1.1.
2013
Tiiman, Ann; Noormägi, Andra; Friedemann, Merlin; Krishtal, Jekaterina; Palumaa, Peep; Tõugu, Vello (2013). Effect of agitation on the peptide fibrillization: Alzheimer’s amyloid- b peptide 1-42 but not amylin and insulin fibrils can grow under quiescent conditions. Journal of Peptide Science, 19 (6), 386−391. DOI: 10.1002/psc.2513.
1.1.
2013
Tiiman, Ann; Palumaa, Peep; Tõugu, Vello (2013). The Missing Link in the Amyloid Cascade of Alzheimer's Disease - Metal Ions. Neurochemistry International, 62 (4), 367−378.
5.1.
2013
Palumaa, P. (2013). Structure and functioning of copper chaperones. FEBS Journal, 280: 38th Congress of the Federation-of-European-Biochemical-Societies (FEBS), Saint Petersburg, RUSSIA, JUL 06-11, 2013. Wiley-Blackwell, 151−151. (Special Issue: SI; Supplement: 1).
5.1.
2013
Friedemann, Merlin; Tougu, Vello; Kirsipuu, Tiina; Palumaa, Peep. (2013). Amyloid beta 1-42 oligomerization in vitro and characterization with SDS-PAGE, MALDI and ESI MS. FEBS Journal SI, 280: 38th Congress of the Federation-of-European-Biochemical-Societies (FEBS), Saint Petersburg, RUSSIA, JUL 06-11, 2013. Wiley-Blackwell, 140−141.
5.1.
2013
Kirsipuu, Tiina; Laks, Katrina; Velthut-Meikas, Agne; Palumaa, Peep. (2013). Amino acid profiling in human follicular fluid and plasma of IVF patients. FEBS Journal, 280: 38th Congress of the Federation-of-European-Biochemical-Societies (FEBS), Saint Petersburg, RUSSIA, JUL 06-11, 2013. Wiley-Blackwell, 282−282. (SI).
5.1.
2013
Laks, Katrina; Kirsipuu, Tiina; Dmitrijeva, Tuuli; Salumets, Andres; Palumaa, Peep (2013). Assessment of blood contamination in biological fluids using MALDI-TOF MS. FEBS Journal, 280: 38th Congress of the Federation-of-European-Biochemical-Societies (FEBS), Saint Petersburg, RUSSIA, JUL 06-11, 2013. Wiley-Blackwell, 489−489. (SI).
1.1.
2012
Howells, C.; Saar, K.; Eaton, E.; Ray, S.; Palumaa, P.; Shabala, L.; Adlard, PA.; Bennett, W.; West, AK.; Guillemin, GJ.; Chung, RS. Exp Neurol. (2012). Redox-active Cu(II)-Aβ causes substantial changes in axonal integrity in cultured cortical neurons in an oxidative-stress dependent manner. Experimental Neurology, 237 (2), 499−506.
1.1.
2012
Banci, L.; Bertini, I.; Cantini, F.; Kozyreva, T.; Massagni, C.; Palumaa, P.; Rubino, JT.; Zovo, K. (2012). Human superoxide dismutase 1 (hSOD1) maturation through interaction with human copper chaperone for SOD1 (hCCS). Proceedings of the National Academy of Sciences, 109 (34), 13555−13560.
1.1.
2012
Tõugu, V.; Palumaa, P. (2012). Coordination of zinc ions to the key proteins of neurodegenerative diseases: amyloid-β peptide, APP, α-synuclein and prion protein. Coordination Chemistry Reviews, 256, 2219−2224.
1.1.
2012
Smimova, Julia; Muhhina, Jekaterina; Tougu, Vello; Palumaa, Peep (2012). Redox and Metal Ion Binding Properties of Human Insulin-like Growth Factor 1 Determined by Electrospray Ionization Mass Spectrometry. Biochemistry, 51 (29), 5851−5859. DOI: 10.1021/bi300494s.
1.1.
2012
Noormägi, A.; Primar, K.; Tõugu, V.; Palumaa, P. (2012). Interference of low-molecular substances with the thioflavin-T fluorescence assay of amyloid fibrils. Journal of Peptide Science, 18 (1), 59−64. DOI: 10.1002/psc.1416.
6.3.
2012
Palumaa, P. (2012). Elu alus. Energia ja energeetika. Horisont, 1, 10−19.
1.1.
2011
Tõugu, Vello; Tiiman, Ann; Palumaa, Peep (2011). Interactions of Zn(II) and Cu(II) ions with Alzheimer’s amyloid-beta peptide. Metal ion binding, contribution to fibrillization and toxicity. Metallomics, 3, 250−261. DOI: 10.1039/c0mt00073f.
1.1.
2010
Zovo, Kairit; Helk, Eneken; Karafin, Ann; Tõugu, Vello; Palumaa, Peep (2010). Label-Free High-Throughput Screening Assay for Inhibitors of Alzheimer’s Amyloid-β Peptide Aggregation Based on MALDI MS. Analytical Chemistry, 82 (20), 8558−8565. DOI: 10.1021/ac101583q.
1.1.
2010
Chung, RS.;, Howells, C.; Eaton, ED.; Shabala, L.; Zovo, K.; Palumaa, P.; Sillard, R.; Woodhouse, A.; Bennett, WR.; Ray, S.; Vickers, JC.; West, AK. (2010). The native copper- and zinc-binding protein metallothionein blocks copper-mediated Abeta aggregation and toxicity in rat cortical neurons. PLoS ONE, 5 (8), 1−11.
1.1.
2010
Noormägi, A.; Gavrilova, J.; Smirnova, J.; Tõugu, V.; Palumaa, P. (2010). Zn(II) ions co-secreted with insulin suppress inherent amyloidogenic properties of monomeric insulin. Biochemical Journal, 430 (3), 511−518. DOI: 10.1042/BJ20100627.
1.1.
2010
Banci, L.; Bertini, I.; Ciofi-Baffoni, S.; Kozyreva, T.; Zovo, K.; Palumaa, P. (2010). Affinity gradients drive copper to cellular destinations. Nature, 465 (7298), 645−648. DOI: 10.1038/nature09018.
1.1.
2010
Skerget, K.; Taler-Vercic, A.; Bavdek, A.; Hodnik, V.; Ceru, S.; Tusek-Znidaric, M.; Kumm, T.; Pitsi, D.; Pompe-Novak, M.; Palumaa, P.; Soriano, S.; Kopitar-Jerala, N.; Turk, V.; Anderluh, G.; Zerovnik, E. (2010). Interaction between oligomers of stefin B and amyloid-beta in vitro and in cells. Journal of Biological Chemistry, 285 (5), 3201−3210. DOI: 10.1074/jbc.M109.024620.
1.1.
2010
Leung, Y.; Pankhurst, M.; Dunlop, S.; Ray, S.; Dittmann, J.; Eaton, E.; Palumaa, P.; Sillard, R.; Chuah, M.; West, A.; Chung, R. (2010). Metallothionein induces a regenerative reactive astrocyte phenotype via JAK/STAT and RhoA signalling pathways. Experimental Neurology, 221 (1), 98−106. DOI: 10.1016/j.expneurol.2009.10.006.
5.1.
2010
Noormägi, A.; Gavrilova, J.; Smirnova, J; Tõugu, V.; Palumaa, P. (2010). Zn(II) ions inhibit fibrillization of monomeric insulin. FEBS Journal, 277: 35th FEBS Congress, Göteburg 26. juuni- 1. juuli 2010. Wiley-Blackwell, 256−256. (Suppl. 1).
5.1.
2010
Kumm, Tiina; Taler-Vercic, Ajda; Skerget, Katja; Friedemann, Merlin; Zerovnik, Eva; Palumaa, Peep (2010). Oligomerization and conformation of amyloidogenic protein human stefin B. Insight from ESI MS. FEBS Journal, 277, 258−258.
1.1.
2009
Ahte, P.; Palumaa, P.; Tamm, T. (2009). Stability and conformation of polycopper-thiolate clusters studied by density functional approach. The Journal of Physical Chemistry A, 113 (32), 9157−9164.
1.1.
2009
Tõugu, V.; Karafin, A.; Zovo, K.; Chung, R.S.; Howells, C.; West, A.K.; Palumaa, P. (2009). Zn(II) and Cu(II)-induced nonfibrillar aggregates of amyloid-beta peptide are transformed to amyloid fibrils, both spontaneously and under the influence of metal chelators. Journal of Neurochemistry, 110, 1784−1795. DOI: 10.1111/j.1471-4159.2009.06269.x.
1.1.
2009
Palumaa, P. (2009). Biological redox switches. Antioxidants and Redox Signaling, 11 (5), 981−983. DOI: 10.1089/ars.2009.2468.
1.1.
2009
Palumaa, P; Zovo, K. (2009). Modulation of redox switches of copper chaperone Cox17 by Zn(II) ions, determined by new ESI MS based approach. Antioxidants and Redox Signaling, 11 (5), 985−995. DOI: 10.1089/ars.2008.2262.
3.1.
2009
Karafin, A.; Palumaa, P.; Tõugu, V. (2009). Monitoring of Aβ fibrillization using an improved fluorimetric method. New Trends in Alzheimer and Parkinson Disorders: ADPD 2009: Alzheimer's and Parkinson's Diseases: Advances, Concepts and New Challenges. 9th International Conference AD/PD 2009. Prague, Czech Republic, March 11-15, 2009. Ed. Fisher, A.; Hanin, I. Bologna, Italy: Medimond, 255−259.
5.2.
2009
Palumaa, Peep; Karafin, Ann; Zovo, Kairit; Chung, Roger S.; Howells, Claire; West, Adrian K.; Tõugu, Vello (2009). Effect of Zn(II) and Cu(II) ions on aggregation and fibrillation of amyloid-β(1-42) peptide. Abstract Book: Sinapsa Neuroscience Conference '09, LjUbljana 26th - 29th September 2009. Toim. Kortnik, Blaž; Oskedar, Damian; Vodušek, Vid V. Ljubljana, Slovenia: SiNAPSA, Slovenian Neuroscience Association, 34.
5.2.
2009
Karafin, Ann; Palumaa, Peep; Tõugu, Vello (2009). Monitoring of amyloid-beta fibrillization using an improved fluorimetric method. In: (799−799).Alzheimer's and Parkinson's Diseases Advances, Concepts and New Challenges Congress, Prague, March 2009. Karger.
1.1.
2008
Banci, L.; Bertini, I.; Ciofi-Baffoni, S.; Hadjiloi, T.; Martinelli, M.; Palumaa, P. (2008). Mitochondrial copper(I) transfer from Cox17 to Sco1 is coupled to electron transfer. Proceedings of the National Academy of Sciences of the United States of America, 19, 6803−6808.
1.1.
2008
Smirnova, J.; Zhukova, L.; Witkiewicz-Kucharczyk, A.; Kopera, E.; Olędzki, J.; Wysłouch-Cieszyńska, A.; Palumaa, P.; Hartwig, A.; Bal, W. (2008). Reaction of the XPA zinc finger with S-nitrosoglutathione. Chemical Research in Toxicology, 21, 386−392.
1.1.
2008
Tõugu, Vello;Karafin, Ann;Palumaa, Peep (2008). Binding of zinc(II) and copper(II) to the full-length Alzheimer's amyloid-β peptide. Journal of Neurochemistry, 104, 1249−1259.
1.1.
2008
Banci, L.; Bertini, I.; Ciofi-Baffoni, S.; Janicka, A.; Martinelli, M.; Kozlowski, H.; Palumaa, P. (2008). A structural-dynamical characterization of Human Cox17. Journal of Biological Chemistry, 283 (12), 7912−7919.
5.1.
2008
Smirnova, J.; Zovo, K.; Chung, R. S.; West, A. K.; Palumaa, P. (2008). Metal-binding properties of unique Cys-deficient mammalian metallothionein - sheep MT-3. FEBS Journal: 33rd FEBS Meeting, Athens, June 28 - July 3, 2008. , 230−230. (275 ).
5.1.
2008
Karafin, A; Palumaa, P; Tougu, V. (2008). Interactions of zinc(II) and copper(II) to the full-length Alzheimer's amyloid-B peptide in vitro. FEBS Journal: 33rd FEBS Meeting, Athens, June 28-July 3, 2008. , 222−222. (275).
1.1.
2007
Voronova, A.; Meyer-Klaucke, W.; Meyer, T.; Rompel, A.; Krebs, B.; Kazantseva, J.; Sillard, R.; Palumaa, P. (2007). Oxidative switches in functioning of mammalian copper chaperone Cox17. Biochemical Journal, 408 (1), 139−148. DOI: 10.1042/BJ20070804.
1.1.
2007
Banci, L.; Bertini, I.; Ciofi-Baffoni, S.; Leontari, I.; Martinelli, M.; Palumaa, P.; Sillard, R.; Wang, S. (2007). Human Sco1 functional studies and pathological implications of P174L mutant. Proceedings of the National Academy of Sciences of the United States of America, 104 (1), 15−20.
1.1.
2007
Massad, T.; Jarvet, J.; Tanner, R.; Tomson, K.; Smirnova, J.; Palumaa, P.; Sugai, M.; Kohno, T.; Vanatalu, K.; Damberg, P. (2007). 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-couplings. Journal of Biomolecular NMR, 38 (2), 107−123.
1.1.
2007
Smirnova, J.; Zhukova, L.; Witkiewicz-Kucharczyk, A.; Kopera, E.; Olędzki, J.; Wysłouch-Cieszyńska, A.; Palumaa, P.; Hartwig, A.; Bal, W. (2007). Quantitative electrospray ionization mass spectrometry of zinc finger oxidation: The reaction of XPA zinc finger with H(2)O(2). Analytical Biochemistry, 369 (2), 226−231.
1.1.
2007
Voronova, A.; Kazantseva, J.; Tuuling, M.; Sokolova, N.; Sillard, R.;L Palumaa, P. (2007). Cox17, a copper chaperone for cytochrome c oxidase: Expression, purification and formation of mixed disulfide adducts with thiol reagents. Protein Expression and Purification, 53 (1), 138−144. DOI: 10.1016/j.pep.2006.11.014.
5.2.
2007
Chekulayeva, L.; Shevchuk, I.; Chekulayev, V.; Palumaa, P. (2007). Porphyrins and bilirubin can suppress the aggregation of Alzheimer beta-amyloid peptide. 30th Estonian Chemistry Days Abstracts of Scientific Conference: 30th Estonian Chemistry Days, Tartu 2007. Taru, Estonia: Tartu University, 165−166.
1.1.
2006
Banci, L.; Bertini, I.; Calderone, V.; Ciofi-Baffoni, S.; Mangani, S.; Martinelli, M.; Palumaa, P.; Wang, S. (2006). A hint for the function of human Sco1 from different structures. Proceedings of the National Academy of Sciences of the United States of America, 103 (23), 8595−8600.
1.1.
2006
Meloni, G.; Zovo, K.; Kazantseva, J.; Palumaa, P.; Vasak, M. (2006). Organization and assembly of metal-thiolate clusters in epithelium-specific metallothionein-4. Journal of Biological Chemistry, 281 (21), 14588−14595. DOI: 10.1074/jbc.M601724200.
1.1.
2005
Palumaa, P.; Tammiste, I.; Kangur, L.; Kruusel, K.; Jörnvall, H.; Sillard, R. (2005). Metal-binding of metallothionein-3 versus metallothionein-2: lower affinity and higher plasticity (2005), BBA. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 1747 (2), 205−211.
5.1.
2005
Palumaa, P.; Voronova, A.; Kangur, L.; Sillard, R.; Meyer-Klaucke, W.; Meyer, T.; Rompel, A. (2005). Mammalian copper chaperone Cox17 exists in two metalloforms, linked by oxidative switch. FEBS Journal, 272, 386−387.
5.2.
2005
Tomson, K.; Vanatalu, K.; Smirnova, J.; Palumaa, P.; Tanner, R.; Jarvet, J.; Gräslund, A. (2005). Production and labeling of recombinant motilin in Escherichia coli. International Conference on Environmental, Industrial and Applied Microbiology, Badajoz, Spain, 15-18 March 2005.
1.1.
2004
Palumaa, P.; Kangur, L.; Voronova, A.; Sillard, R (2004). Metal-binding mechanism of Cox17, a copper chaperone for cytochrome c oxidase. Biochemical Journal, 382, 307−314.
5.2.
2004
Palumaa, P., Sillard, R. (2004). Metal binding mechanism of cytochrome c oxidase copper chaperone Cox17. Abstract book: MBB Conference, Södertälje, Sweden, 11 – 12 March 2004. Stockholm, 46−46.
5.2.
2004
Palumaa, P., Tammiste, I., Kruusel, K., Kangur, L., Jörnvall, H., Sillard, R. (2004). Biochemical and metal-binding properties of brain-specific metallothionein-3. Abstarct book: Swiss Society of Neuropathology XXth International Winter Meeting: „Growth and Death in the Nervous System“ St. Moritz, Switzerland, 24-28 March 2004. Zürich, 45−45.
5.2.
2004
Palumaa, P.; Meyer, T.; Rompel, A.; Kangur, L.; Voronova, A.; Sillard, R. (2004). Mechanism of metal binding by Cox17, a copper chaperone for cytochrome c oxidase. Biometals 2004: 4th International Biometals Symposium (IBS-4), Garmish-Partenkirchen, Germany, 3-5 September 2004. 51−51.
1.1.
2003
Palumaa, P.; Eriste, E.; Kruusel, K.; Kangur, L.; Jornvall, H.; Sillard, R (2003). Metal binding to brain-specific metallotifhonein-3 studied by electrospray ionization mass spectrometry. Cellular and Molecular Biology, 49 (5), 763−768.
1.1.
2003
Eriste, E.; Kruusel, K.; Palumaa, P.; Jornvall, H.; Sillard, R (2003). Purification of recombinant human apometallothionein-3 and reconstitution with zinc. Protein Expression and Purification, 31 (1), 161−165.
1.1.
2002
Palumaa, P.; Njunkova, O.; Pokras, L.; Eriste, E.; Sillard, R. (2002). Evidence for non-isostructural replacement of Zn<2+> with Cd<2+> in the beta-domain of brain-specific metallothionein-3. FEBS Letters, 527, 76−80.
1.1.
2002
Palumaa, P.; Eriste, E.; Njunkova, O.; Pokras, L.; Jörnvall, H.; Sillard, R. (2002). Brain-specific metallothionein-3 has higher metal-binding capacity than ubiquitous metallothioneins and binds metals noncooperatively. Biochemistry, 41 (19), 6158−6163.
5.2.
2002
"Palumaa, Peep;Eriste, Elo;Njunkova, Olga;Pokras, Lesja;Jörnvall, H.;Sillard, Rannar" (2002). Comparison of confirmations of zinc- and cadmium-substituted metallothionein-3 by ESI MS. The 50th ASMS Conference on Mass Spectrometry and Allied Topics. Orlando, puudub−puudub.
1.1.
2001
Vaher, M.; Romero-Isart, N.; Vasak, M.; Palumaa, P (2001). Reactivity of Cd-7-metallothionein with Cu(II) ions: evidence for a cooperative formation of Cd-3,Cu(I)(5)-metallothionein. Journal of Inorganic Biochemistry, 83 (1), 1−6.
1.1.
2001
Kangur, L.; Palumaa, P (2001). The effects of physiologically important nonmetallic ligands in the reactivity of metallothionein towards 5,5'-dithiobis(2-nitrobenzoic acid). European Journal of Biochemistry, 268 (18), 4979−4984.
5.2.
2001
Sillard, R.; Eriste, E.; Njunkova, O.; Pokras, L.; Jörnvall, H.; Wadensten, H.; Renlund, S.; Palumaa, P. (2001). Determination of metal-protein complexes and posttranslational modifications by LC-(ESI-TOF)-MS. Proceedings of the 49th ASMS Conference on Mass Spectrometry and Allied Topics : Chicago, Illinois, May 27-31, 2001. , 11−12.
1.1.
1999
Bonetto, V.; Kangur, L.; Palumaa, P.; Mutt, V.; Jornvall, H.; Sillard, R. (1999). Large-scale HPLC purification of calbindin D9k from porcine intestine. Protein Expression and Purification, 17 (3), 387−391.
3.1.
1998
Palumaa, P.; Lehtme, R. (1998). Biochemical characterization of monomeric and dimeric cadmium-substituted metallothionein-3. Metallothionein IV (63−69).. Basel: Birkhäuser, Boston.
1.1.
1996
Palumaa, P.; Vaher, M. (1996). Metal-induced dimerization of Cd7-metallothionein. Role of Anions. Annals of clinical and laboratory science, 26 (3), 264−268.
1.1.
1993
Palumaa, P.; Vasak, M. (1993). Formation and spectroscopic characterization of a novel monomeric cadmium- and phosphate-containing form of metallothionein. Biochemistry, 32, 2874−2879.
1.1.
1992
Santa, H.; Laatikainen, R.; Lötjonen, S.; Palumaa, P. (1992). Dynamic NMR determination of the N,N-dimethyl inversion rate and apparent Inversion free energy in 2-hydroxy-N,N-dimethyl-2-phenylethylamine. Journal of Chemical Research, (S) (6), 198−199.
1.1.
1992
Palumaa, P.; Vasak, M. (1992). Binding of inorganic phosphate to the cadmium-induced dimeric form of metallothionein from rabbit liver. European Journal of Biochemistry, 205, 1131−1135.
1.1.
1992
Palumaa, P.; Mackay, E A.; Vasak, M. (1992). Nonoxidative cadmium-dependent dimerization of Cd7-metallothionein from rabbit liver. Biochemistry, 31, 2181−2186.
1.1.
1991
Zorko, M.; Palumaa, P.; Kask, K. (1991). Binding of some aromatic ligands to the active site of acetylcholinesterase. Periodicum Biologorum, 2, 355−356.
1.1.
1990
Zorko, M.; Langel, Ü.; Palumaa, P. (1990). Simultaneous action of quaternary ammonium ligands and alkanesulfonylchlorides on electric eel acetylcholinesterase. Periodicum Biologorum, 4, 385−391.
1.1.
1989
Palumaa, P.; Kask, K. (1989). Biomimetic modelling of spatial structure of acetylcholinesterase active site with cyclodextrins. Organic Reactivity, 26, 122−141.
1.1.
1988
Eller, M.; Jarv, J.; Palumaa, P. (1988). Influence of non-radioactive ligands on kinetics of normal-methyl-[3h]scopolamine binding to muscarinic receptor. Organic Reactivity, 25, 372−386.
1.1.
1987
Palumaa, P.; Järv, J.; Schevchenko, V.; Myasojedov, N. (1987). Synthesis f -(N,N-dimethylamino)4,-3H-acetophenon. Radiokhim (USSR), 29 (2), 231−232.
1.1.
1987
Soomets, UV.; Palumaa, PJ.; Yarv, JL. (1987). Mechanism of reaction of n,n-dimethyl-2-phenyl-aziridinium ion in acetylcholinesterase active-center. Bioorganicheskaya Khimiya, 13 (2), 198−203.
1.1.
1985
Palumaa, PJ.; Jarv, JL. (1985). Alkylboronic acid acceleration of acetylcholinesterase alkylation with n,n-dimethyl-2-phenylaziridinium ion. Bioorganicheskaya Khimiya, 11 (9), 1210−1216.
1.1.
1985
Palumaa, P.; Soomets, U.; Jarv, J. (1985). Effects of reaction medium and temperature on solvolysis of n,n-dimethyl-2-phenylaziridinium ion. Organic Reactivity, 22 (2), 238−257.
1.1.
1985
Palumaa, PJ.; Raidaru, GI.; Jarv, JL.; Schevchenko, VP.; Myasoyedov, NF. (1985). Synthesis of tritium labeled n,n-dimethyl-2-phenylaziridinium and its reaction with acetylcholinesterase. Bioorganicheskaya Khimiya, 11 (10), 1348−1352.
1.1.
1984
Palumaa, P.; Jarv, J. (1984). Alkylboronic acids accelerate affinity labeling of acetylcholinesterase with n,n-dimethyl-2-phenylaziridinium ion. Biochimica et Biophysica Acta, 784 (1), 35−39.
1.1.
1984
Palumaa, P.; Raba, R.; Jarv, J. (1984). Site-specificity of butyrylcholinesterase alkylation with n,n-dimethyl-2-phenylaziridinium ion. Biochimica et Biophysica Acta, 791 (1), 15−20.
1.1.
1983
Palumaa, PJ.; Kaambre, TH.; Jarv, JL. (1983). Kinetics of the reaction of n,n-dimethyl-2-phenylaziridinium ions with muscarinic receptor and acetylcholinesterases. Биоорганическая химия, 9 (10), 1348−1356.
1.1.
1982
Palumaa, P.; Mahar, A.; Jarv, J. (1982). Kinetic-analysis of butyrylcholinesterase inhibition with n,n-dimethyl-2-phenylaziridinium ion. Bioorganic Chemistry, 11 (4), 394−403.

Industrial property

16.12.2021